|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
49-503 |
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: 806.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPL 208
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 209 TALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFD 288
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGS-PAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 289 SADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVED 368
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 369 ARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQ 448
Cdd:cd07103 318 AVAKGAKVLTGGKRLGLGG-YFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 449 VFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
24-507 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 724.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 24 SALVQDKALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKL 103
Cdd:PLN02278 20 AGLLRTQGLIGGKWTDAYDGK-TFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 104 IEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAM 183
Cdd:PLN02278 97 IIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 184 ITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLL 263
Cdd:PLN02278 177 ITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGD-APEIGDALLASPKVRKITFTGSTAVGKKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 264 FRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDG 343
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 344 QGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGT-FYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
....
gi 21356737 504 GNLK 507
Cdd:PLN02278 495 GNMN 498
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
28-503 |
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: 662.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 28 QDKALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQH 107
Cdd:COG1012 5 EYPLFIGGEWVAAASGE-TFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 108 SQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRK 187
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 188 AGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNS 267
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGD-GSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 268 ADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCD 347
Cdd:COG1012 241 AENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 348 VQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAV 427
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356737 428 KKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA-AEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
49-499 |
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: 641.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAF--KTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPL 208
Cdd:TIGR01780 79 EILYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 209 TALAVAKLAVDAGIPKGVINVVTTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFD 288
Cdd:TIGR01780 159 SALALARLAEQAGIPKGVLNVITGSRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 289 SADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVED 368
Cdd:TIGR01780 239 DADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 369 ARSKKANIILGGQpLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQ 448
Cdd:TIGR01780 319 AVEKGAKVVTGGK-RHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 21356737 449 VFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:TIGR01780 398 IWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
37-501 |
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: 611.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 37 WVDSSNAkaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMT 116
Cdd:pfam00171 1 WVDSESE--TIEVINPATGEVIATVPAATAEDVDAAIAAARAAF--PAWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 117 AESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSaSPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGC 196
Cdd:pfam00171 77 LENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 197 TVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTnKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICL 276
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTG-SGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 277 ELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINE 356
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 357 MQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRG 436
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNG-YFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356737 437 LAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAE-APFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
24-504 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 594.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 24 SALVQDKALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKL 103
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGE-VIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 104 IEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAM 183
Cdd:PRK11241 83 MMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 184 ITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLL 263
Cdd:PRK11241 163 ITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVV-TGSAGAVGGELTSNPLVRKLSFTGSTEIGRQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 264 FRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDG 343
Cdd:PRK11241 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 344 QGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGN-FFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
.
gi 21356737 504 G 504
Cdd:PRK11241 481 G 481
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
70-503 |
0e+00 |
|
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: 544.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 70 QKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYG 149
Cdd:cd07078 1 DAAVAAARAAF--KAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 150 EIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINV 229
Cdd:cd07078 79 EVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 230 VTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQ 309
Cdd:cd07078 159 VTGD-GDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 310 TCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSL 389
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 390 FYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIIS 469
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 21356737 470 A-AEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07078 398 AePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
33-501 |
1.39e-175 |
|
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: 502.18 E-value: 1.39e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07088 2 INGEFVPSSSGE-TIDVLNPATGEVVATVPAATAEDADRAVDAAEAA--QKAWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAAL 192
Cdd:cd07088 79 KLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 193 AAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIK 272
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVT-GRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 273 RICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGP 352
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 353 LINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKAND 432
Cdd:cd07088 318 LVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 433 TRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
49-499 |
9.21e-174 |
|
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: 497.07 E-value: 9.21e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPL 208
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 209 TALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFD 288
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVV-TGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 289 SADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVED 368
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 369 ARSKKANIILGGQPLP----DKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSE 444
Cdd:cd07114 320 AREEGARVLTGGERPSgadlGAGY-FFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 445 NLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
49-503 |
4.18e-166 |
|
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: 477.44 E-value: 4.18e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESK- 127
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAF--PGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 128 GEVAYGNAFVEWFAEEARRIYGEIVPSAsPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTP 207
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 208 LTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVF 287
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGF-GPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVE 367
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 368 DARSKKANIILGGQPLPD---KGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSE 444
Cdd:cd07093 317 LARAEGATILTGGGRPELpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 445 NLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
33-501 |
1.58e-163 |
|
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: 472.18 E-value: 1.58e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNaKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07119 2 IDGEWVEAAS-GKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSAsPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAAL 192
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 193 AAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIK 272
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVT-GSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 273 RICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGP 352
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 353 LINEMQFNKVSGFVEDARSKKANIILGGQPLPDKG---SLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKK 429
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDElakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356737 430 ANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
27-499 |
1.52e-160 |
|
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: 464.37 E-value: 1.52e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 27 VQDKALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQ 106
Cdd:cd07091 2 QPTGLFINNEFVDSVSGK-TFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 107 HSQEIAEIMTAESGKPINES-KGEVAYGNAFVEWFAEEARRIYGEIVPSaSPNREIIVMKQPIGVAALITPWNFPMAMIT 185
Cdd:cd07091 81 DRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPI-DGNFLAYTRREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 186 RKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFR 265
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVP-GFGPTAGAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 266 NSAD-GIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:cd07091 239 AAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKG-YFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
49-501 |
1.59e-159 |
|
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: 460.46 E-value: 1.59e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAF--PGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGnafVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPL 208
Cdd:cd07106 79 EVGGA---VAWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 209 TALAVAKLAVDAgIPKGVINVVTTnkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFD 288
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG--GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 289 SADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVED 368
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 369 ARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQ 448
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPG-YFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 21356737 449 VFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
33-501 |
2.55e-158 |
|
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: 458.12 E-value: 2.55e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNaKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07138 3 IDGAWVAPAG-TETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGEIVPSASpnreiIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:cd07138 80 QAITLEMGAPITLARAaQVGLGIGHLRAAADALKDFEFEERRGNS-----LVVREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGI 271
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVN-GDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 272 KRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIG 351
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 352 PLINEMQFNKVSGFVEDARSKKANIILGGQPLP---DKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVK 428
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPeglERG-YFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356737 429 KANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNeGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
45-501 |
5.41e-156 |
|
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: 452.06 E-value: 5.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 45 ATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPIN 124
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 125 ESKGEVAYGNA-FVEWFAEEARRIYGEIVPSAsPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPS 203
Cdd:cd07112 82 DALAVDVPSAAnTFRWYAEAIDKVYGEVAPTG-PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 204 EDTPLTALAVAKLAVDAGIPKGVINVVT-TNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADG-IKRICLELGGN 281
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPgFGHTA--GEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 282 APFIVF-DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFN 360
Cdd:cd07112 239 SPNIVFaDAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 361 KVSGFVEDARSKKANIILGGQP-LPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAG 439
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 440 YFYSENLQQVFRVAKRLEVGMVGVN---EGIISaaeAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNcfdEGDIT---TPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
32-499 |
1.86e-154 |
|
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: 448.72 E-value: 1.86e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSNAKaTFEVRNPANGA-VIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQE 110
Cdd:cd07131 2 YIGGEWVDSASGE-TFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 111 IAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGA 190
Cdd:cd07131 79 LARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADG 270
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVV-HGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQI 350
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSL---FYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAV 427
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEkgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356737 428 KKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA-AEAPFGGVKESGVG-REGSKHGIDDYVDIK 499
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAeVHLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
47-503 |
6.32e-154 |
|
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: 446.39 E-value: 6.32e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 47 FEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDT 206
Cdd:cd07150 79 WFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 207 PLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIV 286
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGG-GAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 287 FDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFV 366
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 367 EDARSKKANIILGGQplpdKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENL 446
Cdd:cd07150 318 EDAVAKGAKLLTGGK----YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 447 QQVFRVAKRLEVGMVGVNEG-IISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPtILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
68-501 |
3.10e-151 |
|
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: 438.89 E-value: 3.10e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 68 DAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRI 147
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 YGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLT-ALAVAKLAVDAGIPKGV 226
Cdd:cd07104 79 EGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 227 INVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRN 306
Cdd:cd07104 159 LNVVPGG-GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 307 CGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPlpdK 386
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---E 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 387 GsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEG 466
Cdd:cd07104 315 G-LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 21356737 467 -IISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07104 394 tVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
49-501 |
3.34e-151 |
|
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: 439.76 E-value: 3.34e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWrSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPI-NESK 127
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 128 GEVAYGNAFVEWFAEEARRIYGEIVPSASPNREI----IVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPS 203
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 204 EDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAP 283
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNA-VGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 284 FIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVS 363
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 364 GFVEDARSKKANIILGGQPLP--DKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYF 441
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKG-FYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 442 YSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
50-501 |
1.98e-150 |
|
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: 437.54 E-value: 1.98e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 50 RNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGE 129
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 130 VAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLT 209
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 210 ALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDS 289
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVT-GYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 290 ADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDA 369
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 370 RSKKANIILGGQPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQV 449
Cdd:cd07118 321 RAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 21356737 450 FRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
32-499 |
1.42e-149 |
|
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: 436.30 E-value: 1.42e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSnakATFEVRNPAN-GAVIGKVPNMTVADAQKAIDAAKQAYEskEWRSLTAKDRSNLLKKWHKLIEQHSQE 110
Cdd:cd07097 4 YIDGEWVAGG---DGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFP--AWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 111 IAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGA 190
Cdd:cd07097 79 LARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADG 270
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLV-MGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQI 350
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKVSGFVEDARSKKANIILGGQPL--PDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVK 428
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEG-YYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356737 429 KANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNegiISAAE----APFGGVKESGVG-REGSKHGIDDYVDIK 499
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN---LPTAGvdyhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
47-503 |
5.45e-149 |
|
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: 433.95 E-value: 5.45e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 47 FEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGA--KEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEVAYGNAFVEWFAEEARRIYGEIVP-SASP---NREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKP 202
Cdd:cd07149 79 RKEVDRAIETLRLSAEEAKRLAGETIPfDASPggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 203 SEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSadGIKRICLELGGNA 282
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVT-GSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 283 PFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKV 362
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 363 SGFVEDARSKKANIILGGQPlpdKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFY 442
Cdd:cd07149 316 EEWVEEAVEGGARLLTGGKR---DGA-ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356737 443 SENLQQVFRVAKRLEVGMVGVNEGIISAAEA-PFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
74-503 |
2.57e-148 |
|
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: 428.96 E-value: 2.57e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 74 DAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVP 153
Cdd:cd06534 1 AAARAAF--KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 154 SASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTN 233
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 234 kAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVS 313
Cdd:cd06534 159 -GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 314 ANRFFVQDSVYDKFVGQLKkrvealkigdgqgcdvqigplinemqfnkvsgfvedarskkaniilggqplpdkgslfyap 393
Cdd:cd06534 238 ASRLLVHESIYDEFVEKLV------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 394 TIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA-AE 472
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 21356737 473 APFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
49-501 |
2.03e-146 |
|
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: 427.13 E-value: 2.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESK- 127
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 128 GEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTP 207
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 208 LTALAVAKLAVDaGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVF 287
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGG-GASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVE 367
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 368 DARsKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQ 447
Cdd:cd07092 317 RAP-AHARVLTGGRRAEGPG-YFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 21356737 448 QVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
47-501 |
5.52e-145 |
|
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: 423.68 E-value: 5.52e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 47 FEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEVAYGNAFVEWFAEEARRIYGEIVPS----ASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKP 202
Cdd:cd07145 79 RVEVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 203 SEDTPLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNA 282
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGY-GSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 283 PFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKV 362
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 363 SGFVEDARSKKANIILGGQplPDKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFY 442
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGK--RDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 443 SENLQQVFRVAKRLEVGMVGVNE-GIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
33-499 |
1.24e-143 |
|
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: 421.43 E-value: 1.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07144 12 INNEFVKSSDGE-TIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINE-SKGEVAYGNAFVEWFAEEARRIYGEIVPSaSPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:cd07144 90 AIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPT-SPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGI 271
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIP-GYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 272 KRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRV-EALKIGDGQGCDVQI 350
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGS--LFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVK 428
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkgYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356737 429 KANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
27-501 |
2.71e-143 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 420.08 E-value: 2.71e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 27 VQDKALVDGAWVDSSNAkaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYEskEWRSLTAKDRSNLLKKWHKLIEQ 106
Cdd:PRK13473 1 MQTKLLINGELVAGEGE--KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLKLADAIEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 107 HSQEIAEIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGeivPSA---SPNREIIVMKQPIGVAALITPWNFPMA 182
Cdd:PRK13473 77 NADEFARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEG---KAAgeyLEGHTSMIRRDPVGVVASIAPWNYPLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 183 MITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAgIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKL 262
Cdd:PRK13473 154 MAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVT-GRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 263 LFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGD 342
Cdd:PRK13473 232 VLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 343 GQGCDVQIGPLINEMQFNKVSGFVEDARS-KKANIILGGQPLPDKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFR 421
Cdd:PRK13473 312 PDDEDTELGPLISAAHRDRVAGFVERAKAlGHIRVVTGGEAPDGKGY-YYEPTLLAGARQDDEIVQREVFGPVVSVTPFD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 422 DEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:PRK13473 391 DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
33-503 |
1.33e-141 |
|
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: 416.07 E-value: 1.33e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVdSSNAKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07113 4 IDGRPV-AGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVS-AWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGE-IVPS-ASPNRE---IIVMKQPIGVAALITPWNFPMAMITR 186
Cdd:cd07113 82 QLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGEtLAPSiPSMQGErytAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 187 KAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVttNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRN 266
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVV--NGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 267 SADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGC 346
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 347 DVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVtdVPPSAQ--LYSEEVFGPVVSIIRFRDEE 424
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEG-YFVQPTLV--LARSADsrLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
32-486 |
1.46e-141 |
|
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: 415.81 E-value: 1.46e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSsnAKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEI 111
Cdd:cd07086 2 VIGGEWVGS--GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 112 AEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:cd07086 78 GRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDA----GIPKGVINVVTTnkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNS 267
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG--GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 268 ADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCD 347
Cdd:cd07086 236 ARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 348 VQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLP-DKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEA 426
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356737 427 VKKANDTRRGLAGYFYSENLQQVFRV--AKRLEVGMVGVNEGIISA-AEAPFGGVKESGVGRE 486
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKETGGGRE 458
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
48-503 |
5.10e-140 |
|
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: 411.06 E-value: 5.10e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 48 EVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESK 127
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 128 GEVAYGNAFVEWFAEEARRIYGEIVPS----ASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPS 203
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 204 EDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLFRNSadGIKRICLELGGNAP 283
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREV-LGDAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 284 FIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVS 363
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 364 GFVEDARSKKANIILGGQPlpdKGSLFYaPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYS 443
Cdd:cd07094 317 RWVEEAVEAGARLLCGGER---DGALFK-PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356737 444 ENLQQVFRVAKRLEVGMVGVNEGIISAAEA-PFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
33-501 |
7.30e-140 |
|
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: 411.20 E-value: 7.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07139 3 IGGRWVAPSGSE-TIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESK-GEVAYGNAFVEWFAEEARRI-YGEIVPSASPNReIIVMKQPIGVAALITPWNFPMAMITRKAGA 190
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPGSGGGH-VLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADG 270
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREV--GEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQI 350
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKVSGFVEDARSKKANIILGGQ--PLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVK 428
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRG-WFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356737 429 KANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNeGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
49-501 |
1.05e-139 |
|
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: 410.20 E-value: 1.05e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF--PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRI---YGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSED 205
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 206 TPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFI 285
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVT-GTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 286 VFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGF 365
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 366 VEDARSKKANIILGGQ--PLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYS 443
Cdd:cd07110 318 IARGKEEGARLLCGGRrpAHLEKG-YFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 444 ENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
49-501 |
1.97e-139 |
|
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: 409.70 E-value: 1.97e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRsLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLR-LSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRIYGEIVPSAsPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPL 208
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 209 TALAVAKLAVDAGIPKGVINVVT-TNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVF 287
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTgLGAEA--GAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGcDVQIGPLINEMQFNKVSGFVE 367
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 368 DARSKKANIILGGQPLPDK--GSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSEN 445
Cdd:cd07109 316 RARARGARIVAGGRIAEGApaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356737 446 LQQVFRVAKRLEVGMVGVNE-GIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
69-499 |
4.16e-139 |
|
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: 407.62 E-value: 4.16e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 69 AQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRiY 148
Cdd:cd07100 1 IEAALDRAHAAF--LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEA-F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 149 GEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGV-I 227
Cdd:cd07100 78 LADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 228 NVVTTNKAAP--IGDlfcksPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFR 305
Cdd:cd07100 158 NLLIDSDQVEaiIAD-----PRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 306 NCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPD 385
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 386 KGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNE 465
Cdd:cd07100 313 PGA-FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING 391
|
410 420 430
....*....|....*....|....*....|....
gi 21356737 466 GIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07100 392 MVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-503 |
1.60e-138 |
|
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: 407.21 E-value: 1.60e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 51 NPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG-E 129
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 130 VAYGNAFVEWFAEEARRIYGEIVPsASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLT 209
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 210 ALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDS 289
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVT-GFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 290 ADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDA 369
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 370 RSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQV 449
Cdd:cd07115 319 REEGARLLTGGKRPGARG-FFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 21356737 450 FRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
35-501 |
2.00e-136 |
|
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: 402.45 E-value: 2.00e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 35 GAWVDSSnAKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEI 114
Cdd:cd07151 1 GEWRDGT-SERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 115 MTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAA 194
Cdd:cd07151 78 LIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 195 GCTVVVKPSEDTPLTA-LAVAKLAVDAGIPKGVINVVTTnKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKR 273
Cdd:cd07151 158 GNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVG-AGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 274 ICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPL 353
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 354 INEMQFNKVSGFVEDARSKKANIILGGQPlpdkGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDT 433
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEA----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 434 RRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIIS-AAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-503 |
2.14e-135 |
|
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: 399.41 E-value: 2.14e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 51 NPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSlTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEV 130
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 131 AYGNAFVEWFAEEARRIYGEIVpSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTA 210
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 211 LAVAKLAVDA-GIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDS 289
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSE-GAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 290 ADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDA 369
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 370 RSKKANIILGGQPLPD---KGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENL 446
Cdd:cd07120 320 IAAGAEVVLRGGPVTEglaKGA-FLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356737 447 QQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
49-502 |
2.83e-135 |
|
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: 398.99 E-value: 2.83e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ--KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRIYGEIVPSASPN-----REiivmkqPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPS 203
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSfaytrRE------PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 204 EDTPLTALAVAKLAVDAGIPKGVINVVttNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAP 283
Cdd:cd07090 153 PFTPLTALLLAEILTEAGLPDGVFNVV--QGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 284 FIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVS 363
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 364 GFVEDARSKKANIILGGQPLPD----KGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAG 439
Cdd:cd07090 311 GYIESAKQEGAKVLCGGERVVPedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356737 440 YFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYIC 502
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
49-501 |
7.60e-134 |
|
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: 395.58 E-value: 7.60e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPI-NESK 127
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 128 GEVAYGNAFVEWFAEEARRIYGEIVPsASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTP 207
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 208 LTALAVAKLAVDAgIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVF 287
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVIT-GYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMAS-KFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFV 366
Cdd:cd07108 236 PDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 367 EDARSKK-ANIILGG-QPLPDKGS--LFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFY 442
Cdd:cd07108 316 DLGLSTSgATVLRGGpLPGEGPLAdgFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 443 SENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHG-IDDYVDIKYI 501
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
33-499 |
1.09e-133 |
|
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: 395.33 E-value: 1.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVdSSNAKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:TIGR01804 2 IDGEYV-EDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINES-KGEVAYGNAFVEWFAEEARRIYGEIVPSASPNrEIIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:TIGR01804 79 KLETLDTGKTLQETiVADMDSGADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGI 271
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVV-QGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 272 KRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIG 351
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 352 PLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKG---SLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVK 428
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGlqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356737 429 KANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
30-503 |
1.39e-132 |
|
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: 393.01 E-value: 1.39e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:cd07142 5 KLFINGQFVDAASGK-TFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESK-GEVAYGNAFVEWFAEEARRIYGEIVPSASPNrEIIVMKQPIGVAALITPWNFPMAMITRKA 188
Cdd:cd07142 84 ELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPH-HVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 189 GAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA 268
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVT-GFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 DG-IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCD 347
Cdd:cd07142 242 KSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 348 VQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAV 427
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKG-YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356737 428 KKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
33-496 |
2.75e-131 |
|
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: 389.83 E-value: 2.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07111 26 INGKWVKPENRK-SFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESK-GEVAYGNAFVEWFAeearrIYGEIVPSASPNREiivmkqPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:cd07111 103 VLESLDNGKPIRESRdCDIPLVARHFYHHA-----GWAQLLDTELAGWK------PVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGI 271
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF--GSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 272 KRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIG 351
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 352 PLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKAN 431
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKG-PFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 432 DTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYV 496
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
33-501 |
1.55e-130 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 388.71 E-value: 1.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAY---ESKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:PLN02467 12 IGGEWREPVLGK-RIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYG-EIVPSASPNREI--IVMKQPIGVAALITPWNFPMAMITR 186
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkQKAPVSLPMETFkgYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 187 KAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVT---TNKAAPIgdlfCKSPDVRGISFTGSTEVGKLL 263
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTglgTEAGAPL----ASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 264 FRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGD- 342
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 343 -GQGCdvQIGPLINEMQFNKVSGFVEDARSKKANIILGG-QPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRF 420
Cdd:PLN02467 327 lEEGC--RLGPVVSEGQYEKVLKFISTAKSEGATILCGGkRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 421 RDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKY 500
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQ 484
|
.
gi 21356737 501 I 501
Cdd:PLN02467 485 V 485
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
50-501 |
7.65e-130 |
|
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: 385.04 E-value: 7.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 50 RNPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGE 129
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA--QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 130 VAYGNAFVEWFAEEARRIYG-EIVPSAS--PNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDT 206
Cdd:cd07099 79 VLLALEAIDWAARNAPRVLApRKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 207 PLTALAVAKLAVDAGIPKGVINVVTTnkAAPIGDLFCKS-PDVrgISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFI 285
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTG--DGATGAALIDAgVDK--VAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 286 VFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGF 365
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 366 VEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSEN 445
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGG-PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 446 LQQVFRVAKRLEVGMVGVNEGIISAA--EAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
30-503 |
1.44e-129 |
|
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: 385.55 E-value: 1.44e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYE-SKEWRSLTAKDRSNLLKKWHKLIEQHS 108
Cdd:cd07141 8 KIFINNEWHDSVSGK-TFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 109 QEIAEIMTAESGKPINESKGEVAYGNAFV-EWFAEEARRIYGEIVPsASPNREIIVMKQPIGVAALITPWNFPMAMITRK 187
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYLVDLPGAIKVlRYYAGWADKIHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 188 AGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVT----TNKAApigdlFCKSPDVRGISFTGSTEVGKLL 263
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPgygpTAGAA-----ISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 264 FRNSAD-GIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGD 342
Cdd:cd07141 241 QQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 343 GQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRD 422
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKG-YFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 423 EEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYIC 502
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
.
gi 21356737 503 M 503
Cdd:cd07141 480 I 480
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
68-501 |
8.75e-129 |
|
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: 381.54 E-value: 8.75e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 68 DAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRI 147
Cdd:cd07105 1 DADQAVEAAAAAF--PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 YGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVI 227
Cdd:cd07105 79 IGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 228 NVVTT--NKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFR 305
Cdd:cd07105 159 NVVTHspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 306 NCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDgqgcdVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPD 385
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 386 KGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNE 465
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING 393
|
410 420 430
....*....|....*....|....*....|....*..
gi 21356737 466 GIIS-AAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07105 394 MTVHdEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
32-496 |
1.06e-128 |
|
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: 384.27 E-value: 1.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSnakATFEVRNPAN-GAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQE 110
Cdd:cd07124 36 VIGGKEVRTE---EKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 111 IAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKqPIGVAALITPWNFPMAMITRKAGA 190
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADG 270
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLP-GPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 ------IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:cd07124 269 qpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARsKKANIILGGQPLPD-KGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELaAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA--AEAPFGGVKESGVgreGSKHGIDDYV 496
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGAlvGRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
47-499 |
1.35e-127 |
|
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: 379.28 E-value: 1.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 47 FEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYEskEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEVAYGNAFVEWFAEEARRIYGEIVP----SASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKP 202
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 203 SEDTPLTALAVAKLAVDAGIPKGVINVVTTNKaaPIGDLFCKSPDVRGISFTGSTEVGKLLfRNSAdGIKRICLELGGNA 282
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSR--DDADLLVTDERIKLLSFTGSPAVGWDL-KARA-GKKKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 283 PFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKV 362
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 363 SGFVEDARSKKANIILGGQplpDKGSLFyAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGL-AGYF 441
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGK---RDGALL-EPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLqAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 442 ySENLQQVFRVAKRLEVGMVGVNEgIIS--AAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07147 391 -TRDLEKALRAWDELEVGGVVIND-VPTfrVDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
24-504 |
4.91e-127 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 379.22 E-value: 4.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 24 SALVQDKALVDGAWVDSSNAkATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKL 103
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSG-ETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 104 IEQHSQEIAEIMTAESGKPINE-SKGEVAYGNAFVEWFAEEARRIYGEIVPsASPNREIIVMKQPIGVAALITPWNFPMA 182
Cdd:PRK13252 79 LRERNDELAALETLDTGKPIQEtSVVDIVTGADVLEYYAGLAPALEGEQIP-LRGGSFVYTRREPLGVCAGIGAWNYPIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 183 MITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtnKAAPIGDLFCKSPDVRGISFTGSTEVGKL 262
Cdd:PRK13252 158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQ--GDGRVGAWLTEHPDIAKVSFTGGVPTGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 263 LFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGD 342
Cdd:PRK13252 236 VMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 343 GQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGS---LFYAPTIVTDVPPSAQLYSEEVFGPVVSIIR 419
Cdd:PRK13252 316 PMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFangAFVAPTVFTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 420 FRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
....*..
gi 21356737 500 --YICMG 504
Cdd:PRK13252 476 svQVEMG 482
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
48-499 |
2.23e-126 |
|
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: 376.31 E-value: 2.23e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 48 EVRNPANGAVIGKVPNMTVADAQKAIDAAKqAYESKewrsLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESK 127
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAA-SYRST----LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 128 GEV--AYGNAFVEwfAEEARRIYGEIVPS-ASPN---REIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVK 201
Cdd:cd07146 77 YEVgrAADVLRFA--AAEALRDDGESFSCdLTANgkaRKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 202 PSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLfrNSADGIKRICLELGGN 281
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGE-IGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 282 APFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNK 361
Cdd:cd07146 232 DPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 362 VSGFVEDARSKKANIILGGQplpDKGSLfYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYF 441
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQ---RQGAL-YAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 442 YSENLQQVFRVAKRLEVGMVGVNEGIISAAE-APFGGVKESG-VGREGSKHGIDDYVDIK 499
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGlGGKEGVREAMKEMTNVK 447
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
39-501 |
3.12e-126 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 378.45 E-value: 3.12e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 39 DSSNAKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAE 118
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 119 SGKpineskgevAYGNAFVE---------WFAEEARRIYGE-----IVPSASPNREIivmKQPIGVAALITPWNFPMAMI 184
Cdd:PRK09407 104 TGK---------ARRHAFEEvldvaltarYYARRAPKLLAPrrragALPVLTKTTEL---RQPKGVVGVISPWNYPLTLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 185 TRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDvrGISFTGSTEVGKLLF 264
Cdd:PRK09407 172 VSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVT-GPGPVVGTALVDNAD--YLMFTGSTATGRVLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 265 RNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:PRK09407 249 EQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA---AEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:PRK09407 409 EAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAwgsVDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
52-501 |
1.10e-124 |
|
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: 372.03 E-value: 1.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 52 PANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVA 131
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 132 --------YGNAFVEWFAEEARRiygEIVPSASPNREIivmKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPS 203
Cdd:cd07101 81 dvaivaryYARRAERLLKPRRRR---GAIPVLTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 204 EDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDvrGISFTGSTEVGKLLFRNSADGIKRICLELGGNAP 283
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVT-GPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 284 FIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVS 363
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 364 GFVEDARSKKANIILGGQPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYS 443
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356737 444 ENLQQVFRVAKRLEVGMVGVNEGIISA---AEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
33-501 |
5.14e-123 |
|
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: 368.75 E-value: 5.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07140 10 INGEFVDAEGGK-TYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINES-KGEVAYGNAFVEWFAEEARRIYGEIVP--SASPNREI-IVMKQPIGVAALITPWNFPMAMITRKA 188
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 189 GAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA 268
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINIL-PGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 DG-IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCD 347
Cdd:cd07140 248 VSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 348 VQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE--EE 425
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPG-FFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356737 426 AVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
30-503 |
7.84e-122 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 366.45 E-value: 7.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:PLN02766 22 KLFINGEFVDAASGK-TFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGEIVPSASPNREIiVMKQPIGVAALITPWNFPMAMITRKA 188
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGY-TLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 189 GAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVT----TNKAAPIGDLfckspDVRGISFTGSTEVGKLLF 264
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTgfgpTAGAAIASHM-----DVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 265 RNSA-DGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDG 343
Cdd:PLN02766 255 QAAAtSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 344 QGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKG-YYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICM 503
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVT 493
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
49-501 |
3.14e-121 |
|
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: 363.23 E-value: 3.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 49 VRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKG 128
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF--PEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 129 EVAYGNAFVEWFAEEARRIYGEIVPSaSPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPL 208
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPV-GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 209 TALAVAKLAVDAgIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFD 288
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGAT-AGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 289 SADIEKAVDGAMAS-KFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVE 367
Cdd:cd07107 236 DADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 368 DARSKKANIILGGQPLPDK---GSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSE 444
Cdd:cd07107 316 SAKREGARLVTGGGRPEGPaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356737 445 NLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
33-499 |
7.38e-121 |
|
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: 363.00 E-value: 7.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07143 11 INGEFVDSVHGG-TVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGEIVPSaSPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:cd07143 90 SIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIET-DIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA-DG 270
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVS-GYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQI 350
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKA 430
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEG-YFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 431 NDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
32-501 |
7.87e-121 |
|
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: 362.82 E-value: 7.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEI 111
Cdd:cd07559 4 FINGEWVAPSKGE-YFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 112 AEIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGEIVpsaspnrEI------IVMKQPIGVAALITPWNFPMAMI 184
Cdd:cd07559 81 AVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLS-------EIdedtlsYHFHEPLGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 185 TRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAgIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLF 264
Cdd:cd07559 154 AWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVT-GFGSEAGKPLASHPRIAKLAFTGSTTVGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 265 RNSADGIKRICLELGGNAPFIVFDSA-----DIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALK 339
Cdd:cd07559 232 QYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 340 IGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSL---FYAPTIVTDVPPSAQLYSEEVFGPVVS 416
Cdd:cd07559 312 VGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDkgyFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 417 IIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYV 496
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQ 471
|
....*
gi 21356737 497 DIKYI 501
Cdd:cd07559 472 QTKNI 476
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-499 |
1.33e-119 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 361.82 E-value: 1.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:PLN02466 59 QLLINGQFVDAASGK-TFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINES-KGEVAYGNAFVEWFAEEARRIYGEIVPSASPNrEIIVMKQPIGVAALITPWNFPMAMITRKA 188
Cdd:PLN02466 138 ELAALETWDNGKPYEQSaKAELPMFARLFRYYAGWADKIHGLTVPADGPH-HVQTLHEPIGVAGQIIPWNFPLLMFAWKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 189 GAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA 268
Cdd:PLN02466 217 GPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVS-GFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 -DGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCD 347
Cdd:PLN02466 296 kSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 348 VQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAV 427
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKG-YYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356737 428 KKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
30-501 |
9.41e-119 |
|
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: 357.53 E-value: 9.41e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:cd07117 2 GLFINGEWVKGSSGE-TIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGEIVpSASPNREIIVMKQPIGVAALITPWNFPMAMITRKA 188
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSAN-MIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 189 GAALAAGCTVVVKPSEDTPLTALAVAKLAVDAgIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA 268
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVT-GKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 DGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDV 348
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 349 QIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLP----DKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGF-FIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
28-487 |
7.21e-113 |
|
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: 342.24 E-value: 7.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 28 QDKALVDGAWVDSSNAkaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKeWRSLTAKDRSNLLKKWHKLIEQH 107
Cdd:cd07082 1 QFKYLINGEWKESSGK--TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGW-WPTMPLEERIDCLHKFADLLKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 108 SQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVP--SASPNREII--VMKQPIGVAALITPWNFPMAM 183
Cdd:cd07082 78 KEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgdWFPGTKGKIaqVRREPLGVVLAIGPFNYPLNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 184 ITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTnKAAPIGDLFCKSPDVRGISFTGSTEVGKLL 263
Cdd:cd07082 158 TVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTG-RGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 264 FRNSadGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDG 343
Cdd:cd07082 237 KKQH--PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 344 QGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLpdKGSLFYaPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:cd07082 315 WDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGRE--GGNLIY-PTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNE----GIISaaeAPFGGVKESGVGREG 487
Cdd:cd07082 392 EEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrGPDH---FPFLGRKDSGIGTQG 456
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
32-495 |
3.33e-110 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 336.91 E-value: 3.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSsnaKATFEVRNPANGA-VIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQE 110
Cdd:PRK03137 40 IIGGERITT---EDKIVSINPANKSeVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 111 IAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRiYGEIVPSAS-PNREIIVMKQPIGVAALITPWNFPMAMITRKAG 189
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPVESrPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 190 AALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA- 268
Cdd:PRK03137 194 AAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGS-GSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAk 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 --DG---IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDG 343
Cdd:PRK03137 273 vqPGqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 344 QGCDVqIGPLINEMQFNKVSGFVEDARsKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:PRK03137 353 EDNAY-MGPVINQASFDKIMSYIEIGK-EEGRLVLGGEGDDSKG-YFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA--AEAPFGGVKESGVgreGSKHGIDDY 495
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAivGYHPFGGFNMSGT---DSKAGGPDY 500
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
28-503 |
8.45e-110 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 335.33 E-value: 8.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 28 QDKAL---------VDGAWVDSSNAkATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLK 98
Cdd:PRK09847 10 QDKALslaienrlfINGEYTAAAEN-ETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 99 KWHKLIEQHSQEIAEIMTAESGKPINES-KGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVmKQPIGVAALITPW 177
Cdd:PRK09847 89 KLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 178 NFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGST 257
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVV-TGFGHEAGQALSRHNDIDAIAFTGST 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 258 EVGKLLFRNSADG-IKRICLELGGNAPFIVF-DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRV 335
Cdd:PRK09847 247 RTGKQLLKDAGDSnMKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 336 EALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSkKANIILGGQPLPDKGSLfyAPTIVTDVPPSAQLYSEEVFGPVV 415
Cdd:PRK09847 327 QNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGES-KGQLLLDGRNAGLAAAI--GPTIFVDVDPNASLSREEIFGPVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 416 SIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDY 495
Cdd:PRK09847 404 VVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKF 483
|
....*...
gi 21356737 496 VDIKYICM 503
Cdd:PRK09847 484 TELKTIWI 491
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
97-495 |
1.34e-109 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 331.70 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 97 LKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITP 176
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 177 WNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGS 256
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLV-LGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 257 TEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVE 336
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 337 ALKIGD-GQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVV 415
Cdd:PRK10090 240 AVQFGNpAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKG-YYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 416 SIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDY 495
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEY 398
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
30-501 |
4.87e-105 |
|
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: 322.16 E-value: 4.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:cd07085 2 KLFINGEWVESKTTE-WLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAF--PAWSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESKGEVAYGNAFVEwFAEEARRIY-GEIVPSASPNREIIVMKQPIGVAALITPWNFPmAMITR-K 187
Cdd:cd07085 79 ELARLITLEHGKTLADARGDVLRGLEVVE-FACSIPHLLkGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 188 AGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNS 267
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEA--VNALLDHPDIKAVSFVGSTPVGEYIYERA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 268 ADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCD 347
Cdd:cd07085 235 AANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 348 VQIGPLINEMQFNKVSGFVEDARSKKANIILGG---QPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGI-ISAAEAPFGGVKESGVGREG--SKHGIDDYVDIKYI 501
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSFFGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
55-495 |
4.88e-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: 321.17 E-value: 4.88e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 55 GAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGN 134
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 135 AFVEWFAEEARRIYGEIVPSAsPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTA-LAV 213
Cdd:cd07152 79 GELHEAAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 214 AKLAVDAGIPKGVINVVTTnkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIE 293
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG--GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 294 KAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKK 373
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 374 ANIILGGQplpdKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVA 453
Cdd:cd07152 316 ARLEAGGT----YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 21356737 454 KRLEVGMVGVNEG-IISAAEAPFGGVKESGVG-REGSKHGIDDY 495
Cdd:cd07152 392 DRLRTGMLHINDQtVNDEPHNPFGGMGASGNGsRFGGPANWEEF 435
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
32-496 |
1.44e-103 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 319.50 E-value: 1.44e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSNAKATFevrNPANGA-VIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQE 110
Cdd:TIGR01237 36 VINGERVETENKIVSI---NPCDKSeVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 111 IAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGA 190
Cdd:TIGR01237 111 FSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA-- 268
Cdd:TIGR01237 191 PIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFV-PGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkv 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 ----DGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:TIGR01237 270 qpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARSkKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:TIGR01237 350 SADVYVGPVIDQKSFNKIMEYIEIGKA-EGRLVSGGCGDDSKG-YFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFD 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA--AEAPFGGVKESGVgreGSKHGIDDYV 496
Cdd:TIGR01237 428 EALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAivGYQPFGGFKMSGT---DSKAGGPDYL 498
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
32-501 |
6.79e-100 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 309.00 E-value: 6.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSnaKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKdRSNLLKKWHKLIEQHSQEI 111
Cdd:TIGR04284 4 LIDGKLVAGS--AGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDETDWSRDTAL-RVRCLRQLRDALRAHVEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 112 AEIMTAESGKPINESKGEVAYGN-AFVEWFAEEA-----RRIYGEIVPSASPNREIIVmKQPIGVAALITPWNFPMAMIT 185
Cdd:TIGR04284 81 RELTIAEVGAPRMLTAGAQLEGPvDDLGFAADLAesyawTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQINL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 186 RKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVD-AGIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLF 264
Cdd:TIGR04284 160 AKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHR-LGALLAKDPRVDMVSFTGSTATGRAVM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 265 RNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:TIGR04284 239 ADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGG-QPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDE 423
Cdd:TIGR04284 319 DPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGgRPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 424 EEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYI 501
Cdd:TIGR04284 399 DDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
51-493 |
2.80e-99 |
|
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: 306.48 E-value: 2.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 51 NPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEV 130
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAA--QKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 131 AYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTA 210
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 211 LAVAKLAVDAGIPKGVINVVTTNKAapIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSA 290
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHE--TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 291 DIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDAR 370
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 371 SKKANIILGGQ--PLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQ 448
Cdd:cd07102 318 AKGARALIDGAlfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 21356737 449 VFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGID 493
Cdd:cd07102 398 AEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
51-502 |
4.74e-98 |
|
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: 303.84 E-value: 4.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 51 NPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKP-INESKGE 129
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAA--QREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 130 VAYGNAFVEWFAEearriYGE--IVPSASPNREIIVMK------QPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVK 201
Cdd:cd07098 80 ILVTCEKIRWTLK-----HGEkaLRPESRPGGLLMFYKrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 202 PSEDTPLTAL----AVAKLAVDAGIPKGVINVVTTnkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLE 277
Cdd:cd07098 155 VSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTC--LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 278 LGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEM 357
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 358 QFNKVSGFVEDARSKKANIILGGQPLP---DKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTR 434
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPhpeYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 435 RGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIIS--AAEAPFGGVKESGVGREGSKHGIDDYVDIKYIC 502
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
51-504 |
7.91e-98 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 303.20 E-value: 7.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 51 NPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEV 130
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 131 AYGNAFVEWFAEEARRIYGEiVPS---ASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTP 207
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLAD-EPAdaaAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 208 LTALAVAKLAVDAGIPKGVINVVTTNKAAPIGDLfcKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVF 287
Cdd:PRK09406 164 QTALYLADLFRRAGFPDGCFQTLLVGSGAVEAIL--RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVE 367
Cdd:PRK09406 242 PSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 368 DARSKKANIILGGQPlPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQ 447
Cdd:PRK09406 322 DAVAAGATILCGGKR-PDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356737 448 QVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICMG 504
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
32-488 |
1.94e-91 |
|
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: 287.18 E-value: 1.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSNakaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEI 111
Cdd:cd07130 2 VYDGEWGGGGG---VVTSISPANGEPIARVRQATPEDYESTIKAAQEAF--KEWRDVPAPKRGEIVRQIGDALRKKKEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 112 AEIMTAESGKPINESKGEVAygnafvEW-----FA-EEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMIT 185
Cdd:cd07130 77 GKLVSLEMGKILPEGLGEVQ------EMidicdFAvGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 186 RKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDA----GIPKGVINVVTTnkAAPIGDLFCKSPDVRGISFTGSTEVGK 261
Cdd:cd07130 151 WNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG--GADVGEALVKDPRVPLVSFTGSTAVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 262 LLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIG 341
Cdd:cd07130 229 QVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 342 DGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSlFYAPTIVTdVPPSAQLYSEEVFGPVVSIIRFR 421
Cdd:cd07130 309 DPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGN-YVEPTIVE-GLSDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356737 422 DEEEAVKKANDTRRGLAGYFYSENLQQVFRV--AKRLEVGMVGVNEGiISAAE--APFGGVKESGVGRE-GS 488
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIG-TSGAEigGAFGGEKETGGGREsGS 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
48-487 |
6.60e-89 |
|
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: 280.07 E-value: 6.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 48 EVRNPANGAVIGKVPNMTVADAQKAIDAAKQAY-ESKEWrsLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEVAYGNAFVEWFAEEARRIYGEIVP----SASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKP 202
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 203 SEDTPLTALAVAKLAVDAGIPKGVINVVTTnkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGiKRICLELGGNA 282
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPC--ENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 283 PFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKV 362
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 363 SGFVEDARSKKANIILGGQPLPDKgslFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFY 442
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKRLSDT---TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 21356737 443 SENLQQVFRVAKRLEVGMVGVNEGiiSAAEA---PFGGVKESGVGREG 487
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDH--TAFRVdwmPFAGRRQSGYGTGG 439
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
33-501 |
1.72e-87 |
|
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: 277.54 E-value: 1.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKATFEVRNPanGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07083 23 IGGEWVDTKERMVSVSPFAP--SEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYG--EIVPSASPNREIIVMkQPIGVAALITPWNFPMAMITRKAGA 190
Cdd:cd07083 99 ATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKLLFR---NS 267
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGV-GEEVGAYLTEHERIRGINFTGSLETGKKIYEaaaRL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 268 ADG---IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:cd07083 257 APGqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARSkKANIILGGQpLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYIEHGKN-EGQLVLGGK-RLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 425 --EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA--AEAPFGGVKESGVG-REGSKHGIDDYVDIK 499
Cdd:cd07083 415 faEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAlvGVQPFGGFKLSGTNaKTGGPHYLRRFLEMK 494
|
..
gi 21356737 500 YI 501
Cdd:cd07083 495 AV 496
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
48-496 |
5.18e-87 |
|
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: 276.77 E-value: 5.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 48 EVRNPA-NGAVIGKVPNMTVADAQKAIDAAKQAYEskEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:cd07125 49 PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFA--GWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDT 206
Cdd:cd07125 127 DAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 207 PLTALAVAKLAVDAGIPKGVINVVTTnKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFR-NSADGIKRICL--ELGG-NA 282
Cdd:cd07125 207 PLIAARAVELLHEAGVPRDVLQLVPG-DGEEIGEALVAHPRIDGVIFTGSTETAKLINRaLAERDGPILPLiaETGGkNA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 283 pFIVFDSADIEKAVDGAMASKFRNCGQTCvSANR-FFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNK 361
Cdd:cd07125 286 -MIVDSTALPEQAVKDVVQSAFGSAGQRC-SALRlLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 362 VSGFVEdaRSKKANIILGGQPLPDKGSLFYAPTIVTDVppSAQLYSEEVFGPVVSIIRFRDE--EEAVKKANDTRRGLAG 439
Cdd:cd07125 364 LRAHTE--LMRGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTL 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 440 YFYSENLQQVFRVAKRLEVGMVGVNEGIISAA--EAPFGGVKESGVgreGSKHGIDDYV 496
Cdd:cd07125 440 GIHSRDEREIEYWRERVEAGNLYINRNITGAIvgRQPFGGWGLSGT---GPKAGGPNYL 495
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
51-499 |
7.98e-86 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 272.12 E-value: 7.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 51 NPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEV 130
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGF--RDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 131 AYGNAFVEWFAEEARRIYgEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTA 210
Cdd:PRK13968 91 AKSANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 211 LAVAKLAVDAGIPKGVINVVTTNK---AAPIGDlfcksPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVF 287
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNdgvSQMIND-----SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVE 367
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 368 DARSKKANIILGGQPLPDKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQ 447
Cdd:PRK13968 325 ATLAEGARLLLGGEKIAGAGN-YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 21356737 448 QVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
33-499 |
8.88e-85 |
|
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: 270.09 E-value: 8.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:cd07116 5 IGGEWVAPVKGE-YFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKG-EVAYGNAFVEWFAEEARRIYGEIvPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI-SEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAgIPKGVINVVttNKAAP-IGDLFCKSPDVRGISFTGSTEVGKLLFRNSADG 270
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVV--NGFGLeAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 IKRICLELGGNAPFIVFDS------ADIEKAVDGAMASKFrNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQ 344
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 345 GCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQ--PLPDK-GSLFYAPTIVTDvPPSAQLYSEEVFGPVVSIIRFR 421
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnELGGLlGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 422 DEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIK 499
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
30-501 |
1.04e-76 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 249.03 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:TIGR01722 2 NHWIGGKFAEGASGT-YIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT--WGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAG 189
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 190 AALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAAPigDLFCKSPDVRGISFTGSTEVGKLLF-RNSA 268
Cdd:TIGR01722 159 IAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV--DRLLEHPDVKAVSFVGSTPIGRYIHtTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 269 DGiKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVyDKFVGQLKKRVEALKIGDGQGCDV 348
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 349 QIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKG---SLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEE 425
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGyeeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 426 AVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGI-ISAAEAPFGGVKESGVGREG--SKHGIDDYVDIKYI 501
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIpVPLPYFSFTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
65-496 |
1.47e-76 |
|
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: 247.13 E-value: 1.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 65 TVADAQKAIDAAKQAYESKEWRSLtaKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES--------KGEVAYGNAF 136
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDL--EYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETlltevsgvKNDILHMLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 137 VEWFAEEarriygEIVPSASPNR---EIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAV 213
Cdd:cd07135 81 LKKWAKD------EKVKDGPLAFmfgKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 214 AKLaVDAGIPKGVINVVttNKAAP-IGDLFCKSPDvrGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADI 292
Cdd:cd07135 155 AEL-VPKYLDPDAFQVV--QGGVPeTTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 293 EKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALkIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSK 372
Cdd:cd07135 230 ELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDTTKGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 373 kanIILGGQplPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRV 452
Cdd:cd07135 309 ---VVIGGE--MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHI 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 21356737 453 AKRLEVGMVGVNEGIISAA--EAPFGGVKESGVGREGSKHGIDDYV 496
Cdd:cd07135 384 LTRTRSGGVVINDTLIHVGvdNAPFGGVGDSGYGAYHGKYGFDTFT 429
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
72-493 |
4.25e-76 |
|
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: 246.03 E-value: 4.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 72 AIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEwFAEEARRIYGEI 151
Cdd:cd07095 5 AVAAARAAF--PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 152 VPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVT 231
Cdd:cd07095 82 RATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 232 TNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRI-CLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQT 310
Cdd:cd07095 162 GGRET--GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 311 CVSANRFFV-QDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSl 389
Cdd:cd07095 240 CTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 390 FYAPTIVtDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIIS 469
Cdd:cd07095 319 FLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTG 397
|
410 420
....*....|....*....|....*
gi 21356737 470 AA-EAPFGGVKESGVGREGSKHGID 493
Cdd:cd07095 398 ASsTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
75-491 |
4.22e-75 |
|
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: 243.29 E-value: 4.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 75 AAKQAYeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESK--------GEVAYGNAFVE-WFAEEAR 145
Cdd:cd07134 5 AAQQAH-ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMKPKRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 146 RiygeiVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKG 225
Cdd:cd07134 84 R-----TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 226 ViNVVTtnkaapiGDlfcksPDVRG---------ISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAV 296
Cdd:cd07134 159 V-AVFE-------GD-----AEVAQallelpfdhIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 297 DGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKigdGQGCDVQIGP----LINEMQFNKVSGFVEDARSK 372
Cdd:cd07134 226 KKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFY---GKDAARKASPdlarIVNDRHFDRLKGLLDDAVAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 373 KANIILGGQplPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRV 452
Cdd:cd07134 303 GAKVEFGGQ--FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKV 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 21356737 453 AKRLEVGMVGVNEGIISAAEA--PFGGVKESGVGREGSKHG 491
Cdd:cd07134 381 LARTSSGGVVVNDVVLHFLNPnlPFGGVNNSGIGSYHGVYG 421
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-493 |
9.53e-75 |
|
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: 242.05 E-value: 9.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 70 QKAIDAAKQAYESKEWRSLtaKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES--------KGEVAYG-NAFVEWF 140
Cdd:cd07087 1 AELVARLRETFLTGKTRSL--EWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHAlKHLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 141 AEeaRRIygEIVPSASPNREIIVmKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLaVDA 220
Cdd:cd07087 79 KP--RRV--SVPLLLQPAKAYVI-PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 221 GIPKGVINVVTTnkAAPIGDLFCKSP-DVrgISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGA 299
Cdd:cd07087 153 YFDPEAVAVVEG--GVEVATALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 300 MASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALkIGDGQGCDVQIGPLINEMQFNKVSGFVEDArskkaNIILG 379
Cdd:cd07087 229 AWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 380 GQPlpDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVG 459
Cdd:cd07087 303 GQV--DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSG 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 21356737 460 MVGVNEGIISAA--EAPFGGVKESGVGREGSKHGID 493
Cdd:cd07087 381 GVCVNDVLLHAAipNLPFGGVGNSGMGAYHGKAGFD 416
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
33-482 |
6.92e-72 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 236.39 E-value: 6.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAkaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:PRK09457 5 INGDWIAGQGE--AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF--PAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEiVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAAL 192
Cdd:PRK09457 81 EVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGE-KRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 193 AAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIK 272
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET--GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 273 RI-CLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVY-DKFVGQLKKRVEALKIGDgqgCDVQI 350
Cdd:PRK09457 238 KIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR---WDAEP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKVSGFVEDArskKANII-LGGQPL-----PDKGSLFYAPTIVtDVPPSAQLYSEEVFGPVVSIIRFRDEE 424
Cdd:PRK09457 315 QPFMGAVISEQAAQGLVAA---QAQLLaLGGKSLlemtqLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFD 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 425 EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAA-EAPFGGVKESG 482
Cdd:PRK09457 391 EAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASsAAPFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
30-499 |
3.30e-69 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 229.64 E-value: 3.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKaTFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:PLN00412 17 KYYADGEWRTSSSGK-SVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGE---IV----PSASPNREIIVMKQPIGVAALITPWNFPMA 182
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkfLVsdsfPGNERNKYCLTSKIPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 183 MITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGStEVGKL 262
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCV-TGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 263 LFRNSadGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGD 342
Cdd:PLN00412 252 ISKKA--GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 343 GQGcDVQIGPLINEMQFNKVSGFVEDARSKKANIIlggQPLPDKGSLFYaPTIVTDVPPSAQLYSEEVFGPVVSIIRFRD 422
Cdd:PLN00412 330 PED-DCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 423 EEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNegiisAAEA------PFGGVKESGVGREGSKHGIDDYV 496
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIGSQGITNSINMMT 479
|
...
gi 21356737 497 DIK 499
Cdd:PLN00412 480 KVK 482
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
77-493 |
1.99e-67 |
|
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: 223.13 E-value: 1.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 77 KQAYESKEWRSLtaKDRSNLLKKWHKLIEQHSQEIAEIMTAESGkpiNESKGEVAYGNAFV-------------EWFAEE 143
Cdd:cd07133 8 KAAFLANPPPSL--EERRDRLDRLKALLLDNQDALAEAISADFG---HRSRHETLLAEILPsiagikharkhlkKWMKPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 144 ARRIyGEIVPSASpNReiiVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLaVDAGIP 223
Cdd:cd07133 83 RRHV-GLLFLPAK-AE---VEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 224 KGVINVVTtnKAAPIGDLFCKSP-DvrGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMAS 302
Cdd:cd07133 157 EDEVAVVT--GGADVAAAFSSLPfD--HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 303 KFRNCGQTCVSANRFFV-QDSVyDKFVGQLKKRVEALkIGDGQGCDvQIGPLINEMQFNKVSGFVEDARSKKANII-LGG 380
Cdd:cd07133 233 KLLNAGQTCVAPDYVLVpEDKL-EEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIeLNP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 381 QPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGM 460
Cdd:cd07133 310 AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGG 389
|
410 420 430
....*....|....*....|....*....|....*
gi 21356737 461 VGVNEGIISAA--EAPFGGVKESGVGRegsKHGID 493
Cdd:cd07133 390 VTINDTLLHVAqdDLPFGGVGASGMGA---YHGKE 421
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
41-484 |
2.89e-67 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 233.94 E-value: 2.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 41 SNAKATFEVRNPANGA-VIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAES 119
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 120 GKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREI-IVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTV 198
Cdd:PRK11904 636 GKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESnELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 199 VVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA--DG-IkrIC 275
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLL-PGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAarDGpI--VP 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 276 L--ELGG-NApFIVFDSADIEKAVDGAMASKFRNCGQTCvSANR-FFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIG 351
Cdd:PRK11904 793 LiaETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRC-SALRvLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 352 PLINEMQFNKVSGFVEdARSKKANIILGGqPLPD--KGSLFYAPTIVtDVPPSAQLySEEVFGPVVSIIRFRDEE-EAVK 428
Cdd:PRK11904 871 PVIDAEAKANLDAHIE-RMKREARLLAQL-PLPAgtENGHFVAPTAF-EIDSISQL-EREVFGPILHVIRYKASDlDKVI 946
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 429 KA-NDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAA--EAPFGGVKESGVG 484
Cdd:PRK11904 947 DAiNATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVvgVQPFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
39-484 |
1.78e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 227.06 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 39 DSSNAKATFEVRNPAN-GAVIGKVPNMTVADAQKAIDAAKQAYEskEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTA 117
Cdd:PRK11905 561 GGDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFP--EWSATPAAERAAILERAADLMEAHMPELFALAVR 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 118 ESGKPINESKGEVAYGNAFVEWFAEEARRiygeiVPSASPNReiivmkqPIGVAALITPWNFPMAMITRKAGAALAAGCT 197
Cdd:PRK11905 639 EAGKTLANAIAEVREAVDFLRYYAAQARR-----LLNGPGHK-------PLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 198 VVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSAD-GIKRICL 276
Cdd:PRK11905 707 VLAKPAEQTPLIAARAVRLLHEAGVPKDALQLL-PGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKrSGPPVPL 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 277 --ELGG-NApFIVFDSADIEKAVDGAMASKFRNCGQTCvSANR-FFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGP 352
Cdd:PRK11905 786 iaETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRvLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGP 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 353 LINEMQFNKVSGFVEDARSKKAniILGGQPLPD--KGSLFYAPTIVtDVPPSAQLySEEVFGPVVSIIRFR-DEEEAVKK 429
Cdd:PRK11905 864 VIDAEAQANIEAHIEAMRAAGR--LVHQLPLPAetEKGTFVAPTLI-EIDSISDL-EREVFGPVLHVVRFKaDELDRVID 939
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 430 A-NDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISA--AEAPFGGVKESGVG 484
Cdd:PRK11905 940 DiNATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAvvGVQPFGGEGLSGTG 997
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
77-502 |
1.05e-62 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 212.58 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 77 KQAYESKEWRSLtaKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESK--------GEVAYG-NAFVEWFAEEARRI 147
Cdd:PTZ00381 17 KESFLTGKTRPL--EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLlKHLDEYLKPEKVDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 YGEIVPSASpnrEIIvmKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLaVDAGIPKGVI 227
Cdd:PTZ00381 95 VGVFGPGKS---YII--PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 228 NVVttNKAAPIGDLFCKSP-DVrgISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRN 306
Cdd:PTZ00381 169 RVI--EGGVEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 307 CGQTCVSANRFFVQDSVYDKFVGQLKkrvEALK--IGDGQGCDVQIGPLINEMQFNKVSGFVEDarsKKANIILGGQplP 384
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRSIKDKFIEALK---EAIKefFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE--V 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 385 DKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVN 464
Cdd:PTZ00381 317 DIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 21356737 465 EGIISAAEA--PFGGVKESGVGREGSKHGIDDYVDIKYIC 502
Cdd:PTZ00381 397 DCVFHLLNPnlPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
48-484 |
4.80e-62 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 219.81 E-value: 4.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 48 EVRNPANGA-VIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:COG4230 573 PVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDA 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGEV--A-----YgnafvewFAEEARRIYGEIVPSaspnreiivmkQPIGVAALITPWNFPMAMITRKAGAALAAGCTVV 199
Cdd:COG4230 651 IAEVreAvdfcrY-------YAAQARRLFAAPTVL-----------RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVL 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 200 VKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSAD---GIKRICL 276
Cdd:COG4230 713 AKPAEQTPLIAARAVRLLHEAGVPADVLQLL-PGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAArdgPIVPLIA 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 277 ELGG-NApFIVFDSADIEKAVDGAMASKFRNCGQTCvSANR-FFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLI 354
Cdd:COG4230 792 ETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRC-SALRvLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 355 NEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSLFYAPTIVtDVPPSAQLySEEVFGPVVSIIRFRDEE-EAVKKA-ND 432
Cdd:COG4230 870 DAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLI-EIDSISDL-EREVFGPVLHVVRYKADElDKVIDAiNA 947
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 21356737 433 TRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEA--PFGGVKESGVG 484
Cdd:COG4230 948 TGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGvqPFGGEGLSGTG 1001
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
32-501 |
5.75e-62 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 213.45 E-value: 5.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSNAkATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEI 111
Cdd:PLN02419 117 LIGGSFVESQSS-SFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--WRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 112 AEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAA 191
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 192 LAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVV-TTNKAApigDLFCKSPDVRGISFTGSTEVGKLLFRNSADG 270
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVhGTNDTV---NAICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 271 IKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVS-ANRFFVQDSvyDKFVGQLKKRVEALKIGDGQGCDVQ 349
Cdd:PLN02419 351 GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKLVERAKALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 350 IGPLINEMQFNKVSGFVEDARSKKANIILGGQ----PLPDKGSlFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEE 425
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvPGYEKGN-FIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDE 507
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356737 426 AVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGI-ISAAEAPFGGVKESGVGREG--SKHGIDDYVDIKYI 501
Cdd:PLN02419 508 AISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
28-484 |
4.12e-61 |
|
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: 208.61 E-value: 4.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 28 QDKALVDGAWVDSSNAKAtfeVRNPAN-GAVIGKVPNMTVADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQ 106
Cdd:TIGR01238 37 QAAPIIGHSYKADGEAQP---VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAF--PTWNATPAKERAAKLDRLADLLEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 107 HSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVpsaspnreiivmKQPIGVAALITPWNFPMAMITR 186
Cdd:TIGR01238 112 HMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFS------------VESRGVFVCISPWNFPLAIFTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 187 KAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVtTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRN 266
Cdd:TIGR01238 180 QISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLL-PGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 267 SA---DGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDG 343
Cdd:TIGR01238 259 LAqreDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 344 QGCDVQIGPLINEMQFNKVSGFVEDARSKK---ANIILGGQPLPDKGSlFYAPTIVtDVPPSAQLySEEVFGPVVSIIRF 420
Cdd:TIGR01238 339 HLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGT-FVAPTLF-ELDDIAEL-SEEVFGPVLHVVRY 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 421 RDEE--EAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEA--PFGGVKESGVG 484
Cdd:TIGR01238 416 KAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTG 483
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
93-491 |
4.61e-61 |
|
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: 206.97 E-value: 4.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 93 RSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESkgevaygnafvewFAEEARRIYGEI--------------------- 151
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEILEALKKDLGKSEFEA-------------YMTEIGFVLSEInyaikhlkkwmkpkrvktpll 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 152 -VPSASpnreiIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLaVDAGIPKGVINVV 230
Cdd:cd07136 89 nFPSKS-----YIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 231 T----TNKAapigdLFCKSPDVrgISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRN 306
Cdd:cd07136 163 EggveENQE-----LLDQKFDY--IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 307 CGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDvQIGPLINEMQFNKVSGFVEDArskkaNIILGGQPlpDK 386
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGNT--DR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 387 GSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEG 466
Cdd:cd07136 308 ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDT 387
|
410 420
....*....|....*....|....*..
gi 21356737 467 IISAA--EAPFGGVKESGVgreGSKHG 491
Cdd:cd07136 388 IMHLAnpYLPFGGVGNSGM---GSYHG 411
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
70-493 |
8.13e-59 |
|
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: 200.91 E-value: 8.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 70 QKAIDAAKQAYESKEWRSLtaKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES--------KGEVAYG-NAFVEWF 140
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPL--EFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAiSNLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 141 AEEArriygeiVPSASPNR--EIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLav 218
Cdd:cd07132 79 KPEP-------VKKNLATLldDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 219 dagIPKGVINvvttnkaapigDLFcksPDVRG---------------ISFTGSTEVGKLLFRNSADGIKRICLELGGNAP 283
Cdd:cd07132 150 ---IPKYLDK-----------ECY---PVVLGgveettellkqrfdyIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 284 FIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDvQIGPLINEMQFNKVS 363
Cdd:cd07132 213 CYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 364 GFVEdarskKANIILGGQplPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYS 443
Cdd:cd07132 292 KLLS-----GGKVAIGGQ--TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFS 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 21356737 444 ENLQQVFRVAKRLEVGMVGVNEGI--ISAAEAPFGGVKESGVGREGSKHGID 493
Cdd:cd07132 365 NNKKVINKILSNTSSGGVCVNDTImhYTLDSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
31-486 |
9.38e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 186.19 E-value: 9.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 31 ALVDGAWvdSSNAKATFEVrNPANGAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQE 110
Cdd:PLN02315 23 CYVGGEW--RANGPLVSSV-NPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRAKLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 111 IAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGA 190
Cdd:PLN02315 98 LGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 191 ALAAGCTVVVKPSEDTPLTALAVAKLAVDA----GIPKGVINVVTtnKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRN 266
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFC--GGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 267 SADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGC 346
Cdd:PLN02315 256 VNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 347 DVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSlFYAPTIVtDVPPSAQLYSEEVFGPVVSIIRFRDEEEA 426
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGN-FVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEA 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 427 VKKANDTRRGLAGYFYSENLQQVFRvakrlEVGMVGVNEGII------SAAE--APFGGVKESGVGRE 486
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPETIFK-----WIGPLGSDCGIVnvniptNGAEigGAFGGEKATGGGRE 476
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
3-484 |
2.55e-50 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 185.56 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 3 RQLSGVARTGS------------SLSLCRMRGFSALVQDKALVDGAWVDSSNAKatfeVRNPANGA-VIGKVPNMTVADA 69
Cdd:PRK11809 609 RDLYGKGRANSagldlanehrlaSLSSALLASAHQKWQAAPMLEDPVAAGEMSP----VINPADPRdIVGYVREATPAEV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 70 QKAIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYG 149
Cdd:PRK11809 685 EQALESAVNAAPI--WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFD 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 150 eivpsaspNReiivMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINV 229
Cdd:PRK11809 763 --------ND----THRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQL 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 230 V----TTNKAAPIGDlfcksPDVRGISFTGSTEVGKLLFRN-----SADGiKRICL--ELGGNAPFIVFDSADIEKAVDG 298
Cdd:PRK11809 831 LpgrgETVGAALVAD-----ARVRGVMFTGSTEVARLLQRNlagrlDPQG-RPIPLiaETGGQNAMIVDSSALTEQVVAD 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 299 AMASKFRNCGQTCvSANRFF-VQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANII 377
Cdd:PRK11809 905 VLASAFDSAGQRC-SALRVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 378 LGGQPLPDKGSL--FYAPTIVtDVPPSAQLySEEVFGPVVSIIRFRDEE--EAVKKANDTRRGLAGYFYS---ENLQQVF 450
Cdd:PRK11809 984 QAARENSEDWQSgtFVPPTLI-ELDSFDEL-KREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTridETIAQVT 1061
|
490 500 510
....*....|....*....|....*....|....*.
gi 21356737 451 RVAKrleVGMVGVNEGIISAAEA--PFGGVKESGVG 484
Cdd:PRK11809 1062 GSAH---VGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
77-493 |
1.90e-48 |
|
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: 172.98 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 77 KQAYESKEWRSltAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES-KGEV--------AYGNAFVEWFAEEARRI 147
Cdd:cd07137 9 RETFRSGRTRS--AEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssckLAIKELKKWMAPEKVKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 YGEIVPSaspNREIIvmKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLaVDAGIPKGVI 227
Cdd:cd07137 87 PLTTFPA---KAEIV--SEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 228 NVVTTNKAAPIGDLFCKSPDvrgISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNC 307
Cdd:cd07137 161 KVIEGGVPETTALLEQKWDK---IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 308 -GQTCVSANRFFVQDSVYDKFVGQLKKRVEALkIGDGQGCDVQIGPLINEMQFNKVSGFVEDaRSKKANIILGGQPlpDK 386
Cdd:cd07137 238 nGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGER--DE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 387 GSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEG 466
Cdd:cd07137 314 KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDT 393
|
410 420
....*....|....*....|....*....
gi 21356737 467 IISAA--EAPFGGVKESGVGREGSKHGID 493
Cdd:cd07137 394 VVQYAidTLPFGGVGESGFGAYHGKFSFD 422
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
31-482 |
1.29e-46 |
|
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: 169.69 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 31 ALVDGAWVDSSNAKatfEVRNPAN-GAVIGKVPNMTVADAQKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIE-QHS 108
Cdd:cd07123 35 LVIGGKEVRTGNTG---KQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKAADLLSgKYR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 109 QEI-AEIMTAEsGKPINESKGEVAYGNA-FVEWFAEEARRIYGEIVPSASP---NReiiVMKQPI-GVAALITPWNFpMA 182
Cdd:cd07123 110 YELnAATMLGQ-GKNVWQAEIDAACELIdFLRFNVKYAEELYAQQPLSSPAgvwNR---LEYRPLeGFVYAVSPFNF-TA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 183 MITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNkAAPIGDLFCKSPDVRGISFTGSTEVGKL 262
Cdd:cd07123 185 IGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD-GPVVGDTVLASPHLAGLHFTGSTPTFKS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 263 LFRNSADGIK------RICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVE 336
Cdd:cd07123 264 LWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 337 ALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDAR-SKKANIILGGQPLPDKGsLFYAPTIVTDVPPSAQLYSEEVFGPVV 415
Cdd:cd07123 344 EIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsDPEAEIIAGGKCDDSVG-YFVEPTVIETTDPKHKLMTEEIFGPVL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 416 SIIRFRDE--EEAVKKANDTRR-GLAGYFYSENlQQVFRVAK---RLEVGMVGVNEGIISA--AEAPFGGVKESG 482
Cdd:cd07123 423 TVYVYPDSdfEETLELVDTTSPyALTGAIFAQD-RKAIREATdalRNAAGNFYINDKPTGAvvGQQPFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
77-493 |
9.69e-39 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 147.57 E-value: 9.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 77 KQAYESKEWRSLtaKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES---------KGEVAYGNAFVEWFAEEARRi 147
Cdd:PLN02203 16 RETYESGRTRSL--EWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdevgvltKSANLALSNLKKWMAPKKAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 ygeiVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKlAVDAGIPKGVI 227
Cdd:PLN02203 93 ----LPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-NIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 228 NVVttNKAAPIGDLFCKSPDVRgISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIV--FDSA-DIEKAVDGAMASKF 304
Cdd:PLN02203 168 KVI--EGGPAVGEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 305 RNC-GQTCVSANRFFVQDSVYDKFVGQLKKRVEALkIGDGQGCDVQIGPLINEMQFNKVSGFVEDaRSKKANIILGGQPL 383
Cdd:PLN02203 245 GSCaGQACIAIDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSID 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 384 PDKgsLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGV 463
Cdd:PLN02203 323 EKK--LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTF 400
|
410 420 430
....*....|....*....|....*....|..
gi 21356737 464 NEGIIS-AAEA-PFGGVKESGVGREGSKHGID 493
Cdd:PLN02203 401 NDAIIQyACDSlPFGGVGESGFGRYHGKYSFD 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
139-495 |
7.69e-35 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 136.33 E-value: 7.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 139 WFAEEARRIYGEIVPSASPnreiiVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLA- 217
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLe 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 218 --VDAGIPKGVINVVTTNKAapigdLFCKSPDvrGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKA 295
Cdd:PLN02174 164 qyLDSSAVRVVEGAVTETTA-----LLEQKWD--KIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 296 VDGAMASKFR-NCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALkIGDGQGCDVQIGPLINEMQFNKVSGFVeDARSKKA 374
Cdd:PLN02174 237 VRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLL-DEKEVSD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 375 NIILGGQPlpDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAK 454
Cdd:PLN02174 315 KIVYGGEK--DRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAA 392
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21356737 455 RLEVGMVGVNEGIISAA--EAPFGGVKESGVGREGSKHGIDDY 495
Cdd:PLN02174 393 TVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAF 435
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
70-458 |
3.93e-34 |
|
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: 133.90 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 70 QKAIDAAKQAyeSKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPiNESKGEVAYGNAFVEWFAE--EARRI 147
Cdd:cd07084 2 ERALLAADIS--TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFviYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 YGEIVPSASPNREIIVMKQ--PIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGI-PK 224
Cdd:cd07084 79 PHEPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 225 GVINVVTTNKAApiGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGikRICLELGGNAPFIVFDSADIEKAV-DGAMASK 303
Cdd:cd07084 159 EDVTLINGDGKT--MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVaWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 304 FRNCGQTCVSANRFFV-QDSVYDKFVGQLKKRVEALKIGdgqgcDVQIGPlinEMQFNKVSGfVEDARSKKANIILGGQ- 381
Cdd:cd07084 235 TACSGQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLE-----DLLLGP---VQTFTTLAM-IAHMENLLGSVLLFSGk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 382 --PLPDKGSlFYAPTIVTD--VPPSA-----QLYSEEVFGPVVSIIRFRDEEEA--VKKANDTRRGLAGYFYSENLQQVF 450
Cdd:cd07084 306 elKNHSIPS-IYGACVASAlfVPIDEilktyELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQ 384
|
....*...
gi 21356737 451 RVAKRLEV 458
Cdd:cd07084 385 ELIGNLWV 392
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
30-445 |
5.05e-30 |
|
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: 122.76 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 30 KALVDGAWVDSSNAKATfeVRNPANGAVIGKVPNMTVaDAQKAIDAAKQAyESKEWRSLTAKDRSNLLKKWHKLIEQHSQ 109
Cdd:cd07128 2 QSYVAGQWHAGTGDGRT--LHDAVTGEVVARVSSEGL-DFAAAVAYAREK-GGPALRALTFHERAAMLKALAKYLMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 110 EIAEIMTAeSGKPINESKGEVAYGNAFVEWFAEEARR--------IYGEIVP-SASPN---REIIVMKQpiGVAALITPW 177
Cdd:cd07128 78 DLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlSKDGTfvgQHILTPRR--GVAVHINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 178 NFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGI-PKGVINVVttnkAAPIGDLF--CKSPDVrgISFT 254
Cdd:cd07128 155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLI----CGSVGDLLdhLGEQDV--VAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 255 GSTEVGKLLfRNSADGIKRiclelggNAPFIV-FDS-------ADIE----------KAVDGAMASKfrnCGQTCVSANR 316
Cdd:cd07128 229 GSAATAAKL-RAHPNIVAR-------SIRFNAeADSlnaailgPDATpgtpefdlfvKEVAREMTVK---AGQKCTAIRR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 317 FFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEdARSKKANIILGGQP-------LPDKGSl 389
Cdd:cd07128 298 AFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPDrfevvgaDAEKGA- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356737 390 FYAPTIVTDVPP--SAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSEN 445
Cdd:cd07128 376 FFPPTLLLCDDPdaATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
33-443 |
3.15e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 114.80 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 33 VDGAWVDSSNAKATfeVRNPANGAVIGKVpNMTVADAQKAIDAAKQAyESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIA 112
Cdd:PRK11903 9 VAGRWQAGSGAGTP--LFDPVTGEELVRV-SATGLDLAAAFAFAREQ-GGAALRALTYAQRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 113 EIMTAESGKPINESKGEVAYGNAFVEWFAE------EAR-RIYGEIVPSA-----------SPNReiivmkqpiGVAALI 174
Cdd:PRK11903 85 DIATANSGTTRNDSAVDIDGGIFTLGYYAKlgaalgDARlLRDGEAVQLGkdpafqgqhvlVPTR---------GVALFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 175 TPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGI-PKGVINVVttnkAAPIGDLF--CKSPDVrgI 251
Cdd:PRK11903 156 NAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV----CGSSAGLLdhLQPFDV--V 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 252 SFTGSTEVGKLL------FRNS------ADGIKRiCLELGGNAPfivfDSADIE---KAVDGAMASKfrnCGQTCVSANR 316
Cdd:PRK11903 230 SFTGSAETAAVLrshpavVQRSvrvnveADSLNS-ALLGPDAAP----GSEAFDlfvKEVVREMTVK---SGQKCTAIRR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 317 FFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARsKKANIILGG--QPL---PDKGSLFY 391
Cdd:PRK11903 302 IFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALR-AQAEVLFDGggFALvdaDPAVAACV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 21356737 392 APTI--VTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYS 443
Cdd:PRK11903 381 GPTLlgASDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
72-431 |
1.46e-25 |
|
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: 109.17 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 72 AIDAAKQAYESkeWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARR--IYG 149
Cdd:cd07129 4 AAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 150 EIVPSASPNR------EIIVMKQPIGVAALITPWNFPMAMITrkAG----AALAAGCTVVVKPSEDTPLTALAVAKLAVD 219
Cdd:cd07129 82 ARIDPADPDRqplprpDLRRMLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 220 A----GIPKGVINVVTTNKAApIGDLFCKSPDVRGISFTGSTEVGKLLFRNSA---DGIKrICLELGGNAPFIVFDSA-- 290
Cdd:cd07129 160 AlratGLPAGVFSLLQGGGRE-VGVALVKHPAIKAVGFTGSRRGGRALFDAAAarpEPIP-FYAELGSVNPVFILPGAla 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 291 -DIEKAVDGAMASKFRNCGQTCVSANRFFVQDSV-YDKFVGQLKKRVEAlkigdgqgcdVQIGPLINEmqfNKVSGF--- 365
Cdd:cd07129 238 eRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAA----------APAQTMLTP---GIAEAYrqg 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356737 366 VEDARSKKANIILGGQPLPDKGSLfYAPTI-VTDV-----PPSAQlysEEVFGPVVSIIRFRDEEEAVKKAN 431
Cdd:cd07129 305 VEALAAAPGVRVLAGGAAAEGGNQ-AAPTLfKVDAaaflaDPALQ---EEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
48-457 |
2.59e-14 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 74.94 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 48 EVRNPANGAVIGKVPNMTV-ADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINES 126
Cdd:PRK15398 16 EMLSSQTVSPPAAVGEMGVfASVDDAVAAAKVAQ--QRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 127 KGE----VAYGNAFVEWFAEEARRIYGEIVpsaspnreiIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKP 202
Cdd:PRK15398 94 KIAknvaAAEKTPGVEDLTTEALTGDNGLT---------LIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 203 SedtP----LTALAVAKL---AVDAGIPKGVINVVTTNKAAPIGDLFcKSPDVRGISFTGSTEVGKLLfRNSadGIKRIC 275
Cdd:PRK15398 165 H---PgakkVSLRAIELLneaIVAAGGPENLVVTVAEPTIETAQRLM-KHPGIALLVVTGGPAVVKAA-MKS--GKKAIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 276 LelG-GNAPFIVFDSADIEKA----VDGAmasKFRNcGQTCVSANRFFVQDSVYDKFVGQLKKRvEALKIGDGQGCDVQI 350
Cdd:PRK15398 238 A--GaGNPPVVVDETADIEKAardiVKGA---SFDN-NLPCIAEKEVIVVDSVADELMRLMEKN-GAVLLTAEQAEKLQK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 351 GPLINEMQFNKvsGFVedarSKKANIILG--GQPLPDKGSLfyaptIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVK 428
Cdd:PRK15398 311 VVLKNGGTVNK--KWV----GKDAAKILEaaGINVPKDTRL-----LIVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
410 420 430
....*....|....*....|....*....|.
gi 21356737 429 KANDTRRGL--AGYFYSENLQQVFRVAKRLE 457
Cdd:PRK15398 380 LAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
68-430 |
4.52e-14 |
|
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: 74.22 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 68 DAQKAIDAAKQAYESKewrslTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKgevAYGNAFvewfaeEARRI 147
Cdd:cd07081 3 DAVAAAKVAQQGLSCK-----SQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDK---VIKNHF------AAEYI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 148 YGEIVPSASP-------NREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKP----SEDTPLTALAVAKL 216
Cdd:cd07081 69 YNVYKDEKTCgvltgdeNGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 217 AVDAGIPKGVINVVTtNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSadgiKRICLELGGNAPFIVFDSADIEKAV 296
Cdd:cd07081 149 AVAAGAPENLIGWID-NPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSG----KPAIGVGAGNTPVVIDETADIKRAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 297 DGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRvEALKIGDGQGCDVQIGPLINEMQFNKVSGfvEDARSKKAni 376
Cdd:cd07081 224 QSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQ-GAYKLTAEELQQVQPVILKNGDVNRDIVG--QDAYKIAA-- 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21356737 377 iLGGQPLPDKGS-LFYAPTIVTDVPPSAQlyseEVFGPVVSIIRFRDEEEAVKKA 430
Cdd:cd07081 299 -AAGLKVPQETRiLIGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
67-457 |
1.23e-12 |
|
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: 69.57 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 67 ADAQKAIDAAKQAYesKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGkpineskgevaYGNAfvewfaeEARR 146
Cdd:cd07121 4 ATVDDAVAAAKAAQ--KQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG-----------MGRV-------EDKI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 147 IYGEIVPSASPNREIIVMK-------------QPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSedtP----LT 209
Cdd:cd07121 64 AKNHLAAEKTPGTEDLTTTawsgdngltlveyAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPH---PgakkVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 210 ALAVAKL---AVDAGIPKGVINVVTTNKAAPIGDLFcKSPDVRGISFTGSTEVGKLLfRNSadGIKRICLelG-GNAPFI 285
Cdd:cd07121 141 AYAVELInkaIAEAGGPDNLVVTVEEPTIETTNELM-AHPDINLLVVTGGPAVVKAA-LSS--GKKAIGA--GaGNPPVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 286 VFDSADIEKA----VDGAmasKFRNcGQTCVSANRFFVQDSVYDKFVGQLkKRVEALKIGDGQgcDVQIGPLIneMQFNK 361
Cdd:cd07121 215 VDETADIEKAardiVQGA---SFDN-NLPCIAEKEVIAVDSVADYLIAAM-QRNGAYVLNDEQ--AEQLLEVV--LLTNK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 362 VSGFVEDARSKKANIILG--GQPLPDKGSLfyaptIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGL-- 437
Cdd:cd07121 286 GATPNKKWVGKDASKILKaaGIEVPADIRL-----IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrh 360
|
410 420
....*....|....*....|
gi 21356737 438 AGYFYSENLQQVFRVAKRLE 457
Cdd:cd07121 361 TAIIHSKNVENLTKMARAMQ 380
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
32-425 |
3.79e-12 |
|
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: 68.29 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 32 LVDGAWVDSSNAKatfEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLlkkWHKLIEQHSQEI 111
Cdd:cd07126 2 LVAGKWKGASNYT---TLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLL---YGDVSHRVAHEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 112 AEIMTAE---------SGKPINESKGEVAYGNAFVEWFAEEARRIY--GEIVPSASPNREIIVMKQPIGVAALITPWNFP 180
Cdd:cd07126 76 RKPEVEDffarliqrvAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 181 MAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVttNKAAPIGDLFCKSPDVRGISFTGSTEVG 260
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLI--HSDGPTMNKILLEANPRMTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 261 kllfrnsadgiKRICLELGGNapfIVFDSADIEKAVDGAMASKFR----NC--------GQTCVSANRFFVQDS-VYDKF 327
Cdd:cd07126 234 -----------ERLALELHGK---VKLEDAGFDWKILGPDVSDVDyvawQCdqdayacsGQKCSAQSILFAHENwVQAGI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 328 VGQLKKRVEALKIGdgqgcDVQIGPLI---NEMQFNKVSGFVEDARSKkanIILGGQPLPDK------GSL----FYAPT 394
Cdd:cd07126 300 LDKLKALAEQRKLE-----DLTIGPVLtwtTERILDHVDKLLAIPGAK---VLFGGKPLTNHsipsiyGAYeptaVFVPL 371
|
410 420 430
....*....|....*....|....*....|.
gi 21356737 395 IVTDVPPSAQLYSEEVFGPVVSIIRFRDEEE 425
Cdd:cd07126 372 EEIAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
157-464 |
4.93e-12 |
|
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: 67.90 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 157 PNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKL----AVDAGIPKGVINVVTT 232
Cdd:cd07122 85 EEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 233 NKAAPIGDLFcKSPDVRGISFTGSTEVGKLLFR--NSADGIkriclelG-GNAPFIVFDSADIEKAVDGAMASKFRNCGQ 309
Cdd:cd07122 165 PSIELTQELM-KHPDVDLILATGGPGMVKAAYSsgKPAIGV-------GpGNVPAYIDETADIKRAVKDIILSKTFDNGT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 310 TCVSANRFFVQDSVYDKFVGQLKKrvealkigdgQGCdvqigPLINEMQFNKVSGFVEDARSK-KANIIlgGQPlpdkgs 388
Cdd:cd07122 237 ICASEQSVIVDDEIYDEVRAELKR----------RGA-----YFLNEEEKEKLEKALFDDGGTlNPDIV--GKS------ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 389 lfyAPTIVT----DVPPSAQL-------------YSEEVFGPVVSIIRFRDEEEAVKKAND-TRRGLAGY---FYSENLQ 447
Cdd:cd07122 294 ---AQKIAElagiEVPEDTKVlvaeetgvgpeepLSREKLSPVLAFYRAEDFEEALEKARElLEYGGAGHtavIHSNDEE 370
|
330
....*....|....*..
gi 21356737 448 QVFRVAKRLEVGMVGVN 464
Cdd:cd07122 371 VIEEFALRMPVSRILVN 387
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
103-340 |
3.29e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 64.94 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 103 LIEQHSQEIAEIMTAESGKPINE-----------SKGEVAYGNAFVEWFAEEARRIYGEIVPSaspNREIIVMKQPIGVA 171
Cdd:cd07077 28 ALYDTRQRLASEAVSERGAYIRSlianwiammgcSESKLYKNIDTERGITASVGHIQDVLLPD---NGETYVRAFPIGVT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 172 ALITPWNFPMAMITrKAGAALAAGCTVVVKPSEDTPLTALAVAKL---AVDAGIPKGVINVVTTNKAAPIGDLfCKSPDV 248
Cdd:cd07077 105 MHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLfqaADAAHGPKILVLYVPHPSDELAEEL-LSHPKI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 249 RGISFTGSTEVGKLLfRNSADGIKRIclELGGNAPFIVFDS-ADIEKAVDGAMASKFRNcGQTCVSANRFFVQDSVYD-- 325
Cdd:cd07077 183 DLIVATGGRDAVDAA-VKHSPHIPVI--GFGAGNSPVVVDEtADEERASGSVHDSKFFD-QNACASEQNLYVVDDVLDpl 258
|
250
....*....|....*..
gi 21356737 326 --KFVGQLkkRVEALKI 340
Cdd:cd07077 259 yeEFKLKL--VVEGLKV 273
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
66-478 |
7.30e-10 |
|
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: 61.34 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 66 VADAQKAIDAAKQAYesKEWRSLTAKDRSNL----LKKWHKLI------EQHSQEIAEIMTAESGKPINESKG--EVAYG 133
Cdd:cd07127 83 QCDPDALLAAARAAM--PGWRDAGARARAGVcleiLQRLNARSfemahaVMHTTGQAFMMAFQAGGPHAQDRGleAVAYA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 134 NAFVEWFAEEAR--RIYGEIVPSASPNREIIVmkqPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTAL 211
Cdd:cd07127 161 WREMSRIPPTAEweKPQGKHDPLAMEKTFTVV---PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 212 AVAKLA----VDAGIPKGVINVVTTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSadGIKRICLELGGNAPFIVf 287
Cdd:cd07127 238 ITVQVArevlAEAGFDPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA--RQAQVYTEKAGVNTVVV- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 288 DSADIEKAVDGAMAskFRNC---GQTCVSANRFFV-QDSV--------YDKFVGQLKKRVEALKIGDGQGCDVqIGPLIN 355
Cdd:cd07127 315 DSTDDLKAMLRNLA--FSLSlysGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGLLADPARAAAL-LGAIQS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 356 EMqfnkVSGFVEDARsKKANIILGGQPL--PD-KGSLFYAPTIVT-DVPPSAqLYSEEVFGPVVSIIRFRDEEEAVKKAN 431
Cdd:cd07127 392 PD----TLARIAEAR-QLGEVLLASEAVahPEfPDARVRTPLLLKlDASDEA-AYAEERFGPIAFVVATDSTDHSIELAR 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 432 DTRR---GLAGYFYS---ENLQQVFRVAKRLEV-------GMVGVNEgiiSAAEAPFGGV 478
Cdd:cd07127 466 ESVRehgAMTVGVYStdpEVVERVQEAALDAGValsinltGGVFVNQ---SAAFSDFHGT 522
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
161-430 |
2.89e-06 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 50.18 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 161 IIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPS----EDTPLTALAVAKLAVDAGIPKGVINVVTTNKAA 236
Cdd:PRK13805 102 IIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraqKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 237 PIGDLFcKSPDVRGISFTG---------STevGKllfrnSADGIkriclelG-GNAPFIVFDSADIEKAVDGAMASK-FR 305
Cdd:PRK13805 182 LTNALM-NHPGIALILATGgpgmvkaaySS--GK-----PALGV-------GaGNVPAYIDKTADIKRAVNDILLSKtFD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356737 306 NcGQTCVSANRFFVQDSVYDKFVGQLKKRvealkigdgqGCDvqigpLINEMQFNKVSGFVEDARSKKANIILGGQP--- 382
Cdd:PRK13805 247 N-GMICASEQAVIVDDEIYDEVKEEFASH----------GAY-----FLNKKELKKLEKFIFGKENGALNADIVGQSayk 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 21356737 383 --------LPDKGSLFYAPtiVTDVPPSAQLySEEVFGPVVSIIRFRDEEEAVKKA 430
Cdd:PRK13805 311 iaemagfkVPEDTKILIAE--VKGVGESEPL-SHEKLSPVLAMYKAKDFEDAVEKA 363
|
|
| |
