|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
10-520 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 847.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 10 EFKNEPFTNFSTNENKQAMEHALAKVSKELGREIPLYIGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVAL 89
Cdd:PRK03137 4 PYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 90 EAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSilrPLTKI 169
Cdd:PRK03137 84 EAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGK---PVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 170 EGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIE 249
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 250 VGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQPGQIWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKC 329
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 330 SAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGNGYYIQPT 409
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 410 VFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGA 489
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
490 500 510
....*....|....*....|....*....|.
gi 1958218123 490 QPFGGFNMSGTDSKAGGYDYLLLFTQGKLTS 520
Cdd:PRK03137 481 HPFGGFNMSGTDSKAGGPDYLLLFLQAKTVS 511
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-522 |
0e+00 |
|
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: 763.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 11 FKNEPFTNFSTNENKQAMEHALAKVSKELGREIPLYIGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALE 90
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 91 AFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSEtsilRPLTKIE 170
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRG----FPVEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 171 GENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEV 250
Cdd:cd07124 157 GEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 251 GEYLVEHPKTRFISFTGSRAVGCRIYERASKVQPGQIWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCS 330
Cdd:cd07124 237 GDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 331 AGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYP-VGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDG--NGYYIQ 407
Cdd:cd07124 317 ACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVyMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELaaEGYFVQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 408 PTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALV 487
Cdd:cd07124 397 PTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALV 476
|
490 500 510
....*....|....*....|....*....|....*
gi 1958218123 488 GAQPFGGFNMSGTDSKAGGYDYLLLFTQGKLTSRV 522
Cdd:cd07124 477 GRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTEN 511
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
11-520 |
0e+00 |
|
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: 693.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 11 FKNEPFTNFSTNENKQAMEHALAKVSKELGREIPLYIGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALE 90
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 91 AFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSilrPLTKIE 170
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGK---PVNSRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 171 GENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEV 250
Cdd:TIGR01237 158 GETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 251 GEYLVEHPKTRFISFTGSRAVGCRIYERASKVQPGQIWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCS 330
Cdd:TIGR01237 238 GDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 331 AGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGNGYYIQPT 409
Cdd:TIGR01237 318 AGSRAVVHEKVYDEVVERFVEITESLKVGPPDSaDVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 410 VFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGA 489
Cdd:TIGR01237 398 IFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGY 477
|
490 500 510
....*....|....*....|....*....|.
gi 1958218123 490 QPFGGFNMSGTDSKAGGYDYLLLFTQGKLTS 520
Cdd:TIGR01237 478 QPFGGFKMSGTDSKAGGPDYLALFMQAKTVT 508
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
41-517 |
3.61e-176 |
|
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: 504.66 E-value: 3.61e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 41 REIPLYIGSEKI--STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERK 118
Cdd:COG1012 4 PEYPLFIGGEWVaaASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 119 HEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSIlrPLTkIEGENNQMTYIPLGVGVIISPFNFPLAIMA 198
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETI--PSD-APGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 199 GTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYER 278
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 279 ASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEV 358
Cdd:COG1012 240 AAE------NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 359 GAPAEnyP---VGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDG-NGYYIQPTVFADVDPKARIMQEEIFGPVLALA 433
Cdd:COG1012 314 GDPLD--PgtdMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 434 KAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGAlVGAQPFGGFNMSGTDSKAGGYdYLLLF 513
Cdd:COG1012 392 PFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGRE-GLEEY 469
|
....
gi 1958218123 514 TQGK 517
Cdd:COG1012 470 TETK 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
53-517 |
3.71e-173 |
|
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: 496.28 E-value: 3.71e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 53 STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKN 132
Cdd:pfam00171 4 SESETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 133 WAEADADTAEAIDFFEFYAREMIRLSETSIlrPLTKieGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVI 212
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLDGETL--PSDP--GRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 213 LKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRV 292
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN------LKRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 293 IAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVI 371
Cdd:pfam00171 233 TLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPlDPDTDMGPLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 372 DQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDY 450
Cdd:pfam00171 313 SKAQLERVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958218123 451 GLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAqPFGGFNMSGTdSKAGGYDYLLLFTQGK 517
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGF-GREGGPYGLEEYTEVK 457
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
25-517 |
2.79e-169 |
|
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: 487.86 E-value: 2.79e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 25 KQAMEHALAKVSKELGREIPLYIGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERA 104
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 105 DYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRL-SETSILRPLTkieGENNQMTYIPLGV 183
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLrYPAVEVVPYP---GEDNESFYVGLGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 184 GVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFI 263
Cdd:cd07083 158 GVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 264 SFTGSRAVGCRIYERASKVQPGQIWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYD 343
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 344 QVVEKVTSLVSQLEVGAPAENYP-VGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGNGYYIQPTVFADVDPKARIMQ 422
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEENGTdLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 423 EEIFGPVLAL--AKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMSGT 500
Cdd:cd07083 398 EEIFGPVLSVirYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGT 477
|
490
....*....|....*..
gi 1958218123 501 DSKAGGYDYLLLFTQGK 517
Cdd:cd07083 478 NAKTGGPHYLRRFLEMK 494
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
82-517 |
4.30e-146 |
|
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: 426.24 E-value: 4.30e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 82 DSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETS 161
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 162 ILRPLTkieGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLN 241
Cdd:cd07078 81 IPSPDP---GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 242 YVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASA 321
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE------NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 322 FGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNK- 398
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLdPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 399 TDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYI 478
Cdd:cd07078 312 EGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958218123 479 NKKCTGAlVGAQPFGGFNMSGTdSKAGGYDYLLLFTQGK 517
Cdd:cd07078 392 NDYSVGA-EPSAPFGGVKQSGI-GREGGPYGLEEYTEPK 428
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-513 |
4.08e-134 |
|
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: 398.88 E-value: 4.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 13 NEPFTNFSTNEN--KQAMEHALAKVSKELGREIPLYIGsEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALE 90
Cdd:cd07125 2 NSSFVNRIFDLEvpLEALADALKAFDEKEWEAIPIING-EETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 91 AFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSILRPLTkie 170
Cdd:cd07125 81 AFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 171 GENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEV 250
Cdd:cd07125 158 GELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 251 GEYLVEHPKTRFISFTGSRAVGCRIYE-RASKVQPgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKC 329
Cdd:cd07125 238 GEALVAHPRIDGVIFTGSTETAKLINRaLAERDGP----ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 330 SAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGNGYYIQP 408
Cdd:cd07125 314 SALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 409 TVFADVdpKARIMQEEIFGPVLAL--AKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGAL 486
Cdd:cd07125 394 GIIEIV--GIFDLTTEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAI 471
|
490 500
....*....|....*....|....*..
gi 1958218123 487 VGAQPFGGFNMSGTDSKAGGYDYLLLF 513
Cdd:cd07125 472 VGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
46-517 |
1.89e-127 |
|
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: 380.06 E-value: 1.89e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 46 YIGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLL 125
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 126 VLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSI--LRPLTKIEgennqMTYIPLGVGVIISPFNFPLAIMAGTTVA 203
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLpsTRPGVEVE-----TTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 204 AIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQ 283
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 284 pgqiwlKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVG-APA 362
Cdd:cd07097 239 ------ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGdALD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 363 ENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQ 439
Cdd:cd07097 313 EGVDIGPVVSERQLEKDLRYIEIARSEGaKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYD 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 440 EAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAqPFGGFNMSGTDSKAGGYDYLLLFTQGK 517
Cdd:cd07097 393 EALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEAALEFYTTIK 469
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-514 |
9.37e-124 |
|
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: 372.30 E-value: 9.37e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 12 KNEPFTNFSTN-ENKQAMEHALAKVsKELGREIPLYIGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALE 90
Cdd:cd07123 2 VNEPVLSYAPGsPERAKLQEALAEL-KSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 91 AFESWKQVPAAERADYLVRAAALLR-ERKHEFSSLLVLETGKN-WAEADADTAEAIDFFEFYAREMIRLSETsilRPLTK 168
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNvWQAEIDAACELIDFLRFNVKYAEELYAQ---QPLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 169 IEGENNQMTYIPL-GVGVIISPFNFPlAIMAGTTVAAIVSGNTVILKPADTApVIAAKFV-ELMKEVGLPDGVLNYVPGD 246
Cdd:cd07123 158 PAGVWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTA-VLSNYLVyKILEEAGLPPGVINFVPGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 247 GIEVGEYLVEHPKTRFISFTGSRAVGCRIYERAS------KVQPgqiwlkRVIAEMGGKDGVVVDETADIDAAAKAIVAS 320
Cdd:cd07123 236 GPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryRTYP------RIVGETGGKNFHLVHPSADVDSLVTATVRG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 321 AFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKS--EGRLLNGGN 397
Cdd:cd07123 310 AFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDfSNFMGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 398 KTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALA--KAKDWQEAIAIYNDT-DYGLTGAYFSSSEERISFALD--HMH 472
Cdd:cd07123 390 CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTTsPYALTGAIFAQDRKAIREATDalRNA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958218123 473 CGNLYINKKCTGALVGAQPFGGFNMSGTDSKAGGYDYLLLFT 514
Cdd:cd07123 470 AGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWV 511
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
46-517 |
9.36e-121 |
|
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: 363.21 E-value: 9.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 46 YIGSEKI--STDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSS 123
Cdd:cd07131 2 YIGGEWVdsASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 124 LLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSILRPLTkiegENNQMTY-IPLGVGVIISPFNFPLAIMAGTTV 202
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELP----NKDAMTRrQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 203 AAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKV 282
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 283 QpgqiwlKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP- 361
Cdd:cd07131 238 N------KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 362 -AENYpVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGN----GYYIQPTVFADVDPKARIMQEEIFGPVLALAKA 435
Cdd:cd07131 312 dEETD-MGPLINEAQLEKVLNYNEIGKEEGaTLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 436 KDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVgAQPFGGFNMSGTDSKAGGYDYLLLFTQ 515
Cdd:cd07131 391 SSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTE 469
|
..
gi 1958218123 516 GK 517
Cdd:cd07131 470 WK 471
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
88-515 |
1.38e-113 |
|
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: 340.75 E-value: 1.38e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 88 ALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSILRPLT 167
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 168 kieGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDG 247
Cdd:cd06534 83 ---GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 248 IEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQ 327
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN------LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 328 KCSAGSRAIIVESVYDQVVEKVTslvsqlevgapaenypvgpvidqksfdkvmsyieigksegrllnggnktdgngyyiq 407
Cdd:cd06534 234 ICTAASRLLVHESIYDEFVEKLV--------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 408 pTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGAlV 487
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-G 334
|
410 420
....*....|....*....|....*...
gi 1958218123 488 GAQPFGGFNMSGTdSKAGGYDYLLLFTQ 515
Cdd:cd06534 335 PEAPFGGVKNSGI-GREGGPYGLEEYTR 361
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
60-517 |
2.14e-110 |
|
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: 335.69 E-value: 2.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKN-WAEADA 138
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPiTLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 139 DTAEAIDFFEFYArEMIRLSETSILRPltkiegENNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKP 215
Cdd:cd07093 80 DIPRAAANFRFFA-DYILQLDGESYPQ------DGGALNYVlrqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 216 ADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAE 295
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN------LKPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 296 MGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQK 374
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLdPDTEVGPLISKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 375 SFDKVMSYIEIGKSEG-RLLNGGNKTD----GNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTD 449
Cdd:cd07093 307 HLEKVLGYVELARAEGaTILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 450 YGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSGTdSKAGGYDYLLLFTQGK 517
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRVARRLEAGTVWVN--CWLVRDLRTPFGGVKASGI-GREGGDYSLEFYTELK 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
61-510 |
6.04e-110 |
|
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: 334.40 E-value: 6.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07103 2 INPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREMIRLSETSILRPltkIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAP 220
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSP---APGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKD 300
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT------VKRVSLELGGNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 301 GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKV 379
Cdd:cd07103 232 PFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGlDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 380 MSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFS 458
Cdd:cd07103 312 EALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 459 SSEERISFALDHMHCGNLYINkkcTGALVGAQ-PFGGFNMSG---TDSKAGGYDYL 510
Cdd:cd07103 392 RDLARAWRVAEALEAGMVGIN---TGLISDAEaPFGGVKESGlgrEGGKEGLEEYL 444
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
53-499 |
1.46e-108 |
|
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: 331.84 E-value: 1.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 53 STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKN 132
Cdd:cd07086 10 SGGETFTSRNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 133 WAEADADTAEAIDFFEFYAREMIRL------SEtsilRPltkieGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIV 206
Cdd:cd07086 89 LPEGLGEVQEMIDICDYAVGLSRMLygltipSE----RP-----GHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 207 SGNTVILKPADTAPVIAAKFVELMKEV----GLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKV 282
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 283 qpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP- 361
Cdd:cd07086 239 ------FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 362 AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGN--GYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDW 438
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 439 QEAIAIYNDTDYGLTGAYFSSSEERISFALDHM--HCGNLYINKKCTGALVGAqPFGGFNMSG 499
Cdd:cd07086 393 EEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIGG-AFGGEKETG 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
42-517 |
1.10e-107 |
|
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: 329.55 E-value: 1.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 42 EIP--LYIGSEKI-STDEKIIS-INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFE--SWKQVPAAERADYLVRAAALLR 115
Cdd:cd07091 1 EQPtgLFINNEFVdSVSGKTFPtINPAT-EEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 116 ERKHEFSSLLVLETGKN-WAEADADTAEAIDFFEFYARemirLSEtsilrpltKIEGE-----NNQMTYI---PLGVGVI 186
Cdd:cd07091 80 RDRDELAALESLDNGKPlEESAKGDVALSIKCLRYYAG----WAD--------KIQGKtipidGNFLAYTrrePIGVCGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 187 ISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFT 266
Cdd:cd07091 148 IIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 267 GSRAVGCRIYERASKVQpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVV 346
Cdd:cd07091 228 GSTAVGRTIMEAAAKSN-----LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 347 EKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEE 424
Cdd:cd07091 303 EKFKARAEKRVVGDPFdPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 425 IFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSeerISFALDHMH---CGNLYINkkCTGALVGAQPFGGFNMSGTd 501
Cdd:cd07091 383 IFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKD---INKALRVSRalkAGTVWVN--TYNVFDAAVPFGGFKQSGF- 456
|
490
....*....|....*.
gi 1958218123 502 SKAGGYDYLLLFTQGK 517
Cdd:cd07091 457 GRELGEEGLEEYTQVK 472
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
45-499 |
3.43e-106 |
|
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: 325.23 E-value: 3.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKI--STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFS 122
Cdd:cd07138 1 FYIDGAWVapAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 123 SLLVLETGK-NWAEADADTAEAIDFFEFYAREMIRLSETSilrpltkiEGENNQMTYIPLGVGVIISPFNFPLAIMAGTT 201
Cdd:cd07138 80 QAITLEMGApITLARAAQVGLGIGHLRAAADALKDFEFEE--------RRGNSLVVREPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 202 VAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASK 281
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 282 VqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP 361
Cdd:cd07138 232 T------VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 362 A-ENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGG-NKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAK 436
Cdd:cd07138 306 RdPATTLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGpGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 437 DWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkcTGALVGAQPFGGFNMSG 499
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN---GAAFNPGAPFGGYKQSG 445
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
45-499 |
2.61e-105 |
|
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: 323.37 E-value: 2.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKI--STDEKIISINPgNIDQIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHE 120
Cdd:cd07139 1 LFIGGRWVapSGSETIDVVSP-ATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 121 FSSLLVLETGK-NWAEADADTAEAIDFFEFYArEMIRLSETSILRPltKIEGENNQMTYIPLGVGVIISPFNFPLAIMAG 199
Cdd:cd07139 80 LARLWTAENGMpISWSRRAQGPGPAALLRYYA-ALARDFPFEERRP--GSGGGHVLVRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 200 TTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDgIEVGEYLVEHPKTRFISFTGSRAVGCRIYERA 279
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 280 SKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVG 359
Cdd:cd07139 236 GER------LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 360 APAEnyP---VGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALA 433
Cdd:cd07139 310 DPLD--PatqIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 434 KAKDWQEAIAIYNDTDYGLTGAYFSSSEERisfALD---HMHCGNLYINkkctGALVGAQ-PFGGFNMSG 499
Cdd:cd07139 388 PYDDEDDAVRIANDSDYGLSGSVWTADVER---GLAvarRIRTGTVGVN----GFRLDFGaPFGGFKQSG 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
81-515 |
2.95e-105 |
|
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: 321.79 E-value: 2.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETG----KNWaeadadtaeaidfFEF-YAREMI 155
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGstrpKAA-------------FEVgAAIAIL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 156 RLSETSILRPLTKI-----EGENNQMTYIPLGVGVIISPFNFPLaIMAGTTVA-AIVSGNTVILKPA-DTAPVIAAKFVE 228
Cdd:cd07104 69 REAAGLPRRPEGEIlpsdvPGKESMVRRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDsRTPVTGGLLIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 229 LMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETA 308
Cdd:cd07104 148 IFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRH------LKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 309 DIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEIGK 387
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRdPDTVIGPLINERQVDRVHAIVEDAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 388 SEG-RLLNGGnKTDGNgyYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEER-IS 465
Cdd:cd07104 302 AAGaRLLTGG-TYEGL--FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERaMA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 466 FAlDHMHCGNLYINkkCTGALVGAQ-PFGGFNMSGTDSKAGGYDyLLLFTQ 515
Cdd:cd07104 379 FA-ERLETGMVHIN--DQTVNDEPHvPFGGVKASGGGRFGGPAS-LEEFTE 425
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
60-517 |
6.25e-104 |
|
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: 319.11 E-value: 6.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEAD 137
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 ADTAEAIDFFEFYAremirlsetSILRpltKIEGE------NNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSG 208
Cdd:cd07114 80 AQVRYLAEWYRYYA---------GLAD---KIEGAvipvdkGDYLNFTrrePLGVVAAITPWNSPLLLLAKKLAPALAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 209 NTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiw 288
Cdd:cd07114 148 NTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 289 LKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPV 367
Cdd:cd07114 222 LAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLdPETQM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 368 GPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDG----NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAI 442
Cdd:cd07114 302 GPLATERQLEKVERYVARAREEGaRVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAI 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958218123 443 AIYNDTDYGLTGAYFSSS---EERISFALDhmhCGNLYINkkcT-GALVGAQPFGGFNMSGTDsKAGGYDYLLLFTQGK 517
Cdd:cd07114 382 ALANDSEYGLAAGIWTRDlarAHRVARAIE---AGTVWVN---TyRALSPSSPFGGFKDSGIG-RENGIEAIREYTQTK 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
61-500 |
1.14e-103 |
|
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: 318.39 E-value: 1.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07149 4 ISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREMIRLSETSIlrPLTKIEGENNQMTY---IPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPAD 217
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETI--PFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 218 TAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASkvqpgqiwLKRVIAEMG 297
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 298 GKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSF 376
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLdEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 377 DKVMSYIEIGKSEG-RLLNGGNKtdgNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGA 455
Cdd:cd07149 313 ERIEEWVEEAVEGGaRLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958218123 456 YFSSSEERISFALDHMHCGNLYINKKCTgALVGAQPFGGFNMSGT 500
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
60-517 |
3.60e-103 |
|
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: 317.39 E-value: 3.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADAD 139
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 140 TAEAIDFFEFYAREMIRLSETSIlrPLTkieGENNQMT-YIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADT 218
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETI--PVG---GRNLHYTlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 219 APVIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGG 298
Cdd:cd07107 155 APLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG------IKHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 299 KDGVVV-DETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSF 376
Cdd:cd07107 228 KNALIVfPDADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPtDPATTMGPLVSRQQY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 377 DKVMSYIEIGKSEG-RLLNGGNKTDG----NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYG 451
Cdd:cd07107 308 DRVMHYIDSAKREGaRLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 452 LTGAYFSSSEERISFALDHMHCGNLYINKKCTGALvGAqPFGGFNMSGTDSKAgGYDYLLLFTQGK 517
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL-GA-PFGGVKNSGIGREE-CLEELLSYTQEK 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
60-517 |
1.14e-102 |
|
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: 315.92 E-value: 1.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADAD 139
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 140 -TAEAIDFFEFYAREMirlsetsilrplTKIEGE-----NNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNT 210
Cdd:cd07115 80 dVPRAADTFRYYAGWA------------DKIEGEvipvrGPFLNYTvrePVGVVGAIVPWNFPLMFAAWKVAPALAAGNT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 211 VILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIyeraskVQPGQIWLK 290
Cdd:cd07115 148 VVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKI------MQGAAGNLK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 291 RVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGP 369
Cdd:cd07115 222 RVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDpKTQMGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 370 VIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDT 448
Cdd:cd07115 302 LVSQAQFDRVLDYVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958218123 449 DYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSGTdSKAGGYDYLLLFTQGK 517
Cdd:cd07115 382 EYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGF-GREMGREALDEYTEVK 447
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
61-499 |
1.19e-102 |
|
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: 316.11 E-value: 1.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWK-QVPAAERADYLVRAAALLRERKHEFSSLLVLETGK-NWAEADA 138
Cdd:cd07089 2 INPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 139 DTAEAIDFFEFYArEMIRLSETSILRPLTKIEGENNQMT--YIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPA 216
Cdd:cd07089 81 QVDGPIGHLRYFA-DLADSFPWEFDLPVPALRGGPGRRVvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 217 DTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEM 296
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 297 GGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAEnyP---VGPVIDQ 373
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPAD--PgtvMGPLISA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 374 KSFDKVMSYIEIGKSEG-RLLNGGNKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDY 450
Cdd:cd07089 312 AQRDRVEGYIARGRDEGaRLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDY 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 451 GLTGAYFSSSEERisfALD---HMHCGNLYINkkcTGALVGAQ-PFGGFNMSG 499
Cdd:cd07089 392 GLSGGVWSADVDR---AYRvarRIRTGSVGIN---GGGGYGPDaPFGGYKQSG 438
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
56-499 |
1.60e-101 |
|
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: 313.38 E-value: 1.60e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 56 EKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNW 133
Cdd:cd07112 2 ETFATINPAT-GRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 134 AEADAD-TAEAIDFFEFYArEMIrlsetsilrplTKIEGE-----NNQMTYI---PLGVGVIISPFNFPLaIMAGTTVA- 203
Cdd:cd07112 81 SDALAVdVPSAANTFRWYA-EAI-----------DKVYGEvaptgPDALALItrePLGVVGAVVPWNFPL-LMAAWKIAp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 204 AIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERAskvq 283
Cdd:cd07112 148 ALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYS---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 284 pGQIWLKRVIAEMGGKD-GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP- 361
Cdd:cd07112 224 -GQSNLKRVWLECGGKSpNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 362 AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNK--TDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDW 438
Cdd:cd07112 303 DPATRMGALVSEAHFDKVLGYIESGKAEGaRLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 439 QEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:cd07112 383 EEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSG 441
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
60-499 |
2.16e-101 |
|
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: 312.63 E-value: 2.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES-WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADA 138
Cdd:cd07109 1 VFDPST-GEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 139 DTAEAIDFFEFYAREMIRLSETSIlrPLTkiEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADT 218
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETI--PLG--PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 219 APVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASK-VQPgqiwlkrVIAEMG 297
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEnVVP-------VTLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 298 GKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFD 377
Cdd:cd07109 229 GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 378 KVMSYIEIGKSEG-RLLNGGNKTDG---NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLT 453
Cdd:cd07109 309 RVEGFVARARARGaRIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958218123 454 GAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQ-PFGGFNMSG 499
Cdd:cd07109 389 AGVWTRDGDRALRVARRLRAGQVFVN--NYGAGGGIElPFGGVKKSG 433
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
53-510 |
2.94e-101 |
|
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: 312.66 E-value: 2.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 53 STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKN 132
Cdd:cd07088 10 SSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 133 WAEADADTAEAIDFFEFYArEMIRLSETSILRplTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVI 212
Cdd:cd07088 89 LSLARVEVEFTADYIDYMA-EWARRIEGEIIP--SDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 213 LKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRV 292
Cdd:cd07088 166 IKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEN------ITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 293 IAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVI 371
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFdAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 372 DQKSFDKVMSYIEIGKSEG-RLLNGGNKTDG-NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTD 449
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGaTLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958218123 450 YGLTGAYFSSSEERISFALDHMHCGNLYINKkctGALVGAQPF-GGFNMSGT---DSKAGGYDYL 510
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINR---ENFEAMQGFhAGWKKSGLggaDGKHGLEEYL 461
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
62-508 |
4.90e-100 |
|
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: 308.87 E-value: 4.90e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 62 NPgNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTA 141
Cdd:cd07150 5 NP-ADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 142 EAIDFFEfYAREMIRLSETSILRPLTkiEGENNQMTYIPLGVGVIISPFNFPLaIMAGTTVA-AIVSGNTVILKPADTAP 220
Cdd:cd07150 84 FTPELLR-AAAGECRRVRGETLPSDS--PGTVSMSVRRPLGVVAGITPFNYPL-ILATKKVAfALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKD 300
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRH------LKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 301 GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKV 379
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDpDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 380 MSYIEIGKSEGRLLNGGNKTDGNGYyiQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSS 459
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGKYDGNFY--QPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 460 SEER-ISFALDhMHCGNLYINkkCTGALVGAQ-PFGGFNMSGTDSKAGGYD 508
Cdd:cd07150 392 DLQRaFKLAER-LESGMVHIN--DPTILDEAHvPFGGVKASGFGREGGEWS 439
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-520 |
1.51e-98 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 320.22 E-value: 1.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 12 KNEPFTNFSTNENKQAMEHALAKVSKELGREIPLYIGsekisTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALEA 91
Cdd:PRK11904 523 KNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 92 FESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSIlrPLTKIEG 171
Cdd:PRK11904 598 FPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPE--KLPGPTG 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 172 ENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVG 251
Cdd:PRK11904 676 ESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVG 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 252 EYLVEHPKTRFISFTGSRAVGCRI----YERASKVQPgqiwlkrVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQ 327
Cdd:PRK11904 756 AALTADPRIAGVAFTGSTETARIInrtlAARDGPIVP-------LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQ 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 328 KCSAgSRAIIV-ESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDG--NG 403
Cdd:PRK11904 829 RCSA-LRVLFVqEDIADRVIEMLKGAMAELKVGDPRLlSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGteNG 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 404 YYIQPTVFAdvDPKARIMQEEIFGPVLALA--KAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKK 481
Cdd:PRK11904 908 HFVAPTAFE--IDSISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRN 985
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958218123 482 CTGALVGAQPFGGFNMSGTDSKAGGYDYLLLFTQGKLTS 520
Cdd:PRK11904 986 QIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1024
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
61-499 |
2.18e-98 |
|
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: 305.77 E-value: 2.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADA 138
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 139 DTAEAIDFFEFYAREMIRLSETSILRP---LTKIEGEnnqmtyiPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKP 215
Cdd:cd07119 97 DIDDVANCFRYYAGLATKETGEVYDVPphvISRTVRE-------PVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 216 ADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAE 295
Cdd:cd07119 170 SEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 296 MGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYP-VGPVIDQK 374
Cdd:cd07119 244 LGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTeMGPLVSAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 375 SFDKVMSYIEIGKSEG-RLLNGGNKTDGN----GYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTD 449
Cdd:cd07119 324 HREKVLSYIQLGKEEGaRLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTP 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 450 YGLTGAYFSSS---EERISFALDHmhcGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:cd07119 404 YGLAGAVWTKDiarANRVARRLRA---GTVWIN--DYHPYFAEAPWGGYKQSG 451
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
21-517 |
1.17e-97 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 320.66 E-value: 1.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 21 TNENK-QAMEHALAKVSKELGREIPLyIGSEKISTDEKIIsINPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVP 99
Cdd:PRK11905 533 SDEATlAALDEALNAFAAKTWHAAPL-LAGGDVDGGTRPV-LNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 100 AAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSILRPLtkiegennqmtyi 179
Cdd:PRK11905 611 AAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPL------------- 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 plGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPK 259
Cdd:PRK11905 678 --GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 260 TRFISFTGSRAVGCRIY----ERASKVQPgqiwlkrVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAgSRA 335
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQrtlaKRSGPPVP-------LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA-LRV 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 336 IIV-ESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEGRLLN--GGNKTDGNGYYIQPTVF 411
Cdd:PRK11905 828 LCLqEDVADRVLTMLKGAMDELRIGDPWRlSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHqlPLPAETEKGTFVAPTLI 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 412 aDVDpKARIMQEEIFGPVLALA--KAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGA 489
Cdd:PRK11905 908 -EID-SISDLEREVFGPVLHVVrfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGV 985
|
490 500
....*....|....*....|....*...
gi 1958218123 490 QPFGGFNMSGTDSKAGGYDYLLLFTQGK 517
Cdd:PRK11905 986 QPFGGEGLSGTGPKAGGPLYLGRLVREA 1013
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
61-517 |
1.30e-97 |
|
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: 303.13 E-value: 1.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNW-AEADAD 139
Cdd:cd07108 2 INPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 140 TAEAIDFFEFYAREMirlSEtsilrpltkIEGEN-----NQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTV 211
Cdd:cd07108 81 AAVLADLFRYFGGLA---GE---------LKGETlpfgpDVLTYTvrePLGVVGAILPWNAPLMLAALKIAPALVAGNTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 212 ILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERAS-KVQPgqiwlk 290
Cdd:cd07108 149 VLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAdRLIP------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 291 rVIAEMGGKD-GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVG 368
Cdd:cd07108 222 -VSLELGGKSpMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLdEATDIG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 369 PVIDQKSFDKVMSYIEIGKS--EGRLLNGGNK----TDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAI 442
Cdd:cd07108 301 AIISEKQFAKVCGYIDLGLStsGATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVI 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 443 AIYNDTDYGLTGAYFSSSeerISFALDHMH---CGNLYINkKCTGALVGaQPFGGFNMSGTDSKAGGYDYLLLFTQGK 517
Cdd:cd07108 381 AMANDSHYGLAAYVWTRD---LGRALRAAHaleAGWVQVN-QGGGQQPG-QSYGGFKQSGLGREASLEGMLEHFTQKK 453
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
47-517 |
4.13e-95 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 313.03 E-value: 4.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 47 IGSEKISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLV 126
Cdd:COG4230 561 LIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLV 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 127 LETGKNWAEADADTAEAIDFFEFYAREMIRLsetsilrpltkiegENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIV 206
Cdd:COG4230 641 REAGKTLPDAIAEVREAVDFCRYYAAQARRL--------------FAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 207 SGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIY----ERASKV 282
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINrtlaARDGPI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 283 QPgqiwlkrVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAgSRAIIV-ESVYDQVVEKVTSLVSQLEVGAP 361
Cdd:COG4230 787 VP-------LIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSA-LRVLCVqEDIADRVLEMLKGAMAELRVGDP 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 362 AE-NYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDG--NGYYIQPTVF--ADVDpkarIMQEEIFGPVLALA--K 434
Cdd:COG4230 859 ADlSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcaNGTFVAPTLIeiDSIS----DLEREVFGPVLHVVryK 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 435 AKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMSGTDSKAGGYDYLLLFT 514
Cdd:COG4230 935 ADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFA 1014
|
...
gi 1958218123 515 QGK 517
Cdd:COG4230 1015 TER 1017
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
61-499 |
6.99e-95 |
|
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: 295.59 E-value: 6.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07106 2 INPAT-GEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAR-----EMIRLSETsilrplTKIEgennqMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKP 215
Cdd:cd07106 81 GGAVAWLRYTASldlpdEVIEDDDT------RRVE-----LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 216 ADTAPVIAAKFVELMKEVgLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAE 295
Cdd:cd07106 150 SPFTPLCTLKLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKT------LKRVTLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 296 MGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAEnyP---VGPVID 372
Cdd:cd07106 222 LGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLD--PgttLGPVQN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 373 QKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYG 451
Cdd:cd07106 300 KMQYDKVKELVEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYG 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958218123 452 LTGAYFSSSEERISFALDHMHCGNLYINKKctGALVGAQPFGGFNMSG 499
Cdd:cd07106 380 LGASVWSSDLERAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSG 425
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
61-518 |
6.96e-94 |
|
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: 293.49 E-value: 6.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNIdQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07145 4 RNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREMIRLSETSIlrPLTKIEGENNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPAD 217
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGETI--PVDAYEYNERRIAFTvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 218 TAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMG 297
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 298 GKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSF 376
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLdESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 377 DKVMSYIEIGKSEG-RLLNGGNKTDgnGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGA 455
Cdd:cd07145 315 ERMENLVNDAVEKGgKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958218123 456 YFSSSeerISFAL---DHMHCGNLYINKkcTGAL-VGAQPFGGFNMSGTdSKAGGYDYLLLFTQGKL 518
Cdd:cd07145 393 VFTND---INRALkvaRELEAGGVVIND--STRFrWDNLPFGGFKKSGI-GREGVRYTMLEMTEEKT 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
61-499 |
1.46e-92 |
|
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: 290.02 E-value: 1.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07110 2 INPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREMIRLSETSILRPLTKIEGENNQMTYIPLGVGVIISPFNFPLaIMAGTTVA-AIVSGNTVILKPADTA 219
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPL-LMAAWKVApALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 220 PVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGK 299
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD------IKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 300 DGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDK 378
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 379 VMSYIEIGKSEG-RLLNGGNKTD--GNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGA 455
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958218123 456 YFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
36-517 |
3.09e-92 |
|
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: 290.08 E-value: 3.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 36 SKELGREIPLYIGSE--KISTDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWK-QVPAAERADYLVRAAA 112
Cdd:cd07144 1 GKSYDQPTGLFINNEfvKSSDGETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAFESWWsKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 113 LLRERKHEFSSLLVLETGKNWAEADAD-TAEAIDFFEFYAREMIRLSETSIlrpltkiEGENNQMTYI---PLGVGVIIS 188
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSNALGdLDEIIAVIRYYAGWADKIQGKTI-------PTSPNKLAYTlhePYGVCGQII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 189 PFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGS 268
Cdd:cd07144 153 PWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 269 RAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEK 348
Cdd:cd07144 233 TATGRLVMKAAAQN------LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 349 VTSLVSQ-LEVGAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNK---TDGNGYYIQPTVFADVDPKARIMQ 422
Cdd:cd07144 307 FVEHVKQnYKVGSPfDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 423 EEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINK---KCTGAlvgaqPFGGFNMSG 499
Cdd:cd07144 387 EEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsndSDVGV-----PFGGFKMSG 461
|
490
....*....|....*...
gi 1958218123 500 TDSKAGGYDyLLLFTQGK 517
Cdd:cd07144 462 IGRELGEYG-LETYTQTK 478
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
53-499 |
1.13e-91 |
|
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: 288.05 E-value: 1.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 53 STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKN 132
Cdd:cd07151 7 TSERTIDVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 133 WAEADadtaeaidfFEF-YAREMIRLSETSILRPLTKI-----EGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIV 206
Cdd:cd07151 86 RIKAN---------IEWgAAMAITREAATFPLRMEGRIlpsdvPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 207 SGNTVILKPADTAPV----IAAKFVElmkEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKV 282
Cdd:cd07151 157 LGNAVVLKPASDTPItgglLLAKIFE---EAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 283 qpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA 362
Cdd:cd07151 234 ------LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 363 E-NYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGnktDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQE 440
Cdd:cd07151 308 DpDTVVGPLINESQVDGLLDKIEQAVEEGaTLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEE 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 441 AIAIYNDTDYGLTGAYFSSSEER-ISFAlDHMHCGNLYINKKCTGALVGAqPFGGFNMSG 499
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERgVQFA-RRIDAGMTHINDQPVNDEPHV-PFGGEKNSG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
46-499 |
1.37e-91 |
|
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: 287.93 E-value: 1.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 46 YIGSEKISTDEKIISI-NPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESW-KQVPAAERADYLVRAAALLRERKHEFSS 123
Cdd:cd07082 5 LINGEWKESSGKTIEVySPID-GEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 124 LLVLETGKNWAEADADTAEAIDFFE---FYAREMIRLSETSILRPLTK-IEGennQMTYIPLGVGVIISPFNFPLAIMAG 199
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRdtiEELKRLDGDSLPGDWFPGTKgKIA---QVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 200 TTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERA 279
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 280 SKvqpgqiwlKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVG 359
Cdd:cd07082 241 PM--------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 360 APAENYP-VGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNgyYIQPTVFADVDPKARIMQEEIFGPVLALAKAKD 437
Cdd:cd07082 313 MPWDNGVdITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 438 WQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCT-GalVGAQPFGGFNMSG 499
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrG--PDHFPFLGRKDSG 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
68-500 |
1.66e-91 |
|
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: 286.92 E-value: 1.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 68 QIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADAD-TAEAIDF 146
Cdd:cd07092 8 EEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDeLPGAVDN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 147 FEFYA---REMIRLSETSILRPLTkiegennqmTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAP 220
Cdd:cd07092 88 FRFFAgaaRTLEGPAAGEYLPGHT---------SMIrrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKD 300
Cdd:cd07092 159 LTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT------LKRVHLELGGKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 301 GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKV 379
Cdd:cd07092 232 PVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPdDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 380 MSYIEIGKSEGRLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFS- 458
Cdd:cd07092 312 AGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTr 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958218123 459 --SSEERISFALDHmhcGNLYINkkCTGALVGAQPFGGFNMSGT 500
Cdd:cd07092 392 dvGRAMRLSARLDF---GTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
61-517 |
2.20e-90 |
|
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: 284.20 E-value: 2.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07090 2 IEPAT-GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAR-------EMIRLSETSILrpLTKIEgennqmtyiPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVIL 213
Cdd:cd07090 81 DSSADCLEYYAGlaptlsgEHVPLPGGSFA--YTRRE---------PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 214 KPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVI 293
Cdd:cd07090 150 KPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG------IKHVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 294 AEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVID 372
Cdd:cd07090 223 LELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLdEDTQMGALIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 373 QKSFDKVMSYIEIGKSEG-RLLNGGNKTDG-----NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYN 446
Cdd:cd07090 303 EEHLEKVLGYIESAKQEGaKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRAN 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958218123 447 DTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkcTGALVGAQ-PFGGFNMSGTdSKAGGYDYLLLFTQGK 517
Cdd:cd07090 383 DTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWIN---TYNISPVEvPFGGYKQSGF-GRENGTAALEHYTQLK 450
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
42-507 |
3.59e-89 |
|
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: 282.11 E-value: 3.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 42 EIP--LYIGSEKISTDEK--IISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFE-SW-KQVPAAERADYLVRAAALLR 115
Cdd:cd07143 4 EQPtgLFINGEFVDSVHGgtVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLME 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 116 ERKHEFSSLLVLETGKNWAEADAD-TAEAIDFFEFYAREMIRLSETSIlrpltkiEGENNQMTYI---PLGVGVIISPFN 191
Cdd:cd07143 83 RNLDYLASIEALDNGKTFGTAKRVdVQASADTFRYYGGWADKIHGQVI-------ETDIKKLTYTrhePIGVCGQIIPWN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 192 FPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAV 271
Cdd:cd07143 156 FPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 272 GCRIYERASKVQpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTS 351
Cdd:cd07143 236 GRKVMEAAAKSN-----LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 352 LVSQLEVGAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGN-GYYIQPTVFADVDPKARIMQEEIFGPV 429
Cdd:cd07143 311 KAKKLKVGDPfAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNeGYFIEPTIFTDVTEDMKIVKEEIFGPV 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 430 LALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSGTDSKAGGY 507
Cdd:cd07143 391 VAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSGIGRELGEY 466
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
60-507 |
9.86e-88 |
|
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: 278.22 E-value: 9.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFE--SWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEAD 137
Cdd:cd07142 23 TIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 ADTA-EAIDFFEFYAREMIRLSETSIlrpltkiEGENNQMTYI---PLGVGVIISPFNFPLaIMAGTTVA-AIVSGNTVI 212
Cdd:cd07142 102 YAEVpLAARLFRYYAGWADKIHGMTL-------PADGPHHVYTlhePIGVVGQIIPWNFPL-LMFAWKVGpALACGNTIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 213 LKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqiwLKRV 292
Cdd:cd07142 174 LKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN-----LKPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 293 IAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVI 371
Cdd:cd07142 249 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPfRKGVEQGPQV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 372 DQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDY 450
Cdd:cd07142 329 DKEQFEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958218123 451 GLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSGTDSKAGGY 507
Cdd:cd07142 409 GLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGIY 463
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
43-521 |
2.13e-86 |
|
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: 274.78 E-value: 2.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 43 IPLYIGSEKI-STDEKIISI-NPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHE 120
Cdd:cd07085 1 LKLFINGEWVeSKTTEWLDVyNPAT-GEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 121 FSSLLVLETGKNWAEADADTAEAIDFFEFyAREMIRLSETSILRPLTKieGENNQMTYIPLGVGVIISPFNFPLAIMAGT 200
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEYLENVAR--GIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 201 TVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERAS 280
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK-EAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 281 KVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGA 360
Cdd:cd07085 236 AN------GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 361 PA-ENYPVGPVIDQKSFDKVMSYIEIGKSEGR--LLNG-GNKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALAK 434
Cdd:cd07085 310 GDdPGADMGPVISPAAKERIEGLIESGVEEGAklVLDGrGVKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 435 AKDWQEAIAIYNDTDYGLTGAYFSSS-------EERISfaldhmhCGNLYINkkctgalVG-AQPFGGFNMSGT-DSKAG 505
Cdd:cd07085 390 VDTLDEAIAIINANPYGNGAAIFTRSgaaarkfQREVD-------AGMVGIN-------VPiPVPLAFFSFGGWkGSFFG 455
|
490 500
....*....|....*....|..
gi 1958218123 506 -----GYDYLLLFTQGK-LTSR 521
Cdd:cd07085 456 dlhfyGKDGVRFYTQTKtVTSR 477
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
61-507 |
4.77e-86 |
|
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: 273.84 E-value: 4.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFE---SWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEAD 137
Cdd:cd07141 27 INPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 AD-TAEAIDFFEFYAREMirlsetsilrplTKIEGEN-----NQMTYI---PLGV-GVIIsPFNFPLAIMAGTTVAAIVS 207
Cdd:cd07141 106 LVdLPGAIKVLRYYAGWA------------DKIHGKTipmdgDFFTYTrhePVGVcGQII-PWNFPLLMAAWKLAPALAC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 208 GNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqi 287
Cdd:cd07141 173 GNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSN---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 288 wLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYP 366
Cdd:cd07141 249 -LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDpKTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 367 VGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIY 445
Cdd:cd07141 328 QGPQIDEEQFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958218123 446 NDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSGTDSKAGGY 507
Cdd:cd07141 408 NNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGRELGEY 467
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
45-499 |
6.67e-86 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 273.68 E-value: 6.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKIS--TDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFS 122
Cdd:PRK13252 9 LYIDGAYVEatSGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 123 SLLVLETGKNWAEADAD-TAEAIDFFEFYAR-------EMIRLSETSILrpLTKIEgennqmtyiPLGVGVIISPFNFPL 194
Cdd:PRK13252 88 ALETLDTGKPIQETSVVdIVTGADVLEYYAGlapalegEQIPLRGGSFV--YTRRE---------PLGVCAGIGAWNYPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 195 AIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCR 274
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 275 IYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVS 354
Cdd:PRK13252 236 VMAAAAAS------LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 355 QLEVGAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNK-TDG---NGYYIQPTVFADVDPKARIMQEEIFGP 428
Cdd:PRK13252 310 RIRIGDPmDPATNFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGERlTEGgfaNGAFVAPTVFTDCTDDMTIVREEIFGP 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958218123 429 VLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkcTGALVGAQ-PFGGFNMSG 499
Cdd:PRK13252 390 VMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN---TWGESPAEmPVGGYKQSG 458
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
61-515 |
8.66e-86 |
|
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: 273.71 E-value: 8.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:TIGR01238 56 TNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREmirlsetsilrpltkIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAP 220
Cdd:TIGR01238 136 REAVDFCRYYAKQ---------------VRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQPGQIWLkrvIAEMGGKD 300
Cdd:TIGR01238 201 LIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPL---IAETGGQN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 301 GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKV 379
Cdd:TIGR01238 278 AMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLlTTDVGPVIDAEAKQNL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 380 MSYIE----IGKSEGRLLNGGNKTDGNGYYIQPTVFaDVDPKARiMQEEIFGPVLALA--KAKDWQEAIAIYNDTDYGLT 453
Cdd:TIGR01238 358 LAHIEhmsqTQKKIAQLTLDDSRACQHGTFVAPTLF-ELDDIAE-LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLT 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958218123 454 GAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMSGTDSKAGGYDYLLLFTQ 515
Cdd:TIGR01238 436 MGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQ 497
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
45-499 |
1.90e-85 |
|
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: 272.30 E-value: 1.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKI--STDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFS 122
Cdd:cd07559 3 NFINGEWVapSKGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 123 SLLVLETGKNWAEADADTA-EAIDFFEFYArEMIRLSETSIlrpltkIEGENNQMTYI---PLGV-GVIIsPFNFPLaIM 197
Cdd:cd07559 82 VAETLDNGKPIRETLAADIpLAIDHFRYFA-GVIRAQEGSL------SEIDEDTLSYHfhePLGVvGQII-PWNFPL-LM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 198 AGTTVA-AIVSGNTVILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIY 276
Cdd:cd07559 153 AAWKLApALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 277 ERASKVqpgqiwLKRVIAEMGGK------DGVVVDETADIDAAAKAIVASAFGyQGQKCSAGSRAIIVESVYDQVVEKVT 350
Cdd:cd07559 232 QYAAEN------LIPVTLELGGKspniffDDAMDADDDFDDKAEEGQLGFAFN-QGEVCTCPSRALVQESIYDEFIERAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 351 SLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGN----GYYIQPTVFADVDPKARIMQEE 424
Cdd:cd07559 305 ERFEAIKVGNPLDpETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEE 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958218123 425 IFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:cd07559 385 IFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
45-499 |
1.23e-84 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 269.86 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKISTDEKIISI-NPGNIDQIiGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSS 123
Cdd:PRK13473 5 LLINGELVAGEGEKQPVyNPATGEVL-AEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 124 LLVLETGK-NWAEADADTAEAIDFFEFYA---REMIRLS-------ETSILRpltkiegennqmtYIPLGVGVIISPFNF 192
Cdd:PRK13473 84 LESLNCGKpLHLALNDEIPAIVDVFRFFAgaaRCLEGKAageylegHTSMIR-------------RDPVGVVASIAPWNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 193 PLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVG 272
Cdd:PRK13473 151 PLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 273 CRIYERASKVqpgqiwLKRVIAEMGGKDGVVV-DETADIDAAAKAIVasaFGY--QGQKCSAGSRAIIVESVYDQVVEKV 349
Cdd:PRK13473 230 KHVLSAAADS------VKRTHLELGGKAPVIVfDDADLDAVVEGIRT---FGYynAGQDCTAACRIYAQRGIYDDLVAKL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 350 TSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEIGKSEG--RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIF 426
Cdd:PRK13473 301 AAAVATLKVGDPDdEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVF 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 427 GPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:PRK13473 381 GPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVN--THFMLVSEMPHGGQKQSG 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
75-517 |
1.62e-83 |
|
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: 266.51 E-value: 1.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 75 KGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAr 152
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 153 emirlsetSILRPLtkiEGE--NN---QMTYI----PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIA 223
Cdd:cd07118 94 --------SLARTL---HGDsyNNlgdDMLGLvlrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 224 AKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVV 303
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARN------LKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 304 VDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKVMSY 382
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 383 IEIGKSEG-RLLNGGNKTD-GNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSS 460
Cdd:cd07118 317 VDAGRAEGaTLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 461 EERISFALDHMHCGNLYINKKCTGalvGAQ-PFGGFNMSGTDSKAGGYDyLLLFTQGK 517
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDG---SPElPFGGFKQSGIGRELGRYG-VEEYTELK 450
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
68-515 |
4.50e-83 |
|
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: 264.93 E-value: 4.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 68 QIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFF 147
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 148 eFYAREMIRLSETSILrplTKIEGENNQMTYIPLGVGVIISPFNFPLaIMAGTTVA-AIVSGNTVILKPADTAPV----- 221
Cdd:cd07152 82 -HEAAGLPTQPQGEIL---PSAPGRLSLARRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDPRTPVsggvv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 222 IAakfvELMKEVGLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDG 301
Cdd:cd07152 157 IA----RLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRH------LKKVSLELGGKNA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 302 VVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVM 380
Cdd:cd07152 226 LIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPAtGQVALGPLINARQLDRVH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 381 SYIEIGKSEG-RLLNGGNKtdgNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSS 459
Cdd:cd07152 306 AIVDDSVAAGaRLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISR 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 460 SEERISFALDHMHCGNLYINKKCTGALVGAqPFGGFNMSGTDSKAGGYDYLLLFTQ 515
Cdd:cd07152 383 DVGRAMALADRLRTGMLHINDQTVNDEPHN-PFGGMGASGNGSRFGGPANWEEFTQ 437
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
70-499 |
4.97e-83 |
|
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: 265.07 E-value: 4.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 70 IGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEF 149
Cdd:cd07094 12 IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 150 YAREMIRLSETSIlrPLTKIEGENNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKF 226
Cdd:cd07094 92 AAEEAERIRGEEI--PLDATQGSDNRLAWTirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 227 VELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKvqpgqiwlKRVIAEMGGKDGVVVDE 306
Cdd:cd07094 170 AKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 307 TADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEI 385
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLdEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 386 GKSEGRLLNGGNKTDGNGYYiqPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERIS 465
Cdd:cd07094 322 AVEAGARLLCGGERDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAF 399
|
410 420 430
....*....|....*....|....*....|....
gi 1958218123 466 FALDHMHCGNLYINKKcTGALVGAQPFGGFNMSG 499
Cdd:cd07094 400 KAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
61-499 |
1.48e-82 |
|
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: 263.70 E-value: 1.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNIdQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:cd07099 1 RNPATG-EVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREMIRLSETSILRPLTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAP 220
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELMKEVGLPDGVLNYVPGDGiEVGEYLVEHpKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKD 300
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER------LIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 301 GVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKV 379
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDiGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 380 MSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFS 458
Cdd:cd07099 312 RRHVDDAVAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958218123 459 SSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMSG 499
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
61-510 |
4.19e-81 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 261.55 E-value: 4.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 61 INPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADT 140
Cdd:PLN02278 45 YNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 141 AEAIDFFEFYAREMIRLSETSILRPLTkiegeNNQMTYI--PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADT 218
Cdd:PLN02278 124 AYGASFLEYFAEEAKRVYGDIIPSPFP-----DRRLLVLkqPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 219 APVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGG 298
Cdd:PLN02278 199 TPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT------VKRVSLELGG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 299 KDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFD 377
Cdd:PLN02278 273 NAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFeEGVTQGPLINEAAVQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 378 KVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAY 456
Cdd:PLN02278 353 KVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYI 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 457 FSSSEER---ISFALDhmhCGNLYINkkcTGALVGAQ-PFGGFNMSGT---DSKAGGYDYL 510
Cdd:PLN02278 433 FTRDLQRawrVSEALE---YGIVGVN---EGLISTEVaPFGGVKQSGLgreGSKYGIDEYL 487
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
45-500 |
3.53e-80 |
|
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: 258.53 E-value: 3.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYI-GSEKISTDEKIISI-NPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES-WKQVPAAERADYLVRAAALLRERKHEF 121
Cdd:cd07113 2 HFIdGRPVAGQSEKRLDItNPAT-EQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 122 SSLLVLETGKNWAEA-DADTAEAIDFFEFYAREMIRLSETSILRPLTKIEGENNQMTYI--PLGVGVIISPFNFPLAIMA 198
Cdd:cd07113 81 AQLETLCSGKSIHLSrAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTRrePVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 199 GTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYER 278
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 279 ASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEV 358
Cdd:cd07113 240 AASD------LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 359 GAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAK 436
Cdd:cd07113 314 GSPmDESVMFGPLANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958218123 437 DWQEAIAIYNDTDYGLTGAYFSsseERISFAL---DHMHCGNLYINKKCTgaLVGAQPFGGFNMSGT 500
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWT---NNLSKALryiPRIEAGTVWVNMHTF--LDPAVPFGGMKQSGI 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
45-499 |
1.54e-79 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 257.35 E-value: 1.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKISTDEK--IISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAF-----ESWKQVPAAERADYLVRAAALLRER 117
Cdd:PLN02467 10 LFIGGEWREPVLGkrIPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 118 KHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRL---SETSILRPLTKIEGennqmtYI---PLGVGVIISPFN 191
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALdakQKAPVSLPMETFKG------YVlkePLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 192 FPLaIMAGTTVA-AIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRA 270
Cdd:PLN02467 163 YPL-LMATWKVApALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 271 VGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVT 350
Cdd:PLN02467 242 TGRKIMTAAAQM------VKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 351 SLVSQLEVGAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDG--NGYYIQPTVFADVDPKARIMQEEIF 426
Cdd:PLN02467 316 KWAKNIKISDPlEEGCRLGPVVSEGQYEKVLKFISTAKSEGaTILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 427 GPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEE---RISFALDhmhCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:PLN02467 396 GPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLErceRVSEAFQ---AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
67-499 |
6.38e-79 |
|
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: 254.48 E-value: 6.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 67 DQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDF 146
Cdd:cd07147 9 GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 147 FEFYAREMIRLSETSIlrPLTKIEGENNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIA 223
Cdd:cd07147 89 FRIAAEEATRIYGEVL--PLDISARGEGRQGLVrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 224 AKFVELMKEVGLPDGVLNYVPGDgIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKvqpgqiwlKRVIAEMGGKDGVV 303
Cdd:cd07147 167 LILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--------KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 304 VDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKVMSY 382
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPkDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 383 IEIGKSEG-RLLNGGnKTDGNgyYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSE 461
Cdd:cd07147 318 VNEAVDAGaKLLTGG-KRDGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958218123 462 ERISFALDHMHCGNLYINKKCTgALVGAQPFGGFNMSG 499
Cdd:cd07147 395 EKALRAWDELEVGGVVINDVPT-FRVDHMPYGGVKDSG 431
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
27-512 |
1.63e-77 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 265.30 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 27 AMEHALAKVSKEL-------GREIPLyIGSEkISTDEKIISINPGNIDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVP 99
Cdd:PRK11809 625 ANEHRLASLSSALlasahqkWQAAPM-LEDP-VAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATP 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 100 AAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREmirlsetsilrpltkIEGENNQMTYI 179
Cdd:PRK11809 703 PAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQ---------------VRDDFDNDTHR 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPK 259
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADAR 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 260 TRFISFTGSRAVGcRIYER--ASKVQP-GQ-IWLkrvIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRA 335
Cdd:PRK11809 848 VRGVMFTGSTEVA-RLLQRnlAGRLDPqGRpIPL---IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVL 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 336 IIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEGRL---LNGGNKTD-GNGYYIQPTV 410
Cdd:PRK11809 924 CLQDDVADRTLKMLRGAMAECRMGNPDRlSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDwQSGTFVPPTL 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 411 --FADVDPkariMQEEIFGPVLALAKAKDWQ-----EAIaiyNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCT 483
Cdd:PRK11809 1004 ieLDSFDE----LKREVFGPVLHVVRYNRNQldeliEQI---NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMV 1076
|
490 500 510
....*....|....*....|....*....|.
gi 1958218123 484 GALVGAQPFGGFNMSGTDSKAGG--YDYLLL 512
Cdd:PRK11809 1077 GAVVGVQPFGGEGLSGTGPKAGGplYLYRLL 1107
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
81-499 |
5.36e-77 |
|
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: 248.53 E-value: 5.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLset 160
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 161 siLRP-LTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGV 239
Cdd:cd07100 78 --LADePIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 240 LN--YVPGDGIEvgeYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAI 317
Cdd:cd07100 156 FQnlLIDSDQVE---AIIADPRVRGVTLTGSERAGRAVAAEAGKN------LKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 318 VASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNG 395
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPmDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 396 GNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGN 475
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420
....*....|....*....|....*..
gi 1958218123 476 LYINkkctgALVGAQ---PFGGFNMSG 499
Cdd:cd07100 387 VFIN-----GMVKSDprlPFGGVKRSG 408
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
45-499 |
3.04e-75 |
|
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: 245.44 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSE--KISTDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFS 122
Cdd:cd07117 3 LFINGEwvKGSSGETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 123 SLLVLETGKNWAEADADTA-EAIDFFEFYArEMIRLSETSIlrpltkIEGENNQMTYI---PLGVGVIISPFNFPLAIMA 198
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIpLAADHFRYFA-GVIRAEEGSA------NMIDEDTLSIVlrePIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 199 GTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYER 278
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 279 ASKvqpgqiwlkRVIA---EMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQ 355
Cdd:cd07117 234 AAK---------KLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 356 LEVGAPAE-NYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGN----GYYIQPTVFADVDPKARIMQEEIFGPV 429
Cdd:cd07117 305 VKVGNPLDpDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 430 LALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:cd07117 385 ATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
68-499 |
1.61e-74 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 244.35 E-value: 1.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 68 QIIGKVSKGTSKIVDSAMNVALEAFE--SWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADAD-TAEAI 144
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVdIPAAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 145 DFFEFYAREMirlsetsilrplTKIEGENNQMT-----YI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPA 216
Cdd:PLN02766 127 GLLRYYAGAA------------DKIHGETLKMSrqlqgYTlkePIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 217 DTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqiwLKRVIAEM 296
Cdd:PLN02766 195 EQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN-----LKQVSLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 297 GGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKS 375
Cdd:PLN02766 270 GGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDpRARQGPQVDKQQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 376 FDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTG 454
Cdd:PLN02766 350 FEKILSYIEHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAA 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958218123 455 AYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:PLN02766 430 GIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSG 472
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
60-517 |
8.34e-74 |
|
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: 241.09 E-value: 8.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFE--SWKQVPAAeRADYLVRAAALLRERKHEFSSLLVLETGKNWAEAD 137
Cdd:cd07120 1 SIDPAT-GEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 ADTAEAIDFFEFYARemirLSETSILRPLTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPAD 217
Cdd:cd07120 79 FEISGAISELRYYAG----LARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 218 TAPVIAAKFVELMKEV-GLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEM 296
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT------LKRLGLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 297 GGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVG---APAENypVGPVIDQ 373
Cdd:cd07120 229 GGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGpglDPASD--MGPLIDR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 374 KSFDKVMSYIEIGKSEGR--LLNGGNKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTD 449
Cdd:cd07120 307 ANVDRVDRMVERAIAAGAevVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 450 YGLTGAYFS---SSEERISFALdhmHCGNLYINKKctGALVGAQPFGGFNMSGTdSKAGGYDYLLLFTQGK 517
Cdd:cd07120 387 YGLAASVWTrdlARAMRVARAI---RAGTVWINDW--NKLFAEAEEGGYRQSGL-GRLHGVAALEDFIEYK 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
81-509 |
2.57e-73 |
|
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: 239.10 E-value: 2.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKN-WAEADADTAEA--IDFFEFYAREmiRL 157
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPlWEAQTEVAAMAgkIDISIKAYHE--RT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 158 SETSilrplTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPD 237
Cdd:cd07095 80 GERA-----TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 238 GVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKvQPGQIwlkrvIA-EMGGKDGVVVDETADIDAAAKA 316
Cdd:cd07095 155 GVLNLVQGGR-ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAG-RPGKI-----LAlEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 317 IVASAFGYQGQKCSAGSRAIIVES-VYDQVVEKVTSLVSQLEVGAPAENYP--VGPVIDQKSFDKVMSYIEIGKSEGRLL 393
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPfmGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 394 NGGNKTDGNGYYIQPTVFaDVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHC 473
Cdd:cd07095 308 LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958218123 474 GNLYINKKCTGAlVGAQPFGGFNMSGTDSKAGGY--DY 509
Cdd:cd07095 387 GIVNWNRPTTGA-SSTAPFGGVGLSGNHRPSAYYaaDY 423
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
81-480 |
8.03e-73 |
|
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: 238.30 E-value: 8.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKnwaeADADTAEAIDFFEFYAREMIRLSET 160
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGR----PIAQAGGEIRGMLERARYMISIAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 161 SIL-RPLTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGV 239
Cdd:cd07102 96 ALAdIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 240 LNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIyERASKVQpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVA 319
Cdd:cd07102 176 FQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAI-QRAAAGR-----FIKVGLELGGKDPAYVRPDADLDAAAESLVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 320 SAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGN 397
Cdd:cd07102 249 GAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPlDPSTTLGPVVSARAADFVRAQIADAIAKGaRALIDGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 398 KT---DGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCG 474
Cdd:cd07102 329 LFpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETG 408
|
....*.
gi 1958218123 475 NLYINK 480
Cdd:cd07102 409 TVFMNR 414
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
68-507 |
1.12e-72 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 240.48 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 68 QIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTA-EAI 144
Cdd:PLN02466 84 EVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELpMFA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 145 DFFEFYAREMIRLSETSIlrpltKIEGENN-QMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIA 223
Cdd:PLN02466 164 RLFRYYAGWADKIHGLTV-----PADGPHHvQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 224 AKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqiwLKRVIAEMGGKDGVV 303
Cdd:PLN02466 239 LYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN-----LKPVTLELGGKSPFI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 304 VDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVIDQKSFDKVMSY 382
Cdd:PLN02466 314 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPfKKGVEQGPQIDSEQFEKILRY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 383 IEIG-KSEGRLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSS-- 459
Cdd:PLN02466 394 IKSGvESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQnl 473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958218123 460 -SEERISFALdhmHCGNLYINkkCTGALVGAQPFGGFNMSGTDSKAGGY 507
Cdd:PLN02466 474 dTANTLSRAL---RVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKGIY 517
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
81-499 |
9.92e-72 |
|
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: 234.78 E-value: 9.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSET 160
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 161 SIlrPLTKieGENNQMTY-IPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGV 239
Cdd:cd07105 82 SI--PSDK--PGTLAMVVkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 240 LNYV---PGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKA 316
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK------HLKPVLLELGGKAPAIVLEDADLDAAANA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 317 IVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPaenyPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNG 395
Cdd:cd07105 232 ALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPV----VLGSLVSAAAADRVKELVDDALSKGaKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 396 G-NKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERisfAL---DHM 471
Cdd:cd07105 308 GlADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLAR---ALavaKRI 384
|
410 420 430
....*....|....*....|....*....|.
gi 1958218123 472 HCGNLYINkkctGALVG--AQ-PFGGFNMSG 499
Cdd:cd07105 385 ESGAVHIN----GMTVHdePTlPHGGVKSSG 411
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
60-499 |
4.56e-70 |
|
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: 232.39 E-value: 4.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEAD 137
Cdd:cd07140 25 TINPTD-GSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 AD-TAEAIDFFEFYAREMIRLSETSI----LRPltkiegeNNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGN 209
Cdd:cd07140 104 KThVGMSIQTFRYFAGWCDKIQGKTIpinqARP-------NRNLTLTkrePIGVCGIVIPWNYPLMMLAWKMAACLAAGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 210 TVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqiwL 289
Cdd:cd07140 177 TVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSN-----L 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 290 KRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPV-G 368
Cdd:cd07140 252 KKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDhG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 369 PVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAK--DWQEAIAIY 445
Cdd:cd07140 332 PQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDVDGVLQRA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958218123 446 NDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALvgAQPFGGFNMSG 499
Cdd:cd07140 412 NDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDV--AAPFGGFKQSG 463
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
60-510 |
4.68e-70 |
|
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: 231.90 E-value: 4.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKnwaeaDAD 139
Cdd:cd07111 41 TINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK-----PIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 140 TAEAIDF------FEFYAREMiRLSETSIlrpltkiegennqMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVIL 213
Cdd:cd07111 115 ESRDCDIplvarhFYHHAGWA-QLLDTEL-------------AGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 214 KPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGcRIYERASKvqpGqiWLKRVI 293
Cdd:cd07111 181 KPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVG-RALRRATA---G--TGKKLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 294 AEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVID 372
Cdd:cd07111 254 LELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDkAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 373 QKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYG 451
Cdd:cd07111 334 PAQLKRIRELVEEGRAEGaDVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 452 LTGAYFSsseERISFALD---HMHCGNLYINkkCTGALVGAQPFGGFNMSGTdSKAGG----YDYL 510
Cdd:cd07111 414 LAASVWS---ENLSLALEvalSLKAGVVWIN--GHNLFDAAAGFGGYRESGF-GREGGkeglYEYL 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
56-494 |
6.23e-70 |
|
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: 231.33 E-value: 6.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 56 EKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAE 135
Cdd:cd07130 12 GVVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 136 ADADTAEAIDFFEfYAREMIRLSETSIL---RPltkiegeNNQM--TYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNT 210
Cdd:cd07130 91 GLGEVQEMIDICD-FAVGLSRQLYGLTIpseRP-------GHRMmeQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 211 VILKPADTAPVIAAKFVELMKEV----GLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGS----RAVGCRIYERaskv 282
Cdd:cd07130 163 VVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGStavgRQVGQAVAAR---- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 283 qpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA 362
Cdd:cd07130 238 ------FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 363 E-NYPVGPVIDQKSFDKVMSYIEIGKSE-GRLLNGGNKTDGNGYYIQPTVfADVDPKARIMQEEIFGPVLALAKAKDWQE 440
Cdd:cd07130 312 DdGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEE 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 441 AIAIYNDTDYGLTGAYFSSSEERISFALDHM--HCGNLYINKKCTGALVGAQpFGG 494
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIGGA-FGG 445
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
67-505 |
9.67e-70 |
|
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: 230.32 E-value: 9.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 67 DQIIGKVSKGTSKIVDSAMNVALeAFESwkQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDF 146
Cdd:cd07146 9 GEVVGTVPAGTEEALREALALAA-SYRS--TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 147 FEFYAREMIRLSETSILRPLTKIEGENNQMTYI-PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAK 225
Cdd:cd07146 86 LRFAAAEALRDDGESFSCDLTANGKARKIFTLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 226 FVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASkvqpgqiwLKRVIAEMGGKDGVVVD 305
Cdd:cd07146 166 LADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 306 ETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIE 384
Cdd:cd07146 238 DDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMdPATDMGTVIDEEAAIQIENRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 385 IGKSEGRLLNGGNKTDGNGYYiqPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERI 464
Cdd:cd07146 318 EAIAQGARVLLGNQRQGALYA--PTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTI 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958218123 465 SFALDHMHCGNLYINKKcTGALVGAQPFGGFNMSGTDSKAG 505
Cdd:cd07146 396 KRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
107-510 |
1.38e-69 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 228.85 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 107 LVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYArEMIRLSETSIL---RPltkieGENNQMTYIPLGV 183
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMA-EWARRYEGEIIqsdRP-----GENILLFKRALGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 184 GVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFI 263
Cdd:PRK10090 75 TTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 264 SFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYD 343
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKN------ITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 344 QVVEKVTSLVSQLEVGAPAENYPV--GPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARI 420
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERNDIamGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 421 MQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQpfGGFNMS-- 498
Cdd:PRK10090 309 MHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgi 386
|
410
....*....|...
gi 1958218123 499 -GTDSKAGGYDYL 510
Cdd:PRK10090 387 gGADGKHGLHEYL 399
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
60-499 |
2.98e-69 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 230.17 E-value: 2.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 60 SINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFES--WKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKnwaead 137
Cdd:PRK09847 39 TVDPVT-QAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGK------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 ADTAEAIDFFEFYAREMIRLSETsilrpLTKIEGE-----NNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGN 209
Cdd:PRK09847 112 PIRHSLRDDIPGAARAIRWYAEA-----IDKVYGEvattsSHELAMIvrePVGVIAAIVPWNFPLLLTCWKLGPALAAGN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 210 TVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERAskvqpGQIWL 289
Cdd:PRK09847 187 SVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA-----GDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 290 KRVIAEMGGKDG-VVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPV 367
Cdd:PRK09847 262 KRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDpATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 368 GPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTdGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYND 447
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQLLLDGRNA-GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAND 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958218123 448 TDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALvgAQPFGGFNMSG 499
Cdd:PRK09847 421 SQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSG 470
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-499 |
8.06e-68 |
|
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: 225.27 E-value: 8.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 70 IGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEF 149
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 150 YAREMIRLsetsiLRP---------LTKIEgennqMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAP 220
Cdd:cd07101 89 YARRAERL-----LKPrrrrgaipvLTRTT-----VNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHpkTRFISFTGSRAVGCRIYERASkvqpgqiwlKRVI---AEMG 297
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG---------RRLIgcsLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 298 GKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSF 376
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDyGPDMGSLISQAQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 377 DKVMSYIEIGKSEG-RLLNGGN-KTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTG 454
Cdd:cd07101 308 DRVTAHVDDAVAKGaTVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958218123 455 AYFSSSEERISFALDHMHCGNLYINKKCTGAL--VGAqPFGGFNMSG 499
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNEGYAAAWasIDA-PMGGMKDSG 433
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
62-521 |
3.05e-66 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 222.06 E-value: 3.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 62 NPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTA 141
Cdd:TIGR01722 22 NPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 142 EAIDFFEFYAremirlSETSILRPLTKIEGENNQMTY---IPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADT 218
Cdd:TIGR01722 101 RGLEVVEHAC------GVNSLLKGETSTQVATRVDVYsirQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 219 APVIAAKFVELMKEVGLPDGVLNYVPGDGIEVgEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqiwlKRVIAEMGG 298
Cdd:TIGR01722 175 VPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG------KRVQALGGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 299 KDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVyDQVVEKVTSLVSQLEVGA---PAENYpvGPVIDQKS 375
Cdd:TIGR01722 248 KNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPgddPGAEM--GPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 376 FDKVMSYIEIGKSEGR--LLNG-GNKTDG--NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDY 450
Cdd:TIGR01722 325 KDRVASLIAGGAAEGAevLLDGrGYKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPY 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 451 GLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALvGAQPFGGFNMS-GTDSKAGGYDYLLLFTQGK-LTSR 521
Cdd:TIGR01722 405 GNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPL-PYFSFTGWKDSfFGDHHIYGKQGTHFYTRGKtVTTR 476
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
163-505 |
2.77e-63 |
|
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: 213.70 E-value: 2.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 163 LRPLTKIEGEN-----NQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEV---- 233
Cdd:cd07098 98 LRPESRPGGLLmfykrARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaac 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 234 GLPDGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAA 313
Cdd:cd07098 178 GHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES------LTPVVLELGGKDPAIVLDDADLDQI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 314 AKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEIGKSEG-R 391
Cdd:cd07098 251 ASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLdGDVDVGAMISPARFDRLEELVADAVEKGaR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 392 LLNGGNK----TDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFA 467
Cdd:cd07098 331 LLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRI 410
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958218123 468 LDHMHCGNLYINKKCTGALVGAQPFGGFNMSGTDSKAG 505
Cdd:cd07098 411 ASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
70-499 |
1.51e-62 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 213.20 E-value: 1.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 70 IGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAeadadtaeaiDFFE- 148
Cdd:PRK09407 45 LATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR----------HAFEe 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 149 ---------FYAREMIRLsetsiLRP---------LTKIEgennqMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNT 210
Cdd:PRK09407 115 vldvaltarYYARRAPKL-----LAPrrragalpvLTKTT-----ELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 211 VILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHpkTRFISFTGSRAVGCRIYERASkvqpgqiwlK 290
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG---------R 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 291 RVI---AEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYP 366
Cdd:PRK09407 254 RLIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDySAD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 367 VGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGN-KTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAI 444
Cdd:PRK09407 334 MGSLISEAQLETVSAHVDDAVAKGaTVLAGGKaRPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVER 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958218123 445 YNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGAL--VGAqPFGGFNMSG 499
Cdd:PRK09407 414 ANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWgsVDA-PMGGMKDSG 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
62-510 |
1.56e-62 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 212.07 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 62 NPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTA 141
Cdd:PRK11241 32 NPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 142 EAIDFFEFYAREMIRLSETSIlrpltkiEGENNQMTYI----PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPAD 217
Cdd:PRK11241 111 YAASFIEWFAEEGKRIYGDTI-------PGHQADKRLIvikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 218 TAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMG 297
Cdd:PRK11241 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD------IKKVSLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 298 GKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVG-APAENYPVGPVIDQKSF 376
Cdd:PRK11241 258 GNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGdGLEKGVTIGPLIDEKAV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 377 DKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGA 455
Cdd:PRK11241 338 AKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAY 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958218123 456 YFSSSEERISFALDHMHCGNLYINkkcTGALVG-AQPFGGFNMSG---TDSKAGGYDYL 510
Cdd:PRK11241 418 FYARDLSRVFRVGEALEYGIVGIN---TGIISNeVAPFGGIKASGlgrEGSKYGIEDYL 473
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
68-499 |
6.41e-61 |
|
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: 207.69 E-value: 6.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 68 QIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTA-EAIDF 146
Cdd:cd07116 27 KVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIpLAIDH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 147 FEFYArEMIRLSETSIlrplTKIEGEN-NQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAK 225
Cdd:cd07116 107 FRYFA-GCIRAQEGSI----SEIDENTvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 226 FVELMKEVgLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGK------ 299
Cdd:cd07116 182 LMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN------IIPVTLELGGKspniff 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 300 DGVVVDETADIDAAAKAIVASAFGyQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE-NYPVGPVIDQKSFDK 378
Cdd:cd07116 255 ADVMDADDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDtETMIGAQASLEQLEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 379 VMSYIEIGKSEG-RLLNGGNKT----DGNGYYIQPTVFADVDpKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLT 453
Cdd:cd07116 334 ILSYIDIGKEEGaEVLTGGERNelggLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958218123 454 GAYFSSSEERISFALDHMHCGNLYINkkCTGALVGAQPFGGFNMSG 499
Cdd:cd07116 413 AGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
48-503 |
3.50e-60 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 206.15 E-value: 3.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 48 GSEKISTDEKIISI-NPGNIdQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLV 126
Cdd:PLN00412 22 GEWRTSSSGKSVAItNPSTR-KTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 127 LETGKNWAEADADTAEAIDFFEFYAREMIR-LSETSILRPLTKIEGENNQM---TYIPLGVGVIISPFNFPLAIMAGTTV 202
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAEEGVRiLGEGKFLVSDSFPGNERNKYcltSKIPLGVVLAIPPFNYPVNLAVSKIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 203 AAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAvGCRIYERASKV 282
Cdd:PLN00412 181 PALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDT-GIAISKKAGMV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 283 qPGQIwlkrviaEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA 362
Cdd:PLN00412 260 -PLQM-------ELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 363 ENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGNgyYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAI 442
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN--LIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGI 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958218123 443 AIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINkkcTGALVGAQ--PFGGFNMSGTDSK 503
Cdd:PLN00412 410 HHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN---SAPARGPDhfPFQGLKDSGIGSQ 469
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
45-499 |
1.55e-59 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 204.42 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 45 LYIGSEKIS-TDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSS 123
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 124 LLVLETGKN-WAEADADTAEA----IDFFEFYAREMIRLSE----TSILRpltkiegennqmtYIPLGVGVIISPFNFPL 194
Cdd:PRK09457 82 VIARETGKPlWEAATEVTAMInkiaISIQAYHERTGEKRSEmadgAAVLR-------------HRPHGVVAVFGPYNFPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 195 AIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGdGIEVGEYLVEHPKTRFISFTGSRAVGCR 274
Cdd:PRK09457 149 HLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 275 IYERASKvQPGQIwlkrVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVY-DQVVEKVTSLV 353
Cdd:PRK09457 228 LHRQFAG-QPEKI----LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 354 SQLEVGAP-AENYP-VGPVIDQKSFDKVMsyieigKSEGRLLNGGNKT-------DGNGYYIQPTVFaDVDPKARIMQEE 424
Cdd:PRK09457 303 KRLTVGRWdAEPQPfMGAVISEQAAQGLV------AAQAQLLALGGKSllemtqlQAGTGLLTPGII-DVTGVAELPDEE 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958218123 425 IFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGAlVGAQPFGGFNMSG 499
Cdd:PRK09457 376 YFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
52-499 |
6.72e-58 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 199.32 E-value: 6.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 52 ISTDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGK 131
Cdd:PRK13968 3 ITPATHAISVNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 132 NWAEADADTAEAIDFFEFYARE---MIRLSETSIlrpltkiegENNQ--MTYIPLGVGVIISPFNFPL-AIMAGTtVAAI 205
Cdd:PRK13968 82 PINQARAEVAKSANLCDWYAEHgpaMLKAEPTLV---------ENQQavIEYRPLGTILAIMPWNFPLwQVMRGA-VPIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 206 VSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEyLVEHPKTRFISFTGSRAVGCRIYERASKVqpg 285
Cdd:PRK13968 152 LAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAA--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 286 qiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP--AE 363
Cdd:PRK13968 228 ---LKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrdEE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 364 NYpVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAI 442
Cdd:PRK13968 305 NA-LGPMARFDLRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHAL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 443 AIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKC-TGALVGaqpFGGFNMSG 499
Cdd:PRK13968 384 ELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCaSDARVA---FGGVKKSG 438
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
81-499 |
1.56e-55 |
|
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: 193.02 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAF---ESWkqVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRL 157
Cdd:cd07148 23 IDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 158 SETSILRPLTkiEGENNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVG 234
Cdd:cd07148 101 GGREIPMGLT--PASAGRIAFTtrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 235 LPDGVLNYVPGDgIEVGEYLVEHPKTRFISFTGSRAVGCRIyerASKVQPGqiwlKRVIAEMGGKDGVVVDETADIDAAA 314
Cdd:cd07148 179 LPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWML---RSKLAPG----TRCALEHGGAAPVIVDRSADLDAMI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 315 KAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSYIEIGKSEG-RL 392
Cdd:cd07148 251 PPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTdPDTEVGPLIRPREVDRVEEWVNEAVAAGaRL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 393 LNGGNKTDGNGYyiQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSsseERISFALD--- 469
Cdd:cd07148 331 LCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT---KDLDVALKavr 405
|
410 420 430
....*....|....*....|....*....|
gi 1958218123 470 HMHCGNLYINKKcTGALVGAQPFGGFNMSG 499
Cdd:cd07148 406 RLDATAVMVNDH-TAFRVDWMPFAGRRQSG 434
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
58-499 |
4.31e-51 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 181.09 E-value: 4.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 58 IISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEAD 137
Cdd:PRK09406 3 IATINPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 138 ADTAEAIDFFEFYAR--EMIRLSETSILRpltKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKP 215
Cdd:PRK09406 82 AEALKCAKGFRYYAEhaEALLADEPADAA---AVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 216 ADTAPVIAAKFVELMKEVGLPDGVLN--YVPGDGIEVgeyLVEHPKTRFISFTGSRAVGcriyeRASKVQPGQIwLKRVI 293
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQtlLVGSGAVEA---ILRDPRVAAATLTGSEPAG-----RAVAAIAGDE-IKKTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 294 AEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAP-AENYPVGPVID 372
Cdd:PRK09406 230 LELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPtDPDTDVGPLAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 373 QKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYG 451
Cdd:PRK09406 310 EQGRDEVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 452 LTG-AYFSSSEERISFALDhMHCGNLYINkkctGALVG--AQPFGGFNMSG 499
Cdd:PRK09406 390 LGSnAWTRDEAEQERFIDD-LEAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
46-505 |
8.52e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.49 E-value: 8.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 46 YIGSEKISTDEKIISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLL 125
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 126 VLETGKNWAEADADTAEAIDFFEfYAREMIRLSETSIL---RPltkiegeNNQMTYI--PLGVGVIISPFNFPLAIMAGT 200
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCD-FAVGLSRQLNGSIIpseRP-------NHMMMEVwnPLGIVGVITAFNFPCAVLGWN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 201 TVAAIVSGNTVILKPADTAPVIAAKFVELMKEV----GLPDGVLNYVPGdGIEVGEYLVEHPKTRFISFTGSRAVG---- 272
Cdd:PLN02315 175 ACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGlmvq 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 273 CRIYERASKVqpgqiwlkrvIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSL 352
Cdd:PLN02315 254 QTVNARFGKC----------LLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 353 VSQLEVGAPAENYP-VGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGYYIQPTVfADVDPKARIMQEEIFGPVL 430
Cdd:PLN02315 324 YKQVKIGDPLEKGTlLGPLHTPESKKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958218123 431 ALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERIsFALDHMH---CGNLYINKKCTGALVGAqPFGGFNMSGTDSKAG 505
Cdd:PLN02315 403 YVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETI-FKWIGPLgsdCGIVNVNIPTNGAEIGG-AFGGEKATGGGREAG 478
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
179-514 |
3.46e-46 |
|
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: 167.01 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 179 IPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEvGLPDGVLNYVPGdGIEVGEYLVEHp 258
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAFQVVQG-GVPETTALLEQ- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 259 KTRFISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIV 338
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAK------HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 339 ESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEigKSEGRLLNGGnKTDGNGYYIQPTVFADVDPKA 418
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD--TTKGKVVIGG-EMDEATRFIPPTIVSDVSWDD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 419 RIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMS 498
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDS 414
|
330
....*....|....*.
gi 1958218123 499 GTDSKaGGYDYLLLFT 514
Cdd:cd07135 415 GYGAY-HGKYGFDTFT 429
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
90-499 |
7.54e-46 |
|
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: 165.78 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 90 EAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNwaeadadtaeaiDFFEFYAREMIRLSETS-ILRPLTK 168
Cdd:cd07087 9 ETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKP------------PAEAYLTEIAVVLGEIDhALKHLKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 169 ------------IEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVgLP 236
Cdd:cd07087 77 wmkprrvsvpllLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 237 DGVLNYVPGDGiEVGEYLVEHPktrF--ISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAA 314
Cdd:cd07087 156 PEAVAVVEGGV-EVATALLAEP---FdhIFFTGSPAVGKIVMEAAAK------HLTPVTLELGGKSPCIVDKDANLEVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 315 KAIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEigksEGRLLN 394
Cdd:cd07087 226 RRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD----DGKVVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 395 GGnKTDGNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCG 474
Cdd:cd07087 302 GG-QVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSG 380
|
410 420
....*....|....*....|....*
gi 1958218123 475 NLYINKKCTGALVGAQPFGGFNMSG 499
Cdd:cd07087 381 GVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
43-460 |
3.70e-45 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 167.62 E-value: 3.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 43 IPLYIGSEKISTDEK--IISINPGNiDQIIGKVSKGTSKIVDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHE 120
Cdd:PLN02419 114 VPNLIGGSFVESQSSsfIDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 121 FSSLLVLETGKNWAEADADTAEAIDFFEfYAREMIRLSETSILRPLTKieGENNQMTYIPLGVGVIISPFNFPLAIMAGT 200
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVE-HACGMATLQMGEYLPNVSN--GVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 201 TVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEyLVEHPKTRFISFTGSRAVGCRIYERAS 280
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 281 KVQpgqiwlKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGSRAIIV---ESVYDQVVEKVTSLvsQLE 357
Cdd:PLN02419 349 AKG------KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVgdaKSWEDKLVERAKAL--KVT 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 358 VGAPAENyPVGPVIDQKSFDKVMSYIEIGKSEG-RLLNGGNKTDGNGY----YIQPTVFADVDPKARIMQEEIFGPVLAL 432
Cdd:PLN02419 421 CGSEPDA-DLGPVISKQAKERICRLIQSGVDDGaKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVC 499
|
410 420
....*....|....*....|....*...
gi 1958218123 433 AKAKDWQEAIAIYNDTDYGLTGAYFSSS 460
Cdd:PLN02419 500 MQANSFDEAISIINKNKYGNGAAIFTSS 527
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
165-507 |
3.78e-45 |
|
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: 164.32 E-value: 3.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 165 PLTkIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVlNYVP 244
Cdd:cd07134 86 PLL-LFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 245 GDgIEVGEYLVEHPktrF--ISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAF 322
Cdd:cd07134 164 GD-AEVAQALLELP---FdhIFFTGSPAVGKIVMAAAAKH------LASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 323 GYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQL--EVGAPAENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTD 400
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 401 GNGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINK 480
Cdd:cd07134 314 AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVND 393
|
330 340
....*....|....*....|....*..
gi 1958218123 481 KCTGALVGAQPFGGFNMSGTdSKAGGY 507
Cdd:cd07134 394 VVLHFLNPNLPFGGVNNSGI-GSYHGV 419
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
178-499 |
6.80e-38 |
|
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: 144.57 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 178 YIPLGVGVIISPFNFP--LAIMAgtTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGdGIEVGEYLV 255
Cdd:cd07136 98 YEPYGVVLIIAPWNYPfqLALAP--LIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 256 EhpkTRF--ISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAGS 333
Cdd:cd07136 174 D---QKFdyIFFTGSVRVGKIVMEAAAK------HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 334 RAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEIGKsegrLLNGGNkTDGNGYYIQPTVFAD 413
Cdd:cd07136 245 YVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK----IVFGGN-TDRETLYIEPTILDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 414 VDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDH------------MHCGNLYInkk 481
Cdd:cd07136 320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENlsfgggcindtiMHLANPYL--- 396
|
330
....*....|....*...
gi 1958218123 482 ctgalvgaqPFGGFNMSG 499
Cdd:cd07136 397 ---------PFGGVGNSG 405
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
180-499 |
1.66e-37 |
|
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: 143.52 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAakfvELMKEVgLPdgvlNYVPGD-------GIEVGE 252
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAEL-IP----KYLDKEcypvvlgGVEETT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 253 YLVEHpktRF--ISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCS 330
Cdd:cd07132 171 ELLKQ---RFdyIFYTGSTSVGKIVMQAAAK------HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 331 AGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEigksEGRLLNGGNkTDGNGYYIQPTV 410
Cdd:cd07132 242 APDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS----GGKVAIGGQ-TDEKERYIAPTV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 411 FADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQ 490
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSL 396
|
....*....
gi 1958218123 491 PFGGFNMSG 499
Cdd:cd07132 397 PFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
180-499 |
1.25e-36 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 141.70 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAakfvELMKEVglpdgVLNYVPGD-------GIEVGE 252
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS----KLMAKL-----LTKYLDPSyvrviegGVEVTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 253 YLVEHPkTRFISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSAG 332
Cdd:PTZ00381 180 ELLKEP-FDHIFFTGSPRVGKLVMQAAAE------NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 333 SRAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEigKSEGRLLNGGnKTDGNGYYIQPTVFA 412
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK--DHGGKVVYGG-EVDIENKYVAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 413 DVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPF 492
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPF 409
|
....*..
gi 1958218123 493 GGFNMSG 499
Cdd:PTZ00381 410 GGVGNSG 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
180-509 |
7.09e-32 |
|
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: 127.53 E-value: 7.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGdGIEVGEYLVEHpK 259
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 260 TRFISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGY-QGQKCSAGSRAIIV 338
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAK------HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 339 ESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKTDGNgYYIQPTVFADVDPKA 418
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKN-LYIEPTILLDPPLDS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 419 RIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMS 498
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGES 410
|
330
....*....|.
gi 1958218123 499 GTDSKAGGYDY 509
Cdd:cd07137 411 GFGAYHGKFSF 421
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
174-499 |
4.36e-31 |
|
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: 124.90 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 174 NQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDGVLnyVPGDGIEVGEY 253
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA--VVTGGADVAAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 254 LVEHPktrF--ISFTGSRAVGCRIYERASKVqpgqiwLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGYQGQKCSA 331
Cdd:cd07133 173 FSSLP---FdhLLFTGSTAVGRHVMRAAAEN------LTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 332 GSRAIIVESVYDQVVEKVTSLVSQLevgapaenYPVGP-------VIDQKSFDKVMSYIEIGKSEG-RL--LNGGNKTDG 401
Cdd:cd07133 244 PDYVLVPEDKLEEFVAAAKAAVAKM--------YPTLAdnpdytsIINERHYARLQGLLEDARAKGaRVieLNPAGEDFA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 402 NGYYIQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKK 481
Cdd:cd07133 316 ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT 395
|
330
....*....|....*...
gi 1958218123 482 CTGALVGAQPFGGFNMSG 499
Cdd:cd07133 396 LLHVAQDDLPFGGVGASG 413
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
81-508 |
1.01e-30 |
|
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: 124.27 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAeaiDFFEFYAREMIRLS-- 158
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICG---DQVQLRARAFVIYSyr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 159 -ETSILRPLTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVG-LP 236
Cdd:cd07084 78 iPHEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 237 DGVLNYVPGDGiEVGEYLVEHPKTRFISFTGSRAVGcriyeRASKVQPGQIwlkRVIAEMGGKDGVVVDETADIDAAAKA 316
Cdd:cd07084 158 PEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVA-----EKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 317 I-VASAFGYQGQKCSAGSRAIIVESVYDQ-VVEKVTSLVSQLEVGAPAenypVGPVIdqkSFDKVMSYIEIGKSEGRLLN 394
Cdd:cd07084 229 QcVQDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLL----LGPVQ---TFTTLAMIAHMENLLGSVLL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 395 GGNKTDGN-------GYYIQPTVFADVDP---KARIMQEEIFGPVLALAKAKDWQEAIAI-YNDTDYG-LTGAYFSSSEE 462
Cdd:cd07084 302 FSGKELKNhsipsiyGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLALVLeLLERMHGsLTAAIYSNDPI 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958218123 463 RIS-FALDHMHCGNLY-INKKCTGALVGAQPFGGFNMSGTDSKAGGYD 508
Cdd:cd07084 382 FLQeLIGNLWVAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPE 429
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
180-509 |
2.00e-23 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 103.27 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPViAAKFveLMKEVG--LPDGVLNYVPGdGIEVGEYLVEH 257
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPA-TSAF--LAANIPkyLDSKAVKVIEG-GPAVGEQLLQH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 258 PKTRfISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFGY----QGQKCSAGS 333
Cdd:PLN02203 184 KWDK-IFFTGSPRVGRIIMTAAAK------HLTPVALELGGKCPCIVDSLSSSRDTKVAVNRIVGGKwgscAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 334 RAIIVESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNkTDGNGYYIQPTVFAD 413
Cdd:PLN02203 257 YVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGS-IDEKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 414 VDPKARIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFG 493
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFG 415
|
330
....*....|....*.
gi 1958218123 494 GFNMSGTDSKAGGYDY 509
Cdd:PLN02203 416 GVGESGFGRYHGKYSF 431
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
180-509 |
3.20e-22 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 99.74 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 180 PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVgLPDGVLNYVPGDGIEVGEYLVEhpK 259
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 260 TRFISFTGSRAVGCRIYERASKvqpgqiWLKRVIAEMGGKDGVVVDETADIDAAAKAIVASAFG-YQGQKCSAGSRAIIV 338
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAK------HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 339 ESVYDQVVEKVTSLVSQLEVGAPAENYPVGPVIDQKSFDKVMSYIEIGKSEGRLLNGGNKtDGNGYYIQPTVFADVDPKA 418
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEK-DRENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 419 RIMQEEIFGPVLALAKAKDWQEAIAIYNDTDYGLTGAYFSSSEERISFALDHMHCGNLYINKKCTGALVGAQPFGGFNMS 498
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGES 421
|
330
....*....|.
gi 1958218123 499 GTDSKAGGYDY 509
Cdd:PLN02174 422 GMGAYHGKFSF 432
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
81-304 |
1.48e-21 |
|
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: 97.23 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGknwaeadadtaeaidffefyaremirlset 160
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 161 siLrPLTKIEGE----NNQM----------------------------------TYIPLGVGVIISPFNFPLA--IMAGT 200
Cdd:cd07129 51 --L-PEARLQGElgrtTGQLrlfadlvregswldaridpadpdrqplprpdlrrMLVPLGPVAVFGASNFPLAfsVAGGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 201 TVAAIVSGNTVILK--PA--DTAPVIAAKFVELMKEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIY 276
Cdd:cd07129 128 TASALAAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALF 207
|
250 260
....*....|....*....|....*....
gi 1958218123 277 ERASK-VQPgqiwlKRVIAEMGGKDGVVV 304
Cdd:cd07129 208 DAAAArPEP-----IPFYAELGSVNPVFI 231
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
101-444 |
3.02e-19 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 90.92 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 101 AERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAEAIDFFEFYAREMIRLSETSILRpltkiEGENNQMTYIP 180
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLR-----DGEAVQLGKDP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 181 L-----------GVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVG-LPDGVLNYVPGDGI 248
Cdd:PRK11903 138 AfqgqhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 249 EvgeyLVEHPKT-RFISFTGSRAVGCRIYERASKVQ----------------------PG----QIWLKRVIAEMGGKdg 301
Cdd:PRK11903 218 G----LLDHLQPfDVVSFTGSAETAAVLRSHPAVVQrsvrvnveadslnsallgpdaaPGseafDLFVKEVVREMTVK-- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 302 vvvdetadidaaakaivasafgyQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVM 380
Cdd:PRK11903 292 -----------------------SGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRnDGVRMGPLVSRAQLAAVR 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958218123 381 SYIEIGKSEGRLLNGGNKT------DGNGYYIQPTVF--ADVDPKARIMQEEIFGPVLALAKAKDWQEAIAI 444
Cdd:PRK11903 349 AGLAALRAQAEVLFDGGGFalvdadPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALAL 420
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
146-485 |
2.89e-18 |
|
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: 87.55 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 146 FFEFYAREMIRLSETSILRPlTKIEGENNQMTYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAK 225
Cdd:cd07126 109 FLENFAGDQVRFLARSFNVP-GDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 226 FVELMKEVGLPDGVLNYVPGDGIEVGEYLVEhPKTRFISFTGSRavgcRIYERASKVQPGQIWLkrviaEMGGKDGVVVD 305
Cdd:cd07126 188 FLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSS----KVAERLALELHGKVKL-----EDAGFDWKILG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 306 -ETADIDAAAKAIVASAFGYQGQKCSAGSRAIIVESVYDQ-VVEKVTSLVSQLEVgapaENYPVGPVI---DQKSFDKVM 380
Cdd:cd07126 258 pDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQRKL----EDLTIGPVLtwtTERILDHVD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 381 SYIEIGKSE----GRLLNGGNKTDGNGYYiQPT-VFADVDPKA-----RIMQEEIFGPVLALAKAKDWQE--AIAIYNDT 448
Cdd:cd07126 334 KLLAIPGAKvlfgGKPLTNHSIPSIYGAY-EPTaVFVPLEEIAieenfELVTTEVFGPFQVVTEYKDEQLplVLEALERM 412
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958218123 449 DYGLTGAYFSSSEERISFALDHMHCGNLY--INKKCTGA 485
Cdd:cd07126 413 HAHLTAAVVSNDIRFLQEVLANTVNGTTYagIRARTTGA 451
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
101-444 |
6.18e-18 |
|
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: 86.55 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 101 AERADYLVRAAALLRERKHEFSSLlVLETGKNWAEADADTAEAIDFFEFYA----REMIR---LSETSILrPLTKIEGEN 173
Cdd:cd07128 59 HERAAMLKALAKYLMERKEDLYAL-SAATGATRRDSWIDIDGGIGTLFAYAslgrRELPNahfLVEGDVE-PLSKDGTFV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 174 NQMTYIPL-GVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPA-DTAPViAAKFVELMKEVG-LPDGVLNYVPGDgieV 250
Cdd:cd07128 137 GQHILTPRrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPAtATAYL-TEAVVKDIVESGlLPEGALQLICGS---V 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 251 GEyLVEHPKTR-FISFTGSRAVGCRI--------------YERAS--------KVQPGQ----IWLKRVIAEMGGKdgvv 303
Cdd:cd07128 213 GD-LLDHLGEQdVVAFTGSAATAAKLrahpnivarsirfnAEADSlnaailgpDATPGTpefdLFVKEVAREMTVK---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 304 vdetadidaaakaivasafgyQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPA-ENYPVGPVIDQKSFDKVMSY 382
Cdd:cd07128 288 ---------------------AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRlEGVRMGPLVSREQREDVRAA 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958218123 383 IEIGKSEGRLLNGGNKTD-------GNGYYIQPTVF--ADVDPKARIMQEEIFGPVLALAKAKDWQEAIAI 444
Cdd:cd07128 347 VATLLAEAEVVFGGPDRFevvgadaEKGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIEL 417
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
83-331 |
7.05e-12 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 67.89 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 83 SAMNVALEAfesWKQVPAAERADYLVRAAALLRERKHEFSSLLVLETGKNWAEADADTAE-----AIDFFEFYAREMIRL 157
Cdd:cd07127 91 AAARAAMPG---WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQAGGPhaqdrGLEAVAYAWREMSRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 158 SETSILrplTKIEGENNQM------TYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMK 231
Cdd:cd07127 168 PPTAEW---EKPQGKHDPLamektfTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVAR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 232 EV----GL-PDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIYERASKVQpgqiwlkrVIAEMGGKDGVVVDE 306
Cdd:cd07127 245 EVlaeaGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDS 316
|
250 260
....*....|....*....|....*
gi 1958218123 307 TADIDAAAKAIVASAFGYQGQKCSA 331
Cdd:cd07127 317 TDDLKAMLRNLAFSLSLYSGQMCTT 341
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
158-482 |
1.86e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 65.71 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 158 SETSILRPLTKIEGENNQMTYiPLGVGVIISPFNFPLAimaGTTVA--AIVSGNTVILKPADTAPVIAAKFVELMKEV-- 233
Cdd:cd07077 79 SVGHIQDVLLPDNGETYVRAF-PIGVTMHILPSTNPLS---GITSAlrGIATRNQCIFRPHPSAPFTNRALALLFQAAda 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 234 -GLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVgcriYERASKVQPGqiwlKRVIAEMGGKDGVVVDETADIDA 312
Cdd:cd07077 155 aHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA----VDAAVKHSPH----IPVIGFGAGNSPVVVDETADEER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 313 AAKAIVASAFgYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAENypvgpvidqksfdKVMSYieigksegrl 392
Cdd:cd07077 227 ASGSVHDSKF-FDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQET-------------KPLSK---------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 393 lnggnktdgngyyiqpTVFADVDPKARimqeEIFGPVLALAKAKDW----QEAIAIYNDTDYGLTGAYFSSSEERISFAL 468
Cdd:cd07077 283 ----------------ETTPSFDDEAL----ESMTPLECQFRVLDVisavENAWMIIESGGGPHTRCVYTHKINKVDDFV 342
|
330
....*....|....
gi 1958218123 469 DHMHCGNLYINKKC 482
Cdd:cd07077 343 QYIDTASFYPNESS 356
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
84-488 |
1.48e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 56.89 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 84 AMNVALEAFESWKQvpaaERADYLVRAAALLRER-KHEFSSLLVLETGKNWAEADADTaeaidffEFYAREMIRLSETSI 162
Cdd:cd07081 7 AAKVAQQGLSCKSQ----EMVDLIFRAAAEAAEDaRIDLAKLAVSETGMGRVEDKVIK-------NHFAAEYIYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 163 LRPLTkIEGENNQMTYI---PLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKP---ADTAPVIAAKFV-ELMKEVGL 235
Cdd:cd07081 76 KTCGV-LTGDENGGTLIiaePIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATLLlQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 236 PDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVgcriyeraskVQPGQIWLKRVIAEMGGKDGVVVDETADIDAAAK 315
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAV----------VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 316 AIVASAFGYQGQKCSAGSRAIIVESVYDQVVEKVTSLVSQLEVGAPAE--------NYPVGPVIDQKSFDKVMSYIEIG- 386
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQqvqpvilkNGDVNRDIVGQDAYKIAAAAGLKv 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 387 KSEGRLLNGgnktdgngyyiQPTVFADVDPKArimqEEIFGPVLALAKAKDWQE----AIAIYNDTDYGLTGAYFSSSE- 461
Cdd:cd07081 305 PQETRILIG-----------EVTSLAEHEPFA----HEKLSPVLAMYRAANFADadakALALKLEGGCGHTSAMYSDNIk 369
|
410 420
....*....|....*....|....*....
gi 1958218123 462 --ERISFALDHMHCGNLYINKKCTGALVG 488
Cdd:cd07081 370 aiENMNQFANAMKTSRFVKNGPCSQGGLG 398
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
81-443 |
2.08e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 56.48 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYL--VRAAAllRERKHEFSSLLVLETG---------KNWAEADadtaeaidffef 149
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIeaIREAL--LSNAEELAEMAVEETGmgrvedkiaKNHLAAE------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 150 yaremiRLSETSILRPlTKIEGENNqMT---YIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKF 226
Cdd:cd07121 72 ------KTPGTEDLTT-TAWSGDNG-LTlveYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 227 VELM----KEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVGCRIyeRASKvqpgqiwlKRVIAEMGGKDGV 302
Cdd:cd07121 144 VELInkaiAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAA--LSSG--------KKAIGAGAGNPPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 303 VVDETADIDAAAKAIvasafgYQGQK------CSAGSRAIIVESVYDQVVEKVTS----LVSQLEVGAPAEN---YPVGP 369
Cdd:cd07121 214 VVDETADIEKAARDI------VQGASfdnnlpCIAEKEVIAVDSVADYLIAAMQRngayVLNDEQAEQLLEVvllTNKGA 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958218123 370 VIDQKSfdkvmsyieIGKSEGRLLNGGNKTDGNGyyiQPTVFADVDPKARIMQEEIFGPVLALAKAKDWQEAIA 443
Cdd:cd07121 288 TPNKKW---------VGKDASKILKAAGIEVPAD---IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
81-443 |
1.16e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 51.06 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 81 VDSAMNVALEAFESWKQVPAAERADYL--VRAAAllRERKHEFSSLLVLETG---------KNwaeadadtaeaidffef 149
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIdaIREAL--LPHAEELAELAVEETGmgrvedkiaKN----------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 150 yaREMIRLSE-TSILRP--------LTKIEgennqmtYIPLGVGVIISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAP 220
Cdd:PRK15398 99 --VAAAEKTPgVEDLTTealtgdngLTLIE-------YAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 221 VIAAKFVELM----KEVGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGSRAVgcriyeraskVQPGQIWLKRVIAEM 296
Cdd:PRK15398 170 KVSLRAIELLneaiVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAV----------VKAAMKSGKKAIGAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 297 GGKDGVVVDETADIDAAAKAIvasafgYQGQK------CSAGSRAIIVESVYDQ----------------VVEKVTSLVS 354
Cdd:PRK15398 240 AGNPPVVVDETADIEKAARDI------VKGASfdnnlpCIAEKEVIVVDSVADElmrlmekngavlltaeQAEKLQKVVL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 355 QlEVGAPaenypvgpvidQKSFdkvmsyieIGKSEGRLLNG-GNKTDGNgyyiQPTVFADVDPKARIMQEEIFGPVLALA 433
Cdd:PRK15398 314 K-NGGTV-----------NKKW--------VGKDAAKILEAaGINVPKD----TRLLIVETDANHPFVVTELMMPVLPVV 369
|
410
....*....|
gi 1958218123 434 KAKDWQEAIA 443
Cdd:PRK15398 370 RVKDVDEAIA 379
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
80-268 |
2.03e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.18 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 80 IVDSAmNVALEAFESWKQvpaaERADYLVRAAALLRERKHEF-SSLLVLETG---------KNwaeadadtaeaidFF-- 147
Cdd:cd07122 4 LVERA-RKAQREFATFSQ----EQVDKIVEAVAWAAADAAEElAKMAVEETGmgvvedkviKN-------------HFas 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958218123 148 EFYAREMIRLSETSILRpltkiEGENNQMTYIPLGVGVI--ISPFNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAK 225
Cdd:cd07122 66 EYVYNDIKDMKTVGVIE-----EDEEKGIVEIAEPVGVIaaLIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIE 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958218123 226 FVELMKE----VGLPDGVLNYVPGDGIEVGEYLVEHPKTRFISFTGS 268
Cdd:cd07122 141 AAKIMREaavaAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG 187
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
168-238 |
4.49e-03 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 39.45 E-value: 4.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958218123 168 KIEGENNQMTYIPLGVGVIIS-P----FNFPLAIMAGTTVAAIVSGNTVILKPADTAPVIAAKFVELMKEVGLPDG 238
Cdd:cd08190 292 RPPGYPVDHPHVPHGLSVALTaPavfrFTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNG 367
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