|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-532 |
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: 973.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 11 PVNEPVNSYAPGTNEKTLLEAAIKEARGQEKDIPMYIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALA 90
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 91 AKEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATMLGQSKNAYQAEIDSACELADFLRFNVAYMTEIYSQQPPANAKG 170
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 171 VWNRVEQRPLEGFVFALTPFNFTAIAGNLPSCVAMMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAG 250
Cdd:cd07123 161 VWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 251 DVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSA 330
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 331 ASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSADAEVVIGGQYDKSKGYFIHP 410
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 411 TVILAKKADYETMSEELFGPVLTIYVYEDDKWEETLELVDKTSIYALTGSIISQCRYAIDEATYALRNAAGNFYINDKCT 490
Cdd:cd07123 401 TVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1819620888 491 GAVVGQQPFGGARGSGTNDKAGSMINLFRWVSPRTIKETFHP 532
Cdd:cd07123 481 GAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
13-542 |
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: 788.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 13 NEPVNSYAPGTNEKTLLEAAIKEARGQEKDIPMYIGGEEVRTGN-KAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAA 91
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNeRIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 92 KEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATMLGQSKNAYQAEIDSACELADFLRFNVAYMTEIYSQQPpANAKGV 171
Cdd:TIGR01236 82 KKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQP-ISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 172 WNRVEQRPLEGFVFALTPFNFTAIAGNLPSCVAMMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGD 251
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 252 VIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAA 331
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 332 SRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSADA-EVVIGGQYDKSKGYFIHP 410
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAlTILYGGKYDDSQGYFVEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 411 TVILAKKADYETMSEELFGPVLTIYVYEDDKWEETLELVDKTSIYALTGSIISQCRYAIDEATYALRNAAGNFYINDKCT 490
Cdd:TIGR01236 401 TVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKCT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1819620888 491 GAVVGQQPFGGARGSGTNDKAGSMINLFRWVSPRTIKETFHPETDYRYPFLG 542
Cdd:TIGR01236 481 GAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
40-530 |
2.85e-150 |
|
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: 439.56 E-value: 2.85e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 40 EKDIPMYIGGEEVR--TGNKAKLTPPHDhQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTK 117
Cdd:COG1012 3 TPEYPLFIGGEWVAaaSGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL-EE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 118 YRYKINAATMLGQSKNAYQA--EIDSAcelADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAI 195
Cdd:COG1012 81 RREELAALLTLETGKPLAEArgEVDRA---ADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 196 AGNLPSCVAM-MGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNI 274
Cdd:COG1012 157 LAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 275 WKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQS 354
Cdd:COG1012 237 AAAAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 355 FKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKsSADAEVVIGGQY-DKSKGYFIHPTVILAKKADYETMSEELFGPVLT 433
Cdd:COG1012 311 LKVGDPLDPGTDMGPLISEAQLERVLAYIEDAV-AEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 434 IYVYEDdkWEETLELVDKTsIYALTGSIISQCRYAIDEATYALRnaAGNFYINDKCTGAvVGQQPFGGARGSGTNDKAGS 513
Cdd:COG1012 390 VIPFDD--EEEAIALANDT-EYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGR 463
|
490
....*....|....*..
gi 1819620888 514 MiNLFRWVSPRTIKETF 530
Cdd:COG1012 464 E-GLEEYTETKTVTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
29-530 |
5.19e-142 |
|
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: 419.29 E-value: 5.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 29 LEAAIKEARG-QEKDIPMYIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIF 107
Cdd:cd07083 4 MREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 108 LKAAELVSTKYRYKINAATMLGqSKNaYQAEIDSACELADFLRFNVAYMTEIYSQQP-PANAKGVWNRVEQRPLeGFVFA 186
Cdd:cd07083 84 LKAADLLRRRRRELIATLTYEV-GKN-WVEAIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGL-GAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 187 LTPFNFT-AIAGNLPSCVAMMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFT 265
Cdd:cd07083 161 ISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 266 GSTGVFQNIWKTIGENIHRYKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLR 345
Cdd:cd07083 241 GSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 346 TRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSadAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSE 425
Cdd:cd07083 321 ERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE--GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 426 ELFGPVLTIYVYEDDKWEETLELVDKTSiYALTGSIISQCRYAIDEATYALrnAAGNFYINDKCTGAVVGQQPFGGARGS 505
Cdd:cd07083 399 EIFGPVLSVIRYKDDDFAEALEVANSTP-YGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGFKLS 475
|
490 500
....*....|....*....|....*
gi 1819620888 506 GTNDKAGSMINLFRWVSPRTIKETF 530
Cdd:cd07083 476 GTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-530 |
1.62e-127 |
|
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: 382.34 E-value: 1.62e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 12 VNEPVNSYAPGTNeKTLLEAAIKEARGQ-EKDIPMYIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALA 90
Cdd:cd07124 2 RNEPFTDFADEEN-RAAFRAALARVREElGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 91 AKEKWENLPWEQRAAIFLKAAELVSTKyRYKINAATMLGQSKNAYQAEIDsACELADFLRFnVAYMTEIYSQQPPANAKG 170
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADAD-VAEAIDFLEY-YAREMLRLRGFPVEMVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 171 VWNRVEQRPLeGFVFALTPFNF-TAIAGNLPSCVAMMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINlvYVSGPDA 249
Cdd:cd07124 158 EDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVN--FLPGPGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 250 --GDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTYPRIVGETGGKDFILAHPSADI--AVlnTALVRGAFEFQG 325
Cdd:cd07124 235 evGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLdeAA--EGIVRSAFGFQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 326 QKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSsaDAEVVIGGQYD--KS 403
Cdd:cd07124 313 QKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKS--EGRLLLGGEVLelAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 404 KGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQCRYAIDEATYALRnaAGNF 483
Cdd:cd07124 391 EGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIANDTE-YGLTGGVFSRSPEHLERARREFE--VGNL 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1819620888 484 YINDKCTGAVVGQQPFGGARGSGTNDKAGSMINLFRWVSPRTIKETF 530
Cdd:cd07124 466 YANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
13-530 |
1.95e-112 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 343.84 E-value: 1.95e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 13 NEPVNSYAPGTNEKTLlEAAIKEARGQ-EKDIPMYIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAA 91
Cdd:PRK03137 7 HEPFTDFSVEENVEAF-EEALKKVEKElGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 92 KEKWENLPWEQRAAIFLKAAELVSTKyRYKINAATMLGQSKNAYQAEIDSAcELADFLRFNVAYMTEIYSQQPPANAKGV 171
Cdd:PRK03137 86 FETWKKWSPEDRARILLRAAAIIRRR-KHEFSAWLVKEAGKPWAEADADTA-EAIDFLEYYARQMLKLADGKPVESRPGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 172 WNRVEQRPLeGFVFALTPFNF-TAI-AGNLPSCVAmMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDA 249
Cdd:PRK03137 164 HNRYFYIPL-GVGVVISPWNFpFAImAGMTLAAIV-AGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 250 GDVIFKHPDFAGIHFTGStgvfqniwKTIGENIHRY--KTYP------RIVGETGGKDFILAHPSADIAVLNTALVRGAF 321
Cdd:PRK03137 242 GDYLVDHPKTRFITFTGS--------REVGLRIYERaaKVQPgqiwlkRVIAEMGGKDAIVVDEDADLDLAAESIVASAF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 322 EFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFsNFINAVIDEKAFDKITSYIDRAKSsaDAEVVIGGQYD 401
Cdd:PRK03137 314 GFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKE--EGRLVLGGEGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 402 KSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQCRYAIDEATYALRnaAG 481
Cdd:PRK03137 391 DSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANNTE-YGLTGAVISNNREHLEKARREFH--VG 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1819620888 482 NFYINDKCTGAVVGQQPFGGARGSGTNDKAGSMINLFRWVSPRTIKETF 530
Cdd:PRK03137 466 NLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
63-513 |
1.70e-106 |
|
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: 326.41 E-value: 1.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 63 PHDhQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKINAATMLGQSKNAYQA--EID 140
Cdd:pfam00171 14 PAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLL-EERKDELAELETLENGKPLAEArgEVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 141 SAcelADFLRFNVAYMTEIYSQQPPaNAKGVWNRVEQRPLeGFVFALTPFNFTA--IAGNLPSCVAMmGNVVVWKPSNTQ 218
Cdd:pfam00171 92 RA---IDVLRYYAGLARRLDGETLP-SDPGRLAYTRREPL-GVVGAITPWNFPLllPAWKIAPALAA-GNTVVLKPSELT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 219 IYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGK 298
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 299 DFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDK 378
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 379 ITSYIDRAKsSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDkTSIYALT 458
Cdd:pfam00171 320 VLKYVEDAK-EEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE--EEAIEIAN-DTEYGLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1819620888 459 GSIISQcryAIDEATYALRNA-AGNFYINDKCTGAVVGqQPFGGARGSGTNDKAGS 513
Cdd:pfam00171 396 AGVFTS---DLERALRVARRLeAGMVWINDYTTGDADG-LPFGGFKQSGFGREGGP 447
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-530 |
4.43e-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: 319.50 E-value: 4.43e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 13 NEPVNSYAPGTNEKTLLEA--AIKEARGqeKDIPMYIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALA 90
Cdd:TIGR01237 3 HEPFTDFADEENRQAFFKAlaTVKEQLG--KTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 91 AKEKWENLPWEQRAAIFLKAAELVSTKyRYKINAATMLGQSKNAYQAEIDSAcELADFLRFNVAYMTEIYSQQPPANAKG 170
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVNSREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 171 VWNRVEQRPLeGFVFALTPFNFT-AIAGNLPSCVAMMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDA 249
Cdd:TIGR01237 159 ETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 250 GDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCS 329
Cdd:TIGR01237 238 GDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 330 AASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSsaDAEVVIGGQYDKSKGYFIH 409
Cdd:TIGR01237 318 AGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKA--EGRLVSGGCGDDSKGYFIG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 410 PTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQCRYAIDEATYALRnaAGNFYINDKC 489
Cdd:TIGR01237 396 PTIFADVDRKARLAQEEIFGPVVAFIRASD--FDEALEIANNTE-YGLTGGVISNNRDHINRAKAEFE--VGNLYFNRNI 470
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1819620888 490 TGAVVGQQPFGGARGSGTNDKAGSMINLFRWVSPRTIKETF 530
Cdd:TIGR01237 471 TGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
82-526 |
1.94e-98 |
|
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: 304.90 E-value: 1.94e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 82 EDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATM-LGQSKNAYQAEIDSAcelADFLRFNVAYMTEIY 160
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLeTGKPIEEALGEVARA---ADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 161 SQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAIAGNLPSCVA-MMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVI 239
Cdd:cd07078 78 GEVIPSPDPGELAIVRREPL-GVVGAITPWNFPLLLAAWKLAPAlAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 240 NLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLNTALVRG 319
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 320 AFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKsSADAEVVIGGQ 399
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAK-AEGAKLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 400 YDKS-KGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSIISQCRYAIDEATYALRn 478
Cdd:cd07078 310 RLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELANDT-EYGLAAGVFTRDLERALRVAERLE- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1819620888 479 aAGNFYINDKcTGAVVGQQPFGGARGSGTNdKAGSMINLFRWVSPRTI 526
Cdd:cd07078 386 -AGTVWINDY-SVGAEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-512 |
4.44e-76 |
|
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: 249.42 E-value: 4.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 29 LEAAIKEARGQE-KDIPMyIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIF 107
Cdd:cd07125 19 LADALKAFDEKEwEAIPI-INGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 108 LKAAELVStKYRYKINAATMLGQSKNAYQAeIDSACELADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFAL 187
Cdd:cd07125 98 EKAADLLE-ANRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGR-GVFVCI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 188 TPFNF-TAI-AGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFT 265
Cdd:cd07125 175 SPWNFpLAIfTGQIAAALAA-GNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 266 GSTGVFQNIWKTigeNIHRYKTYPRIVGETGGKDFILAHPSADI--AVLNtaLVRGAFEFQGQKCSAASRAYIPQSLWSD 343
Cdd:cd07125 254 GSTETAKLINRA---LAERDGPILPLIAETGGKNAMIVDSTALPeqAVKD--VVQSAFGSAGQRCSALRLLYLQEEIAER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 344 LRtRMEKD-IQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRakSSADAEVVIGGQYDKSKGYFIHPTVILAKKADYET 422
Cdd:cd07125 329 FI-EMLKGaMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTEL--MRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDLT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 423 msEELFGPVLTIYVYEDDKWEETLELVDKTSiYALTGSIISqcryaIDEAT---YALRNAAGNFYINDKCTGAVVGQQPF 499
Cdd:cd07125 406 --TEVFGPILHVIRFKAEDLDEAIEDINATG-YGLTLGIHS-----RDEREieyWRERVEAGNLYINRNITGAIVGRQPF 477
|
490
....*....|...
gi 1819620888 500 GGARGSGTNDKAG 512
Cdd:cd07125 478 GGWGLSGTGPKAG 490
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
86-526 |
6.01e-68 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 223.65 E-value: 6.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 86 DAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATM-LGQSKNAYQAEIDsacELADFLRFNVAYMTEIYSQQP 164
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLeTGKPIEEALGEVA---RAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 165 PANAKGVWNRVEQRPLeGFVFALTPFNFTAIAGNLPSCVAM-MGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVY 243
Cdd:cd06534 78 PSPDPGGEAYVRREPL-GVVGVITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 244 VSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEF 323
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 324 QGQKCSAASRAYIPQSLWsdlrtrmekdiqsfkiggtedfsnfinaviDEkafdkitsYIDRAKssadaevviggqydks 403
Cdd:cd06534 231 AGQICTAASRLLVHESIY------------------------------DE--------FVEKLV---------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 404 kgyfihpTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSIISQCRYAIDEATYALRnaAGNF 483
Cdd:cd06534 257 -------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALANDT-EYGLTAGVFTRDLNRALRVAERLR--AGTV 324
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1819620888 484 YINDKCTGaVVGQQPFGGARGSGTNDKAGSMiNLFRWVSPRTI 526
Cdd:cd06534 325 YINDSSIG-VGPEAPFGGVKNSGIGREGGPY-GLEEYTRTKTV 365
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-506 |
9.24e-67 |
|
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: 222.98 E-value: 9.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVstKYRYKINAATMLGQSKNAYQAEIDSACELADF 148
Cdd:cd07150 11 VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIM--ERRADDLIDLLIDEGGSTYGKAWFETTFTPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 149 LRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAIAGNLPSCVAM-MGNVVVWKPSNTQIYSANVIME 227
Cdd:cd07150 89 LRAAAGECRRVRGETLPSDSPGTVSMSVRRPL-GVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 228 VFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGenihryKTYPRIVGETGGKD--FILAHP 305
Cdd:cd07150 168 IMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNplIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 306 SADIAVlnTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDR 385
Cdd:cd07150 242 DLDYAV--RAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 386 AKSSAdAEVVIGGQYDkskGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQc 465
Cdd:cd07150 320 AVAKG-AKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDA--EEALELANDTE-YGLSAAILTN- 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1819620888 466 ryAIDEAT-YALRNAAGNFYINDKC--TGAVVgqqPFGGARGSG 506
Cdd:cd07150 392 --DLQRAFkLAERLESGMVHINDPTilDEAHV---PFGGVKASG 430
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
46-506 |
2.91e-66 |
|
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: 222.12 E-value: 2.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAA-ELVSTKYRYKINA 124
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGdELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 125 ATMLGQSKNAYQAEIDSAcelADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNF-TAIAG--NLPS 201
Cdd:cd07097 84 TREEGKTLPEARGEVTRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPL-GVVGLITPWNFpIAIPAwkIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 202 CVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEN 281
Cdd:cd07097 160 LAY--GNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 282 IHRYKTyprivgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTE 361
Cdd:cd07097 238 GARVQL------EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 362 DFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDKS--KGYFIHPTVILAKKADYETMSEELFGPVLTIYVYED 439
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARSEG-AKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 440 dkWEETLELVDKTSiYALTGSIISQcryAIDEATYALRNA-AGNFYINDKCTGaVVGQQPFGGARGSG 506
Cdd:cd07097 391 --YDEALAIANDTE-FGLSAGIVTT---SLKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSS 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
46-507 |
2.76e-64 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 217.22 E-value: 2.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEVRTGNKAKLTP--PHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVstKYRYKIN 123
Cdd:cd07131 2 YIGGEWVDSASGETFDSrnPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELL--KKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 124 AATM---LGQSKNAYQAEIDSACELADFlrfnVA------YMTEIYSQQPPANAKGVwnrveQRPLeGFVFALTPFNF-T 193
Cdd:cd07131 80 ARLVtreMGKPLAEGRGDVQEAIDMAQY----AAgegrrlFGETVPSELPNKDAMTR-----RQPI-GVVALITPWNFpV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 194 AIAG--NLPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVF 271
Cdd:cd07131 150 AIPSwkIFPALVC--GNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 272 QNIWKTIGenihryKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKD 351
Cdd:cd07131 228 ERIGETCA------RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVER 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 352 IQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSaDAEVVIGGQ----YDKSKGYFIHPTVILAKKADYETMSEEL 427
Cdd:cd07131 302 AKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEE-GATLLLGGErltgGGYEKGYFVEPTVFTDVTPDMRIAQEEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 428 FGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQcryAIDEATYALRNA-AGNFYINDKCTGAVVgQQPFGGARGSG 506
Cdd:cd07131 381 FGPVVALIEVSSL--EEAIEIANDTE-YGLSSAIYTE---DVNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSG 453
|
.
gi 1819620888 507 T 507
Cdd:cd07131 454 N 454
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
81-506 |
6.56e-63 |
|
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: 212.01 E-value: 6.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKInAATMLGQSKNAY---QAEIDSAcelADFLRFNVAYMT 157
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEIL-EERRDEI-ADWLIRESGSTRpkaAFEVGAA---IAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 158 EIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAIAGNLPSCVAM-MGNVVVWKPS-NTQIYSANVIMEVFIEAGLP 235
Cdd:cd07104 77 RPEGEILPSDVPGKESMVRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 236 KGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHryktypRIVGETGGKDFILAHPSADIAVLNTA 315
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLK------KVALELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 316 LVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKsSADAEVV 395
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAV-AAGARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 396 IGGQYDkskGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQcryAIDEAT-Y 474
Cdd:cd07104 309 TGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVELANDTE-YGLSAAVFTR---DLERAMaF 379
|
410 420 430
....*....|....*....|....*....|....*
gi 1819620888 475 ALRNAAGNFYINDKcT---GAVVgqqPFGGARGSG 506
Cdd:cd07104 380 AERLETGMVHINDQ-TvndEPHV---PFGGVKASG 410
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
69-507 |
2.84e-58 |
|
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: 200.48 E-value: 2.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKINAATMLGQSKNAYQA---EIDSACE- 144
Cdd:cd07093 9 VLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLI-EARADELALLESLDTGKPITLArtrDIPRAAAn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 145 ---LADFlrfnVAYM-TEIYSQQPpanakGVWNRVEQRPLeGFVFALTPFNftaiagnLP---------SCVAMmGNVVV 211
Cdd:cd07093 88 frfFADY----ILQLdGESYPQDG-----GALNYVLRQPV-GVAGLITPWN-------LPlmlltwkiaPALAF-GNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 212 WKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTypri 291
Cdd:cd07093 150 LKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 292 vgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVI 371
Cdd:cd07093 226 --ELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 372 DEKAFDKITSYIDRAKsSADAEVVIGG----QYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLE 447
Cdd:cd07093 304 SKEHLEKVLGYVELAR-AEGATILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819620888 448 LVDKTsIYALTGSIISQcryaiDEATyALRNA----AGNFYINdkCTGAVVGQQPFGGARGSGT 507
Cdd:cd07093 381 LANDT-PYGLAAYVWTR-----DLGR-AHRVArrleAGTVWVN--CWLVRDLRTPFGGVKASGI 435
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
46-513 |
1.41e-57 |
|
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: 199.20 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEV--RTGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAA-KEKWENLPWEQRAAIFLKAAELVStKYRYKI 122
Cdd:cd07113 3 FIDGRPVagQSEKRLDITNPATEQ-VIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE-QHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 123 NAATMLGQSKN-AYQAEIDSACELAdFLRFNVAYMTEIYSQ--QP--PANAKGVWNRVEQRPLEGFVFALTPFNFTAIAG 197
Cdd:cd07113 81 AQLETLCSGKSiHLSRAFEVGQSAN-FLRYFAGWATKINGEtlAPsiPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 198 NLPSCVAMM-GNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGpDAGDVIFKHPDFAGIHFTGSTGVFQNIWK 276
Cdd:cd07113 160 VWKIGAALAtGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 277 TIGENIHRYKTyprivgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFK 356
Cdd:cd07113 239 QAASDLTRVTL------ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 357 IGGTEDFSNFINAVIDEKAFDKITSYIDRAKsSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYV 436
Cdd:cd07113 313 VGSPMDESVMFGPLANQPHFDKVCSYLDDAR-AEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 437 YEDDkwEETLELVDKTSiYALTGSIISQcryAIDEA-TYALRNAAGNFYINDKC--TGAVvgqqPFGGARGSGTNDKAGS 513
Cdd:cd07113 392 YEDE--EELIQLINDTP-FGLTASVWTN---NLSKAlRYIPRIEAGTVWVNMHTflDPAV----PFGGMKQSGIGREFGS 461
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
60-507 |
1.11e-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: 196.28 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 60 LTPPHDhQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVstKYRYKINAATM---LGQSKNAYQ 136
Cdd:cd07149 3 VISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLL--EERREEFARTIaleAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 137 AEIDSACELadfLRFNVAYMTEIYSQQPPANA-KGVWNRVE---QRPLeGFVFALTPFNF----------TAIAGnlpsc 202
Cdd:cd07149 80 KEVDRAIET---LRLSAEEAKRLAGETIPFDAsPGGEGRIGftiREPI-GVVAAITPFNFplnlvahkvgPAIAA----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 203 vammGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniwktiGENI 282
Cdd:cd07149 151 ----GNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAV--------GEAI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 283 HRYKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTED 362
Cdd:cd07149 219 ARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 363 FSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDkskGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkW 442
Cdd:cd07149 299 EDTDVGPMISEAEAERIEEWVEEAVEGG-ARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDT--L 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819620888 443 EETLELVDKtSIYALTGSIISQcryAIDEATYALRN-AAGNFYINDKCTgAVVGQQPFGGARGSGT 507
Cdd:cd07149 373 DEAIAMAND-SPYGLQAGVFTN---DLQKALKAARElEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-524 |
1.96e-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: 194.36 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 24 NEKTLLEAAIKEARGQEKDIPMYIGGEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQR 103
Cdd:TIGR01238 19 SELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 104 AAIFLKAAELVSTKYRYKInaATMLGQSKNAYQAEIDSACELADFLRFnvaymteiYSQQppanAKGVWNRVEQRPLeGF 183
Cdd:TIGR01238 99 AAKLDRLADLLELHMPELM--ALCVREAGKTIHNAIAEVREAVDFCRY--------YAKQ----VRDVLGEFSVESR-GV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 184 VFALTPFNFT-AI-AGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAG 261
Cdd:TIGR01238 164 FVCISPWNFPlAIfTGQISAALAA-GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 262 IHFTGSTGVFQNIWKTIGEnihRYKTYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLW 341
Cdd:TIGR01238 243 VAFTGSTEVAQLINQTLAQ---REDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 342 SDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYID--RAKSSADAEVVIGGQYDKSKGYFIHPTVIlaKKAD 419
Cdd:TIGR01238 320 DRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEhmSQTQKKIAQLTLDDSRACQHGTFVAPTLF--ELDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 420 YETMSEELFGPVLTIYVYEDDKWEETLELVDKTSiYALTGSIISQcryaiDEATYAL---RNAAGNFYINDKCTGAVVGQ 496
Cdd:TIGR01238 398 IAELSEEVFGPVLHVVRYKARELDQIVDQINQTG-YGLTMGVHSR-----IETTYRWiekHARVGNCYVNRNQVGAVVGV 471
|
490 500
....*....|....*....|....*...
gi 1819620888 497 QPFGGARGSGTNDKAGSMINLFRWVSPR 524
Cdd:TIGR01238 472 QPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
76-522 |
1.62e-54 |
|
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: 190.59 E-value: 1.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 76 GTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINA-ATMLGQSKNAYQAEIDSACEladFLRFNVA 154
Cdd:cd07151 29 ASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWlIRESGSTRIKANIEWGAAMA---ITREAAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 155 YMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNF----------TAIAgnlpscvamMGNVVVWKP-SNTQIYSAN 223
Cdd:cd07151 106 FPLRMEGRILPSDVPGKENRVYREPL-GVVGVISPWNFplhlsmrsvaPALA---------LGNAVVLKPaSDTPITGGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 224 VIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHryktypRIVGETGGKDFILA 303
Cdd:cd07151 176 LLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK------KVALELGGNNPFVV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 304 HPSADI-AVLNTALVrGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSY 382
Cdd:cd07151 250 LEDADIdAAVNAAVF-GKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 383 IDRAKsSADAEVVIGGQYDkskGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSII 462
Cdd:cd07151 329 IEQAV-EEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALELANDTE-YGLSGAVF 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 463 SQcryAIDEAT-YALRNAAGNFYINDKctgaVVGQQP---FGGARGSGTNDKAGS-MINLF---RWVS 522
Cdd:cd07151 402 TS---DLERGVqFARRIDAGMTHINDQ----PVNDEPhvpFGGEKNSGLGRFNGEwALEEFttdKWIS 462
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
75-506 |
3.14e-54 |
|
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: 189.66 E-value: 3.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 75 EGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTkyrykiNA---ATML----GQSKNAYQAEIDSAcelAD 147
Cdd:cd07106 15 VASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEA------NAeelARLLtleqGKPLAEAQFEVGGA---VA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 148 FLRFNVAYM--TEIYSQQPPAnakgvwnRVEQR--PLeGFVFALTPFNFTAI--AGNLPSCVaMMGNVVVWKPSNTQIYS 221
Cdd:cd07106 86 WLRYTASLDlpDEVIEDDDTR-------RVELRrkPL-GVVAAIVPWNFPLLlaAWKIAPAL-LAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 222 ANVIMEVFIEAgLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryKtypRIVGETGGKDFI 301
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVV-SGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTL---K---RVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 302 LAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITS 381
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 382 YIDRAKSSaDAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSI 461
Cdd:cd07106 309 LVEDAKAK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE--DEVIARANDS-EYGLGASV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1819620888 462 ISQcryAIDEA-TYALRNAAGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:cd07106 385 WSS---DLERAeAVARRLEAGTVWIN--THGALDPDAPFGGHKQSG 425
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
60-507 |
7.09e-54 |
|
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: 188.74 E-value: 7.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 60 LTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKyrykinaATMLG-----QSKNA 134
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREH-------AEELAlidalDCGNP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 135 YQAEIDSACELADFLRFNVAYMTEIYSQQPPANAKGvWNRVEQRPLeGFVFALTPFN----FTA--IAGNLpscvaMMGN 208
Cdd:cd07107 73 VSAMLGDVMVAAALLDYFAGLVTELKGETIPVGGRN-LHYTLREPY-GVVARIVAFNhplmFAAakIAAPL-----AAGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 209 VVVWKPSNTQIYSANVIMEVFIEAgLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRykty 288
Cdd:cd07107 146 TVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKH---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 289 prIVGETGGKDFILAHPSADIAVLNTALVRGA-FEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFI 367
Cdd:cd07107 221 --VTLELGGKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 368 NAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDK----SKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwE 443
Cdd:cd07107 299 GPLVSRQQYDRVMHYIDSAKREG-ARLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--A 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 444 ETLELVDKTSiYALTGSIISQcryAIDEA-TYALRNAAGNFYINDKCT---GAvvgqqPFGGARGSGT 507
Cdd:cd07107 376 EMVAQANGVE-YGLTAAIWTN---DISQAhRTARRVEAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
46-506 |
1.76e-53 |
|
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: 188.16 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEVRT-GNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAA-KEKWENLPWEQRAAIFLKAAELVStKYRYKIN 123
Cdd:cd07082 5 LINGEWKESsGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK-ENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 124 AATML--GQSKNAYQAEIDSAcelADFLRFNVAYMTEIYSQQPP----ANAKGVWNRVEQRPLeGFVFALTPFN------ 191
Cdd:cd07082 83 NLLMWeiGKTLKDALKEVDRT---IDYIRDTIEELKRLDGDSLPgdwfPGTKGKIAQVRREPL-GVVLAIGPFNyplnlt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 192 FTAIAgnlPSCVamMGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVF 271
Cdd:cd07082 159 VSKLI---PALI--MGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 272 QNIWKtigenIHRYKtypRIVGETGGKDFILAHPSADIAvlNTA--LVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRME 349
Cdd:cd07082 234 NRLKK-----QHPMK---RLVLELGGKDPAIVLPDADLE--LAAkeIVKGALSYSGQRCTAIKRVLVHESVADELVELLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 350 KDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDksKGYFIHPTVILAKKADYETMSEELFG 429
Cdd:cd07082 304 EEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKG-ATVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 430 PVLTIYVYEDDkwEETLELVDKtSIYALTGSIISQCRYAIDEATYALRnaAGNFYINDKCtgavvgQQ-----PFGGARG 504
Cdd:cd07082 381 PVLPIIRVNDI--EEAIELANK-SNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhfPFLGRKD 449
|
..
gi 1819620888 505 SG 506
Cdd:cd07082 450 SG 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
66-506 |
3.04e-53 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 187.16 E-value: 3.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 66 HQHVLGYYHEGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVSTKyRYKINAATMLGQSKNAYQA--EIDS 141
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 142 AcelADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTA--IAGNLPSCVAMmGNVVVWKPSNTQI 219
Cdd:cd07118 85 A---ADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPI-GVVGIITPWNFPFliLSQKLPFALAA-GCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 220 YSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRyktypriVG-ETGGK 298
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK-------VSlELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 299 DFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDK 378
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 379 ITSYIDRAKSSAdAEVVIGG-QYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYAL 457
Cdd:cd07118 313 ITDYVDAGRAEG-ATLLLGGeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDT--VDEAIALANDTV-YGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1819620888 458 TGSIISQcryAIDEATYALRNA-AGNFYINDKCTGAVvgQQPFGGARGSG 506
Cdd:cd07118 389 SAGVWSK---DIDTALTVARRIrAGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
69-507 |
4.71e-53 |
|
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: 186.79 E-value: 4.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATM-LGQSKNAYQAEIDSACELad 147
Cdd:cd07145 11 VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIeVGKPIKQSRVEVERTIRL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 148 fLRFNVAYMTEIYSQQPPANA-KGVWNRV--EQRPLEGFVFALTPFNFTA------IAGNLPscvamMGNVVVWKPSNTQ 218
Cdd:cd07145 89 -FKLAAEEAKVLRGETIPVDAyEYNERRIafTVREPIGVVGAITPFNFPAnlfahkIAPAIA-----VGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 219 IYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGenihryKTYPRIVGETGGK 298
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 299 DFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDK 378
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 379 ITSYIDRAKsSADAEVVIGGQYDksKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALT 458
Cdd:cd07145 317 MENLVNDAV-EKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKD--DEEAVEIANSTE-YGLQ 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1819620888 459 GSIISQcryAIDEATYALRN-AAGNFYINDKcTGAVVGQQPFGGARGSGT 507
Cdd:cd07145 391 ASVFTN---DINRALKVARElEAGGVVINDS-TRFRWDNLPFGGFKKSGI 436
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
15-512 |
1.11e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 193.23 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 15 PVNSYAPG---------TNEKTL--LEAAIKEARGQEKDI-PMyIGGEeVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVE 82
Cdd:COG4230 519 PRDLYGPErrnsagldlSDEAVLaaLSAALAAAAEKQWQAaPL-IAGE-AASGEARPVRNPADHSDVVGTVVEATAADVE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 83 DAIDAALAAKEKWENLPWEQRAAIFLKAAELvstkyrYKINAATML-------GQSKNAYQAEIdsaCELADFLRFnvay 155
Cdd:COG4230 597 AALAAAQAAFPAWSATPVEERAAILERAADL------LEAHRAELMallvreaGKTLPDAIAEV---REAVDFCRY---- 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 156 mteiYSQQppanAKGVW-NRVEQRPLeGFVFALTPFNFT-AI-----AGNLpscVAmmGNVVVWKPS-NTQIYSANVImE 227
Cdd:COG4230 664 ----YAAQ----ARRLFaAPTVLRGR-GVFVCISPWNFPlAIftgqvAAAL---AA--GNTVLAKPAeQTPLIAARAV-R 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 228 VFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEnihRYKTYPRIVGETGGkdfilahpsa 307
Cdd:COG4230 729 LLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAA---RDGPIVPLIAETGG---------- 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 308 diavLN------TAL--------VRGAFEFQGQKCSAASRAYIPQslwsDLRTRMEKDIQS----FKIGGTEDFSNFINA 369
Cdd:COG4230 796 ----QNamivdsSALpeqvvddvLASAFDSAGQRCSALRVLCVQE----DIADRVLEMLKGamaeLRVGDPADLSTDVGP 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 370 VIDEKAFDKITSYIDRAKssADAEVVIGGQYDKS--KGYFIHPTVI-LAKKADyetMSEELFGPVLTIYVYEDDKWEETL 446
Cdd:COG4230 868 VIDAEARANLEAHIERMR--AEGRLVHQLPLPEEcaNGTFVAPTLIeIDSISD---LEREVFGPVLHVVRYKADELDKVI 942
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819620888 447 ELVDKTSiYALTGSIISQcryaIDE-ATYALRNA-AGNFYINDKCTGAVVGQQPFGGaRG-SGTNDKAG 512
Cdd:COG4230 943 DAINATG-YGLTLGVHSR----IDEtIDRVAARArVGNVYVNRNIIGAVVGVQPFGG-EGlSGTGPKAG 1005
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
63-506 |
2.29e-52 |
|
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: 184.56 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 63 PHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVStKYRYKINAATMLGQSKNAYQAEIDSA 142
Cdd:cd07115 4 PATGE-LIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 143 CELADFLRFNVAYMTEIYSQQPPANAkGVWNRVEQRPLeGFVFALTPFNFtaiagnlPSCVAMM--------GNVVVWKP 214
Cdd:cd07115 82 PRAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPV-GVVGAIVPWNF-------PLMFAAWkvapalaaGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 215 SNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTyprivgE 294
Cdd:cd07115 153 AELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSL------E 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 295 TGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEK 374
Cdd:cd07115 227 LGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 375 AFDKITSYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSi 454
Cdd:cd07115 307 QFDRVLDYVDVGREEG-ARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTE- 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1819620888 455 YALTGSIISQCRYAIDEATYALRnaAGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:cd07115 383 YGLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
76-513 |
1.27e-51 |
|
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: 183.15 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 76 GTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKyryKINAATML----GQSKNAYQAEIDSACELADFlrf 151
Cdd:cd07086 32 ASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKK---KEALGRLVslemGKILPEGLGEVQEMIDICDY--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 152 NVA-----YMTEIYSQQPPANAKGVWNrveqrPLeGFVFALTPFNF-TAIAG-NLpsCVAMM-GNVVVWKPSNTQIYSAN 223
Cdd:cd07086 106 AVGlsrmlYGLTIPSERPGHRLMEQWN-----PL-GVVGVITAFNFpVAVPGwNA--AIALVcGNTVVWKPSETTPLTAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 224 VIMEVFIEA----GLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniWKTIGENIHRYktYPRIVGETGGKD 299
Cdd:cd07086 178 AVTKILAEVleknGLPPGVVNLV-TGGGDGGELLVHDPRVPLVSFTGSTEV----GRRVGETVARR--FGRVLLELGGNN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 300 FILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKI 379
Cdd:cd07086 251 AIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 380 TSYIDRAKSSaDAEVVIGGQY--DKSKGYFIHPTVILAKKADYETMSEELFGPVLtiYVYEDDKWEETLELVDKTSiYAL 457
Cdd:cd07086 331 LNAIEIAKSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL--YVIKFDSLEEAIAINNDVP-QGL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819620888 458 TGSIISQcryAIDEATYALRNA---AGNFYINDKCTGAVVGqQPFGGARGSGTNDKAGS 513
Cdd:cd07086 407 SSSIFTE---DLREAFRWLGPKgsdCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESGS 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
69-506 |
1.87e-51 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 182.25 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKInAATM-------LGQSKnayqAEIDS 141
Cdd:cd07103 9 VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI-RERAEDL-ARLLtleqgkpLAEAR----GEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 142 AcelADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTA------IAGNLPScvammGNVVVWKPS 215
Cdd:cd07103 83 A---ASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPV-GVVAAITPWNFPAamitrkIAPALAA-----GCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 216 NTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryKtypRIVGET 295
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV---K---RVSLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 296 GGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIG-GTEDFSNfINAVIDEK 374
Cdd:cd07103 228 GGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGnGLDEGTD-MGPLINER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 375 AFDKITSYIDRAKsSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSi 454
Cdd:cd07103 307 AVEKVEALVEDAV-AKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE--DEVIARANDTP- 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1819620888 455 YALTGSIISQcryaiDEATyALRNA----AGNFYINdkcTGAVVG-QQPFGGARGSG 506
Cdd:cd07103 383 YGLAAYVFTR-----DLAR-AWRVAealeAGMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
45-506 |
4.15e-51 |
|
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: 182.02 E-value: 4.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEV--RTGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKE--KWENLPWEQRAAIFLKAAELVStKYRY 120
Cdd:cd07091 6 LFINNEFVdsVSGKTFPTINPATEE-VICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIE-RDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 121 KINAATMLGQSK---NAYQAEIDsacELADFLRFNVAYMTEIYSQQPPANaKGVWNRVEQRPLeGFVFALTPFNFTAI-- 195
Cdd:cd07091 84 ELAALESLDNGKpleESAKGDVA---LSIKCLRYYAGWADKIQGKTIPID-GNFLAYTRREPI-GVCGQIIPWNFPLLml 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 196 AGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIW 275
Cdd:cd07091 159 AWKLAPALAA-GNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 276 KTIGENihrykTYPRIVGETGGKDFILAHPSADI--AVLNTALvrGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQ 353
Cdd:cd07091 238 EAAAKS-----NLKKVTLELGGKSPNIVFDDADLdkAVEWAAF--GIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 354 SFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLT 433
Cdd:cd07091 311 KRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEG-ATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819620888 434 IYVYEDDkwEETLELVDKTsIYALTGSIISQcryAIDEATYALRN-AAGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:cd07091 390 ILKFKTE--DEVIERANDT-EYGLAAGVFTK---DINKALRVSRAlKAGTVWVN--TYNVFDAAVPFGGFKQSG 455
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
23-512 |
2.42e-50 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 186.61 E-value: 2.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 23 TNEKTL--LEAAIKEARGQE-KDIPMyIGGEEVRTGNKAkLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLP 99
Cdd:PRK11905 533 SDEATLaaLDEALNAFAAKTwHAAPL-LAGGDVDGGTRP-VLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 100 WEQRAAIFLKAAELvstkyrYKINAATML-------GQS-KNAyqaeIDSACELADFLRFnvaymteiYSQQppanAKGV 171
Cdd:PRK11905 611 AAERAAILERAADL------MEAHMPELFalavreaGKTlANA----IAEVREAVDFLRY--------YAAQ----ARRL 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 172 WNRVEQRPLeGFVFALTPFNFT-AI-----AGNLpscvaMMGNVVVWKPS-NTQIYSANVImEVFIEAGLPKGVINLVYV 244
Cdd:PRK11905 669 LNGPGHKPL-GPVVCISPWNFPlAIftgqiAAAL-----VAGNTVLAKPAeQTPLIAARAV-RLLHEAGVPKDALQLLPG 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 245 SGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEnihRYKTYPRIVGETGGKDfilahpsADIaVLNTAL-------- 316
Cdd:PRK11905 742 DGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAK---RSGPPVPLIAETGGQN-------AMI-VDSSALpeqvvadv 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 317 VRGAFEFQGQKCSAASRAYIpQSLWSDLRTRMEKD-IQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSADAEVV 395
Cdd:PRK11905 811 IASAFDSAGQRCSALRVLCL-QEDVADRVLTMLKGaMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQ 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 396 IGGQYDKSKGYFIHPTVI-LAKKADyetMSEELFGPVLTIYVYEDDKWEETLELVDKTSiYALTGSIISQcryaIDE--A 472
Cdd:PRK11905 890 LPLPAETEKGTFVAPTLIeIDSISD---LEREVFGPVLHVVRFKADELDRVIDDINATG-YGLTFGLHSR----IDEtiA 961
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1819620888 473 TYALRNAAGNFYINDKCTGAVVGQQPFGGaRG-SGTNDKAG 512
Cdd:PRK11905 962 HVTSRIRAGNIYVNRNIIGAVVGVQPFGG-EGlSGTGPKAG 1001
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
61-518 |
8.47e-50 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 177.94 E-value: 8.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 61 TPPhDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTkyRYKINAATMLGQSKNAY--QAE 138
Cdd:cd07108 2 INP-ATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALETGNALrtQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 139 IDSACeLADFLRFNVAYMTEIYSQQPPANaKGVWNRVEQRPLeGFVFALTPFN--FTAIAGNLPSCVAMmGNVVVWKPSN 216
Cdd:cd07108 79 PEAAV-LADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPL-GVVGAILPWNapLMLAALKIAPALVA-GNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 217 TQIYSANVIMEVFIEAgLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEnihryktypRIVG--- 293
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD---------RLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 294 ETGGKDFILAHPSADI-AVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVID 372
Cdd:cd07108 225 ELGGKSPMIVFPDADLdDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIIS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 373 EKAFDKITSYIDRAKSSADAEVVIGG----QYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLEL 448
Cdd:cd07108 305 EKQFAKVCGYIDLGLSTSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDE--DEVIAM 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819620888 449 VDKTSiYALTGSIISQcryAIDEA-TYALRNAAGNFYINdKCTGAVVGQQpFGGARGSGTNDKAG--SMINLF 518
Cdd:cd07108 383 ANDSH-YGLAAYVWTR---DLGRAlRAAHALEAGWVQVN-QGGGQQPGQS-YGGFKQSGLGREASleGMLEHF 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
74-506 |
9.70e-50 |
|
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: 177.74 E-value: 9.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 74 HEGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVSTkyrykiNAAT---------------MLGQSKNayq 136
Cdd:cd07114 14 PEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEA------NAEElaeletrdngklireTRAQVRY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 137 aeidsaceLADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFN--FTAIAGNLPSCVAMmGNVVVWKP 214
Cdd:cd07114 85 --------LAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPL-GVVAAITPWNspLLLLAKKLAPALAA-GNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 215 SNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTyprivgE 294
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTL------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 295 TGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEK 374
Cdd:cd07114 229 LGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 375 AFDKITSYIDRAKsSADAEVVIGGQ----YDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVD 450
Cdd:cd07114 309 QLEKVERYVARAR-EEGARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIALAN 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819620888 451 KTSiYALTGSIISQcryaidEATYALRNA----AGNFYIND-KCTGAVVgqqPFGGARGSG 506
Cdd:cd07114 386 DSE-YGLAAGIWTR------DLARAHRVAraieAGTVWVNTyRALSPSS---PFGGFKDSG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
7-526 |
1.18e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 184.25 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 7 NVPTPVN----EPVNSYAPGTN---EKTLLEAAIKEARGQEKDIPMYIGGeevrTGNKAKLTPPHDHQHVLGYYHEGTKN 79
Cdd:PRK11904 510 KIPLPRDifgpERKNSKGLNLNdrsELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 80 HVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELvstkyrYKINAATML-------GQSKNAYQAEIDSAcelADFLRFn 152
Cdd:PRK11904 586 QVEQALAAARAAFPAWSRTPVEERAAILERAADL------LEANRAELIalcvreaGKTLQDAIAEVREA---VDFCRY- 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 153 vaymteiYSQQppanAK-------------GVWNRVEqrpLEG---FVfALTPFNFT-AI-AGNLPScvAMM-GNVVVWK 213
Cdd:PRK11904 656 -------YAAQ----ARrlfgapeklpgptGESNELR---LHGrgvFV-CISPWNFPlAIfLGQVAA--ALAaGNTVIAK 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 214 PS-NTQIYSANVImEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEnihryKTYPRI- 291
Cdd:PRK11904 719 PAeQTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAA-----RDGPIVp 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 292 -VGETGGKDfilahpsADIaVLNTAL--------VRGAFEFQGQKCSAASRAYIPQslwsDLRTRMEKDI----QSFKIG 358
Cdd:PRK11904 793 lIAETGGQN-------AMI-VDSTALpeqvvddvVTSAFRSAGQRCSALRVLFVQE----DIADRVIEMLkgamAELKVG 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 359 GTEDFSNFINAVIDEKAFDKITSYIDRAKSSAD--AEVVIGGqyDKSKGYFIHPTVILAKKADYetMSEELFGPVLTIYV 436
Cdd:PRK11904 861 DPRLLSTDVGPVIDAEAKANLDAHIERMKREARllAQLPLPA--GTENGHFVAPTAFEIDSISQ--LEREVFGPILHVIR 936
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 437 YEDDKWEETLELVDKTSiYALTGSIISQcryaIDE-ATYALRNA-AGNFYINDKCTGAVVGQQPFGGARGSGTNDKAGSM 514
Cdd:PRK11904 937 YKASDLDKVIDAINATG-YGLTLGIHSR----IEEtADRIADRVrVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGP 1011
|
570
....*....|..
gi 1819620888 515 INLFRWVSPRTI 526
Cdd:PRK11904 1012 HYLLRFATEKTV 1023
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
76-506 |
2.82e-49 |
|
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: 176.27 E-value: 2.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 76 GTKNHVEDAIDAALAAKEKWE-NLPWEQRAAIFLKAAELVStKYRYKINAATMLGQSKNAYQAEIDsACELADFLRFNVA 154
Cdd:cd07109 16 GGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIR-EHADELARLESLDTGKPLTQARAD-VEAAARYFEYYGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 155 YMTEIYSQQPPANAkGVWNRVEQRPLeGFVFALTPFNFTA-IAGNLPSCVAMMGNVVVWKPSNTQIYSANVIMEVFIEAG 233
Cdd:cd07109 94 AADKLHGETIPLGP-GYFVYTVREPH-GVTGHIIPWNYPLqITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 234 LPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLN 313
Cdd:cd07109 172 LPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQIVFADADLEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 314 TALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIG-GTEDFSnfINAVIDEKAFDKITSYIDRAKSSaDA 392
Cdd:cd07109 246 PVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpGLEDPD--LGPLISAKQLDRVEGFVARARAR-GA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 393 EVVIGG---QYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQcryAI 469
Cdd:cd07109 323 RIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIALANGTD-YGLVAGVWTR---DG 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 1819620888 470 DEATY-ALRNAAGNFYINDKCTGAVVgQQPFGGARGSG 506
Cdd:cd07109 397 DRALRvARRLRAGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
81-506 |
3.28e-48 |
|
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: 173.39 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKINAATMLGQSKNAYQA--EIDSAcelADFLRFNVAYMTE 158
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLL-KKRAEEFAKIIACEGGKPIKDArvEVDRA---IDTLRLAAEEAER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 159 IYSQQPPANA-KGVWNR---VEQRPLeGFVFALTPFNF--TAIAGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEA 232
Cdd:cd07094 99 IRGEEIPLDAtQGSDNRlawTIREPV-GVVLAITPFNFplNLVAHKLAPAIAT-GCPVVLKPASKTPLSALELAKILVEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 233 GLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniwktiGENIHRYKTYPRIVGETGGKDFILAHPSADIAVL 312
Cdd:cd07094 177 GVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAV--------GEALRANAGGKRIALELGGNAPVIVDRDADLDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 313 NTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAkSSADA 392
Cdd:cd07094 249 IEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEA-VEAGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 393 EVVIGGQYDKSkgyFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQcryAIDEA 472
Cdd:cd07094 328 RLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDD--FEEAIRIANSTD-YGLQAGIFTR---DLNVA 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1819620888 473 TYALRN-AAGNFYINDKcTGAVVGQQPFGGARGSG 506
Cdd:cd07094 399 FKAAEKlEVGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
46-486 |
1.12e-47 |
|
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: 172.45 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEV--RTGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKIN 123
Cdd:cd07088 1 YINGEFVpsSSGETIDVLNPATGE-VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLI-RENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 124 AATMLGQSKNAYQA--EIDSAcelADFLRfnvaYMTE---------IYSQQPPANAkgvwnRVEQRPLeGFVFALTPFNF 192
Cdd:cd07088 79 KLIVEEQGKTLSLArvEVEFT---ADYID----YMAEwarriegeiIPSDRPNENI-----FIFKVPI-GVVAGILPWNF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 193 TA--IAGNL-PSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTG 269
Cdd:cd07088 146 PFflIARKLaPALVT--GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 270 VFQNIWKTIGENIhrykTYPRIvgETGGK-DFILAhPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRM 348
Cdd:cd07088 224 AGQKIMEAAAENI----TKVSL--ELGGKaPAIVM-KDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 349 EKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGG-QYDKSKGYFIHPTVILAKKADYETMSEEL 427
Cdd:cd07088 297 VEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAG-ATLLTGGkRPEGEKGYFYEPTVLTNVRQDMEIVQEEI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 428 FGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQcryAIDEATYALRN-AAGNFYIN 486
Cdd:cd07088 376 FGPVLPVVKFSS--LDEAIELANDSE-YGLTSYIYTE---NLNTAMRATNElEFGETYIN 429
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
81-522 |
1.24e-47 |
|
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: 171.71 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKINAATM--LGQSKNAYQAEIDSAcelADFLRFNVAYMTE 158
Cdd:cd07152 15 VDRAAARAAAAQRAWAATPPRERAAVLRRAADLL-EEHADEIADWIVreSGSIRPKAGFEVGAA---IGELHEAAGLPTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 159 IYSQQPPANAkGVWNRVEQRPLeGFVFALTPFNFtaiagnlPSCVAM--------MGNVVVWKPS-NTQIYSANVIMEVF 229
Cdd:cd07152 91 PQGEILPSAP-GRLSLARRVPL-GVVGVISPFNF-------PLILAMrsvapalaLGNAVVLKPDpRTPVSGGVVIARLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 230 IEAGLPKGVINlVYVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniWKTIGENIHRykTYPRIVGETGGKDFILAHPSADI 309
Cdd:cd07152 162 EEAGLPAGVLH-VLPGGADAGEALVEDPNVAMISFTGSTAV----GRKVGEAAGR--HLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 310 AVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSyIDRAKSS 389
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHA-IVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 390 ADAEVVIGGQYDkskGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQcryAI 469
Cdd:cd07152 314 AGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVALANDTE-YGLSAGIISR---DV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819620888 470 DEA-TYALRNAAGNFYINDKcTGAVVGQQPFGGARGSGTNDKAGSMINL-----FRWVS 522
Cdd:cd07152 385 GRAmALADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGPANWeeftqWQWVT 442
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
46-506 |
3.96e-47 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 170.76 E-value: 3.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGE--EVRTGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTkyRYKIN 123
Cdd:cd07138 2 YIDGAwvAPAGTETIDVINPATEE-VIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEA--RADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 124 AATM-------LGQSKNAyQAE-----IDSACELADFLRFnvaymteiysQQPPANAkgvwnRVEQRPLeGFVFALTPFN 191
Cdd:cd07138 79 AQAItlemgapITLARAA-QVGlgighLRAAADALKDFEF----------EERRGNS-----LVVREPI-GVCGLITPWN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 192 FTA--IAGNL-PSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGST 268
Cdd:cd07138 142 WPLnqIVLKVaPALAA--GCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGST 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 269 GVFQNIWKTIGENIHRyktypriVG-ETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTR 347
Cdd:cd07138 220 RAGKRVAEAAADTVKR-------VAlELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 348 MEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQyDK----SKGYFIHPTVILAKKADYETM 423
Cdd:cd07138 293 AAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEG-ARLVAGGP-GRpeglERGYFVKPTVFADVTPDMTIA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 424 SEELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSIisqcrYAIDEATyALRNA----AGNFYINDkctGAVVGQQPF 499
Cdd:cd07138 371 REEIFGPVLSIIPYDDE--DEAIAIANDT-PYGLAGYV-----WSADPER-ARAVArrlrAGQVHING---AAFNPGAPF 438
|
....*..
gi 1819620888 500 GGARGSG 506
Cdd:cd07138 439 GGYKQSG 445
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
63-506 |
4.84e-47 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 170.22 E-value: 4.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 63 PHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAiFLKA-AELVsTKYRYKINAATMLGQSKNAYQAEID- 140
Cdd:cd07110 4 PATEA-TIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAK-YLRAiAEGV-RERREELAELEARDNGKPLDEAAWDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 141 ---SAC-----ELADFLRFNVAymteiysQQPPANAKGVWNRVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmGNV 209
Cdd:cd07110 81 ddvAGCfeyyaDLAEQLDAKAE-------RAVPLPSEDFKARVRREPV-GVVGLITPWNFpllMAAWKVAPALAA--GCT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 210 VVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHryktyp 289
Cdd:cd07110 151 VVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIK------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 290 RIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINA 369
Cdd:cd07110 225 PVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 370 VIDEKAFDKITSYIDRAKsSADAEVVIGGQY--DKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLE 447
Cdd:cd07110 305 LVSQAQYEKVLSFIARGK-EEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE--DEAIA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819620888 448 LVDKTSiYALTGSIISQCRYAIDEATYALRnaAGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:cd07110 382 LANDSE-YGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
59-506 |
5.61e-47 |
|
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: 170.12 E-value: 5.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 59 KLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVStKYRYKINAATML--GQSKNAYQ 136
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE-ERFEELAETIVLeaGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 137 AEIDSAcelADFLRFNVAYMTEIYSQQPP----ANAKGVWNRVEQRPLeGFVFALTPFNF--TAIAGNLPSCVAMmGNVV 210
Cdd:cd07147 80 GEVARA---IDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPI-GPVSAITPFNFplNLVAHKVAPAIAA-GCPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 211 VWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAgDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENihryktypR 290
Cdd:cd07147 155 VLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKARAGKK--------K 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 291 IVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAV 370
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 371 IDEKAFDKITSYIDRAkSSADAEVVIGGqydKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVD 450
Cdd:cd07147 306 ISESEAERVEGWVNEA-VDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDD--FDEALAAVN 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1819620888 451 KtSIYALTGSIISQcryAIDEATYALRN-AAGNFYINDKCTGAvVGQQPFGGARGSG 506
Cdd:cd07147 380 D-SKFGLQAGVFTR---DLEKALRAWDElEVGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-506 |
9.02e-47 |
|
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: 169.73 E-value: 9.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWenlPW----EQRAAIFLKAAE-LVSTKYRYKINAATMLGQSKNAYQAEIDSAc 143
Cdd:cd07089 9 VIGTAPDAGAADVDAAIAAARRAFDTG---DWstdaEERARCLRQLHEaLEARKEELRALLVAEVGAPVMTARAMQVDG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 144 eLADFLRFNVAYMTEIYSQQ---PPANAKGVWNRVEQRPLEGFVFALTPFNF---TAIAGNLPSCVAmmGNVVVWKPSNT 217
Cdd:cd07089 85 -PIGHLRYFADLADSFPWEFdlpVPALRGGPGRRVVRREPVGVVAAITPWNFpffLNLAKLAPALAA--GNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 218 QIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHryktypRIVGETGG 297
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK------RVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 298 KDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFD 377
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 378 KITSYIDRAKSSAdAEVVIGGQY--DKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDkTSIY 455
Cdd:cd07089 316 RVEGYIARGRDEG-ARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDD--DEAVRIAN-DSDY 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1819620888 456 ALTGSIISQcryaiDEATyALRNA----AGNFYINdkcTGAVVG-QQPFGGARGSG 506
Cdd:cd07089 392 GLSGGVWSA-----DVDR-AYRVArrirTGSVGIN---GGGGYGpDAPFGGYKQSG 438
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
43-505 |
2.99e-46 |
|
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: 168.46 E-value: 2.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 43 IPMYIGGEEVR--TGNKAKLTPPHdHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRY 120
Cdd:cd07085 1 LKLFINGEWVEskTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLL-EENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 121 KINAATMLGQSKNAYQAE---------IDSACELADFLrfnvayMTEiYSQQppaNAKGVWNRVEQRPLeGFVFALTPFN 191
Cdd:cd07085 79 ELARLITLEHGKTLADARgdvlrglevVEFACSIPHLL------KGE-YLEN---VARGIDTYSYRQPL-GVVAGITPFN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 192 FTAIAGN--LPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYvSGPDAGDVIFKHPDFAGIHFTGSTG 269
Cdd:cd07085 148 FPAMIPLwmFPMAIAC-GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVH-GGKEAVNALLDHPDIKAVSFVGSTP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 270 VFQNIWKTIGENIHRYKTYprivgeTGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAyIPQSLWSD-LRTRM 348
Cdd:cd07085 226 VGEYIYERAAANGKRVQAL------GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVA-VAVGDEADeWIPKL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 349 EKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKsSADAEVVIGGQYDK----SKGYFIHPTVILAKKADYETMS 424
Cdd:cd07085 299 VERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGV-EEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 425 EELFGPVLTIyVYEDDkWEETLELVDK------TSIYALTGSIISQCRYAIDeatyalrnaAGNFYINdkctgaV----- 493
Cdd:cd07085 378 EEIFGPVLSI-VRVDT-LDEAIAIINAnpygngAAIFTRSGAAARKFQREVD---------AGMVGIN------Vpipvp 440
|
490
....*....|..
gi 1819620888 494 VGQQPFGGARGS 505
Cdd:cd07085 441 LAFFSFGGWKGS 452
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
45-506 |
3.81e-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: 168.35 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEVRT--GNKAKLTPPHDHQHVLGYYHEGTKNhVEDAIDAALAA-KEKWENLPWEQRAAIFLKAAELVStKYRYK 121
Cdd:cd07144 10 LFINNEFVKSsdGETIKTVNPSTGEVIASVYAAGEED-VDKAVKAARKAfESWWSKVTGEERGELLDKLADLVE-KNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 122 INAATMLGQSKNAYQAEIDSACELADFLRFNVAYMTEIYSQQ-PPANAKGVWnrVEQRPLeGFVFALTPFNFT-AIAG-N 198
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTiPTSPNKLAY--TLHEPY-GVCGQIIPWNYPlAMAAwK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 199 LPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTI 278
Cdd:cd07144 165 LAPALAA-GNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 279 GENIHryktypRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDI-QSFKI 357
Cdd:cd07144 244 AQNLK------AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 358 GGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDK---SKGYFIHPTVILAKKADYETMSEELFGPVLTI 434
Cdd:cd07144 318 GSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEG-AKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819620888 435 YVYEDDkwEETLELVDKTSiYALTGSIISQcryAIDEA-TYALRNAAGNFYIN---DKCTGAvvgqqPFGGARGSG 506
Cdd:cd07144 397 SKFKTY--EEAIKKANDTT-YGLAAAVFTK---DIRRAhRVARELEAGMVWINssnDSDVGV-----PFGGFKMSG 461
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
81-506 |
8.18e-46 |
|
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: 167.01 E-value: 8.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVStKYRYKINAATMLGQSK---NAYQAEIDSAcelADFLRFNVAY 155
Cdd:cd07112 26 VDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIE-AHRDELALLETLDMGKpisDALAVDVPSA---ANTFRWYAEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 156 MTEIYSQQPPAnAKGVWNRVEQRPLeGFVFALTPFNFTAI--AGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAG 233
Cdd:cd07112 102 IDKVYGEVAPT-GPDALALITREPL-GVVGAVVPWNFPLLmaAWKIAPALAA-GNSVVLKPAEQSPLTALRLAELALEAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 234 LPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniwktiGENIHRY------KtypRIVGETGGKD-FILAHPS 306
Cdd:cd07112 179 LPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEV--------GRRFLEYsgqsnlK---RVWLECGGKSpNIVFADA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 307 ADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRA 386
Cdd:cd07112 248 PDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 387 KSSAdAEVVIGGQ--YDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSIISQ 464
Cdd:cd07112 328 KAEG-ARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVALANDS-VYGLAASVWTS 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1819620888 465 cryAIDEA-TYALRNAAGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:cd07112 404 ---DLSRAhRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSG 441
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
69-528 |
9.87e-46 |
|
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: 166.72 E-value: 9.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKINAATMLGQSKNAYQAeIDSACELADF 148
Cdd:cd07101 8 PLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLV-LERRDELLDLIQLETGKARRHA-FEEVLDVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 149 LRFnvaYMTEIYSQQPPANAKGVW-----NRVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmGNVVVWKPSNTQIY 220
Cdd:cd07101 86 ARY---YARRAERLLKPRRRRGAIpvltrTTVNRRPK-GVVGVISPWNYpltLAVSDAIPALLA--GNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 221 SANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFagIHFTGSTGVFQNIWKTIGEnihryktypRIVG---ETGG 297
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGR---------RLIGcslELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 298 KDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFD 377
Cdd:cd07101 229 KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 378 KITSYIDRAKSSAdAEVVIGGQYDKSKG-YFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYA 456
Cdd:cd07101 309 RVTAHVDDAVAKG-ATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAIELANDTD-YG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 457 LTGSIisqcrYAIDEAT---YALRNAAGNFYINDKCT---GAVvgQQPFGGARGSGTNDKAGSMiNLFRWVSPRTIKE 528
Cdd:cd07101 385 LNASV-----WTRDGARgrrIAARLRAGTVNVNEGYAaawASI--DAPMGGMKDSGLGRRHGAE-GLLKYTETQTVAV 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
46-506 |
1.70e-45 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 166.72 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEVR--TGNKAKLTPPHDhQHVLGYYHEGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVstkyryK 121
Cdd:cd07119 1 YIDGEWVEaaSGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKI------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 122 INAATM-----LGQSKNAYQAEIDSACELADFlRFNVAYMTEIYSQQPPANAKgVWNRVEQRPLeGFVFALTPFNFT--- 193
Cdd:cd07119 74 EDAEELarletLNTGKTLRESEIDIDDVANCF-RYYAGLATKETGEVYDVPPH-VISRTVREPV-GVCGLITPWNYPllq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 194 ---AIAgnlPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGV 270
Cdd:cd07119 151 aawKLA---PALAA--GNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 271 FQNIWKTIGENIHryktypRIVGETGGK--DFILAHPSADIAVLNtALVrGAFEFQGQKCSAASRAYIPQSLWSDLRTRM 348
Cdd:cd07119 226 GRSIMRAAAGNVK------KVALELGGKnpNIVFADADFETAVDQ-ALN-GVFFNAGQVCSAGSRLLVEESIHDKFVAAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 349 EKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQY----DKSKGYFIHPTVILAKKADYETMS 424
Cdd:cd07119 298 AERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEG-ARLVCGGKRptgdELAKGYFVEPTIFDDVDRTMRIVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 425 EELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSIISQcryaidEATYALRNA----AGNFYINDkcTGAVVGQQPFG 500
Cdd:cd07119 377 EEIFGPVLTVERFDTE--EEAIRLANDT-PYGLAGAVWTK------DIARANRVArrlrAGTVWIND--YHPYFAEAPWG 445
|
....*.
gi 1819620888 501 GARGSG 506
Cdd:cd07119 446 GYKQSG 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
69-506 |
1.94e-45 |
|
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: 165.98 E-value: 1.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAAlaaKEKWENLPWEQRAAifLKAAELVSTKYRYKINAATM-----------LGQSKNAYQA 137
Cdd:cd07120 9 VIGTYADGGVAEAEAAIAAA---RRAFDETDWAHDPR--LRARVLLELADAFEANAERLarllalengkiLGEARFEISG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 138 EIDSACELADFLRFNVAYMTEIysqQPpanakGVWNRVEQRPLeGFVFALTPFNFTAIagnL------PSCVAmmGNVVV 211
Cdd:cd07120 84 AISELRYYAGLARTEAGRMIEP---EP-----GSFSLVLREPM-GVAGIIVPWNSPVV---LlvrslaPALAA--GCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 212 WKPSNTQIYSANVIMEVFIEA-GLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniWKTIGENIHryKTYPR 290
Cdd:cd07120 150 VKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTAT----GRAIMAAAA--PTLKR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 291 IVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAV 370
Cdd:cd07120 224 LGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 371 IDEKAFDKITSYIDRAKSSADAEVVIGG--QYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDKweETLEL 448
Cdd:cd07120 304 IDRANVDRVDRMVERAIAAGAEVVLRGGpvTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA--EAVAL 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819620888 449 VDKTsIYALTGSIISQcryaidEATYALRNA----AGNFYINDKctGAVVGQQPFGGARGSG 506
Cdd:cd07120 382 ANDT-DYGLAASVWTR------DLARAMRVArairAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
45-506 |
1.94e-45 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 166.37 E-value: 1.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEVR--TGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKI 122
Cdd:cd07559 3 NFINGEWVApsKGEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 123 NAATM-----LGQSKNAyqaEIDSAcelADFLRFnvaYMTEIYSQQPPANA--KGVWNRVEQRPLeGFVFALTPFNFTAI 195
Cdd:cd07559 82 VAETLdngkpIRETLAA---DIPLA---IDHFRY---FAGVIRAQEGSLSEidEDTLSYHFHEPL-GVVGQIIPWNFPLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 196 AGN---LPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAgLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQ 272
Cdd:cd07559 152 MAAwklAPALAA--GNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 273 NIWKTIGENIhryktYPRIVgETGGK-------DFILAHPSADIAVLNTALvrgAFEF-QGQKCSAASRAYIPQSLWSDL 344
Cdd:cd07559 229 LIMQYAAENL-----IPVTL-ELGGKspniffdDAMDADDDFDDKAEEGQL---GFAFnQGEVCTCPSRALVQESIYDEF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 345 RTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSaDAEVVIGGQY----DKSKGYFIHPTVILAKKADY 420
Cdd:cd07559 300 IERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEE-GAEVLTGGERltlgGLDKGYFYEPTLIKGGNNDM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 421 ETMSEELFGPVLTIYVYEDDkwEETLELVDKTsIYALTGSIISQcryaidEATYALRNA----AGNFYINdkCTGAVVGQ 496
Cdd:cd07559 379 RIFQEEIFGPVLAVITFKDE--EEAIAIANDT-EYGLGGGVWTR------DINRALRVArgiqTGRVWVN--CYHQYPAH 447
|
490
....*....|
gi 1819620888 497 QPFGGARGSG 506
Cdd:cd07559 448 APFGGYKKSG 457
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
49-524 |
2.20e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 171.70 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 49 GEEVRTGNKAKLTPPHDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINaatML 128
Cdd:PRK11809 652 EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMG---LL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 129 ----GQSKNAYQAEIDSAcelADFLRFnvaymteiYSQQppanAKGVWNRVEQRPLeGFVFALTPFNFT-AI-AGNLPSC 202
Cdd:PRK11809 729 vreaGKTFSNAIAEVREA---VDFLRY--------YAGQ----VRDDFDNDTHRPL-GPVVCISPWNFPlAIfTGQVAAA 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 203 VAMmGNVVVWKPS-NTQIYSANVImEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEN 281
Cdd:PRK11809 793 LAA-GNSVLAKPAeQTPLIAAQAV-RILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGR 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 282 IH-RYKTYPRIvGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAAsRAYIPQSLWSDLRTRMEKD-IQSFKIGG 359
Cdd:PRK11809 871 LDpQGRPIPLI-AETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSAL-RVLCLQDDVADRTLKMLRGaMAECRMGN 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 360 TEDFSNFINAVIDEKAFDKITSYID--RAKSSADAEVVIGGQYDKSKGYFIHPTVIlaKKADYETMSEELFGPVLTIYVY 437
Cdd:PRK11809 949 PDRLSTDIGPVIDAEAKANIERHIQamRAKGRPVFQAARENSEDWQSGTFVPPTLI--ELDSFDELKREVFGPVLHVVRY 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 438 EDDKWEETLELVDKTSiYALTGSIISQcryaIDE--ATYALRNAAGNFYINDKCTGAVVGQQPFGGARGSGTNDKAGSMI 515
Cdd:PRK11809 1027 NRNQLDELIEQINASG-YGLTLGVHTR----IDEtiAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPL 1101
|
....*....
gi 1819620888 516 NLFRWVSPR 524
Cdd:PRK11809 1102 YLYRLLATR 1110
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
69-512 |
1.99e-44 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 162.91 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKwenLPWEQRAAIFLKAAELVSTKyryKINAATML----GQSKNAYQAEIDSACe 144
Cdd:cd07146 11 VVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEAR---REEFARLItlesGLCLKDTRYEVGRAA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 145 laDFLRFNVAYMT----EIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNF------TAIAgnlPSCVAmmGNVVVWKP 214
Cdd:cd07146 84 --DVLRFAAAEALrddgESFSCDLTANGKARKIFTLREPL-GVVLAITPFNHplnqvaHKIA---PAIAA--NNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 215 SNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGenihryktYPRIVGE 294
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 295 TGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEK 374
Cdd:cd07146 228 LGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 375 AFDKITSYIDRAkSSADAEVVIGGQYDkskGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSi 454
Cdd:cd07146 308 AAIQIENRVEEA-IAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDL--DEAIAISNSTA- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 455 YALTGSIISQCRYAIDEATYALRNAAGNfyINDKcTGAVVGQQPFGGARGSGTNDKAG 512
Cdd:cd07146 381 YGLSSGVCTNDLDTIKRLVERLDVGTVN--VNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
81-506 |
3.33e-44 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 161.86 E-value: 3.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAIFLKAAELV-STKYRYkinAATM-------LGQSKnayqAEIDSACELADFLRFN 152
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLrERKDEL---ARLItlemgkpIAEAR----AEVEKCAWICRYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 153 V-AYMTEIYSQQPPANAKgvwnrVEQRPLeGFVFALTPFNF------TAIAGNLpscvaMMGNVVVWKP-SNTQiYSANV 224
Cdd:cd07100 74 AeAFLADEPIETDAGKAY-----VRYEPL-GVVLGIMPWNFpfwqvfRFAAPNL-----MAGNTVLLKHaSNVP-GCALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 225 IMEVFIEAGLPKGVINLVYVSGPDAGDVIfKHPDFAGIHFTGSTGVFQNIWKTIGENIhryKtypRIVGETGGKD-FILA 303
Cdd:cd07100 142 IEELFREAGFPEGVFQNLLIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNL---K---KSVLELGGSDpFIVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 304 hPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYI 383
Cdd:cd07100 215 -DDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 384 DRAKSsADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIIS 463
Cdd:cd07100 294 EEAVA-AGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIALANDSP-FGLGGSVFT 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1819620888 464 QCRYAIDEAtyALRNAAGNFYINDkctgaVVGQQ---PFGGARGSG 506
Cdd:cd07100 370 TDLERAERV--ARRLEAGMVFING-----MVKSDprlPFGGVKRSG 408
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-513 |
2.15e-43 |
|
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: 160.77 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 40 EKDIPMYIGGEEVRT--GNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKE-KW-ENLPWEQRAAIFLKAAELVS 115
Cdd:cd07143 4 EQPTGLFINGEFVDSvhGGTVKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLME 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 116 TKYRYkINAATMLGQSKNAYQAEIDSACELADFLRFNVAYMTEIYSQQPPANAKGV-WNRVEqrPLeGFVFALTPFNFTA 194
Cdd:cd07143 83 RNLDY-LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLtYTRHE--PI-GVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 195 I--AGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQ 272
Cdd:cd07143 159 LmcAWKIAPALAA-GNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 273 NIWKTIGENihrykTYPRIVGETGGKDFILAHPSADI--AVLNTAlvRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEK 350
Cdd:cd07143 238 KVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLesAVVWTA--YGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 351 DIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKsSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGP 430
Cdd:cd07143 311 KAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGK-AEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 431 VLTIYVYEDDkwEETLELVDkTSIYALTGSIISQCRYAIDEATYALRnaAGNFYINdkCTGAVVGQQPFGGARGSGTNDK 510
Cdd:cd07143 390 VVAVIKFKTE--EEAIKRAN-DSTYGLAAAVFTNNINNAIRVANALK--AGTVWVN--CYNLLHHQVPFGGYKQSGIGRE 462
|
...
gi 1819620888 511 AGS 513
Cdd:cd07143 463 LGE 465
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
77-486 |
4.38e-43 |
|
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: 159.33 E-value: 4.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 77 TKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKA-AELVSTKYRYKINAATMLGQSKNAYQAEIDSACELADflrfnvaY 155
Cdd:cd07102 16 SLEAVRAALERARAAQKGWRAVPLEERKAIVTRAvELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERAR-------Y 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 156 MTEIY----SQQPPANAKGVWNRVEQRPLeGFVFALTPFN---FTAIAGNLPSCVAmmGNVVVWKPSNTQIYSANVIMEV 228
Cdd:cd07102 89 MISIAeealADIRVPEKDGFERYIRREPL-GVVLIIAPWNypyLTAVNAVIPALLA--GNAVILKHSPQTPLCGERFAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 229 FIEAGLPKGVINLVYVSGPDAGDVIfKHPDFAGIHFTGSTGVFQNIWKTIGenihryktyPRIVG---ETGGKDFILAHP 305
Cdd:cd07102 166 FAEAGLPEGVFQVLHLSHETSAALI-ADPRIDHVSFTGSVAGGRAIQRAAA---------GRFIKvglELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 306 SADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDR 385
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 386 AKSSAdAEVVIGGQ---YDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSII 462
Cdd:cd07102 316 AIAKG-ARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSD--AEAIALMNDSE-YGLTASVW 391
|
410 420
....*....|....*....|....*.
gi 1819620888 463 SQcryaIDEATYALRNA--AGNFYIN 486
Cdd:cd07102 392 TK----DIARAEALGEQleTGTVFMN 413
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
80-522 |
6.12e-43 |
|
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: 158.51 E-value: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 80 HVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVStKYRYKINAATM--LGQSKNAYQAEIDSAcelADFLRFNVAYMT 157
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLE-SRRDEFIEAMMeeTGATAAWAGFNVDLA---AGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 158 EIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAIAGNLPSCVAMM-GNVVVWKPSNTQIYSANVIMEVFIEAGLPK 236
Cdd:cd07105 77 QIIGGSIPSDKPGTLAMVVKEPV-GVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 237 GVINLVYVSGPDAGDVI---FKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYktypriVGETGGKDFILAHPSADIAVLN 313
Cdd:cd07105 156 GVLNVVTHSPEDAPEVVealIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPV------LLELGGKAPAIVLEDADLDAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 314 TALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEdfsnfINAVIDEKAFDKITSYIDRAKSSAdAE 393
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKG-AK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 394 VVIGGQYDKSK-GYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQcryaiDEA 472
Cdd:cd07105 304 LVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE--EEAVRIANDSE-YGLSAAVFTR-----DLA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819620888 473 TyALRNA----AGNFYINdkctGAVVG---QQPFGGARGSGT---NDKAGsmINLF---RWVS 522
Cdd:cd07105 376 R-ALAVAkrieSGAVHIN----GMTVHdepTLPHGGVKSSGYgrfNGKWG--IDEFtetKWIT 431
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-506 |
7.11e-43 |
|
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: 159.01 E-value: 7.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 68 HVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKyRYKINAATMLGQSKNAYQA--EIDSAcel 145
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEArvDIDSS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 146 ADFLRFNVAYMTEIYSQQPP-ANAKGVWNRVEqrPLeGFVFALTPFNF---TAIAGNLPSCvaMMGNVVVWKPSNTQIYS 221
Cdd:cd07090 84 ADCLEYYAGLAPTLSGEHVPlPGGSFAYTRRE--PL-GVCAGIGAWNYpiqIASWKSAPAL--ACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 222 ANVIMEVFIEAGLPKGVINLVYvSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhRYKTYprivgETGGKDFI 301
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQ-GGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI-KHVTL-----ELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 302 LAHPSADIAVlntaLVRGA----FEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFD 377
Cdd:cd07090 232 IIFDDADLEN----AVNGAmmanFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 378 KITSYIDRAKSSAdAEVVIGGQYDKSK-----GYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKT 452
Cdd:cd07090 308 KVLGYIESAKQEG-AKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTE--EEVIRRANDT 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 453 SiYALTGSI----ISQCRYAIDEATyalrnaAGNFYINDKCTGAVvgQQPFGGARGSG 506
Cdd:cd07090 385 T-YGLAAGVftrdLQRAHRVIAQLQ------AGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
80-512 |
1.16e-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: 157.82 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 80 HVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTK----------------YRYKINAATMLGQ---SKNAYQAeid 140
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANkeelarlisretgkplWEAQTEVAAMAGKidiSIKAYHE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 141 saceladflrfnvaYMTEiySQQPPANAKGVwnrVEQRPLeGFVFALTPFNFTAIAGN---LPSCVAmmGNVVVWKPSNT 217
Cdd:cd07095 78 --------------RTGE--RATPMAQGRAV---LRHRPH-GVMAVFGPFNFPGHLPNghiVPALLA--GNTVVFKPSEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 218 QIYSANVIMEVFIEAGLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGS--TGVFqniwktigenIHR-YKTYP-RIVG 293
Cdd:cd07095 136 TPAVAELMVELWEEAGLPPGVLNLV-QGGRETGEALAAHEGIDGLLFTGSaaTGLL----------LHRqFAGRPgKILA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 294 -ETGGKDFILAHPSADI-AVLNTAlVRGAFEFQGQKCSAASRAYIPQSLWSD-LRTRMEKDIQSFKIGG-TEDFSNFINA 369
Cdd:cd07095 205 lEMGGNNPLVVWDVADIdAAAYLI-VQSAFLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGApDAEPPFMGPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 370 VIDEKAFDKITSYIDRAKSSadAEVVIGGQYDKSKGYFIHPTVILAKKADyETMSEELFGPVLTIYVYEDdkWEETLELV 449
Cdd:cd07095 284 IIAAAAARYLLAQQDLLALG--GEPLLAMERLVAGTAFLSPGIIDVTDAA-DVPDEEIFGPLLQVYRYDD--FDEAIALA 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819620888 450 DKTSiYALTGSIISQcryaiDEATY--ALRNA-AGNFYINDKCTGAvVGQQPFGGARGSGtNDKAG 512
Cdd:cd07095 359 NATR-FGLSAGLLSD-----DEALFerFLARIrAGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPS 416
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
45-506 |
4.03e-42 |
|
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: 157.23 E-value: 4.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEVRTGNKA--KLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKI 122
Cdd:cd07117 3 LFINGEWVKGSSGEtiDSYNPANGE-TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 123 NAATM-----LGQSKNAyqaEIDSAcelADFLRFnvaYMTEIYSQQPPANA--KGVWNRVEQRPLeGFVFALTPFNFTAI 195
Cdd:cd07117 82 MVETLdngkpIRETRAV---DIPLA---ADHFRY---FAGVIRAEEGSANMidEDTLSIVLREPI-GVVGQIIPWNFPFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 196 --AGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAgLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQN 273
Cdd:cd07117 152 maAWKLAPALAA-GNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 274 IWKTIGENIhryktYPRIVgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQ 353
Cdd:cd07117 230 VAIAAAKKL-----IPATL-ELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 354 SFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSaDAEVVIGGQ----YDKSKGYFIHPTVILAKKADYETMSEELFG 429
Cdd:cd07117 304 NVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEE-GAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 430 PVLTIYVYEDDkwEETLELVDKtSIYALTGSIISQcryaidEATYALRNA----AGNFYINdkCTGAVVGQQPFGGARGS 505
Cdd:cd07117 383 PVATVIKFKTE--DEVIDMAND-SEYGLGGGVFTK------DINRALRVAraveTGRVWVN--TYNQIPAGAPFGGYKKS 451
|
.
gi 1819620888 506 G 506
Cdd:cd07117 452 G 452
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-506 |
3.01e-41 |
|
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: 154.30 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLK--------AAELVSTkyrykINAATmlGQSKNAYQAEID 140
Cdd:cd07099 8 VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRwkraladhADELAEL-----LHAET--GKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 141 SACELADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmGNVVVWKPSNT 217
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPY-GVVGVISPWNYpllTPMGDIIPALAA--GNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 218 QIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFagIHFTGSTGvfqnIWKTIGENIHRYKTyPrIVGETGG 297
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAGVDK--VAFTGSVA----TGRKVMAAAAERLI-P-VVLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 298 KDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFD 377
Cdd:cd07099 230 KDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 378 KITSYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKtSIYAL 457
Cdd:cd07099 310 IVRRHVDDAVAKG-AKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE--DEAIALAND-SRYGL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1819620888 458 TGSIISQCRYAIDEATYALRnaAGNFYINDKCTGAVVGQQPFGGARGSG 506
Cdd:cd07099 386 SASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
75-507 |
7.02e-41 |
|
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: 154.04 E-value: 7.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 75 EGTKNHVEDAIDAALAAKEK---WENLPWEQRAAIFLKAAELVSTKYRYKINAATMLGQS--KNAYQAEIDSACELadfL 149
Cdd:cd07141 40 EGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKpfSKSYLVDLPGAIKV---L 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 150 RFNVAYMTEIYSQQPPANAKG-VWNRVEqrPLeGFVFALTPFNFTAI--AGNLPSCVAMmGNVVVWKPSN----TQIYSA 222
Cdd:cd07141 117 RYYAGWADKIHGKTIPMDGDFfTYTRHE--PV-GVCGQIIPWNFPLLmaAWKLAPALAC-GNTVVLKPAEqtplTALYLA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 223 NVIMEvfieAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENihrykTYPRIVGETGGK--DF 300
Cdd:cd07141 193 SLIKE----AGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKS-----NLKRVTLELGGKspNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 301 ILAHPSADIAVLNTALvrGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKIT 380
Cdd:cd07141 264 VFADADLDYAVEQAHE--ALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 381 SYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGS 460
Cdd:cd07141 342 ELIESGKKEG-AKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT--IDEVIERANNTT-YGLAAA 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1819620888 461 IISQcryAIDEATY---ALRnaAGNFYINdkCTGAVVGQQPFGGARGSGT 507
Cdd:cd07141 418 VFTK---DIDKAITfsnALR--AGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
69-507 |
1.03e-40 |
|
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: 152.87 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVStkyrykinaatmlgqsKNAYQ-AEIDSAC---- 143
Cdd:cd07092 9 EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE----------------ENAEElAALESRNtgkp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 144 -------ELA---DFLRFnvaYMTEIYSQQPPAN---AKGVWNRVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmG 207
Cdd:cd07092 73 lhlvrddELPgavDNFRF---FAGAARTLEGPAAgeyLPGHTSMIRREPI-GVVAQIAPWNYplmMAAWKIAPALAA--G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 208 NVVVWKPSNTQIYSANVIMEvFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKT 287
Cdd:cd07092 147 NTVVLKPSETTPLTTLLLAE-LAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 288 yprivgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFI 367
Cdd:cd07092 226 ------ELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 368 NAVIDEKAFDKITSYIDRAKssADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLE 447
Cdd:cd07092 300 GPLNSAAQRERVAGFVERAP--AHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIE 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 448 LVDKTSiYALTGSIISQCRYAIDEATYALRnaAGNFYINDKctGAVVGQQPFGGARGSGT 507
Cdd:cd07092 376 LANDVE-YGLASSVWTRDVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
46-506 |
2.26e-40 |
|
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: 152.34 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEVR--TGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVSTKYR-- 119
Cdd:cd07139 2 FIGGRWVApsGSETIDVVSPATEE-VVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 120 YKINAATM---LGQSKNAYQ----AEIDSACELADflrfNVAYMTEiysqQPPANAKGVwnRVEQRPLeGFVFALTPFN- 191
Cdd:cd07139 81 ARLWTAENgmpISWSRRAQGpgpaALLRYYAALAR----DFPFEER----RPGSGGGHV--LVRREPV-GVVAAIVPWNa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 192 --FTAIAGNLPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGSTG 269
Cdd:cd07139 150 plFLAALKIAPALAA--GCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVV-PADREVGEYLVRHPGVDKVSFTGSTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 270 VFQNIWKTIGENIHRYKTyprivgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRME 349
Cdd:cd07139 227 AGRRIAAVCGERLARVTL------ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 350 KDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQY--DKSKGYFIHPTVILAKKADYETMSEEL 427
Cdd:cd07139 301 AAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEG-ARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 428 FGPVLTIYVYEDDkwEETLELVDKtSIYALTGSIISQcryaiDEATyALRNA----AGNFYINdkctGAVVG-QQPFGGA 502
Cdd:cd07139 380 FGPVLSVIPYDDE--DDAVRIAND-SDYGLSGSVWTA-----DVER-GLAVArrirTGTVGVN----GFRLDfGAPFGGF 446
|
....
gi 1819620888 503 RGSG 506
Cdd:cd07139 447 KQSG 450
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
75-512 |
1.30e-38 |
|
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: 147.64 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 75 EGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVStKYRYKINAATMLGQSKNAYQAEIDSACELADFLRFN 152
Cdd:cd07142 37 EGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 153 VAYMTEIYSQQPPANAKGVWNRVEQrPLeGFVFALTPFNFTAIAGNLPSCVAMM-GNVVVWKPSNTQIYSANVIMEVFIE 231
Cdd:cd07142 116 AGWADKIHGMTLPADGPHHVYTLHE-PI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 232 AGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRYKTYprivgETGGKDFILAHPSADI-A 310
Cdd:cd07142 194 AGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTL-----ELGGKSPFIVCEDADVdK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 311 VLNTALVrGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGgtEDFSNFINA--VIDEKAFDKITSYIDRAKS 388
Cdd:cd07142 269 AVELAHF-ALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVG--DPFRKGVEQgpQVDKEQFEKILSYIEHGKE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 389 SAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQCRYA 468
Cdd:cd07142 346 EG-ATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT--VDEVIKRANNSK-YGLAAGVFSKNIDT 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1819620888 469 IDEATYALRnaAGNFYINdkCTGAVVGQQPFGGARGSGTNDKAG 512
Cdd:cd07142 422 ANTLSRALK--AGTVWVN--CYDVFDASIPFGGYKMSGIGREKG 461
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
45-506 |
3.35e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 146.80 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEVRTGNKAKL--TPPHDHQHVlGYYHEGTKNHVEDAIDAALAAKEK-----WENLPWEQRAAiFLKA-AELVST 116
Cdd:PLN02467 10 LFIGGEWREPVLGKRIpvVNPATEETI-GDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAK-YLRAiAAKITE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 117 KYRYKINAATM-LGQSKNAYQAEID--SAC-----ELADFLRfnvAYMTEIYSQqPPANAKGvwnRVEQRPLeGFVFALT 188
Cdd:PLN02467 88 RKSELAKLETLdCGKPLDEAAWDMDdvAGCfeyyaDLAEALD---AKQKAPVSL-PMETFKG---YVLKEPL-GVVGLIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 189 PFNF---TAIAGNLPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFT 265
Cdd:PLN02467 160 PWNYpllMATWKVAPALAA--GCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 266 GSTGVFQNIWKTIGENIHryktyPrIVGETGGKDFILAHPSADI--AVLNTALvrGAFEFQGQKCSAASRAYIPQSLWSD 343
Cdd:PLN02467 238 GSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLdkAVEWAMF--GCFWTNGQICSATSRLLVHERIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 344 LRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDK--SKGYFIHPTVILAKKADYE 421
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEG-ATILCGGKRPEhlKKGFFIEPTIITDVTTSMQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 422 TMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQCRYAIDEATYALRnaAGNFYINdkCTGAVVGQQPFGG 501
Cdd:PLN02467 389 IWREEVFGPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFCQAPWGG 461
|
....*
gi 1819620888 502 ARGSG 506
Cdd:PLN02467 462 IKRSG 466
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
75-526 |
4.80e-38 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 146.56 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 75 EGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTkyrykiNAATML-------GQSKNAYQAEIdsaCELAD 147
Cdd:PRK09407 50 VSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLE------NREELLdlvqletGKARRHAFEEV---LDVAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 148 FLRF--NVA--YMTeiysqqpPANAKGVW-----NRVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmGNVVVWKPS 215
Cdd:PRK09407 121 TARYyaRRApkLLA-------PRRRAGALpvltkTTELRQPK-GVVGVISPWNYpltLAVSDAIPALLA--GNAVVLKPD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 216 NTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFagIHFTGS--TGvfqniwKTIGENIHRyktypRIVG 293
Cdd:PRK09407 191 SQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGStaTG------RVLAEQAGR-----RLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 294 ---ETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAV 370
Cdd:PRK09407 258 fslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 371 IDEKAFDKITSYIDRAKsSADAEVVIGGQYDKSKG-YFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELV 449
Cdd:PRK09407 338 ISEAQLETVSAHVDDAV-AKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV--DEAVERA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 450 DKTSiYALTGSIisqcrYAIDEAT---YALRNAAGNFYINDKCT---GAVvgQQPFGGARGSGTNDKAGSMiNLFRWVSP 523
Cdd:PRK09407 415 NDTP-YGLNASV-----WTGDTARgraIAARIRAGTVNVNEGYAaawGSV--DAPMGGMKDSGLGRRHGAE-GLLKYTES 485
|
...
gi 1819620888 524 RTI 526
Cdd:PRK09407 486 QTI 488
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
63-506 |
6.73e-37 |
|
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: 142.44 E-value: 6.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 63 PHDHQHvLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAiFLKAAELVSTKYRYKINAATMLGQSKNAYQA---EI 139
Cdd:cd07098 3 PATGQH-LGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRK-VLRSLLKYILENQEEICRVACRDTGKTMVDAslgEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 140 DSACELadfLRFNVAYMTEIYSQQPPANAKGVW---NRVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmGNVVVWK 213
Cdd:cd07098 81 LVTCEK---IRWTLKHGEKALRPESRPGGLLMFykrARVEYEPL-GVVGAIVSWNYpfhNLLGPIIAALFA--GNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 214 PSNTQIYSA----NVIMEVFIEAGLPKGVINLVYVSgPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktYP 289
Cdd:cd07098 155 VSEQVAWSSgfflSIIRECLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESL-----TP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 290 RIVgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINA 369
Cdd:cd07098 229 VVL-ELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 370 VIDEKAFDKITSYIDRAkSSADAEVVIGGQYDKS----KGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEET 445
Cdd:cd07098 308 MISPARFDRLEELVADA-VEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD--EEA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819620888 446 LELVDKTsIYALTGSI----ISQCRYAIDEATyalrnaAGNFYINDKCTGAVVGQQPFGGARGSG 506
Cdd:cd07098 385 VEIANST-EYGLGASVfgkdIKRARRIASQLE------TGMVAINDFGVNYYVQQLPFGGVKGSG 442
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
45-506 |
6.93e-36 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 139.66 E-value: 6.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEVR-TGNKAKLTPPhDHQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTkyrykiN 123
Cdd:PRK13473 5 LLINGELVAgEGEKQPVYNP-ATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEE------N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 124 AATMLG-QSKNA---YQAEIDSacEL---ADFLRFnvaYMTEIYSQQPPANAK---GVWNRVEQRPLeGFVFALTPFNF- 192
Cdd:PRK13473 78 ADEFARlESLNCgkpLHLALND--EIpaiVDVFRF---FAGAARCLEGKAAGEyleGHTSMIRRDPV-GVVASIAPWNYp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 193 ---------TAIAGnlpscvammGNVVVWKPSNTQIYSANVIMEVFIEAgLPKGVINLVYVSGPDAGDVIFKHPDFAGIH 263
Cdd:PRK13473 152 lmmaawklaPALAA---------GNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 264 FTGSTGVFQNIWKTIGENIHRYKTyprivgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSD 343
Cdd:PRK13473 222 LTGSIATGKHVLSAAADSVKRTHL------ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 344 LRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETM 423
Cdd:PRK13473 296 LVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 424 SEELFGPVLTIYVYEDDkwEETLELVDkTSIYALTGSIISQCRYAIDEATYALRnaAGNFYINDKCTgaVVGQQPFGGAR 503
Cdd:PRK13473 376 QREVFGPVVSVTPFDDE--DQAVRWAN-DSDYGLASSVWTRDVGRAHRVSARLQ--YGCTWVNTHFM--LVSEMPHGGQK 448
|
...
gi 1819620888 504 GSG 506
Cdd:PRK13473 449 QSG 451
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
81-506 |
1.28e-34 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 136.24 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKyryKINAATMLGQ--SKNAYQA--EIDS-ACELADFLRfnvAY 155
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALLEEN---KEELAEVIARetGKPLWEAatEVTAmINKIAISIQ---AY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 156 MTEIY-SQQPPANAKGVwnrVEQRPLeGFVFALTPFNFTAIAGN---LPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIE 231
Cdd:PRK09457 113 HERTGeKRSEMADGAAV---LRHRPH-GVVAVFGPYNFPGHLPNghiVPALLA--GNTVVFKPSELTPWVAELTVKLWQQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 232 AGLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGS--TGVFqniwktigenIHR-YKTYPRIVG--ETGGKDFILAHPS 306
Cdd:PRK09457 187 AGLPAGVLNLV-QGGRETGKALAAHPDIDGLLFTGSanTGYL----------LHRqFAGQPEKILalEMGGNNPLVIDEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 307 ADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSD-LRTRMEKDIQSFKIGG-TEDFSNFINAVIDEKAFDKITSYID 384
Cdd:PRK09457 256 ADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRwDAEPQPFMGAVISEQAAQGLVAAQA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 385 RAKSSADAEVVIGGQYDKSKGyFIHPTVI----LAKKADyetmsEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGS 460
Cdd:PRK09457 336 QLLALGGKSLLEMTQLQAGTG-LLTPGIIdvtgVAELPD-----EEYFGPLLQVVRYDD--FDEAIRLANNTR-FGLSAG 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1819620888 461 IISQcryaiDEATYA---LRNAAGNFYINDKCTGAvVGQQPFGGARGSG 506
Cdd:PRK09457 407 LLSD-----DREDYDqflLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
75-523 |
1.57e-34 |
|
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: 135.99 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 75 EGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATMLGQSKNAYQAEIDSACELADFlrfnva 154
Cdd:cd07111 55 QAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHF------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 155 YMTEIYSQQPPANAKGvWNRVeqrpleGFVFALTPFNFTAIAGNLPSCVAM-MGNVVVWKPSNTQIYSANVIMEVFIEAG 233
Cdd:cd07111 129 YHHAGWAQLLDTELAG-WKPV------GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 234 LPKGVINLVyvSGPDA-GDVIFKHPDFAGIHFTGSTGVFQNIWKTIGenihryKTYPRIVGETGGKDFILAHPSADIAVL 312
Cdd:cd07111 202 LPPGVLNIV--TGNGSfGSALANHPGVDKVAFTGSTEVGRALRRATA------GTGKKLSLELGGKSPFIVFDDADLDSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 313 NTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdA 392
Cdd:cd07111 274 VEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEG-A 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 393 EVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDKweETLELVDKTSiYALTGSIISQCRYAIDEA 472
Cdd:cd07111 353 DVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAK--EAVALANNTP-YGLAASVWSENLSLALEV 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1819620888 473 TYALRnaAGNFYINdkCTGAVVGQQPFGGARGSGTNdKAGSMINLFRWVSP 523
Cdd:cd07111 430 ALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKEGLYEYLRP 475
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
75-448 |
1.62e-34 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 135.80 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 75 EGTKNHVEDAIDAALAAKEKWENLPWEQRAAIflkaAELVSTKYRYKINAATML-----GQSKNAYQAEIDsacELADFL 149
Cdd:cd07130 30 QATPEDYESTIKAAQEAFKEWRDVPAPKRGEI----VRQIGDALRKKKEALGKLvslemGKILPEGLGEVQ---EMIDIC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 150 RFNVAYMTEIYSQQPPANAKG-----VWNrveqrPLeGFVFALTPFNF-TAIAG-NlpSCVAMM-GNVVVWKPSN----T 217
Cdd:cd07130 103 DFAVGLSRQLYGLTIPSERPGhrmmeQWN-----PL-GVVGVITAFNFpVAVWGwN--AAIALVcGNVVVWKPSPttplT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 218 QIYSANVIMEVFIEAGLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGSTGVfqniWKTIGENIHRYktYPRIVGETGG 297
Cdd:cd07130 175 AIAVTKIVARVLEKNGLPGAIASLV-CGGADVGEALVKDPRVPLVSFTGSTAV----GRQVGQAVAAR--FGRSLLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 298 KDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFD 377
Cdd:cd07130 248 NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVD 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819620888 378 KITSYIDRAKSSaDAEVVIGGQYDKSKGYFIHPTVILAKKaDYETMSEELFGPVLtiYVYEDDKWEETLEL 448
Cdd:cd07130 328 NYLAAIEEAKSQ-GGTVLFGGKVIDGPGNYVEPTIVEGLS-DAPIVKEETFAPIL--YVLKFDTLEEAIAW 394
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
69-506 |
3.86e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 135.33 E-value: 3.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKE--KWENLPWEQRAAIFLKAAELVSTKYRY-----KINAATMLGQSKnayQAEIDS 141
Cdd:PLN02766 48 VIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEElaaldTIDAGKLFALGK---AVDIPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 142 AcelADFLRFNVAYMTEIYSQQPPANAKgVWNRVEQRPLeGFVFALTPFNFTAIAGNLPSCVAMM-GNVVVWKPSNTQIY 220
Cdd:PLN02766 125 A---AGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPI-GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 221 SANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENihrykTYPRIVGETGGKDF 300
Cdd:PLN02766 200 SALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS-----NLKQVSLELGGKSP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 301 ILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKIT 380
Cdd:PLN02766 275 LLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKIL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 381 SYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEddKWEETLELVDKTSiYALTGS 460
Cdd:PLN02766 355 SYIEHGKREG-ATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFK--TVEEAIKKANNTK-YGLAAG 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1819620888 461 IISQcryAIDEATYALRNA-AGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:PLN02766 431 IVTK---DLDVANTVSRSIrAGTIWVN--CYFAFDPDCPFGGYKMSG 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
177-486 |
6.03e-34 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 132.94 E-value: 6.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 177 QRPLeGFVFALTPFNFT--AIAGNL-PSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVI 253
Cdd:PRK10090 69 KRAL-GVTTGILPWNFPffLIARKMaPALLT--GNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 254 FKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASR 333
Cdd:PRK10090 146 AGNPKVAMVSMTGSVSAGEKIMAAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 334 AYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNF-INAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTV 412
Cdd:PRK10090 220 VYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEG-ARVALGGKAVEGKGYYYPPTL 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819620888 413 ILAKKADYETMSEELFGPVLTIYVYedDKWEETLELVDKtSIYALTGSIISQcryAIDEATYALRNAA-GNFYIN 486
Cdd:PRK10090 299 LLDVRQEMSIMHEETFGPVLPVVAF--DTLEEAIAMAND-SDYGLTSSIYTQ---NLNVAMKAIKGLKfGETYIN 367
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
81-506 |
7.98e-33 |
|
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: 131.08 E-value: 7.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQ-----RAAIFLKAAELVStkyRYKINAATMLGQSKNA-YQAEIDSACELA-DFLRFNV 153
Cdd:cd07140 42 VEDVDRAVAAAKEAFENGEWGKmnardRGRLMYRLADLME---EHQEELATIESLDSGAvYTLALKTHVGMSiQTFRYFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 154 AYMTEIYSQQPPAN-AKGvwNRV----EQRPLeGFVFALTPFNF--TAIAGNLPSCVAMmGNVVVWKPSNTQIYSANVIM 226
Cdd:cd07140 119 GWCDKIQGKTIPINqARP--NRNltltKREPI-GVCGIVIPWNYplMMLAWKMAACLAA-GNTVVLKPAQVTPLTALKFA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 227 EVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENihrykTYPRIVGETGGKDFILAHPS 306
Cdd:cd07140 195 ELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVS-----NLKKVSLELGGKSPLIIFAD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 307 ADiavLNTALVRG---AFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYI 383
Cdd:cd07140 270 CD---MDKAVRMGmssVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYC 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 384 DRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDKWEETLELVDKTSiYALTGSIIS 463
Cdd:cd07140 347 ERGVKEG-ATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTE-YGLASGVFT 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1819620888 464 QcryAIDEATY-ALRNAAGNFYINDKCTGAVVGqqPFGGARGSG 506
Cdd:cd07140 425 K---DINKALYvSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
45-512 |
1.03e-30 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 125.69 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 45 MYIGGEEVRTGNkAKLTPPHDHQ--HVLGYYHEGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVStKYRY 120
Cdd:PLN02466 60 LLINGQFVDAAS-GKTFPTLDPRtgEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 121 KINAATMLGQSKNAYQAEIDSACELADFLRFNVAYMTEIYSQQPPANAKgvwNRVE--QRPLeGFVFALTPFNFTAI--- 195
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGP---HHVQtlHEPI-GVAGQIIPWNFPLLmfa 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 196 --AGNLPSCvammGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVfqn 273
Cdd:PLN02466 214 wkVGPALAC----GNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDT--- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 274 iWKTIGENIHRYKTYPrIVGETGGKDFILAHPSADI--AVlntALVRGAFEF-QGQKCSAASRAYIPQSLWSDL----RT 346
Cdd:PLN02466 287 -GKIVLELAAKSNLKP-VTLELGGKSPFIVCEDADVdkAV---ELAHFALFFnQGQCCCAGSRTFVHERVYDEFvekaKA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 347 RMEKDI--QSFKIGGTEdfsnfiNAVIDEKAFDKITSYIdRAKSSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMS 424
Cdd:PLN02466 362 RALKRVvgDPFKKGVEQ------GPQIDSEQFEKILRYI-KSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 425 EELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSIISQCRYAIDEATYALRnaAGNFYINdkCTGAVVGQQPFGGARG 504
Cdd:PLN02466 435 DEIFGPVQSILKFKD--LDEVIRRANNTR-YGLAAGVFTQNLDTANTLSRALR--VGTVWVN--CFDVFDAAIPFGGYKM 507
|
....*...
gi 1819620888 505 SGTNDKAG 512
Cdd:PLN02466 508 SGIGREKG 515
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
77-506 |
3.04e-30 |
|
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: 123.72 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 77 TKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRYKINAATMLGQS--KNAYQAEIDSAcelADFLRfnva 154
Cdd:cd07116 36 TAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKpvRETLAADIPLA---IDHFR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 155 YMTEIYSQQPPANAKGVWNRVEQ---RPLeGFVFALTPFNFTAIAGN---LPSCVAmmGNVVVWKPSNTQIYSANVIMEV 228
Cdd:cd07116 109 YFAGCIRAQEGSISEIDENTVAYhfhEPL-GVVGQIIPWNFPLLMATwklAPALAA--GNCVVLKPAEQTPASILVLMEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 229 fIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIhryktYPrIVGETGGKD---FILAHP 305
Cdd:cd07116 186 -IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IP-VTLELGGKSpniFFADVM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 306 SADIAVLNTALvRGAFEF---QGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSY 382
Cdd:cd07116 259 DADDAFFDKAL-EGFVMFalnQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 383 IDRAKSSAdAEVVIGGQY----DKSKGYFIHPTVILaKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTsIYALT 458
Cdd:cd07116 338 IDIGKEEG-AEVLTGGERnelgGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKDE--EEALEIANDT-LYGLG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1819620888 459 GSIISQcryAIDEATYALRN-AAGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:cd07116 413 AGVWTR---DGNTAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
78-507 |
3.26e-30 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 123.65 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 78 KNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVstkyrykINAATMLGQSKNAYQ--------AEIDSAcelADFL 149
Cdd:PLN02278 61 RAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLI-------IANKEDLAQLMTLEQgkplkeaiGEVAYG---ASFL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 150 RFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNF-----TAIAGnlPSCVAmmGNVVVWKPSNTQIYSANV 224
Cdd:PLN02278 131 EYFAEEAKRVYGDIIPSPFPDRRLLVLKQPV-GVVGAITPWNFplamiTRKVG--PALAA--GCTVVVKPSELTPLTALA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 225 IMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGenihryKTYPRIVGETGGKDFILAH 304
Cdd:PLN02278 206 AAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA------ATVKRVSLELGGNAPFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 305 PSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYID 384
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 385 RAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKT----SIYALTGS 460
Cdd:PLN02278 360 DAVSKG-AKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTeaglAAYIFTRD 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1819620888 461 IISQCRYAideatYALRNaaGNFYINDKCTGAVVGqqPFGGARGSGT 507
Cdd:PLN02278 437 LQRAWRVS-----EALEY--GIVGVNEGLISTEVA--PFGGVKQSGL 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
67-526 |
2.13e-29 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 121.54 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 67 QHVLGYYHEGTKNHVEDAIDAALAAKEK--WENLPWEQRAAIFLKAAELVStKYRYKINAATMLGQSKNAYQAEIDSACE 144
Cdd:PRK09847 45 QAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLME-AHAEELALLETLDTGKPIRHSLRDDIPG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 145 LADFLRFNVAYMTEIYSQQPPANAKGVwNRVEQRPLeGFVFALTPFNFTAIAGNL---PSCVAmmGNVVVWKPSNTQIYS 221
Cdd:PRK09847 124 AARAIRWYAEAIDKVYGEVATTSSHEL-AMIVREPV-GVIAAIVPWNFPLLLTCWklgPALAA--GNSVILKPSEKSPLS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 222 ANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENihrykTYPRIVGETGGK--D 299
Cdd:PRK09847 200 AIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKsaN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 300 FILAH-PSADIAVLNTAlvRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDK 378
Cdd:PRK09847 275 IVFADcPDLQQAASATA--AGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 379 ITSYIDRAKSSADaeVVIGGQYDKSKGYfIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKtSIYALT 458
Cdd:PRK09847 353 VHSFIREGESKGQ--LLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAND-SQYGLG 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 459 GSIISqcRYAIDEATYALRNAAGNFYINDKCTGAVVgqQPFGGARGSGtNDKAGSMINLFRWVSPRTI 526
Cdd:PRK09847 427 AAVWT--RDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
77-464 |
1.65e-28 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 118.71 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 77 TKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVStKYRYKINAATMLGQSKNAYQA--EIDSACELADFL-RFNV 153
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILK-EHKAPIAECLVKEIAKPAKDAvtEVVRSGDLISYTaEEGV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 154 AYMTE---IYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFT---AIAGNLPSCVAmmGNVVVWKPSNTQIYSANVIME 227
Cdd:PLN00412 130 RILGEgkfLVSDSFPGNERNKYCLTSKIPL-GVVLAIPPFNYPvnlAVSKIAPALIA--GNAVVLKPPTQGAVAALHMVH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 228 VFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFT-GSTGVfqniwktigeNIHRYKTYPRIVGETGGKDFILAHPS 306
Cdd:PLN00412 207 CFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGI----------AISKKAGMVPLQMELGGKDACIVLED 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 307 ADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNfINAVIDEKAFDKITSYIDRA 386
Cdd:PLN00412 277 ADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMDA 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 387 KSSADAEVviggQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVDKTSiYALTGSIISQ 464
Cdd:PLN00412 356 KEKGATFC----QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV--EEGIHHCNASN-FGLQGCVFTR 426
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
77-506 |
2.75e-28 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 117.53 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 77 TKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKyRYKInAATM---LGQSKNAYQAEidsACELADFLRFNV 153
Cdd:PRK09406 21 TDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAE-ADQV-AALMtleMGKTLASAKAE---ALKCAKGFRYYA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 154 AYMTEIYSQQPpANAKGVWNR---VEQRPLeGFVFALTPFNF---TAIAGNLPSCvaMMGNVVVWKPSNTQIYSANVIME 227
Cdd:PRK09406 96 EHAEALLADEP-ADAAAVGASrayVRYQPL-GVVLAVMPWNFplwQVVRFAAPAL--MAGNVGLLKHASNVPQTALYLAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 228 VFIEAGLPKGVINLVYVsGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHryKTypriVGETGGKDFILAHPSA 307
Cdd:PRK09406 172 LFRRAGFPDGCFQTLLV-GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIK--KT----VLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 308 DIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAk 387
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 388 SSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSI----YALTGSIIS 463
Cdd:PRK09406 324 VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIANATTFglgsNAWTRDEAE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1819620888 464 QCRYAIDEatyalrnAAGNFYINdkctGAVVG--QQPFGGARGSG 506
Cdd:PRK09406 402 QERFIDDL-------EAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
174-507 |
2.14e-27 |
|
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: 114.62 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 174 RVEQRPLeGFVFALTPFNF----------TAIAGnlpscvammGNVVVWKPSNTQIYSANVIMEVfIEAGLPKGVINLVY 243
Cdd:cd07135 103 RIRKEPL-GVVLIIGPWNYpvllalsplvGAIAA---------GCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 244 VSGPDAGDVIFKHPDFagIHFTGSTgvfqNIWKTIGENIHRYKTyPrIVGETGGKDFILAHPSADIAVLNTALVRGAFEF 323
Cdd:cd07135 172 GGVPETTALLEQKFDK--IFYTGSG----RVGRIIAEAAAKHLT-P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 324 QGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINaVIDEKAFDKITSYIDRAKssadAEVVIGGQYDKS 403
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTR-IVNPRHFNRLKSLLDTTK----GKVVIGGEMDEA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 404 KgYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELV---DKTsiyaLTGSIISQCRYAIDEATYALRnaA 480
Cdd:cd07135 319 T-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDL--DEAIKVInsrDTP----LALYIFTDDKSEIDHILTRTR--S 389
|
330 340
....*....|....*....|....*..
gi 1819620888 481 GNFYINDKCTGAVVGQQPFGGARGSGT 507
Cdd:cd07135 390 GGVVINDTLIHVGVDNAPFGGVGDSGY 416
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
46-506 |
4.49e-27 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 114.23 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGE--EVRTGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVsTKYRYKIN 123
Cdd:PRK11241 14 LINGEwlDANNGEVIDVTNPANGD-KLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLM-MEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 124 AATMLGQSKNAYQA--EIDSAcelADFLRFNVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAI-----A 196
Cdd:PRK11241 92 RLMTLEQGKPLAEAkgEISYA---ASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPI-GVTAAITPWNFPAAmitrkA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 197 GnlPSCVAmmGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWK 276
Cdd:PRK11241 168 G--PALAA--GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 277 TIGENIHRYKTyprivgETGGKDFILAHPSADIavlnTALVRGA----FEFQGQKCSAASRAYIPQSLWSDLRTRMEKDI 352
Cdd:PRK11241 244 QCAKDIKKVSL------ELGGNAPFIVFDDADL----DKAVEGAlaskFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 353 QSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVL 432
Cdd:PRK11241 314 SKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKG-ARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819620888 433 TIYVYEDDkwEETLELVDKTSiYALTGSIisqcrYAIDEATYALRNAAGNFYINDKCTGAVVGQ-QPFGGARGSG 506
Cdd:PRK11241 393 PLFRFKDE--ADVIAQANDTE-FGLAAYF-----YARDLSRVFRVGEALEYGIVGINTGIISNEvAPFGGIKASG 459
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
69-506 |
1.86e-26 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 112.67 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRyKINAATMLGQSKnAYQ----AEIDSAce 144
Cdd:PRK13252 34 VLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND-ELAALETLDTGK-PIQetsvVDIVTG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 145 lADFLrfnvaymtEIYSQQPPAnAKGvwnrvEQRPLEGFVFALT---PFNFTA-I-AGNLPSCVAM--------MGNVVV 211
Cdd:PRK13252 110 -ADVL--------EYYAGLAPA-LEG-----EQIPLRGGSFVYTrrePLGVCAgIgAWNYPIQIACwksapalaAGNAMI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 212 WKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGpDAGDVIFKHPDFAGIHFTGSTG----VFQNIWKTIGEnihrykt 287
Cdd:PRK13252 175 FKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPtgkkVMAAAAASLKE------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 288 yprIVGETGGKDFILAHPSADI--AVlnTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSN 365
Cdd:PRK13252 247 ---VTMELGGKSPLIVFDDADLdrAA--DIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 366 FINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQY----DKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDk 441
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEG-ARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE- 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819620888 442 wEETLELVDKTSiYALTGSIISQcryaidEATYALRNA----AGNFYINdkCTGAVVGQQPFGGARGSG 506
Cdd:PRK13252 400 -DEVIARANDTE-YGLAAGVFTA------DLSRAHRVIhqleAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
69-506 |
1.59e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 106.48 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 69 VLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRA--------AIFLKAAELVSTKYRykinaatMLGQSKNAYQAEID 140
Cdd:PRK13968 19 QLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAqklrdigkALRARSEEMAQMITR-------EMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 141 SACELADFlrfnvaymteiYSQQPPA----------NAKGVwnrVEQRPLeGFVFALTPFNF---TAIAGNLPSCVAmmG 207
Cdd:PRK13968 92 KSANLCDW-----------YAEHGPAmlkaeptlveNQQAV---IEYRPL-GTILAIMPWNFplwQVMRGAVPILLA--G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 208 NVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGpDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGENIHRykt 287
Cdd:PRK13968 155 NGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADN-DGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKK--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 288 yprIVGETGGKD-FI-LAHPSADIAVlnTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSN 365
Cdd:PRK13968 231 ---CVLELGGSDpFIvLNDADLELAV--KAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 366 FINAVIDEKAFDKITSYIdRAKSSADAEVVIGGQYDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEET 445
Cdd:PRK13968 306 ALGPMARFDLRDELHHQV-EATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDA--EHA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819620888 446 LELVDKtSIYALTGSIisqcrYAIDEA---TYALRNAAGNFYINDKCtgAVVGQQPFGGARGSG 506
Cdd:PRK13968 383 LELAND-SEFGLSATI-----FTTDETqarQMAARLECGGVFINGYC--ASDARVAFGGVKKSG 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
43-451 |
2.69e-24 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 106.75 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 43 IPMYIGGEEVRTGNKA---KLTPPHdhQHVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKY- 118
Cdd:PLN02419 114 VPNLIGGSFVESQSSSfidVINPAT--QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMd 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 119 RYKINAATMLGQSKNAYQAEIDSACELADFLrfnVAYMTEIYSQQPPANAKGVWNRVEQRPLeGFVFALTPFNFTAIAGN 198
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHA---CGMATLQMGEYLPNVSNGVDTYSIREPL-GVCAGICPFNFPAMIPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 199 LPSCVAMM-GNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVINLVYVSGpDAGDVIFKHPDFAGIHFTGSTGVFQNIWKT 277
Cdd:PLN02419 268 WMFPVAVTcGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN-DTVNAICDDEDIRAVSFVGSNTAGMHIYAR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 278 IGENihryktYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYI--PQSLWSDlrtRMEKDIQSF 355
Cdd:PLN02419 347 AAAK------GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSWED---KLVERAKAL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 356 KIGGTEDFSNFINAVIDEKAFDKITSYI-----DRAKSSADAEVVIGGQYDksKGYFIHPTVILAKKADYETMSEELFGP 430
Cdd:PLN02419 418 KVTCGSEPDADLGPVISKQAKERICRLIqsgvdDGAKLLLDGRDIVVPGYE--KGNFIGPTILSGVTPDMECYKEEIFGP 495
|
410 420
....*....|....*....|.
gi 1819620888 431 VLTiyVYEDDKWEETLELVDK 451
Cdd:PLN02419 496 VLV--CMQANSFDEAISIINK 514
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
182-506 |
2.81e-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: 105.39 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 182 GFVFALTPFN--FTAIAGNLPSCVAMmGNVVVWKPS----NTQIYSANVIMEVFIEaglpkgviNLVYV--SGPDAGDVI 253
Cdd:cd07134 102 GVCLIISPWNypFNLAFGPLVSAIAA-GNTAILKPSeltpHTSAVIAKIIREAFDE--------DEVAVfeGDAEVAQAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 254 FKHPdFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASR 333
Cdd:cd07134 173 LELP-FDHIFFTGSPAVGKIVMAAAAKHL------ASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 334 AYIPQSLWSDLRTRMEKDIQSF-----KIGGTEDFSNfinaVIDEKAFDKITSYIDRAKSsADAEVVIGGQYDKSKGYfI 408
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFygkdaARKASPDLAR----IVNDRHFDRLKGLLDDAVA-KGAKVEFGGQFDAAQRY-I 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 409 HPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELV-DKTSIYALtgSIISQCRYAIDeatYALRN-AAGNFYIN 486
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYED--LDEVIEYInAKPKPLAL--YVFSKDKANVN---KVLARtSSGGVVVN 392
|
330 340
....*....|....*....|
gi 1819620888 487 DKCTGAVVGQQPFGGARGSG 506
Cdd:cd07134 393 DVVLHFLNPNLPFGGVNNSG 412
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
81-526 |
3.51e-24 |
|
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: 105.40 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKyRYKINAATMLGQSKNAYQAEIDSACELADFLRFNVAYMTEIy 160
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 161 sQQPPANAKGVW----NRVEQRPLeGFVFALTPFNF--TAIAGNLPSCVAMmGNVVVWKPSNTQIYSANVIMEVFIEAG- 233
Cdd:cd07084 79 -PHEPGNHLGQGlkqqSHGYRWPY-GPVLVIGAFNFplWIPLLQLAGALAM-GNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 234 LPKGVINLVYVSGpDAGDVIFKHPDFAGIHFTGSTGVfqniwktiGENIHRYKTYPRIVGETGGKDFILAHPSAD-IAVL 312
Cdd:cd07084 156 LPPEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRV--------AEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 313 NTALVRGAFEFQGQKCSAASRAYIP-----QSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKItsyidraK 387
Cdd:cd07084 227 AWQCVQDMTACSGQKCTAQSMLFVPenwskTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLLGS-------V 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 388 SSADAEVVIGGQYDKSKGYFIHPTVILAKKAD---YETMSEELFGPVLTIYVYEDDKWEETLELVDKTSiYALTGSIISQ 464
Cdd:cd07084 300 LLFSGKELKNHSIPSIYGACVASALFVPIDEIlktYELVTEEIFGPFAIVVEYKKDQLALVLELLERMH-GSLTAAIYSN 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819620888 465 CRYAIDEATYALRNAAGNFYINDKCTGAVVGQQPFGGARGSGTNDKAGSMINLFRWVSPRTI 526
Cdd:cd07084 379 DPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
174-506 |
1.63e-23 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 102.99 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 174 RVEQRPLeGFVFALTPFNF---TAIAgnlPSCVAMM-GNVVVWKPSNTQIYSANVIMEVfIEAGLPKGVINLVYVsGPDA 249
Cdd:cd07087 95 YVIPEPL-GVVLIIGPWNYplqLALA---PLIGAIAaGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEG-GVEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 250 GDVIFKHP-DFagIHFTGSTGVFQNIWKTIGENIhrykTyPrIVGETGGKDFILAHPSADIAVlnTA--LVRGAFEFQGQ 326
Cdd:cd07087 169 ATALLAEPfDH--IFFTGSPAVGKIVMEAAAKHL----T-P-VTLELGGKSPCIVDKDANLEV--AArrIAWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 327 KCSAASRAYIPQSLWSDLRTRMEKDIQSFkIGGTEDFSNFINAVIDEKAFDKITSYIDrakssaDAEVVIGGQYDKSKGY 406
Cdd:cd07087 239 TCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLD------DGKVVIGGQVDKEERY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 407 fIHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTS----IYALTGSiiSQCRYAIDEATyalrnAAGN 482
Cdd:cd07087 312 -IAPTILDDVSPDSPLMQEEIFGPILPILTYDD--LDEAIEFINSRPkplaLYLFSED--KAVQERVLAET-----SSGG 381
|
330 340
....*....|....*....|....
gi 1819620888 483 FYINDKCTGAVVGQQPFGGARGSG 506
Cdd:cd07087 382 VCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
46-513 |
1.43e-21 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 97.98 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 46 YIGGEEVRTGNKAKLTPPHDHQhVLGYYHEGTKNHVEDAIDAALAAKEKWENLPWEQRAAIFLKAAELVSTKYRY----- 120
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYlgrlv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 121 KINAATMLGQSKNAYQAEIDsACELADFLRFNVAYMTeIYSQQPPANAKGVWNrveqrPLeGFVFALTPFNFTAIAGNLP 200
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIID-MCDFAVGLSRQLNGSI-IPSERPNHMMMEVWN-----PL-GIVGVITAFNFPCAVLGWN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 201 SCVAMM-GNVVVWKPSNT----QIYSANVIMEVFIEAGLPkGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIW 275
Cdd:PLN02315 175 ACIALVcGNCVVWKGAPTtpliTIAMTKLVAEVLEKNNLP-GAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 276 KTIGENihryktYPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSF 355
Cdd:PLN02315 254 QTVNAR------FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 356 KIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdAEVVIGGQYDKSKGYFIHPTVIlAKKADYETMSEELFGPVLtiY 435
Cdd:PLN02315 328 KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQG-GKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVL--Y 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 436 VYEDDKWEETLELvDKTSIYALTGSIISQCRYAIDEATYALRNAAGNFYINDKCTGAVVGqQPFGGARGSGTNDKAGS 513
Cdd:PLN02315 404 VMKFKTLEEAIEI-NNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS 479
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
82-508 |
1.98e-20 |
|
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: 94.02 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 82 EDAIDAALAA-----KEKWENLPWEQRAAIFLKAAELVSTKY-RYKINAATMLGQSKNAYQAEIDSACELADFLRFNVAY 155
Cdd:cd07148 20 WAAIDKALDTahalfLDRNNWLPAHERIAILERLADLMEERAdELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 156 MT--EIYSQQPPANAkGVWNRVEQRPLeGFVFALTPFNF----------TAIAGNLPscvammgnvVVWKPSNTQIYSAN 223
Cdd:cd07148 100 LGgrEIPMGLTPASA-GRIAFTTREPI-GVVVAISAFNHplnlivhqvaPAIAAGCP---------VIVKPALATPLSCL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 224 VIMEVFIEAGLPKGVINLVyVSGPDAGDVIFKHPDFAGIHFTGSTGVFqniWKTigenihRYKTYP--RIVGETGGKDFI 301
Cdd:cd07148 169 AFVDLLHEAGLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARVG---WML------RSKLAPgtRCALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 302 LAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITS 381
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 382 YIDRAkSSADAEVVIGGQYDKSKGYfiHPTVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTSiYALTGSI 461
Cdd:cd07148 319 WVNEA-VAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDD--LDEAIAQANSLP-VAFQAAV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1819620888 462 ISQcryAIDEATYALRN-AAGNFYINDKcTGAVVGQQPFGGARGSGTN 508
Cdd:cd07148 393 FTK---DLDVALKAVRRlDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
179-439 |
1.95e-19 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 91.24 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 179 PLeGFVFALTPFNFTAIAGnLPSCVAMM--GNVVVWKPSNTQIYSANVIMEVFIEAgLPKGVINlVYVSGPDAGDVIFKH 256
Cdd:PTZ00381 109 PL-GVVLVIGAWNYPLNLT-LIPLAGAIaaGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVR-VIEGGVEVTTELLKE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 257 PdFAGIHFTGSTGVFQNIWKTIGENIhryktYPRIVgETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASRAYI 336
Cdd:PTZ00381 185 P-FDHIFFTGSPRVGKLVMQAAAENL-----TPCTL-ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 337 PQSLWSDLRTRMEKDIQSFkIGgtEDF--SNFINAVIDEKAFDKITSYIDRAKSsadaEVVIGGQYDKSKGYfIHPTVIL 414
Cdd:PTZ00381 258 HRSIKDKFIEALKEAIKEF-FG--EDPkkSEDYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIV 329
|
250 260
....*....|....*....|....*
gi 1819620888 415 AKKADYETMSEELFGPVLTIYVYED 439
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYEN 354
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
116-439 |
5.30e-19 |
|
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: 89.49 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 116 TK-YRYKINAATMLGQSKNAYQAEIDSACElADFLRFNV-AYMTEI--------------------------YSQQPpan 167
Cdd:cd07136 16 TKdVEFRIEQLKKLKQAIKKYENEILEALK-KDLGKSEFeAYMTEIgfvlseinyaikhlkkwmkpkrvktpLLNFP--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 168 AKGvwnRVEQRPLeGFVFALTPFNFT----------AIAGnlpscvammGNVVVWKPSNTQIYSANVIMEVfIEAGLPKg 237
Cdd:cd07136 92 SKS---YIYYEPY-GVVLIIAPWNYPfqlalapligAIAA---------GNTAVLKPSELTPNTSKVIAKI-IEETFDE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 238 viNLVYVSGPDAgDVIFK--HPDFAGIHFTGSTGVfqniWKTIGENIHRYKTyPrIVGETGGKDFILAHPSADIAVLNTA 315
Cdd:cd07136 157 --EYVAVVEGGV-EENQEllDQKFDYIFFTGSVRV----GKIVMEAAAKHLT-P-VTLELGGKSPCIVDEDANLKLAAKR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 316 LVRGAFEFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSF---KIGGTEDFSNFINavidEKAFDKITSYIDrakssaDA 392
Cdd:cd07136 228 IVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFygeDPLESPDYGRIIN----EKHFDRLAGLLD------NG 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1819620888 393 EVVIGGQYDKsKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYED 439
Cdd:cd07136 298 KIVFGGNTDR-ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDT 343
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
189-506 |
1.94e-14 |
|
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: 75.34 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 189 PFNFT------AIAGnlpscvammGNVVVWKPSNTQIYSANVIMEVfieagLPKGVIN---LVYVSGPDAGDVIFKHpDF 259
Cdd:cd07132 113 PLQLTlvplvgAIAA---------GNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecyPVVLGGVEETTELLKQ-RF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 260 AGIHFTGSTGVfqniwktiGENIH----RYKTypRIVGETGGKDFILAHPSADIAVLNTALVRGAFEFQGQKCSAASraY 335
Cdd:cd07132 178 DYIFYTGSTSV--------GKIVMqaaaKHLT--PVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD--Y 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 336 I--PQSLWSDLRTRMEKDIQSF---KIGGTEDFSNFINavidEKAFDKITSYIDRAKssadaeVVIGGQYDKSKGYfIHP 410
Cdd:cd07132 246 VlcTPEVQEKFVEALKKTLKEFygeDPKESPDYGRIIN----DRHFQRLKKLLSGGK------VAIGGQTDEKERY-IAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 411 TVILAKKADYETMSEELFGPVLTIYVYEDdkWEETLELVDKTS----IYALTGSiiSQCRYAIDEATyalrnAAGNFYIN 486
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNN--LDEAIEFINSREkplaLYVFSNN--KKVINKILSNT-----SSGGVCVN 385
|
330 340
....*....|....*....|
gi 1819620888 487 DKCTGAVVGQQPFGGARGSG 506
Cdd:cd07132 386 DTIMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
165-507 |
2.65e-12 |
|
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: 68.59 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 165 PANAKgvwnrVEQRPLeGFVFALTPFNFT----------AIAGnlpscvammGNVVVWKPSNTQIYSANVIMEVfIEAGL 234
Cdd:cd07137 92 PAKAE-----IVSEPL-GVVLVISAWNFPfllslepvigAIAA---------GNAVVLKPSELAPATSALLAKL-IPEYL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 235 PKGVINLVYvSGPDAGDVIFKHpDFAGIHFTGSTGVFQNIWKTIGENIhryktYPrIVGETGGKDFILAHPSADIAVLNT 314
Cdd:cd07137 156 DTKAIKVIE-GGVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHL-----TP-VTLELGGKCPVIVDSTVDLKVAVR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 315 ALVRGAFEF-QGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFkIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdaE 393
Cdd:cd07137 228 RIAGGKWGCnNGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVAD--K 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 394 VVIGGQYDKSKGYfIHPTVILAKKADYETMSEELFGPVLTIYVYEddKWEETLELVDKTS----IYALTGSIISQCRYaI 469
Cdd:cd07137 305 IVHGGERDEKNLY-IEPTILLDPPLDSSIMTEEIFGPLLPIITVK--KIEESIEIINSRPkplaAYVFTKNKELKRRI-V 380
|
330 340 350
....*....|....*....|....*....|....*...
gi 1819620888 470 DEATyalrnaAGNFYINDKCTGAVVGQQPFGGARGSGT 507
Cdd:cd07137 381 AETS------SGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
173-506 |
1.93e-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: 65.97 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 173 NRVEQRPLeGFVFALTPFNF----------TAIAGnlpscvammGNVVVWKPSNTQIYSANVIMEVFIEAGLPKGVinLV 242
Cdd:cd07133 95 AEVEYQPL-GVVGIIVPWNYplylalgpliAALAA---------GNRVMIKPSEFTPRTSALLAELLAEYFDEDEV--AV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 243 YVSGPDAGDViFKHPDFAGIHFTGSTGVFQNIWKTIGENIhrykTyPrIVGETGGKDFILAHPSADIAVLNTALVRGAFE 322
Cdd:cd07133 163 VTGGADVAAA-FSSLPFDHLLFTGSTAVGRHVMRAAAENL----T-P-VTLELGGKSPAIIAPDADLAKAAERIAFGKLL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 323 FQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSF--KIGGTEDFSnfinAVIDEKAFDKITSYIDRAKSS-ADAEVVIGGQ 399
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNPDYT----SIINERHYARLQGLLEDARAKgARVIELNPAG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 400 YDKSKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYedDKWEETLELV--------------DKTSIYALTGSIISqc 465
Cdd:cd07133 312 EDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTY--DSLDEAIDYInarprplalyyfgeDKAEQDRVLRRTHS-- 387
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1819620888 466 ryaideatyalrnaaGNFYINDKCTGAVVGQQPFGGARGSG 506
Cdd:cd07133 388 ---------------GGVTINDTLLHVAQDDLPFGGVGASG 413
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
165-539 |
2.05e-11 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 66.29 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 165 PANAKgvwnrVEQRPLeGFVFALTPFNFT----------AIAGnlpscvammGNVVVWKPSNTQIYSANvimevFIEAGL 234
Cdd:PLN02203 99 PATAE-----VVPEPL-GVVLIFSSWNFPiglslepligAIAA---------GNAVVLKPSELAPATSA-----FLAANI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 235 PKGVINL---VYVSGPDAGDVIFKHPdFAGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGK-DFILAHPSA--D 308
Cdd:PLN02203 159 PKYLDSKavkVIEGGPAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKcPCIVDSLSSsrD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 309 IAVLNTALVRGAF-EFQGQKCSAASRAYIPQSLWSDLRTRMEKDIQSFkIGGTEDFSNFINAVIDEKAFDKITSYIDraK 387
Cdd:PLN02203 232 TKVAVNRIVGGKWgSCAGQACIAIDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLK--D 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 388 SSADAEVVIGGQYDKsKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYedDKWEETLELVDKT----SIYALTGSiiS 463
Cdd:PLN02203 309 PRVAASIVHGGSIDE-KKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITV--KKIEDSIAFINSKpkplAIYAFTNN--E 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819620888 464 QCRYAIDEATyalrnAAGNFYINDKCTGAVVGQQPFGGARGSGTNDKAGSMInlFRWVSPR--TIKETFHPETDYRYP 539
Cdd:PLN02203 384 KLKRRILSET-----SSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHGKYS--FDTFSHEkaVLRRSLLTEFEFRYP 454
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
179-449 |
2.57e-11 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 66.14 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 179 PLEGFVFALTPFNFtAIAGNL----PSCVAMMGNVVvwKPSNTQIYSANVIMEVFIEAG-LPKGVINLVyvSGpDAGDvI 253
Cdd:cd07128 143 PRRGVAVHINAFNF-PVWGMLekfaPALLAGVPVIV--KPATATAYLTEAVVKDIVESGlLPEGALQLI--CG-SVGD-L 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 254 FKHPD-FAGIHFTGSTGVFQniwktigenihRYKTYPRIVGEtgGKDFILAHPSADIAVLNTALVRGAFEFQ-------- 324
Cdd:cd07128 216 LDHLGeQDVVAFTGSAATAA-----------KLRAHPNIVAR--SIRFNAEADSLNAAILGPDATPGTPEFDlfvkevar 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 325 ------GQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVID----EKAFDKItsyidrAKSSADAEV 394
Cdd:cd07128 283 emtvkaGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSreqrEDVRAAV------ATLLAEAEV 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819620888 395 VIGGQ-------YDKSKGYFIHPTVILAKKADYETMSE--ELFGPVLTIYVYEDDkwEETLELV 449
Cdd:cd07128 357 VFGGPdrfevvgADAEKGAFFPPTLLLCDDPDAATAVHdvEAFGPVATLMPYDSL--AEAIELA 418
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
179-455 |
8.31e-10 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 61.26 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 179 PLEGFVFALTPFNFTAIAGNLPSCVAMMGNV-VVWKPSNTQIYSANVIMEVFIEAG-LPKGVINLVYVSGPD------AG 250
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLAGVpVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGlldhlqPF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 251 DVIfkhpdfagiHFTGSTgvfqniwktigENIHRYKTYPRIVGEtgGKDFILAHPSADIAVLNTALVRGAFEFQ------ 324
Cdd:PRK11903 227 DVV---------SFTGSA-----------ETAAVLRSHPAVVQR--SVRVNVEADSLNSALLGPDAAPGSEAFDlfvkev 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 325 --------GQKCSAASRAYIPQSLWSDLRTRMEKDIQSFKIGGTEDFSNFINAVIDEKAFDKITSYIDRAKssADAEVVI 396
Cdd:PRK11903 285 vremtvksGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALR--AQAEVLF 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819620888 397 GG------QYDKSKGYFIHPTVILAKKADYETMSE--ELFGPVLTIYVYEDDkwEETLELVDK------TSIY 455
Cdd:PRK11903 363 DGggfalvDADPAVAACVGPTLLGASDPDAATAVHdvEVFGPVATLLPYRDA--AHALALARRgqgslvASVY 433
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
182-506 |
2.45e-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: 59.82 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 182 GFVFALTPFNFTAiagNLPSCVAM----MGNvvvwKPSNTQIYSANVIMEVFI----EAGLPKGVINLVYVSGPDAGDVI 253
Cdd:cd07126 144 GPVAIITPFNFPL---EIPALQLMgalfMGN----KPLLKVDSKVSVVMEQFLrllhLCGMPATDVDLIHSDGPTMNKIL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 254 fKHPDFAGIHFTGSTGVFQNIWKtigenihryKTYPRIVGETGGKDF-ILAHPSADIAVLNTALVRGAFEFQGQKCSAAS 332
Cdd:cd07126 217 -LEANPRMTLFTGSSKVAERLAL---------ELHGKVKLEDAGFDWkILGPDVSDVDYVAWQCDQDAYACSGQKCSAQS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 333 RAYIPQSlWSD--LRTRM-----EKDIQSFKIGGTEDFSNfinavidekafDKITSYIDRAKSSADAEVVIGGQ----YD 401
Cdd:cd07126 287 ILFAHEN-WVQagILDKLkalaeQRKLEDLTIGPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGKpltnHS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 402 KSKGY-FIHPTVI------LAKKADYETMSEELFGPVLTIYVYEDDKWEETLELVDKTSIYaLTGSIISQCRYAIDEATY 474
Cdd:cd07126 355 IPSIYgAYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIRFLQEVLA 433
|
330 340 350
....*....|....*....|....*....|....
gi 1819620888 475 ALRNAAGNFYINDKCTGAVVGQ--QPFGGARGSG 506
Cdd:cd07126 434 NTVNGTTYAGIRARTTGAPQNHwfGPAGDPRGAG 467
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
165-506 |
4.55e-09 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 58.90 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 165 PANAKGVwnrveQRPLeGFVFALTPFNFTAIAGNLPSCVAM-MGNVVVWKPSNTQIYSANVIMEVfIEAGLPKGVINLVY 243
Cdd:PLN02174 103 PASAEIV-----SEPL-GVVLVISAWNYPFLLSIDPVIGAIsAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 244 VSGPDAGDVIFKHPDfaGIHFTGSTGVFQNIWKTIGENIhryktyPRIVGETGGKDFILAHPSADIAVLNTALVRGAFEF 323
Cdd:PLN02174 176 GAVTETTALLEQKWD--KIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGC 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 324 Q-GQKCSAASRAYIPQSLWSDLRTRMEKDIQSFkIGGTEDFSNFINAVIDEKAFDKITSYIDRAKSSAdaEVVIGGQYDK 402
Cdd:PLN02174 248 NnGQACISPDYILTTKEYAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSD--KIVYGGEKDR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 403 sKGYFIHPTVILAKKADYETMSEELFGPVLTIYVYEDDkwEETLELVdKTSIYALTGSIISQCRYAidEATYALRNAAGN 482
Cdd:PLN02174 325 -ENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNL--EESFDVI-RSRPKPLAAYLFTHNKKL--KERFAATVSAGG 398
|
330 340
....*....|....*....|....
gi 1819620888 483 FYINDKCTGAVVGQQPFGGARGSG 506
Cdd:PLN02174 399 IVVNDIAVHLALHTLPFGGVGESG 422
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
81-501 |
6.34e-07 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 51.77 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 81 VEDAIDAALAAKEKWENLPWEQRAAiFLKA---------AELVSTKyrykiNAATMLGQSKNayQAEIDSACE----LAD 147
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAA-FLEAiadeiealgDELVARA-----HAETGLPEARL--QGELGRTTGqlrlFAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 148 FLRFNVAYMTEIYSQQPPANAKGVWN-RVEQRPLeG--FVFALT--PFNFTAIAGNLPSCVAMmGNVVVWK-----PSNT 217
Cdd:cd07129 73 LVREGSWLDARIDPADPDRQPLPRPDlRRMLVPL-GpvAVFGASnfPLAFSVAGGDTASALAA-GCPVVVKahpahPGTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 218 QIYsANVIMEVFIEAGLPKGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQNIWKTIGEnihRYKTYPrIVGETGG 297
Cdd:cd07129 151 ELV-ARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAA---RPEPIP-FYAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 298 KD--FI----LAHPSADIA-VLNTALVRGAfefqGQKCSAASRAYIPQSlwsdlrtrmekdiqsfkiggtEDFSNFINAV 370
Cdd:cd07129 226 VNpvFIlpgaLAERGEAIAqGFVGSLTLGA----GQFCTNPGLVLVPAG---------------------PAGDAFIAAL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819620888 371 IDE---------------KAFDKitsYIDRAKSSADAEVVIGGQyDKSKGYFIHPTVILAKKADY---ETMSEELFGPVL 432
Cdd:cd07129 281 AEAlaaapaqtmltpgiaEAYRQ---GVEALAAAPGVRVLAGGA-AAEGGNQAAPTLFKVDAAAFladPALQEEVFGPAS 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819620888 433 TIYVYEDDkwEETLELVDKT--SiyaLTGSIISQcryAIDEATY-----ALRNAAGNFYINDKCTG-AVVGQQPFGG 501
Cdd:cd07129 357 LVVRYDDA--AELLAVAEALegQ---LTATIHGE---EDDLALArellpVLERKAGRLLFNGWPTGvEVCPAMVHGG 425
|
|
| |
