|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-490 |
0e+00 |
|
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: 756.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSA 198
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 199 LALAILAERAGIPDGLFSVLPTDNArMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDA 278
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPA-EIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 279 DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAV 358
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 359 TKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWK 438
Cdd:cd07103 320 AKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 439 VTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07103 400 VAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-494 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 709.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 7 LLGRLKDQTLVREQMLVGGKWSSEGvNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMR 86
Cdd:PLN02278 13 ALVKLRNAGLLRTQGLIGGKWTDAY-DGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 87 KFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWN 166
Cdd:PLN02278 92 RWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 167 FPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTE 246
Cdd:PLN02278 172 FPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV-MGDAPEIGDALLASPKVRKITFTGSTA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 247 VGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSAL 326
Cdd:PLN02278 251 VGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 327 QVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFK 406
Cdd:PLN02278 331 VVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 407 FDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:PLN02278 411 FKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
....*...
gi 1229267232 487 YVCMGGIG 494
Cdd:PLN02278 491 YVCLGNMN 498
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
39-486 |
0e+00 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 688.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSA 198
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 199 LALAILAERAGIPDGLFSVLPTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDA 278
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 279 DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAV 358
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 359 TKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWK 438
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1229267232 439 VTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
10-491 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 663.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 10 RLKDQTLVREQMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFY 89
Cdd:PRK11241 2 QLNDSTLFRQQALINGEWL-DANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 90 EEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPS 169
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 170 AMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGR 249
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVV-TGSAGAVGGELTSNPLVRKLSFTGSTEIGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 250 ILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVL 329
Cdd:PRK11241 240 QLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 330 DGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDT 409
Cdd:PRK11241 320 DGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 410 VEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVC 489
Cdd:PRK11241 400 EADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMC 479
|
..
gi 1229267232 490 MG 491
Cdd:PRK11241 480 IG 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
15-490 |
0e+00 |
|
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: 610.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 15 TLVREQMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVA 94
Cdd:COG1012 2 TTPEYPLFIGGEWV-AAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 95 NAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCR 174
Cdd:COG1012 81 RREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 175 KIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQ 254
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGD-GSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 255 GAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFES 334
Cdd:COG1012 240 AAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 335 GATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDR-DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEV 413
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229267232 414 IELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTEL-APFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
33-488 |
0e+00 |
|
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: 562.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 33 NGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLA 112
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 113 EARGEIAYGASYIEWFGEEAKRVYGDTIPGhQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLPTDNARmFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPF 272
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAE-VGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTGLIST-ELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-490 |
1.94e-176 |
|
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: 502.51 E-value: 1.94e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 61 ASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTI 140
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 141 PGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPT 220
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 221 DnARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCV 300
Cdd:cd07078 162 D-GDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 301 CANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARG-GTFVQ 379
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 380 PTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTEL 459
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420 430
....*....|....*....|....*....|..
gi 1229267232 460 -APFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07078 401 sAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
33-488 |
1.10e-166 |
|
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: 479.07 E-value: 1.10e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 33 NGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLA 112
Cdd:cd07088 11 SGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 113 EARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:cd07088 91 LARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPF 272
Cdd:cd07088 171 ETPLNALEFAELVDEAGLPAGVLNIVTGRGSVV-GDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:cd07088 250 IVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDR-DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAN 431
Cdd:cd07088 330 MVERAVEAGATLLTGGKRpEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229267232 432 DLRNVWKVTEALEYGMVGVNTGlistelaPF-------GGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07088 410 NLNTAMRATNELEFGETYINRE-------NFeamqgfhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-488 |
2.79e-145 |
|
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: 423.89 E-value: 2.79e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKA--SQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPL 196
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 197 SALALAILAERAGIPDGLFSVLPTDnARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFD 276
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGF-GPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 277 DADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDD 356
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 357 AVTKGATVVVGGDR----DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07114 320 AREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-488 |
2.74e-144 |
|
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: 420.40 E-value: 2.74e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 58 EVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYG 137
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 138 DTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSA-LALAILAERAGIPDGLFS 216
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 217 VLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAG 296
Cdd:cd07104 161 VVPGGGSEI-GDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 297 QTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDargGT 376
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 377 FVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLIS 456
Cdd:cd07104 317 FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN 396
|
410 420 430
....*....|....*....|....*....|...
gi 1229267232 457 TE-LAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07104 397 DEpHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-490 |
7.12e-144 |
|
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: 420.43 E-value: 7.12e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEAR-GE 117
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKRVYGDTIPgHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLS 197
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAERAGIPDGLFSVLptdnaRMFGEEV----CSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFI 273
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVV-----HGFGPEAgaalVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 274 VFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGH 353
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 354 IDDAVTKGATVVVGGDRDA----RGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFF 429
Cdd:cd07093 315 VELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 430 ANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
39-490 |
8.40e-144 |
|
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: 420.20 E-value: 8.40e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSA 198
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 199 LALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDA 278
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEV-GDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 279 DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAV 358
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 359 TKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWK 438
Cdd:cd07150 322 AKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1229267232 439 VTEALEYGMVGVNTGLISTEL-APFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07150 399 LAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
20-488 |
1.81e-139 |
|
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: 410.06 E-value: 1.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAE 97
Cdd:cd07091 5 GLFINNEFV-DSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 98 DLAVILTSEMGKPLAE-ARGEIAYGASYIEWFGEEAKRVYGDTIPghQADKRL-LVIKQPVGVVAAIAPWNFPSAMVCRK 175
Cdd:cd07091 84 ELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIP--IDGNFLaYTRREPIGVCGQIIPWNFPLLMLAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 176 IAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPtDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQG 255
Cdd:cd07091 162 LAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVP-GFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 256 AQK-IMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFES 334
Cdd:cd07091 241 AKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 335 GATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVI 414
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229267232 415 ELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
22-488 |
1.03e-138 |
|
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: 407.79 E-value: 1.03e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKWSSegvNGTRINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLA 100
Cdd:cd07097 4 YIDGEWVA---GGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 101 VILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPAL 180
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 181 ASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSvLPTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIM 260
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFN-LVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 261 KLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGP 340
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 341 LINDEAVAKLYGHIDDAVTKGATVVVGGDRDARG--GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELAN 418
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 419 DTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTEL-APFGGVKQSGFG-REGSKYGMDDFLSMKYV 488
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-488 |
4.12e-137 |
|
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: 403.27 E-value: 4.12e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIP--GHQADKRLLVI--KQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPvdAYEYNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPF 272
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVV-TGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDRDarGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 433 LRNVWKVTEALEYGMVGVN-TGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07145 398 INRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-490 |
2.68e-135 |
|
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: 395.44 E-value: 2.68e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 64 DAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGH 143
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 144 QADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnA 223
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG-G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 224 RMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCAN 303
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 304 RIYVQSGIHDRFVEKLAmrvsalqvldgfesgatigplindeavaklyghiddavtkgatvvvggdrdarggtfvqpTLL 383
Cdd:cd06534 240 RLLVHESIYDEFVEKLV------------------------------------------------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 384 SGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTEL-APF 462
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPF 339
|
410 420
....*....|....*....|....*...
gi 1229267232 463 GGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-488 |
1.41e-133 |
|
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: 392.98 E-value: 1.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 59 VRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGD 138
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 139 TiPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVL 218
Cdd:cd07100 81 E-PIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 219 PTDNARMfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQT 298
Cdd:cd07100 160 LIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 299 CVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFV 378
Cdd:cd07100 238 CIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 379 QPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTE 458
Cdd:cd07100 318 PPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDP 397
|
410 420 430
....*....|....*....|....*....|
gi 1229267232 459 LAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07100 398 RLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
39-486 |
4.72e-133 |
|
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: 392.28 E-value: 4.72e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASyieWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSA 198
Cdd:cd07106 81 GGAVA---WLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 199 LALAILAERAgIPDGLFSVLPTDNArmFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDA 278
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDE--LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 279 DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAV 358
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 359 TKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWK 438
Cdd:cd07106 315 AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1229267232 439 VTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-490 |
1.36e-132 |
|
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: 391.57 E-value: 1.36e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIPGHQA----DKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASpggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKimKLSLELGGNAPF 272
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVV-TGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07149 318 WVEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTglIST---ELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07149 395 LQKALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
22-484 |
2.14e-129 |
|
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: 384.39 E-value: 2.14e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKWSsEGVNGTRINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLA 100
Cdd:cd07131 2 YIGGEWV-DSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 101 VILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPAL 180
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 181 ASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIM 260
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVV-HGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 261 KLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGP 340
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 341 LINDEAVAKLYGHIDDAVTKGATVVVGGDRDARG----GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIEL 416
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229267232 417 ANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTEL-APFGGVKQSGFGREGSKYGMDDFLS 484
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGHREAGTTALDAFT 468
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-488 |
3.58e-129 |
|
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: 383.19 E-value: 3.58e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 25 GKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILT 104
Cdd:cd07151 1 GEWR-DGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 105 SEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGC 184
Cdd:cd07151 80 RESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 185 AIVFKPAAETPLSA-LALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLS 263
Cdd:cd07151 160 AVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEI-GDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 264 LELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLIN 343
Cdd:cd07151 239 LELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLIN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 344 DEAVAKLYGHIDDAVTKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFG 423
Cdd:cd07151 319 ESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 424 LAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTE-LAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07151 396 LSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-491 |
3.83e-129 |
|
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: 382.81 E-value: 3.83e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASYIEWFGEEAKRVYGDTIP---GHQADKRllviKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETP 195
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPlpgGSFAYTR----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 196 LSALALAILAERAGIPDGLFSVLPTDNArmFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVF 275
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGE--TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 276 DDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHID 355
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 356 DAVTKGATVVVGGDR-----DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFA 430
Cdd:cd07090 315 SAKQEGAKVLCGGERvvpedGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229267232 431 NDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK--YVCMG 491
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKtvYVEMG 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-488 |
2.28e-128 |
|
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: 381.66 E-value: 2.28e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAEDLA 100
Cdd:cd07119 2 IDGEWV-EAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 101 VILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPgHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPAL 180
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 181 ASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIM 260
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLV-TGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 261 KLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGP 340
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 341 LINDEAVAKLYGHIDDAVTKGATVVVGGDRDARG----GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIEL 416
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 417 ANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
39-486 |
3.05e-128 |
|
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: 380.79 E-value: 3.05e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKK--WAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEAR- 115
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 116 GEIAYGASYIEWFGEEAKRVYGDTIP-GHQADKrlLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAET 194
Cdd:cd07112 86 VDVPSAANTFRWYAEAIDKVYGEVAPtGPDALA--LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 195 PLSALALAILAERAGIPDGLFSVLPTdnarmFGEEVCS----NPVVKKLTFTGSTEVGRILMAQGAQKIMK-LSLELGGN 269
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPG-----FGHTAGEalglHMDVDALAFTGSTEVGRRFLEYSGQSNLKrVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 270 APFIVFDDA-DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVA 348
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 349 KLYGHIDDAVTKGATVVVGGDRD--ARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAA 426
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229267232 427 YFFANDLRNVWKVTEALEYGMVGVNT---GLISTelaPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCfdeGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
37-490 |
4.06e-128 |
|
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: 380.24 E-value: 4.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIPG----HQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLPTDnARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKimKLSLELGGNAPF 272
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGE-REVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--RIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07094 318 WVEEAVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTG-LISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-488 |
2.15e-127 |
|
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: 378.10 E-value: 2.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 40 LNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIA 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 120 YGASYIEWFGEEAKRVYGDT-IPGHQ--ADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPL 196
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRkVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 197 SALALAILAERAGIPDGLFSVLPTDNARmfGEEVCSNpVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFD 276
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGAT--GAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 277 DADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDD 356
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 357 AVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNV 436
Cdd:cd07099 318 AVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 437 WKVTEALEYGMVGVN----TGLISTelAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07099 398 EAIARRLEAGAVSINdvllTAGIPA--LPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-488 |
1.10e-125 |
|
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: 374.00 E-value: 1.10e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPL-AEARGE 117
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKRVYGDTIPGHQaDKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLS 197
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGP-DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAERAgIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDD 277
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVI-TGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 278 ADLDQAVEGAMLS-KFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDD 356
Cdd:cd07108 238 ADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 357 AV-TKGATVVVGG----DRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAN 431
Cdd:cd07108 318 GLsTSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229267232 432 DLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGM-DDFLSMKYV 488
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTV 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
22-473 |
2.16e-125 |
|
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: 374.21 E-value: 2.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKWSSEGvnGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAV 101
Cdd:cd07086 2 VIGGEWVGSG--GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 102 ILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALA 181
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 182 SGCAIVFKPAAETPLSALALAILAERA----GIPDGLFSVLpTDNARmFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQ 257
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLV-TGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 258 KIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGAT 337
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 338 IGPLINDEAVAKLYGHIDDAVTKGATVVVGGDR--DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIE 415
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 416 LANDTEFGLAAYFFANDLRNVWKVTEA--LEYGMVGVNTGLISTEL-APFGGVKQSGFGRE 473
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRE 458
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-488 |
1.09e-124 |
|
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: 371.29 E-value: 1.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 40 LNPSTMDVLASLPSAGLAEVRASIDAAKASQKK--WAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGE 117
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLS 197
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDD 277
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIV-TGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 278 ADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDA 357
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 358 VTKGATVVVGGDRDARG-GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNV 436
Cdd:cd07118 321 RAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 437 WKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-486 |
2.86e-124 |
|
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: 370.68 E-value: 2.86e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKW-SSEGVNgtRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAV 101
Cdd:cd07138 3 IDGAWvAPAGTE--TIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 102 ILTSEMGKPLAEARG-EIAYGASYIEWFGEEAK-----RVYGDTipghqadkrlLVIKQPVGVVAAIAPWNFPSAMVCRK 175
Cdd:cd07138 81 AITLEMGAPITLARAaQVGLGIGHLRAAADALKdfefeERRGNS----------LVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 176 IAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQG 255
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVV-GEALSAHPDVDMVSFTGSTRAGKRVAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 256 AQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESG 335
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 336 ATIGPLINDEAVAKLYGHIDDAVTKGATVVVGG-DRDAR--GGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEE 412
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229267232 413 VIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTElAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPG-APFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-486 |
4.02e-123 |
|
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: 368.06 E-value: 4.02e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAEDLA 100
Cdd:cd07139 3 IGGRWV-APSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 101 VILTSEMGKPLAEAR-GEIAYGASYIEWFGEEAKRV-YGDTIPGhQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAP 178
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPG-SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 179 ALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnaRMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQK 258
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD--REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 259 IMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATI 338
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 339 GPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDAR--GGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIEL 416
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 417 ANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNtGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
20-490 |
5.57e-123 |
|
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: 367.97 E-value: 5.57e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAE 97
Cdd:cd07142 5 KLFINGQFV-DAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 98 DLAVILTSEMGKPLAEAR-GEIAYGASYIEWFGEEAKRVYGDTIPGHQAdKRLLVIKQPVGVVAAIAPWNFPSAMVCRKI 176
Cdd:cd07142 84 ELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 177 APALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGA 256
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIV-TGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 257 QKIMK-LSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESG 335
Cdd:cd07142 242 KSNLKpVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 336 ATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIE 415
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 416 LANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-490 |
9.68e-123 |
|
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: 366.38 E-value: 9.68e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG-E 117
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKRVYGDTIPghqADKRLL--VIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETP 195
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIP---VRGPFLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 196 LSALALAILAERAGIPDGLFSVLPtDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVF 275
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVT-GFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 276 DDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHID 355
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 356 DAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRN 435
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 436 VWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-486 |
2.44e-121 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 363.36 E-value: 2.44e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVI 102
Cdd:TIGR01804 2 IDGEYV-EDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 103 LTSEMGKPLAEA-RGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKrLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALA 181
Cdd:TIGR01804 81 ETLDTGKTLQETiVADMDSGADVFEFFAGLAPALNGEIIPLGGPSF-AYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 182 SGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMK 261
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEV-GPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 262 LSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPL 341
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 342 INDEAVAKLYGHIDDAVTKGATVVVGGDR----DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELA 417
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRpenvGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229267232 418 NDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
29-488 |
2.64e-121 |
|
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: 363.65 E-value: 2.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 29 SEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAA-KASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEM 107
Cdd:cd07144 17 VKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAArKAFESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 108 GKPL-AEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQAdKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAI 186
Cdd:cd07144 97 GKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPN-KLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 187 VFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLEL 266
Cdd:cd07144 176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVA-GSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLEC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 267 GGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRV-SALQVLDGFESGATIGPLINDE 345
Cdd:cd07144 255 GGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 346 AVAKLYGHIDDAVTKGATVVVGGDRDARG---GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEF 422
Cdd:cd07144 335 QYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTY 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 423 GLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07144 415 GLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
39-486 |
7.46e-121 |
|
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: 361.95 E-value: 7.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWA-KVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG- 116
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIPGHQADKRL----LVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLPTdNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPF 272
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTG-SDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDRDAR--GGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFA 430
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 431 NDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-488 |
1.25e-120 |
|
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: 361.17 E-value: 1.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWA-KVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGE 117
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKRVYGDTIPgHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLS 197
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAERAGIPDGLFSVLPTdnarmFGEEV----CSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFI 273
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTG-----LGAEAgaalVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 274 VFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGfESGATIGPLINDEAVAKLYGH 353
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 354 IDDAVTKGATVVVGGDR---DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFA 430
Cdd:cd07109 314 VARARARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 431 NDLRNVWKVTEALEYGMVGVNT----GLISTelaPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNygagGGIEL---PFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-488 |
1.50e-120 |
|
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: 359.97 E-value: 1.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 58 EVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYG 137
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 138 DTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSV 217
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 218 LPT--DNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNA 295
Cdd:cd07105 161 VTHspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 296 GQTCVCANRIYVQSGIHDRFVEKLAMRVSALqvldgFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGG-DRDARG 374
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 375 GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGL 454
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1229267232 455 ISTE-LAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07105 396 VHDEpTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
15-493 |
1.24e-119 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 359.58 E-value: 1.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 15 TLVREQMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVA 94
Cdd:PRK13252 3 RQPLQSLYIDGAYV-EATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 95 NAEDLAVILTSEMGKPLAEAR-GEIAYGASYIEWFGEEAKRVYGDTIPGHQAD----KRllvikQPVGVVAAIAPWNFPS 169
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 170 AMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNArmFGEEVCSNPVVKKLTFTGSTEVGR 249
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR--VGAWLTEHPDIAKVSFTGGVPTGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 250 ILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVL 329
Cdd:PRK13252 235 KVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 330 DGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDR----DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVF 405
Cdd:PRK13252 315 DPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 406 KFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSM 485
Cdd:PRK13252 395 TFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQI 474
|
490
....*....|
gi 1229267232 486 K--YVCMGGI 493
Cdd:PRK13252 475 KsvQVEMGPF 484
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-488 |
1.86e-119 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 358.84 E-value: 1.86e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSSEGvnGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDL 99
Cdd:PRK13473 4 KLLINGELVAGE--GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 100 AVILTSEMGKPLAEARG-EIAYGASYIEWFGEEAK----RVYGDTIPGHQADKRllviKQPVGVVAAIAPWNFPSAMVCR 174
Cdd:PRK13473 82 ARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARclegKAAGEYLEGHTSMIR----RDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 175 KIAPALASGCAIVFKPAAETPLSALALAILAERAgIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQ 254
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVV-TGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 255 GAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFES 334
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 335 GATIGPLINDEAVAKLYGHIDDAVTKG-ATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEV 413
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 414 IELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-488 |
3.21e-118 |
|
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: 354.71 E-value: 3.21e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEAR-GE 117
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAK----RVYGDTIPGHQADKRllviKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAE 193
Cdd:cd07092 81 LPGAVDNFRFFAGAARtlegPAAGEYLPGHTSMIR----REPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 194 TPLSALALAILAERaGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFI 273
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASA-GDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 274 VFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGH 353
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 354 IDDAvTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDL 433
Cdd:cd07092 315 VERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 434 RNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
20-486 |
5.38e-118 |
|
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: 355.11 E-value: 5.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDL 99
Cdd:cd07559 2 DNFINGEWV-APSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 100 AVILTSEMGKPLAEARG-EIAYGASYIEWF-----GEE--AKRVYGDTIPghqadkrlLVIKQPVGVVAAIAPWNFPSAM 171
Cdd:cd07559 81 AVAETLDNGKPIRETLAaDIPLAIDHFRYFagvirAQEgsLSEIDEDTLS--------YHFHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 172 VCRKIAPALASGCAIVFKPAAETPLSALALAILAERAgIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRIL 251
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVV-TGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 252 MAQGAQKIMKLSLELGGNAPFIVFDDA-----DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSAL 326
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 327 QVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDR----DARGGTFVQPTLLSGATKDMKVAREETFAPLA 402
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 403 PVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDF 482
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
....
gi 1229267232 483 LSMK 486
Cdd:cd07559 471 QQTK 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
18-488 |
7.92e-116 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 350.57 E-value: 7.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 18 REQMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKK-----WAKVSAKERSLIMRKFYEEV 92
Cdd:PLN02467 7 RRQLFIGGEWR-EPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 93 VANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGD-----TIPGHQADKRLLviKQPVGVVAAIAPWNF 167
Cdd:PLN02467 86 TERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkapvSLPMETFKGYVL--KEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 168 PSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEV 247
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVV-TGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 248 GRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQ 327
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 328 VLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDR--DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVF 405
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpeHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 406 KFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSM 485
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
...
gi 1229267232 486 KYV 488
Cdd:PLN02467 483 KQV 485
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-488 |
8.78e-116 |
|
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: 348.57 E-value: 8.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASYIEWFGEEAKRV---YGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETP 195
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 196 LSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVF 275
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVV-TGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 276 DDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHID 355
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 356 DAVTKGATVVVGGDRDARG--GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDL 433
Cdd:cd07110 320 RGKEEGARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 434 RNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
21-488 |
7.10e-115 |
|
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: 347.21 E-value: 7.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 21 MLVGGKWSSeGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS-QKKWA-KVSAKERSLIMRKFYEEVVANAED 98
Cdd:cd07143 9 LFINGEFVD-SVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 99 LAVILTSEMGKP-LAEARGEIAYGASYIEWFGEEAKRVYGDTIpgHQADKRLLVIK-QPVGVVAAIAPWNFPSAMVCRKI 176
Cdd:cd07143 88 LASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVI--ETDIKKLTYTRhEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 177 APALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGA 256
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVV-SGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 257 Q-KIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESG 335
Cdd:cd07143 245 KsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 336 ATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIE 415
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229267232 416 LANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-486 |
7.90e-115 |
|
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: 346.15 E-value: 7.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIP--------GHQAdkrlLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVF 188
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisargeGRQG----LVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 189 KPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKimKLSLELGG 268
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA--DLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 269 NAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVA 348
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 349 KLYGHIDDAVTKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYF 428
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 429 FANDLRNVWKVTEALEYGmvGVNTGLIST---ELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07147 390 FTRDLEKALRAWDELEVG--GVVINDVPTfrvDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
32-490 |
1.89e-114 |
|
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: 346.26 E-value: 1.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 32 VNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKK---WAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMG 108
Cdd:cd07141 19 VSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 109 KPLAEAR-GEIAYGASYIEWFGEEAKRVYGDTIPghqADKRLLVI--KQPVGVVAAIAPWNFPSAMVCRKIAPALASGCA 185
Cdd:cd07141 99 KPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIP---MDGDFFTYtrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 186 IVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILM-AQGAQKIMKLSL 264
Cdd:cd07141 176 VVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTA-GAAISSHPDIDKVAFTGSTEVGKLIQqAAGKSNLKRVTL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 265 ELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLIND 344
Cdd:cd07141 255 ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 345 EAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGL 424
Cdd:cd07141 335 EQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGL 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 425 AAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07141 415 AAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
20-486 |
3.01e-114 |
|
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: 345.59 E-value: 3.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDL 99
Cdd:cd07117 2 GLFINGEWV-KGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 100 AVILTSEMGKPLAEARG-EIAYGASYIEWFgeeAKRVYGDTIPGHQADKRLL--VIKQPVGVVAAIAPWNFPSAMVCRKI 176
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYF---AGVIRAEEGSANMIDEDTLsiVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 177 APALASGCAIVFKPAAETPLSALALAILAERAgIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGA 256
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIV-TGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 257 QKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGA 336
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 337 TIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDR----DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEE 412
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229267232 413 VIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
22-477 |
2.67e-112 |
|
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: 340.32 E-value: 2.67e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKWssEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAK-VSAKERSLIMRKFYEEVVANAEDLA 100
Cdd:cd07082 5 LINGEW--KESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 101 VILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRL----LVIKQPVGVVAAIAPWNFPSAMVCRKI 176
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 177 APALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGA 256
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVV-TGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 257 QKimKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGA 336
Cdd:cd07082 242 MK--RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 337 TIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRdaRGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIEL 416
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 417 ANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTgliSTELA----PFGGVKQSGFGREGSKY 477
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQRGpdhfPFLGRKDSGIGTQGIGD 459
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
37-486 |
1.71e-111 |
|
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: 337.41 E-value: 1.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAkASQKKwaKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALA-ASYRS--TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTIP---GHQADKRLLV-IKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAA 192
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFScdlTANGKARKIFtLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 193 ETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKimKLSLELGGNAPF 272
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVV-TGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYG 352
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 353 HIDDAVTKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTGL-ISTELAPFGGVKQSGFG-REGSKYGMDDFLSMK 486
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
1-472 |
1.79e-111 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 339.93 E-value: 1.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 1 MAISSTLLGRLKDQTLVREQMLVGGKWSSEGvngTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKE 80
Cdd:PRK09407 1 ATTTALPMPAPSALTFERLRRLTARVDGAAG---PTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 81 RSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI---AYGASYiewfgeeakrvYGDTIPGHQADKR------LL- 150
Cdd:PRK09407 78 RAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVldvALTARY-----------YARRAPKLLAPRRragalpVLt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 151 ---VIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnarmfG 227
Cdd:PRK09407 147 kttELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGP-----G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 228 EEVcSNPVVKK---LTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANR 304
Cdd:PRK09407 222 PVV-GTALVDNadyLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 305 IYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGdrDAR---GGTFVQPT 381
Cdd:PRK09407 301 IYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGG--KARpdlGPLFYEPT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 382 LLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLI----ST 457
Cdd:PRK09407 379 VLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAaawgSV 458
|
490
....*....|....*
gi 1229267232 458 ElAPFGGVKQSGFGR 472
Cdd:PRK09407 459 D-APMGGMKDSGLGR 472
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
35-490 |
2.29e-109 |
|
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: 332.87 E-value: 2.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 35 TRINVLNPSTMDVLASLPSAGLAEVRASIDAAK-ASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAE 113
Cdd:cd07113 15 KRLDITNPATEQVIASVASATEADVDAAVASAWrAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 114 ARG-EIAYGASYIEWFGEEAKRVYGDT----IPGHQADK-RLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIV 187
Cdd:cd07113 95 SRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 188 FKPAAETPLSALALAILAERAGIPDGLFSVLPTDNArmFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELG 267
Cdd:cd07113 175 IKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA--VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 268 GNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAV 347
Cdd:cd07113 253 GKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 348 AKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAY 427
Cdd:cd07113 333 DKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTAS 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229267232 428 FFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07113 413 VWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-486 |
2.74e-108 |
|
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: 329.21 E-value: 2.74e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 40 LNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIA 119
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 120 YGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSAL 199
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 200 ALAILAERAGIPDGLFSVLPTDNARMfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDAD 279
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETS--AALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 280 LDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVT 359
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 360 KGATVVVGG---DRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNV 436
Cdd:cd07102 319 KGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 437 WKVTEALEYGMVGVNTG-LISTELaPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07102 399 EALGEQLETGTVFMNRCdYLDPAL-AWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
30-490 |
8.59e-108 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 329.86 E-value: 8.59e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 30 EGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEM 107
Cdd:PLN02766 31 DAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 108 GKPLAEARG-EIAYGASYIEWFGEEAKRVYGDTIPgHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAI 186
Cdd:PLN02766 111 GKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLK-MSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 187 VFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMK-LSLE 265
Cdd:PLN02766 190 VVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTA-GAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKqVSLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 266 LGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDE 345
Cdd:PLN02766 269 LGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 346 AVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLA 425
Cdd:PLN02766 349 QFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 426 AYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:PLN02766 429 AGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVT 493
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
20-488 |
1.99e-107 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 329.85 E-value: 1.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAE 97
Cdd:PLN02466 59 QLLINGQFV-DAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 98 DLAVILTSEMGKPLAEARG-EIAYGASYIEWFGEEAKRVYGDTIPG---HQADkrllVIKQPVGVVAAIAPWNFPSAMVC 173
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPAdgpHHVQ----TLHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 174 RKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVL----PTDnarmfGEEVCSNPVVKKLTFTGSTEVGR 249
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVsgfgPTA-----GAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 250 ILMAQGAQKIMK-LSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQV 328
Cdd:PLN02466 289 IVLELAAKSNLKpVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 329 LDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFD 408
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 409 TVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-488 |
5.05e-106 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 322.07 E-value: 5.05e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 85 MRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAP 164
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 165 WNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGS 244
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLV-LGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 245 TEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVS 324
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 325 ALQVLDGFESGA-TIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAP 403
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 404 VFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFL 483
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYL 399
|
....*
gi 1229267232 484 SMKYV 488
Cdd:PRK10090 400 QTQVV 404
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
42-472 |
6.69e-106 |
|
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: 323.11 E-value: 6.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 42 PSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYG 121
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 122 ASYIEWFGEEAKRVYGD-----TIPGHQadkRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPL 196
Cdd:cd07101 83 AIVARYYARRAERLLKPrrrrgAIPVLT---RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 197 SALALAILAERAGIPDGLFSVLPTDnarmfGEEVcSNPVVKK---LTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFI 273
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGP-----GSEV-GGAIVDNadyVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 274 VFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGH 353
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 354 IDDAVTKGATVVVGGD-RDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07101 314 VDDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTGLIST---ELAPFGGVKQSGFGR 472
Cdd:cd07101 394 GARGRRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGR 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-489 |
1.30e-105 |
|
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: 322.71 E-value: 1.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 41 NPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEAR-GEIA 119
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 120 YGASYIEWF---GEEA---KRVYGDTIPGHqadKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAE 193
Cdd:cd07098 82 VTCEKIRWTlkhGEKAlrpESRPGGLLMFY---KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 194 TPLSALALAILAERA----GIPDGLFSVLP-TDNArmfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGG 268
Cdd:cd07098 159 VAWSSGFFLSIIREClaacGHDPDLVQLVTcLPET---AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 269 NAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVA 348
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 349 KLYGHIDDAVTKGATVVVGGDRDAR----GGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGL 424
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 425 AAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELA--PFGGVKQSGFGREGSKYGMDDFLSMKYVC 489
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-490 |
4.64e-105 |
|
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: 321.22 E-value: 4.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 40 LNPSTMDVLASLPSAGLAEVRASIDAAKASQKK--WAkVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGE 117
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKRVYGDTI---PGHQAdkrlLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAET 194
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIepePGSFS----LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 195 PLSALALAIL-AERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFI 273
Cdd:cd07120 157 AQINAAIIRIlAEIPSLPAGVVNLF-TESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 274 VFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGH 353
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 354 IDDAVTKGATVVVGGDRDARG---GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFA 430
Cdd:cd07120 316 VERAIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 431 NDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
46-471 |
4.70e-105 |
|
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: 320.78 E-value: 4.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 46 DVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYI 125
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 126 EWFGEEAKRVYGDTIPghQADKRL-LVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAIL 204
Cdd:cd07152 82 HEAAGLPTQPQGEILP--SAPGRLsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 205 A-ERAGIPDGLFSVLPTDNARmfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQA 283
Cdd:cd07152 160 LfEEAGLPAGVLHVLPGGADA--GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 284 VEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGAT 363
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 364 VVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEAL 443
Cdd:cd07152 318 LEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420
....*....|....*....|....*....
gi 1229267232 444 EYGMVGVNTGLISTE-LAPFGGVKQSGFG 471
Cdd:cd07152 395 RTGMLHINDQTVNDEpHNPFGGMGASGNG 423
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
37-491 |
6.97e-102 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 313.21 E-value: 6.97e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARG 116
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 117 EIAYGASYIEWFGEEAKRVYGDTiPGHQAD---KRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAE 193
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 194 TPLSALALAILAERAGIPDGLFSVLPTDNARMfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFI 273
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 274 VFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGH 353
Cdd:PRK09406 240 VMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 354 IDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDL 433
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229267232 434 RNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCMG 491
Cdd:PRK09406 400 AEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
20-488 |
3.04e-101 |
|
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: 312.51 E-value: 3.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKAS--QKKWAKVSAKERSLIMRKFYEEVVANAE 97
Cdd:cd07140 7 QLFINGEFV-DAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 98 DLAVILTSEMGKPLAEA-RGEIAYGASYIEWFGEEAKRVYGDTIPGHQA--DKRL-LVIKQPVGVVAAIAPWNFPSAMVC 173
Cdd:cd07140 86 ELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 174 RKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPtDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMA 253
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILP-GSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 254 QGA-QKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGF 332
Cdd:cd07140 245 SCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 333 ESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDT--V 410
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229267232 411 EEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-488 |
6.95e-97 |
|
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: 300.06 E-value: 6.95e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEI 118
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 119 AYGASYIEWFGEEAKRVYGDTIP-GHQAdkRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLS 197
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPvGGRN--LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAeRAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDD 277
Cdd:cd07107 159 ALRLAELA-REVLPPGVFNILPGDGATA-GAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 278 ADLDQAVEGAMLS-KFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDD 356
Cdd:cd07107 237 ADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 357 AVTKGATVVVGGDR----DARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07107 317 AKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 433 LRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
20-480 |
1.65e-94 |
|
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: 294.81 E-value: 1.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 20 QMLVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDL 99
Cdd:cd07085 2 KLFINGEWV-ESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 100 AVILTSEMGKPLAEARGEIAYGASYIEwFGEEAKRVY-GDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPsAMV-CRKIA 177
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVE-FACSIPHLLkGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIpLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 178 PALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnaRMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQ 257
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGG--KEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 258 KIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGAT 337
Cdd:cd07085 237 NGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 338 IGPLINDEAVAKLYGHIDDAVTKGATVVVGGdRDAR-----GGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEE 412
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDG-RGVKvpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 413 VIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGlISTELA--PFGGVKQSGFGrEGSKYGMD 480
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVP-IPVPLAffSFGGWKGSFFG-DLHFYGKD 463
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
17-483 |
2.06e-94 |
|
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: 295.67 E-value: 2.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 17 VREQ------MLVGGKW-SSEGvngtRINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKF 88
Cdd:cd07124 25 VREElgreypLVIGGKEvRTEE----KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 89 YEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIpGHQADKRLLVIKQPVGVVAAIAPWNFP 168
Cdd:cd07124 101 AALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPV-EMVPGEDNRYVYRPLGVGAVISPWNFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 169 SAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVG 248
Cdd:cd07124 180 LAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEV-GDYLVEHPDVRFIAFTGSREVG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 249 -RIL-----MAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMR 322
Cdd:cd07124 259 lRIYeraakVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 323 VSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVtKGATVVVGGDRD--ARGGTFVQPTLLSGATKDMKVAREETFAP 400
Cdd:cd07124 339 TKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLelAAEGYFVQPTIFADVPPDHRLAQEEIFGP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 401 LAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVN---TGLIStELAPFGGVKQSGFgreGSKY 477
Cdd:cd07124 418 VLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALV-GRQPFGGFKMSGT---GSKA 493
|
....*.
gi 1229267232 478 GMDDFL 483
Cdd:cd07124 494 GGPDYL 499
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
23-483 |
2.04e-93 |
|
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: 291.99 E-value: 2.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVI 102
Cdd:cd07111 26 INGKWV-KPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 103 LTSEMGKPLAEAR-GEIAYGASYIEWFGEEAKRVygDT-IPGHQadkrllvikqPVGVVAAIAPWNFPSAMVCRKIAPAL 180
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLL--DTeLAGWK----------PVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 181 ASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNArmFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIM 260
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS--FGSALANHPGVDKVAFTGSTEVGRALRRATAGTGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 261 KLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGP 340
Cdd:cd07111 251 KLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 341 LINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDT 420
Cdd:cd07111 331 IVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229267232 421 EFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFL 483
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
22-475 |
8.25e-90 |
|
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: 282.56 E-value: 8.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKWSSegvNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAV 101
Cdd:cd07130 2 VYDGEWGG---GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 102 ILTSEMGKPLAEARGEI---------AYGASyiewfgeeaKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMV 172
Cdd:cd07130 79 LVSLEMGKILPEGLGEVqemidicdfAVGLS---------RQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 173 CRKIAPALASGCAIVFKPAAETPLSALALAILAERA----GIPDGLFSVLPTDNARmfGEEVCSNPVVKKLTFTGSTEVG 248
Cdd:cd07130 150 GWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADV--GEALVKDPRVPLVSFTGSTAVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 249 RILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQV 328
Cdd:cd07130 228 RQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 329 LDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSGAtKDMKVAREETFAPLAPVFKFD 408
Cdd:cd07130 308 GDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 409 TVEEVIELANDTEFGLAAYFFANDLRNVWKVTEAL--EYGMVGVNTGLISTEL-APFGGVKQSGFGRE-GS 475
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
40-488 |
3.77e-89 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 280.21 E-value: 3.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 40 LNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIA 119
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 120 YGASYIEWFGEEAKRVYgDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSAL 199
Cdd:PRK13968 92 KSANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 200 ALAILAERAGIPDGLFSVLPTDNARMfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDAD 279
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGV--SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 280 LDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVT 359
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 360 KGATVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKV 439
Cdd:PRK13968 329 EGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQM 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1229267232 440 TEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:PRK13968 409 AARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
23-486 |
4.75e-87 |
|
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: 275.48 E-value: 4.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWSSEgVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVI 102
Cdd:cd07116 5 IGGEWVAP-VKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 103 LTSEMGKPLAEARG--------EIAYGASYIEWFGEEAKRVYGDTIPGHqadkrllvIKQPVGVVAAIAPWNFPSAMVCR 174
Cdd:cd07116 84 ETWDNGKPVRETLAadiplaidHFRYFAGCIRAQEGSISEIDENTVAYH--------FHEPLGVVGQIIPWNFPLLMATW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 175 KIAPALASGCAIVFKPAAETPLSALALAILAERAgIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRILMAQ 254
Cdd:cd07116 156 KLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEA-GKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 255 GAQKIMKLSLELGGNAPFIVF------DDADLDQAVEGAMLSKFrNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQV 328
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 329 LDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARG----GTFVQPTLLSGATKdMKVAREETFAPLAPV 404
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKGGNK-MRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 405 FKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLS 484
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
..
gi 1229267232 485 MK 486
Cdd:cd07116 472 TK 473
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
33-490 |
3.11e-83 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 265.99 E-value: 3.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 33 NGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKA--SQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKP 110
Cdd:PRK09847 33 ENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGvfERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 111 LAEA-RGEIAYGASYIEWFGEEAKRVYGDTIPGhQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFK 189
Cdd:PRK09847 113 IRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 190 PAAETPLSALALAILAERAGIPDGLFSVLPTdnarmFGEE----VCSNPVVKKLTFTGSTEVGRILMAQGAQKIMK-LSL 264
Cdd:PRK09847 192 PSEKSPLSAIRLAGLAKEAGLPDGVLNVVTG-----FGHEagqaLSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKrVWL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 265 ELGGNAPFIVFDDA-DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLIN 343
Cdd:PRK09847 267 EAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 344 DEAVAKLYGHIDDAVTKGATVVVGgdRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFG 423
Cdd:PRK09847 347 CAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYG 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 424 LAAYFFANDLRNVWKVTEALEYGMVGVNTGLISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYVCM 490
Cdd:PRK09847 425 LGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-480 |
3.59e-80 |
|
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: 256.04 E-value: 3.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 58 EVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEwFGEEA--KRV 135
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAyhERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 136 YGDTIPGhqADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLF 215
Cdd:cd07095 80 GERATPM--AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 216 SVLptDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKIMK-LSLELGGNAPFIVFDDADLDQAVEGAMLSKFRN 294
Cdd:cd07095 158 NLV--QGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 295 AGQTCVCANRIYV-QSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDAR 373
Cdd:cd07095 236 AGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 374 GGTFVQPTLLSgATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDlRNVWKVTEA-LEYGMVGVN- 451
Cdd:cd07095 316 GTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFLArIRAGIVNWNr 393
|
410 420 430
....*....|....*....|....*....|.
gi 1229267232 452 --TGLISTelAPFGGVKQSGFGREGSKYGMD 480
Cdd:cd07095 394 ptTGASST--APFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
37-481 |
3.99e-75 |
|
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: 243.87 E-value: 3.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 37 INVLNPSTMDVLASLPSAGLAEVRASIDAAKA---SQKKWakVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAE 113
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHAlflDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 114 ARGEIAYGASYIEWFGEEAKRVYGDTIP-GHQ---ADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFK 189
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPmGLTpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 190 PAAETPLSALALAILAERAGIPDGLFSVLPTDNARmfGEEVCSNPVVKKLTFTGSTEVGRIL---MAQGAqkimKLSLEL 266
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV--AEKLVTDPRVAFFSFIGSARVGWMLrskLAPGT----RCALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 267 GGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEA 346
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 347 VAKLYGHIDDAVTKGATVVVGGDRdaRGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAA 426
Cdd:cd07148 313 VDRVEEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 427 YFFANDLRNVWKVTEALEYGMVGVN--TGLiSTELAPFGGVKQSGFGREGSKYGMDD 481
Cdd:cd07148 391 AVFTKDLDVALKAVRRLDATAVMVNdhTAF-RVDWMPFAGRRQSGYGTGGIPYTMHD 446
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
21-483 |
2.74e-72 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 237.91 E-value: 2.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 21 MLVGGKWssegVNGT-RINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAED 98
Cdd:PRK03137 39 LIIGGER----ITTEdKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 99 LAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRvYGDTIPGHQ---ADKRLLVIkqPVGVVAAIAPWNFPSAMVCRK 175
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPVESrpgEHNRYFYI--PLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 176 IAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARmFGEEVCSNPVVKKLTFTGSTEVG-RIL--- 251
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE-VGDYLVDHPKTRFITFTGSREVGlRIYera 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 252 --MAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVL 329
Cdd:PRK03137 271 akVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 330 DGfESGATIGPLINDEAVAKLYGHIDDAVTKGaTVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDT 409
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 410 VEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVN---TGLISTeLAPFGGVKQSGfgrEGSKYGMDDFL 483
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVG-YHPFGGFNMSG---TDSKAGGPDYL 501
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
60-482 |
5.30e-71 |
|
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: 232.12 E-value: 5.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 60 RASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEAR--------GEIAYGASYIE-WFGe 130
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 131 eAKRVygdTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGI 210
Cdd:cd07134 80 -PKRV---RTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 211 PDGLFSV------------LPTDNarMFgeevcsnpvvkkltFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDA 278
Cdd:cd07134 156 EDEVAVFegdaevaqalleLPFDH--IF--------------FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 279 DLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEklAMRVSALQVLDGFE---SGATIGPLINDEAVAKLYGHID 355
Cdd:cd07134 220 DLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVE--HLKAEIEKFYGKDAarkASPDLARIVNDRHFDRLKGLLD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 356 DAVTKGATVVVGGDRDArGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRN 435
Cdd:cd07134 298 DAVAKGAKVEFGGQFDA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKAN 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229267232 436 VWKVTEALEYGMVGVNTGLI---STELaPFGGVKQSGFGREGSKYGMDDF 482
Cdd:cd07134 377 VNKVLARTSSGGVVVNDVVLhflNPNL-PFGGVNNSGIGSYHGVYGFKAF 425
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
33-480 |
5.30e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 228.69 E-value: 5.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 33 NGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLA 112
Cdd:PRK09457 13 QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 113 EARGEIAYGA--------SYIEWFGEEAkrvygDTIPGHQADKRllviKQPVGVVAAIAPWNFPSAMVCRKIAPALASGC 184
Cdd:PRK09457 93 EAATEVTAMInkiaisiqAYHERTGEKR-----SEMADGAAVLR----HRPHGVVAVFGPYNFPGHLPNGHIVPALLAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 185 AIVFKPAAETPLSALALAILAERAGIPDGLFSVLPtdNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGA---QKImk 261
Cdd:PRK09457 164 TVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQ--GGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAgqpEKI-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 262 LSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIH-DRFVEKLAMRVSALQVLDGFESGAT-IG 339
Cdd:PRK09457 240 LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAEPQPfMG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 340 PLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSgATKDMKVAREETFAPLAPVFKFDTVEEVIELAND 419
Cdd:PRK09457 320 AVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANN 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 420 TEFGLAAYFFANDlRNVW-KVTEALEYGMVGVN---TGLISTelAPFGGVKQSGFGREGSKYGMD 480
Cdd:PRK09457 399 TRFGLSAGLLSDD-REDYdQFLLEIRAGIVNWNkplTGASSA--APFGGVGASGNHRPSAYYAAD 460
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
30-471 |
1.75e-68 |
|
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: 227.85 E-value: 1.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 30 EGVNGTRINVLNPSTMD-VLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMG 108
Cdd:cd07125 41 ETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 109 KPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVF 188
Cdd:cd07125 121 KTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 189 KPAAETPLSALALAILAERAGIPDGLFSVLPTDNARmFGEEVCSNPVVKKLTFTGSTEVGRIL---MAQGAQKIMKLSLE 265
Cdd:cd07125 201 KPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEE-IGEALVAHPRIDGVIFTGSTETAKLInraLAERDGPILPLIAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 266 LGG-NApFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLIND 344
Cdd:cd07125 280 TGGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 345 EAVAKLYGHIdDAVTKGATVVVGGDRDARGGTFVQPTLLSGatKDMKVAREETFAPLAPV--FKFDTVEEVIELANDTEF 422
Cdd:cd07125 359 PAGKLLRAHT-ELMRGEAWLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPILHVirFKAEDLDEAIEDINATGY 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 423 GLAAYFFANDLRNVWKVTEALEYGMVGVN---TGLIsTELAPFGGVKQSGFG 471
Cdd:cd07125 436 GLTLGIHSRDEREIEYWRERVEAGNLYINrniTGAI-VGRQPFGGWGLSGTG 486
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
36-485 |
6.69e-67 |
|
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: 223.59 E-value: 6.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 36 RINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEA 114
Cdd:TIGR01237 47 KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 115 RGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAET 194
Cdd:TIGR01237 127 DAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 195 PLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVG-RI-----LMAQGAQKIMKLSLELGG 268
Cdd:TIGR01237 207 PVIAAKFVEILEEAGLPKGVVQFVPGSGSEV-GDYLVDHPKTSLITFTGSREVGtRIferaaKVQPGQKHLKRVIAEMGG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 269 NAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVA 348
Cdd:TIGR01237 286 KDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 349 KLYGHIDDAVTKGaTVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYF 428
Cdd:TIGR01237 366 KIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGV 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 429 FANDLRNVWKVTEALEYGMVGVN---TGLIsTELAPFGGVKQSGfgrEGSKYGMDDFLSM 485
Cdd:TIGR01237 445 ISNNRDHINRAKAEFEVGNLYFNrniTGAI-VGYQPFGGFKMSG---TDSKAGGPDYLAL 500
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-474 |
3.34e-66 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 221.55 E-value: 3.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAV 101
Cdd:PLN00412 19 YADGEWR-TSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 102 ILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYG-------DTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCR 174
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 175 KIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGStEVGrILMAQ 254
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCV-TGKGSEIGDFLTMHPGVNCISFTGG-DTG-IAISK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 255 GAQKImKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVldGF-E 333
Cdd:PLN00412 255 KAGMV-PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV--GPpE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 334 SGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDargGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEV 413
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 414 IELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLI-STELAPFGGVKQSGFGREG 474
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArGPDHFPFQGLKDSGIGSQG 470
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-488 |
1.51e-64 |
|
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: 217.06 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 8 LGRLKDQTLVREQMLVGGKWSSEGVNGTRINVLNPStmDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRK 87
Cdd:cd07083 8 LRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPS--EVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 88 FYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYG--DTIPGHQADKRLLVIkQPVGVVAAIAPW 165
Cdd:cd07083 86 AADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 166 NFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNArMFGEEVCSNPVVKKLTFTGST 245
Cdd:cd07083 165 NFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGE-EVGAYLTEHERIRGINFTGSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 246 EVGRILMAQGAQK------IMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKL 319
Cdd:cd07083 244 ETGKKIYEAAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 320 AMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGaTVVVGGDRDARGGTFVQPTLLSGATKDMKVAREETFA 399
Cdd:cd07083 324 LKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 400 PLAPV--FKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVN---TGLIsTELAPFGGVKQSGFG-RE 473
Cdd:cd07083 403 PVLSVirYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkiTGAL-VGVQPFGGFKLSGTNaKT 481
|
490
....*....|....*
gi 1229267232 474 GSKYGMDDFLSMKYV 488
Cdd:cd07083 482 GGPHYLRRFLEMKAV 496
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
77-482 |
2.13e-64 |
|
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: 214.70 E-value: 2.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 77 SAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEAR-GEIAYGASYIE--------WFgeEAKRVYgdtIPGHQADK 147
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDhalkhlkkWM--KPRRVS---VPLLLQPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 148 RLLVIKQPVGVVAAIAPWNFPsamVCRKIAP---ALASGCAIVFKPAAETPLSAlalailaerAGIPDGLFSVLPTDNAR 224
Cdd:cd07087 93 KAYVIPEPLGVVLIIGPWNYP---LQLALAPligAIAAGNTVVLKPSELAPATS---------ALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 225 MF--GEEVCsnpvvKKLT--------FTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRN 294
Cdd:cd07087 161 VVegGVEVA-----TALLaepfdhifFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 295 AGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESgATIGPLINDEAVAKLYGHIDDAvtkgaTVVVGGDRDaRG 374
Cdd:cd07087 236 AGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKES-PDYGRIINERHFDRLASLLDDG-----KVVIGGQVD-KE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 375 GTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGL 454
Cdd:cd07087 309 ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL 388
|
410 420 430
....*....|....*....|....*....|.
gi 1229267232 455 I---STELaPFGGVKQSGFGREGSKYGMDDF 482
Cdd:cd07087 389 LhaaIPNL-PFGGVGNSGMGAYHGKAGFDTF 418
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-488 |
8.99e-59 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 204.21 E-value: 8.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 1 MAISSTLLGRLKDQTlVREQM------LVGGKWSsEGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWA 74
Cdd:PLN02419 91 LALRSSWLSTSPEQS-TQPQMpprvpnLIGGSFV-ESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 75 KVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQ 154
Cdd:PLN02419 169 NTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIRE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 155 PVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfgEEVCSNP 234
Cdd:PLN02419 249 PLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV--NAICDDE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 235 VVKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIyVQSGIHDR 314
Cdd:PLN02419 327 DIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKS 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 315 FVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVTKGATVVVGGdRDA-----RGGTFVQPTLLSGATKD 389
Cdd:PLN02419 406 WEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDG-RDIvvpgyEKGNFIGPTILSGVTPD 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 390 MKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGL-ISTELAPFGGVKQS 468
Cdd:PLN02419 485 MECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKAS 564
|
490 500
....*....|....*....|..
gi 1229267232 469 GFGREG--SKYGMDDFLSMKYV 488
Cdd:PLN02419 565 FAGDLNfyGKAGVDFFTQIKLV 586
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
48-482 |
4.76e-57 |
|
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: 195.52 E-value: 4.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 48 LASLPSAgLAEVRASIDAAKASQKKWAKVSakersliMRKFYEEVVANAEDLAVILTSEMGKP-----LAE---ARGEIA 119
Cdd:cd07135 4 LDEIDSI-HSRLRATFRSGKTKDLEYRLWQ-------LKQLYWAVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 120 YGASYIEWFGEEAKRvyGDTIPGHQADKrLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSAL 199
Cdd:cd07135 76 HMLKNLKKWAKDEKV--KDGPLAFMFGK-PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 200 ALAILAERAgIPDGLFSVL----PTDNARM---FGeevcsnpvvkKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPF 272
Cdd:cd07135 153 LLAELVPKY-LDPDAFQVVqggvPETTALLeqkFD----------KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 273 IVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAmrvsalQVLDGF-ESGAT----IGPLINDEAV 347
Cdd:cd07135 222 IVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELK------KVLDEFyPGGANaspdYTRIVNPRHF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 348 AKLYGHIDDavTKGaTVVVGGDRDArGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAY 427
Cdd:cd07135 296 NRLKSLLDT--TKG-KVVIGGEMDE-ATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALY 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229267232 428 FFANDLRNVWKVTEALEYGMVGVNTGLISTEL--APFGGVKQSGFGREGSKYGMDDF 482
Cdd:cd07135 372 IFTDDKSEIDHILTRTRSGGVVINDTLIHVGVdnAPFGGVGDSGYGAYHGKYGFDTF 428
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-473 |
6.04e-57 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 197.36 E-value: 6.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWsseGVNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVI 102
Cdd:PLN02315 25 VGGEW---RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 103 LTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALAS 182
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 183 GCAIVFKPAAETP----LSALALAILAERAGIPDGLFSVLPtdNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQK 258
Cdd:PLN02315 182 GNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFC--GGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 259 IMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATI 338
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 339 GPLINDEAVAKLYGHIDDAVTKGATVVVGGDRDARGGTFVQPTLLSgATKDMKVAREETFAPLAPVFKFDTVEEVIELAN 418
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229267232 419 DTEFGLAAYFFANDLRNV--WKVTEALEYGMVGVNTGLISTEL-APFGGVKQSGFGRE 473
Cdd:PLN02315 419 SVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGRE 476
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
151-488 |
7.37e-55 |
|
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: 189.62 E-value: 7.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 151 VIKQPVGVVAAIAPWNFPSAMVcrkIAP---ALASGCAIVFKPAAETPLSALALAILAERAGIPDGL------------F 215
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVavvtggadvaaaF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 216 SVLPTDnarmfgeevcsnpvvkKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNA 295
Cdd:cd07133 174 SSLPFD----------------HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 296 GQTCVCANRIYVQSGIHDRFVEKLAMRVSALqvldgFESGAT---IGPLINDEAVAKLYGHIDDAVTKGATVV---VGGD 369
Cdd:cd07133 238 GQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-----YPTLADnpdYTSIINERHYARLQGLLEDARAKGARVIelnPAGE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 370 RDARGGTFVqPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVG 449
Cdd:cd07133 313 DFAATRKLP-PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVT 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1229267232 450 VNTGL--ISTELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07133 392 INDTLlhVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
151-486 |
1.24e-53 |
|
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: 186.94 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 151 VIKQPVGVVAAIAPWNFPSAMVcrkIAP---ALASG-CAIVfKPAAETPLSALALAILAERAgIPDGLFSVLPTDNArmf 226
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGnTAVL-KPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVE--- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 227 geevcsnpVVKKLT--------FTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQT 298
Cdd:cd07136 168 --------ENQELLdqkfdyifFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 299 CVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGaTIGPLINDEAVAKLYGHIDDavtkgATVVVGGDRDaRGGTFV 378
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDN-----GKIVFGGNTD-RETLYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 379 QPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTGLI--S 456
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlA 392
|
330 340 350
....*....|....*....|....*....|
gi 1229267232 457 TELAPFGGVKQSGFGREGSKYGMDDFLSMK 486
Cdd:cd07136 393 NPYLPFGGVGNSGMGSYHGKYSFDTFSHKK 422
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
79-494 |
2.12e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 187.16 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 79 KERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEA--------RGEIAYGASYIEwfgEEAKRVYGDTiPGHQADKRLL 150
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLLKHLD---EYLKPEKVDT-VGVFGPGKSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 151 VIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAgIPDGLFSVLPTDNarmfgeev 230
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGV-------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 231 csnPVVKKLT--------FTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCA 302
Cdd:PTZ00381 176 ---EVTTELLkepfdhifFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 303 NRIYVQSGIHDRFVEKLAmRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDavtKGATVVVGGDRD--ARggtFVQP 380
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALK-EAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDieNK---YVAP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 381 TLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNTG---LIST 457
Cdd:PTZ00381 326 TIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCvfhLLNP 405
|
410 420 430
....*....|....*....|....*....|....*..
gi 1229267232 458 ELaPFGGVKQSGFGREGSKYGMDDFLSMKYVCMGGIG 494
Cdd:PTZ00381 406 NL-PFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTG 441
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
39-487 |
4.99e-49 |
|
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: 175.87 E-value: 4.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTM-DVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGE 117
Cdd:TIGR01238 55 VTNPADRrDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 IAYGASYIEWFGEEAKrvygDTIPGHQAdkrllvikQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLS 197
Cdd:TIGR01238 135 VREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRIL---MAQGAQKIMKLSLELGGNAPFIV 274
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADV-GAALTSDPRIAGVAFTGSTEVAQLInqtLAQREDAPVPLIAETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 275 FDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHI 354
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 355 DDAVTKGATV---VVGGDRDARGGTFVQPTLLSgaTKDMKVAREETFAPLAPV--FKFDTVEEVIELANDTEFGLAAYFF 429
Cdd:TIGR01238 362 EHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVvrYKARELDQIVDQINQTGYGLTMGVH 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229267232 430 ANDLRNVWKVTEALEYGMVGVNTGLISTELA--PFGGVKQSGFG-REGSKYGMDDFLSMKY 487
Cdd:TIGR01238 440 SRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTGpKAGGPHYLYRLTQVQY 500
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
28-424 |
5.26e-48 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 178.13 E-value: 5.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 28 SSEGVNGTRINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKF---YEevvANAEDLAVIL 103
Cdd:PRK11905 560 AGGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAadlME---AHMPELFALA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 104 TSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYGDtiPGHQadkrllvikqPVGVVAAIAPWNFPSAMVCRKIAPALASG 183
Cdd:PRK11905 637 VREAGKTLANAIAEVREAVDFLRYYAAQARRLLNG--PGHK----------PLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 184 CAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnARMFGEEVCSNPVVKKLTFTGSTEVGRIL---MAQGAQKIM 260
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGD-GRTVGAALVADPRIAGVMFTGSTEVARLIqrtLAKRSGPPV 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 261 KLSLELGG-NApFIVFDDADLDQAVEGAMLSKFRNAGQTCvCANRI-YVQSGIHDRFVEKL--AMRvsALQVLDGFESGA 336
Cdd:PRK11905 784 PLIAETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDVADRVLTMLkgAMD--ELRIGDPWRLST 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 337 TIGPLINDEAVAKLYGHIDDAVTKGATV-VVGGDRDARGGTFVQPTLLS-GATKDMKvarEETFAPLAPV--FKFDTVEE 412
Cdd:PRK11905 860 DVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIEiDSISDLE---REVFGPVLHVvrFKADELDR 936
|
410
....*....|..
gi 1229267232 413 VIELANDTEFGL 424
Cdd:PRK11905 937 VIDDINATGYGL 948
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
31-424 |
5.07e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 169.22 E-value: 5.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 31 GVNGTRINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGK 109
Cdd:PRK11904 558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 110 PLAEARGEIAYGASYIEWFGEEAKRVYGD--TIPGHQADKRLLVIkQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIV 187
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRYYAAQARRLFGApeKLPGPTGESNELRL-HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVI 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 188 FKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGRIL---MAQGAQKIMKLSL 264
Cdd:PRK11904 717 AKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATV-GAALTADPRIAGVAFTGSTETARIInrtLAARDGPIVPLIA 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 265 ELGG-NApFIVFDDADLDQAVEGAMLSKFRNAGQTCvCANRI-YVQSGIHDRFVEKL--AMRvsALQVLDGFESGATIGP 340
Cdd:PRK11904 796 ETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRC-SALRVlFVQEDIADRVIEMLkgAMA--ELKVGDPRLLSTDVGP 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 341 LINDEAVAKLYGHIdDAVTKGATVVVGGD--RDARGGTFVQPTLLsgATKDMKVAREETFAPLAPV--FKFDTVEEVIEL 416
Cdd:PRK11904 872 VIDAEAKANLDAHI-ERMKREARLLAQLPlpAGTENGHFVAPTAF--EIDSISQLEREVFGPILHVirYKASDLDKVIDA 948
|
....*...
gi 1229267232 417 ANDTEFGL 424
Cdd:PRK11904 949 INATGYGL 956
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
85-490 |
3.84e-42 |
|
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: 155.84 E-value: 3.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 85 MRKFYEEvvaNAEDLAVILTSEMGKPLAEA--------RGEIAYGASYI-EWfgeeAKRVYGDTIPGHQADkRLLVIKQP 155
Cdd:cd07132 29 LLRMLEE---NEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpEW----MKPEPVKKNLATLLD-DVYIYKEP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 156 VGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSalalailaerAGIpdgLFSVLPT--DNaRMFgeevcsn 233
Cdd:cd07132 101 LGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPAT----------AKL---LAELIPKylDK-ECY------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 234 PVV-------KKLT--------FTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQT 298
Cdd:cd07132 160 PVVlggveetTELLkqrfdyifYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 299 CVCANRIYVQSGIHDRFVEKLAmrvsalQVLDGF------ESgATIGPLINDEAVAKLYGHIddavtKGATVVVGGDRDA 372
Cdd:cd07132 240 CIAPDYVLCTPEVQEKFVEALK------KTLKEFygedpkES-PDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 373 rGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEALEYGMVGVNT 452
Cdd:cd07132 308 -KERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVND 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1229267232 453 GL--ISTELAPFGGVKQSGFGREGSKYGMDDFlSMKYVCM 490
Cdd:cd07132 387 TImhYTLDSLPFGGVGNSGMGAYHGKYSFDTF-SHKRSCL 425
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
22-424 |
2.40e-40 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 155.48 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGkwssEGVNGTRINVLNPSTM-DVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKF---YEevvANAE 97
Cdd:COG4230 561 LIAG----EAASGEARPVRNPADHsDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAadlLE---AHRA 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 98 DLAVILTSEMGKPLAEARGEI--A------YGAsyiewfgeEAKRVYGDTIPGHqadkrllvikqPVGVVAAIAPWNFPS 169
Cdd:COG4230 634 ELMALLVREAGKTLPDAIAEVreAvdfcryYAA--------QARRLFAAPTVLR-----------GRGVFVCISPWNFPL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 170 AMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVGR 249
Cdd:COG4230 695 AIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETV-GAALVADPRIAGVAFTGSTETAR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 250 ILMAQGAQK---IMKLSLELGG-NApFIVFDDADLDQAVEGAMLSKFRNAGQTCvCANRI-YVQSGIHDRFVEKL--AMR 322
Cdd:COG4230 774 LINRTLAARdgpIVPLIAETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRC-SALRVlCVQEDIADRVLEMLkgAMA 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 323 vsALQVldgfesG-----AT-IGPLINDEAVAKLYGHIDDAVTKGATV-VVGGDRDARGGTFVQPTL--LSGAtKDMKva 393
Cdd:COG4230 852 --ELRV------GdpadlSTdVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLieIDSI-SDLE-- 920
|
410 420 430
....*....|....*....|....*....|...
gi 1229267232 394 rEETFAPLAPV--FKFDTVEEVIELANDTEFGL 424
Cdd:COG4230 921 -REVFGPVLHVvrYKADELDKVIDAINATGYGL 952
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
3-471 |
3.29e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 155.13 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 3 ISSTLLgRLKDQTLVREQMLVGgkwssEGVNGTRINVLNPS-TMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKER 81
Cdd:PRK11809 633 LSSALL-ASAHQKWQAAPMLED-----PVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAER 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 82 SLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKRVYG-DTipgHQadkrllvikqPVGVVA 160
Cdd:PRK11809 707 AAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDnDT---HR----------PLGPVV 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 161 AIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnarmfGEEV----CSNPVV 236
Cdd:PRK11809 774 CISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGR-----GETVgaalVADARV 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 237 KKLTFTGSTEVGRILM--------AQGaqKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCvCANRIY-V 307
Cdd:PRK11809 849 RGVMFTGSTEVARLLQrnlagrldPQG--RPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRC-SALRVLcL 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 308 QSGIHDRFVEKL--AMRVSALQVLDGFESgaTIGPLINDEAVAKLYGHIDDAVTKGATV---VVGGDRDARGGTFVQPTL 382
Cdd:PRK11809 926 QDDVADRTLKMLrgAMAECRMGNPDRLST--DIGPVIDAEAKANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVPPTL 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 383 LS-GATKDMKvarEETFAPLAPV--FKFDTVEEVIELANDTEFGLAayfFANDLR---NVWKVTEALEYGMVGVNTGLIS 456
Cdd:PRK11809 1004 IElDSFDELK---REVFGPVLHVvrYNRNQLDELIEQINASGYGLT---LGVHTRideTIAQVTGSAHVGNLYVNRNMVG 1077
|
490
....*....|....*..
gi 1229267232 457 TELA--PFGGVKQSGFG 471
Cdd:PRK11809 1078 AVVGvqPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
8-469 |
4.69e-40 |
|
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: 151.59 E-value: 4.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 8 LGRLKDQTlVREQMLVGGKwssEGVNGTRINVLNPST-MDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMR 86
Cdd:cd07123 23 LAELKSLT-VEIPLVIGGK---EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 87 KfyeevvanAEDL------AVILTSEM---GKPLAEArgEIAYGASYIEWF---GEEAKRVYGDTIPGHQADKRLLVIKQ 154
Cdd:cd07123 99 K--------AADLlsgkyrYELNAATMlgqGKNVWQA--EIDAACELIDFLrfnVKYAEELYAQQPLSSPAGVWNRLEYR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 155 PV-GVVAAIAPWNFPSAMVCRKIAPALAsGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDnARMFGEEVCSN 233
Cdd:cd07123 169 PLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD-GPVVGDTVLAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 234 PVVKKLTFTGSTEVGRILMAQGAQKIM------KLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYV 307
Cdd:cd07123 247 PHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 308 QSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIDDAVT-KGATVVVGGDRDARGGTFVQPTLLsgA 386
Cdd:cd07123 327 PESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTVI--E 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 387 TKDMKVA--REETFAPLAPVFKFD--TVEEVIELANDT-EFGLAAYFFANDLRNVWKVTEALEY--GMVGVN---TGLIS 456
Cdd:cd07123 405 TTDPKHKlmTEEIFGPVLTVYVYPdsDFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRNaaGNFYINdkpTGAVV 484
|
490
....*....|...
gi 1229267232 457 TElAPFGGVKQSG 469
Cdd:cd07123 485 GQ-QPFGGARASG 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
56-488 |
1.29e-39 |
|
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: 148.33 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 56 LAEVRASIDAAKASQKKWakvsakeRSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEA-RGEIAYGASYI--------E 126
Cdd:cd07137 5 VRELRETFRSGRTRSAEW-------RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 127 WFGEEAKRVYGDTIPGHQAdkrllVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSAlalailae 206
Cdd:cd07137 78 WMAPEKVKTPLTTFPAKAE-----IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 207 rAGIPDGLFSVLPTDNARMFGEEVCSNPVV-----KKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLD 281
Cdd:cd07137 145 -ALLAKLIPEYLDTKAIKVIEGGVPETTALleqkwDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 282 QAVEGAMLSKF-RNAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGaTIGPLINDEAVAKLYGHIDDAVTK 360
Cdd:cd07137 224 VAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 361 gATVVVGGDRDARgGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVT 440
Cdd:cd07137 303 -DKIVHGGERDEK-NLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229267232 441 EALEYGMVGVNTGLISTELA--PFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:cd07137 381 AETSSGGVTFNDTVVQYAIDtlPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
56-488 |
6.68e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 136.39 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 56 LAEVRASIDAAKASQKKWAKVSakersliMRKFYEEVVANAEDLAVILTSEMGKPLAEA-RGEIAYGASYI--------E 126
Cdd:PLN02203 12 VAELRETYESGRTRSLEWRKSQ-------LKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVGVLTKSAnlalsnlkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 127 WFGEEAKRVYGDTIPGhqadkRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAilae 206
Cdd:PLN02203 85 WMAPKKAKLPLVAFPA-----TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 207 rAGIPDGLFS--VLPTDNARMFGEEVCSNPVvKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIV--FDDA-DLD 281
Cdd:PLN02203 156 -ANIPKYLDSkaVKVIEGGPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 282 QAVEGAMLSKFRN-AGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESGaTIGPLINDEAVAKLYGHIDDAVTK 360
Cdd:PLN02203 234 VAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 361 gATVVVGGDRDARgGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVT 440
Cdd:PLN02203 313 -ASIVHGGSIDEK-KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRIL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229267232 441 EALEYGMVGVNTGLI--STELAPFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:PLN02203 391 SETSSGSVTFNDAIIqyACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
56-488 |
3.00e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 120.15 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 56 LAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANaedlaviLTSEMGKPLAEA--------RGEIAYGASYIE- 126
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAA-------LRDDLGKPELESsvyevsllRNSIKLALKQLKn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 127 WFGEEAKRVYGDTIPGHQAdkrllVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAE 206
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 207 RAGIPDGLFSV--LPTDNARMFGEEVcsnpvvKKLTFTGSTEVGRILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAV 284
Cdd:PLN02174 164 QYLDSSAVRVVegAVTETTALLEQKW------DKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 285 EGAMLSKFR-NAGQTCVCANRIYVQSGIHDRFVEKLAMRVSALQVLDGFESgATIGPLINDEAVAKLYGHIDDAVTKGaT 363
Cdd:PLN02174 238 RRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES-KDMSRIVNSTHFDRLSKLLDEKEVSD-K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 364 VVVGGDRDaRGGTFVQPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFANDLRNVWKVTEAL 443
Cdd:PLN02174 316 IVYGGEKD-RENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1229267232 444 EYGMVGVNTglISTELA----PFGGVKQSGFGREGSKYGMDDFLSMKYV 488
Cdd:PLN02174 395 SAGGIVVND--IAVHLAlhtlPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-461 |
2.73e-24 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 105.01 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 59 VRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEArGEIAYGASYIEWFgeeAKRVYGD 138
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRAR---AFVIYSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 139 TIPGHQADKRLLVIKQ-------PVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGI- 210
Cdd:cd07084 77 RIPHEPGNHLGQGLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 211 PDGLFSVLPTDNARMFGeeVCSNPVVKKLTFTGSTEVGRILMAQGAQkiMKLSLELGGNAPFIVFDDAD-----LDQAVE 285
Cdd:cd07084 157 PPEDVTLINGDGKTMQA--LLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQavdyvAWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 286 GAMLSkfrnAGQTCVCANRIYVQSGIHDR-FVEKLAMRVSALQVldgfeSGATIGPLINDEA---VAKLYGHIDDAVTKG 361
Cdd:cd07084 233 DMTAC----SGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKL-----EDLLLGPVQTFTTlamIAHMENLLGSVLLFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 362 ATVVVGGDRDARGGTFVQPTLL---SGATKDMKVAREETFAPLAPVFKF--DTVEEVIELANDTEFGLAAYFFANDLRNV 436
Cdd:cd07084 304 GKELKNHSIPSIYGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFL 383
|
410 420
....*....|....*....|....*
gi 1229267232 437 WKVTEALEYGMVGVNTGLISTELAP 461
Cdd:cd07084 384 QELIGNLWVAGRTYAILRGRTGVAP 408
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-449 |
1.02e-19 |
|
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: 91.45 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 59 VRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASYIEWFGEEAKR--VY 136
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 137 GDTI--------PGHQADKRLLviKQPVGVVAAIAPWNFPSAmvcrkI-------APALASGCAIVFK--PA--AETPLS 197
Cdd:cd07129 81 DARIdpadpdrqPLPRPDLRRM--LVPLGPVAVFGASNFPLA-----FsvaggdtASALAAGCPVVVKahPAhpGTSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 198 ALALAILAERAGIPDGLFSVLpTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQK---ImKLSLELGGNAPFIV 274
Cdd:cd07129 154 ARAIRAALRATGLPAGVFSLL-QGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepI-PFYAELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 275 FDDA------DLDQAVEGAMLskfRNAGQTCVCANRIYVQSGIH-DRFVEKLAMRVSALQ--------VLDGFESGatig 339
Cdd:cd07129 232 LPGAlaergeAIAQGFVGSLT---LGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPaqtmltpgIAEAYRQG---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 340 plindeaVAKLYGHiddavtKGATVVVGGDRDARGGTfVQPTLL--SGAT-KDMKVAREETFAPLAPVFKFDTVEEVIEL 416
Cdd:cd07129 305 -------VEALAAA------PGVRVLAGGAAAEGGNQ-AAPTLFkvDAAAfLADPALQEEVFGPASLVVRYDDAAELLAV 370
|
410 420 430
....*....|....*....|....*....|....*
gi 1229267232 417 ANDTEFGLAA--YFFANDLRNVWKVTEALEYgMVG 449
Cdd:cd07129 371 AEALEGQLTAtiHGEEDDLALARELLPVLER-KAG 404
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
23-432 |
1.50e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 88.22 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 23 VGGKWSsEGvNGTRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVI 102
Cdd:PRK11903 9 VAGRWQ-AG-SGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 103 LTSEMGKPLAEAR----GEIAYGASYIEWfgeeakrvyGDTIpghqADKRLLVIKQPV------------------GVVA 160
Cdd:PRK11903 87 ATANSGTTRNDSAvdidGGIFTLGYYAKL---------GAAL----GDARLLRDGEAVqlgkdpafqgqhvlvptrGVAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 161 AIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGI-PDGLFSVLPTDNARMFgEEVCSNPVVkkl 239
Cdd:PRK11903 154 FINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLL-DHLQPFDVV--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 240 TFTGSTEVGRILMAQGA--QKIMKLSLE---------LGGNAPfivfDDADLDQAVEGAMLSKFRNAGQTCVCANRIYVQ 308
Cdd:PRK11903 230 SFTGSAETAAVLRSHPAvvQRSVRVNVEadslnsallGPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 309 SGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIdDAVTKGATVVVGG------DRDARGGTFVQPTL 382
Cdd:PRK11903 306 EALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGggfalvDADPAVAACVGPTL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229267232 383 L--SGATKDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:PRK11903 385 LgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
157-432 |
9.69e-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: 85.78 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 157 GVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGI-PDGLFSVLPTDNARMFgEEVCSNPV 235
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLL-DHLGEQDV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 236 VkklTFTGSTEVGRIL------MAQGAQKIMKL-SLELGGNAPFIVFDDADLD---QAVEGAMLSKfrnAGQTCVCANRI 305
Cdd:cd07128 225 V---AFTGSAATAAKLrahpniVARSIRFNAEAdSLNAAILGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 306 YVQSGIHDRFVEKLAMRVSALQVLDGFESGATIGPLINDEAVAKLYGHIdDAVTKGATVVVGG-------DRDARGGTFV 378
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGpdrfevvGADAEKGAFF 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229267232 379 QPTLLSGATKDMKVAREET--FAPLAPVFKFDTVEEVIELANDTEFGLAAYFFAND 432
Cdd:cd07128 378 PPTLLLCDDPDAATAVHDVeaFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
57-424 |
8.78e-10 |
|
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: 60.71 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 57 AEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSE--MGKP---LAEARGeIAYGASYIEWFGEE 131
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGRVedkIAKNHL-AAEKTPGTEDLTTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 132 AkrVYGDtipghqaDKRLLVIKQPVGVVAAIAPWNFPSA-MVCRKIApALASGCAIVFKP----AAETPLSALALAILAE 206
Cdd:cd07121 83 A--WSGD-------NGLTLVEYAPFGVIGAITPSTNPTEtIINNSIS-MLAAGNAVVFNPhpgaKKVSAYAVELINKAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 207 RAGIPDGLFSVL--PT-DNArmfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKImklslelG---GNAPFIVFDDADL 280
Cdd:cd07121 153 EAGGPDNLVVTVeePTiETT----NELMAHPDINLLVVTGGPAVVKAALSSGKKAI-------GagaGNPPVVVDETADI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 281 DQA----VEGAmlsKFRNaGQTCVCANRIYVQSGIHDRFVEKL----AMRVSALQVLDGFESGATI--GPLINDEAVAKL 350
Cdd:cd07121 222 EKAardiVQGA---SFDN-NLPCIAEKEVIAVDSVADYLIAAMqrngAYVLNDEQAEQLLEVVLLTnkGATPNKKWVGKD 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 351 YGHIDDAvtkgATVVVGGDrdarggtfvqPTLLSGAT-KDMKVAREETFAPLAPVFKFDTVEEVIELANDTEFGL 424
Cdd:cd07121 298 ASKILKA----AGIEVPAD----------IRLIIVETdKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGN 358
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
22-440 |
4.21e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 58.66 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 22 LVGGKW--SSEgvngtRINVLNPSTMDVLASLPSAGLAEVRASIDAAKASQKKWAKVSAK--ERSLI-----MRKFYEEV 92
Cdd:cd07126 2 LVAGKWkgASN-----YTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERYLLygdvsHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 93 VANAEDLAVILTSE-MGKPLAEARGEIAYGASYIEWFGEEAKRVY--GDTIPGHQADKRLLVIKQPVGVVAAIAPWNFPS 169
Cdd:cd07126 77 KPEVEDFFARLIQRvAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 170 AMVCRKIAPALASGCAIVFKPAAETPLSALALAILAERAGIPDGLFSVLPTDNARMfgEEVCSNPVVKKLTFTGSTEVGR 249
Cdd:cd07126 157 EIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTM--NKILLEANPRMTLFTGSSKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 250 ilmaqgaqkimKLSLELGGNapfIVFDDADLDQAVEGAMLSKF--------RNA----GQTC-----VCANRIYVQSGIH 312
Cdd:cd07126 235 -----------RLALELHGK---VKLEDAGFDWKILGPDVSDVdyvawqcdQDAyacsGQKCsaqsiLFAHENWVQAGIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 313 DRfVEKLAMRVSaLQVLdgfesgaTIGPLI--NDEAVAKlygHIDD-AVTKGATVVVGGdRDARGGTF------VQPTLL 383
Cdd:cd07126 301 DK-LKALAEQRK-LEDL-------TIGPVLtwTTERILD---HVDKlLAIPGAKVLFGG-KPLTNHSIpsiygaYEPTAV 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229267232 384 ------SGATKDMKVAREETFAPLAPVFKFDTVEE--VIELANDTEFGLAAYFFANDLRNVWKVT 440
Cdd:cd07126 368 fvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVL 432
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
61-322 |
1.07e-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: 57.28 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 61 ASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAE-------ARGEIAYGAsyieWFGEEAK 133
Cdd:cd07081 3 DAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNV----YKDEKTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 134 RVYGDTIPGhqadkRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFK--PAAE--TPLSALALAILAERAG 209
Cdd:cd07081 79 GVLTGDENG-----GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSphPRAKkvTQRAATLLLQAAVAAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 210 IPDGLFSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEvgrilMAQGAQKIMKLSLELG-GNAPFIVFDDADLDQAVEGAM 288
Cdd:cd07081 154 APENLIGWIDNPSIEL-AQRLMKFPGIGLLLATGGPA-----VVKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVQSIV 227
|
250 260 270
....*....|....*....|....*....|....
gi 1229267232 289 LSKFRNAGQTCVCANRIYVQSGIHDRFVEKLAMR 322
Cdd:cd07081 228 KSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQ 261
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
39-424 |
1.55e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.83 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 39 VLNPSTMDVLASLPSAGL-AEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGE 117
Cdd:PRK15398 17 MLSSQTVSPPAAVGEMGVfASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 118 ----IAYGASYIEWFGEEAkrVYGDtipghqaDKRLLVIKQPVGVVAAIAPWNFPSA-MVCRKIApALASGCAIVFKP-- 190
Cdd:PRK15398 97 knvaAAEKTPGVEDLTTEA--LTGD-------NGLTLIEYAPFGVIGAVTPSTNPTEtIINNAIS-MLAAGNSVVFSPhp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 191 --AAETPLSALALAILAERAGIPDGLFSVL--PT-DNArmfgEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKImklsle 265
Cdd:PRK15398 167 gaKKVSLRAIELLNEAIVAAGGPENLVVTVaePTiETA----QRLMKHPGIALLVVTGGPAVVKAAMKSGKKAI------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 266 lG---GNAPFIVFDDADLDQA----VEGAmlsKFRNaGQTCVCANRIYVQSGIHDRFVEKLAmrvsalqvldgfESGATi 338
Cdd:PRK15398 237 -GagaGNPPVVVDETADIEKAardiVKGA---SFDN-NLPCIAEKEVIVVDSVADELMRLME------------KNGAV- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 339 gpLINDEAVAKLyghiDDAVTKGATVV----VGgdRDAR-----GGTFV--QPTLLSGAT-KDMKVAREETFAPLAPVFK 406
Cdd:PRK15398 299 --LLTAEQAEKL----QKVVLKNGGTVnkkwVG--KDAAkileaAGINVpkDTRLLIVETdANHPFVVTELMMPVLPVVR 370
|
410
....*....|....*...
gi 1229267232 407 FDTVEEVIELANDTEFGL 424
Cdd:PRK15398 371 VKDVDEAIALAVKLEHGN 388
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
56-451 |
4.57e-08 |
|
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: 55.56 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 56 LAEVRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLA--VILTS--------EMGKPLAEARG--EIAYGAs 123
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAhaVMHTTgqafmmafQAGGPHAQDRGleAVAYAW- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 124 yiewfgEEAKRVYGDTI---PGHQAD-----KRLLVIkqPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKP--AAE 193
Cdd:cd07127 162 ------REMSRIPPTAEwekPQGKHDplameKTFTVV--PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPhpAAI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 194 TPLSALALAILA--ERAGIPDGLFSVLPTDNARMFGEEVCSNPVVKKLTFTGSTEVGRILMAQGAQKimKLSLELGGNAP 271
Cdd:cd07127 234 LPLAITVQVAREvlAEAGFDPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQA--QVYTEKAGVNT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 272 FIVFDDADLDQAVEGAMLSKFRNAGQTCVCANRIYV-QSGIHDR-----FVEKLAMRVSALQVL--DGFESGATIGPLIN 343
Cdd:cd07127 312 VVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIQTDdgrksFDEVAADLAAAIDGLlaDPARAAALLGAIQS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 344 DEAVAKlyghIDDAVTKGATVVVGGDR------DARGGTfvqPTLLSGATKDMKVAREETFAPLAPVFKFDTVEEVIELA 417
Cdd:cd07127 392 PDTLAR----IAEARQLGEVLLASEAVahpefpDARVRT---PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
410 420 430
....*....|....*....|....*....|....*..
gi 1229267232 418 NDT--EFG-LAAYFFANDLRNVWKVTEAleYGMVGVN 451
Cdd:cd07127 465 RESvrEHGaMTVGVYSTDPEVVERVQEA--ALDAGVA 499
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
59-319 |
1.34e-07 |
|
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: 53.65 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 59 VRASIDAAKASQKKWAKVSAKERSLIMRKFYEEVVANAEDLAVILTSEMGKPLAEARGEIAYGASyiEWFGEEAKRVYGD 138
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFAS--EYVYNDIKDMKTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 139 TIPGHQADKRLLVIKQPVGVVAAIAPWNFPSAMVCRKIAPALASGCAIVFKP---AAETPLSALAL-AILAERAGIPDGL 214
Cdd:cd07122 79 GVIEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 215 FSVLPTDNARMfGEEVCSNPVVKKLTFTGSTEvgrilMAQGAQKIMKLSLELG-GNAPFIVFDDADLDQAVEGAMLSK-F 292
Cdd:cd07122 159 IQWIEEPSIEL-TQELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKtF 232
|
250 260
....*....|....*....|....*....
gi 1229267232 293 RNAgqtCVCA--NRIYVQSGIHDRFVEKL 319
Cdd:cd07122 233 DNG---TICAseQSVIVDDEIYDEVRAEL 258
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
59-328 |
1.54e-05 |
|
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: 47.22 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 59 VRASIDAAKASQKKWAKVSAKERslimRKFYEEVVANAEDLAVILTSEMGKPLAEARGeiAYGASyiewfgeeaKRVYGD 138
Cdd:cd07077 22 INAIANALYDTRQRLASEAVSER----GAYIRSLIANWIAMMGCSESKLYKNIDTERG--ITASV---------GHIQDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 139 TIPghqADKRLLVIKQPVGVVAAIAPWNFPSAMVcRKIAPALASGCAIVFKPAAETPLSALALAILAERA---GIPDGLF 215
Cdd:cd07077 87 LLP---DNGETYVRAFPIGVTMHILPSTNPLSGI-TSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229267232 216 SVLPTDNARMfGEEVCSNPVVKKLTFTGSTEVgrILMAQGAQKIMKLSLELGGNAPFIVFDDADLDQAVEGAMLSKFRNa 295
Cdd:cd07077 163 LYVPHPSDEL-AEELLSHPKIDLIVATGGRDA--VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD- 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1229267232 296 GQTCVCANRIYVQSGIHDRFVE--KLAMRVSALQV 328
Cdd:cd07077 239 QNACASEQNLYVVDDVLDPLYEefKLKLVVEGLKV 273
|
|
| |
