|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
30-480 |
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: 828.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 190 LAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 270 IDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALT 349
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 350 RGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRV 429
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 505180169 430 SEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQ 480
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
6-481 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 763.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 6 SDLFRQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILE 85
Cdd:PLN02278 20 AGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 86 NKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:PLN02278 100 NKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 246 AESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:PLN02278 260 AATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 326 VQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIE 405
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 406 QANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQG 481
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-482 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 719.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 1 MSVFHSDLFRQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWH 80
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 81 HLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPA 160
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 161 AMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRV 240
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 241 LMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGD 320
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 321 GSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDE 400
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 401 QEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQ 480
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
..
gi 505180169 481 GL 482
Cdd:PRK11241 481 GL 482
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
30-476 |
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: 699.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 190 LAMAELANQAGIPQGVINVVTG-QSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAL 348
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 349 TRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWR 428
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 505180169 429 VSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
9-482 |
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: 674.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 9 FRQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKT 88
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 89 ALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAG 168
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 169 PALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES 248
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQI 328
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 329 GPLINADAGRKVQSLLDDALTRGATLLTGGKAHPL-GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGREGSEHGIEDYLEMKYLCQGL 482
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-476 |
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: 603.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 19 WRDAADGTsLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQ 98
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 99 GKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPgADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMV 178
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 179 IKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGG 258
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 259 NAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGR 338
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 339 KVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYF 418
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 505180169 419 YSNDAARIWRVSEQLEYGMVGINTGLISN-EVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
51-476 |
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: 543.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 51 QQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEI 130
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 131 IPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVT 210
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 211 GQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCV 290
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 291 CVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLG-GNFFT 369
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 370 PTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV 449
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420
....*....|....*....|....*...
gi 505180169 450 -APFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07078 401 sAPFGGVKQSGIGREGGPYGLEEYTEPK 428
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
15-476 |
0e+00 |
|
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: 516.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAG 174
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 175 CTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSL 254
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 255 ELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINA 334
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 335 DAGRKVQSLLDDALTRGATLLTGGKAHPLG-GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYG 413
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 414 LASYFYSNDAARIWRVSEQLEYGMVGINTGlisNEVAPFG---GVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
32-479 |
3.26e-171 |
|
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: 489.38 E-value: 3.26e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE-GEIA 110
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 111 YAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTAL 190
Cdd:cd07093 83 RAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 191 AMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADI 270
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 271 DKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTR 350
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 351 GATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARI 426
Cdd:cd07093 322 GATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 505180169 427 WRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07093 402 HRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
32-476 |
1.99e-167 |
|
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: 480.12 E-value: 1.99e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAAL--PAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 190 LAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07114 163 LELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 270 IDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALT 349
Cdd:cd07114 243 LDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARARE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 350 RGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07114 323 EGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLAR 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 505180169 426 IWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07114 403 AHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
30-476 |
3.05e-166 |
|
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: 476.64 E-value: 3.05e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQgkRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIED-DDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 190 LAMAELANQAgIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 270 IDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALT 349
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 350 RGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRV 429
Cdd:cd07106 316 KGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 505180169 430 SEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07106 396 ARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
3-476 |
3.31e-161 |
|
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: 464.76 E-value: 3.31e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 3 VFHSDLFrqqalIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA--WRALTAAQRAALLKNWH 80
Cdd:cd07091 1 EQPTGLF-----INNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 81 HLILENKTALAQIMTAEQGKPLAE-AEGEIAYAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFP 159
Cdd:cd07091 76 DLIERDRDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPIDG-NFLAYTRREPIGVCGQIIPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 160 AAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGR 239
Cdd:cd07091 155 LLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 240 VLMRQCAES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKV 318
Cdd:cd07091 235 TIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 319 GDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFE 398
Cdd:cd07091 315 GDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180169 399 DEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
32-478 |
2.44e-158 |
|
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: 456.79 E-value: 2.44e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAY 111
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 112 AASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALA 191
Cdd:cd07150 85 TPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 192 MAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADID 271
Cdd:cd07150 165 IAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 272 KAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRG 351
Cdd:cd07150 245 YAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 352 ATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSE 431
Cdd:cd07150 325 AKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 505180169 432 QLEYGMVGINTGLISNE-VAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07150 402 RLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
49-478 |
9.05e-156 |
|
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: 449.29 E-value: 9.05e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 49 EAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANG 128
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 129 EIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT-ALAMAELANQAGIPQGVIN 207
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 208 VVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQ 287
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 288 TCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHplgGNF 367
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 368 FTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISN 447
Cdd:cd07104 318 YQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVND 397
|
410 420 430
....*....|....*....|....*....|..
gi 505180169 448 E-VAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07104 398 EpHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-476 |
4.08e-154 |
|
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: 446.56 E-value: 4.08e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEAE--------GEIAYAASFIEWFAEQGKRANGeiipspgadkrlMVIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:cd07138 83 TLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERRGNS------------LVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 327 QIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLG---GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEV 403
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGlerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINtGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
30-479 |
3.65e-152 |
|
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: 440.88 E-value: 3.65e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEIIP---SPGADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANET 185
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPfdaSPGGEGRIgFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 186 PFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAesIKKLSLELGGNAPFIVF 265
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 266 DDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLD 345
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 346 DALTRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07149 321 EAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 426 IWRVSEQLEYGMVGINTglISN---EVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07149 398 ALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-476 |
2.35e-150 |
|
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: 437.51 E-value: 2.35e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAAL--PAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRlMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 333 NADAGRKVQSLLDDALTRGATLLTGGKAhPLG-----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKR-PTGdelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT-GLISNEvAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFAE-APWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
14-476 |
1.65e-146 |
|
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: 427.53 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTSLAVSNPSTGATL-GQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 333 NADAGRKVQSLLDDALTRGATLLTGGKA----HPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQAN 408
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 409 NTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
28-478 |
5.15e-146 |
|
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: 425.61 E-value: 5.15e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 108 EIAYAASFIEWFAEQGKRANGEIIPSPGAD--KRLMVI--RQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEynERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 184 ETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFI 263
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 344 LDDALTRGATLLTGGKAHPlgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDA 423
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 424 ARIWRVSEQLEYGMVGIN-TGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07145 399 NRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-476 |
4.58e-145 |
|
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: 423.52 E-value: 4.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAAL--PAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:cd07139 83 LWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKK 251
Cdd:cd07139 163 AAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 252 LSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPL 331
Cdd:cd07139 242 VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 332 INADAGRKVQSLLDDALTRGATLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANN 409
Cdd:cd07139 322 ASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINtGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07139 402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
30-476 |
2.25e-143 |
|
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: 418.96 E-value: 2.25e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAW-RALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEG- 107
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 108 EIAYAASFIEWFAEQGKRANGEII----PSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDlpvpALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 184 ETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFI 263
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 344 LDDALTRGATLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSN 421
Cdd:cd07089 321 IARGRDEGARLVTGGGrpAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505180169 422 DAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
50-469 |
3.69e-143 |
|
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: 417.25 E-value: 3.69e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 50 AQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRAN-G 128
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLaD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 129 EIIPSPGadKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINV 208
Cdd:cd07100 81 EPIETDA--GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 209 VTGQSREIGAVFtGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQT 288
Cdd:cd07100 159 LLIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 289 CVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFF 368
Cdd:cd07100 238 CIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 369 TPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNE 448
Cdd:cd07100 318 PPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDP 397
|
410 420
....*....|....*....|.
gi 505180169 449 VAPFGGVKQSGLGREGSEHGI 469
Cdd:cd07100 398 RLPFGGVKRSGYGRELGRFGI 418
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-476 |
3.96e-143 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 418.93 E-value: 3.96e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWrDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALA 91
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 92 QIMTAEQGKPL-AEAEGEIAYAASFIEWFAE-----QGKRAnGEIIPspgaDKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:PRK13473 83 RLESLNCGKPLhLALNDEIPAIVDVFRFFAGaarclEGKAA-GEYLE----GHTSMIRRDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 246 AESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:PRK13473 237 ADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 326 VQIGPLINADAGRKVQSLLDDALTRG-ATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVI 404
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 405 EQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT-GLISNEvAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNThFMLVSE-MPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-479 |
4.89e-143 |
|
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: 414.32 E-value: 4.89e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 55 DAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSP 134
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 135 GADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSR 214
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 215 EIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNR 294
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 295 FYIHRAVYDQFCDKFVarvaalkvgdgsesdvqigplinadagrkvqsllddaltrgatlltggkahplggnfftpTVIG 374
Cdd:cd06534 241 LLVHESIYDEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 375 DVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFG 453
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFG 340
|
410 420
....*....|....*....|....*.
gi 505180169 454 GVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
30-478 |
8.75e-142 |
|
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: 414.83 E-value: 8.75e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFA---EQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETP 186
Cdd:cd07110 81 DDVAGCFEYYAdlaEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 187 FTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFD 266
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 267 DADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDD 346
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 347 ALTRGATLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07110 321 GKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505180169 425 RIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
17-477 |
1.37e-141 |
|
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: 414.39 E-value: 1.37e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 17 GSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTA 96
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 97 EQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCT 176
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 177 MVIKPANETPFTA-LAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLE 255
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 256 LGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINAD 335
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 336 AGRKVQSLLDDALTRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLA 415
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 416 SYFYSNDAARIWRVSEQLEYGMVGINTGLISNE-VAPFGGVKQSGLGREGSEHGIEDYLEMKY 477
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKW 460
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-476 |
3.11e-141 |
|
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: 413.54 E-value: 3.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 25 GTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA--WRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPL 102
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 103 AEA-EGEIAYAASFIEWFAEQGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKP 181
Cdd:cd07112 81 SDAlAVDVPSAANTFRWYAEAIDKVYGEVAPT-GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 182 ANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-IKKLSLELGGNA 260
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 261 PFIVFDDA-DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRK 339
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 340 VQSLLDDALTRGATLLTGGKAHPL--GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASY 417
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 418 FYSNDAARIWRVSEQLEYGMVGINT---GLISnevAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCfdeGDIT---TPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
14-476 |
8.67e-141 |
|
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: 412.80 E-value: 8.67e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGtsLAVSNPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:cd07097 4 YIDGEWVAGGDG--EENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 333 NADAGRKVQSLLDDALTRGATLLTGGKAHPLG--GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNT 410
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180169 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-479 |
1.29e-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: 411.44 E-value: 1.29e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 108 EIAYAASFIEWFAEQGKRANGEIIPSP---GADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqGSDNRLaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 184 ETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAesIKKLSLELGGNAPFI 263
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 344 LDDALTRGATLLTGGKahpLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDA 423
Cdd:cd07094 319 VEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 424 ARIWRVSEQLEYGMVGINTG-LISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
32-478 |
7.07e-140 |
|
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: 409.69 E-value: 7.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAY 111
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 112 AASFIEWFAEQGKR--ANGEIIPSPG-ADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07099 82 ALEAIDWAARNAPRvlAPRKVPTGLLmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 189 ALAMAELANQAGIPQGVINVVTGqSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTG-DGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAL 348
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 349 TRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWR 428
Cdd:cd07099 320 AKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505180169 429 VSEQLEYGMVGIN----TGLISNevAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07099 400 IARRLEAGAVSINdvllTAGIPA--LPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-478 |
6.96e-139 |
|
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: 407.02 E-value: 6.96e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 108 EIAYAASFIEWFAEQGKRANGEIIP---SPGADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGEGRQgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 184 ETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAEsiKKLSLELGGNAPFI 263
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 344 LDDALTRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDA 423
Cdd:cd07147 318 VNEAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 424 ARIWRVSEQLEYGmvgintGLISNEV-------APFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07147 395 EKALRAWDELEVG------GVVINDVptfrvdhMPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-482 |
1.18e-137 |
|
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: 404.13 E-value: 1.18e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEG-EIA 110
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 111 YAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTAL 190
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 191 AMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADI 270
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 271 DKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTR 350
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 351 GATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVS 430
Cdd:cd07115 322 GARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 505180169 431 EQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQGL 482
Cdd:cd07115 402 AALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
14-466 |
4.74e-137 |
|
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: 403.48 E-value: 4.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTsLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:cd07086 2 VIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 174 GCTMVIKPANETPFTALAMAELANQA----GIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESI 249
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 250 KKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 330 PLINADAGRKVQSLLDDALTRGATLLTGGKA--HPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 408 NNTIYGLASYFYSNDAARI--WRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGRE-GSE 466
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGREsGSD 462
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
30-477 |
3.22e-136 |
|
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: 400.16 E-value: 3.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAE-AEGE 108
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 109 IAYAASFIEWFA----EQGKRANGEIIPSPGAdkrlMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANE 184
Cdd:cd07092 81 LPGAVDNFRFFAgaarTLEGPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 185 TPFTALAMAELAnQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIV 264
Cdd:cd07092 157 TPLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 265 FDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLL 344
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 345 DDAlTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07092 316 ERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505180169 425 RIWRVSEQLEYGMVGINT-GLISNEvAPFGGVKQSGLGREGSEHGIEDYLEMKY 477
Cdd:cd07092 395 RAMRLSARLDFGTVWVNThIPLAAE-MPHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
33-476 |
5.50e-136 |
|
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: 399.79 E-value: 5.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 33 PSTGATLGQIPNMGRAEAQQAVDAATAALPA--WRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIA 110
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 111 YAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTAL 190
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 191 AMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADI 270
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 271 DKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTR 350
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 351 GATLLTGGKAHPLG-GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRV 429
Cdd:cd07118 324 GATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTV 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 505180169 430 SEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07118 404 ARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-476 |
4.89e-135 |
|
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: 398.32 E-value: 4.89e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA-WRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPL-AEAEGEIAYAASFIEWFAEQGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07144 92 EALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPT-SPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVA-ALKVGDGSESDVQIGPL 331
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 332 INADAGRKVQSLLDDALTRGATLLTGGKAHPLG---GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQAN 408
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180169 409 NTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
30-476 |
7.03e-135 |
|
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: 396.99 E-value: 7.03e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA-WRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGE 108
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 109 IAYAASFIEWFAEQGKRANGEIIPsPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 189 ALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSEsDVQIGPLINADAGRKVQSLLDDAL 348
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 349 TRGATLLTGGKA---HPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07109 319 ARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 505180169 426 IWRVSEQLEYGMVGINTGLISNEVA-PFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGIElPFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-476 |
1.14e-134 |
|
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: 397.49 E-value: 1.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 3 VFHSDLFrqqalIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAAL---PAWRALTAAQRAALLKNW 79
Cdd:cd07141 4 IKYTKIF-----INNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 80 HHLILENKTALAQIMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNF 158
Cdd:cd07141 79 ADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 159 PAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVG 238
Cdd:cd07141 158 PLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 239 RVLMRQCAES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALK 317
Cdd:cd07141 238 KLIQQAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 318 VGDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKF 397
Cdd:cd07141 318 VGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180169 398 EDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
10-480 |
2.56e-133 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 394.87 E-value: 2.56e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 10 RQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA-----WRALTAAQRAALLKNWHHLIL 84
Cdd:PLN02467 7 RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 85 ENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQG---KRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAA 161
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAealDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 162 MITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVL 241
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 242 MRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDG 321
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 322 SESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKA-HPLGGNFFT-PTVIGDVQPGSLLLQEEIFGPVAALVKFED 399
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFIePTIITDVTTSMQIWREEVFGPVLCVKTFST 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 400 EQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:PLN02467 407 EDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVT 486
|
.
gi 505180169 480 Q 480
Cdd:PLN02467 487 K 487
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
30-479 |
5.09e-132 |
|
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: 389.74 E-value: 5.09e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEIIPSPG---ADKRlmviRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETP 186
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGgsfAYTR----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 187 FTALAMAELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFD 266
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 267 DADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDD 346
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 347 ALTRGATLLTGG-KAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSN 421
Cdd:cd07090 316 AKQEGAKVLCGGeRVVPEdgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505180169 422 DAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
5-476 |
7.08e-132 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 390.40 E-value: 7.08e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 5 HSDLFRQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLIL 84
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 85 ENKTALAQIMTAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGADkRLMVIRQGVGVCAAITPWNFPAAMI 163
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGS-FVYTRREPLGVCAGIGAWNYPIQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 164 TRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMR 243
Cdd:PRK13252 160 CWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 244 QCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQtcVCVN--RFYIHRAVYDQFCDKFVARVAALKVGDG 321
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 322 SESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLG----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKF 397
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTF 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180169 398 EDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-480 |
2.93e-130 |
|
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: 385.16 E-value: 2.93e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAAL--PAWRAlTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEII-PSPGADKrlMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIePEPGSFS--LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 189 ALAMAE-LANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDD 267
Cdd:cd07120 160 NAAIIRiLAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 268 ADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDA 347
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 348 LTRGATLLTGGKAHPLG---GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07120 320 IAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 425 RIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQ 480
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
30-476 |
2.98e-129 |
|
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: 382.86 E-value: 2.98e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPL-AEAEGE 108
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 109 IAYAASFIEWFAEQGKRANGEIIPsPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 189 ALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 269 DIDKAVEGALIA-KFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDA 347
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 348 L-TRGATLLTGGKAHPLG----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSND 422
Cdd:cd07108 319 LsTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505180169 423 AARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGS-EHGIEDYLEMK 476
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKK 453
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
15-476 |
3.38e-129 |
|
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: 383.01 E-value: 3.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGADKrLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:TIGR01804 82 TLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPSF-AYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 174 GCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLS 253
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 254 LELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLIN 333
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 334 ADAGRKVQSLLDDALTRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANN 409
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:TIGR01804 401 TEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
21-474 |
4.10e-128 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 382.30 E-value: 4.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 21 DAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGK 100
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 101 PLAEAEGEIAYAASFIEWFAEQG------KRANGEIipsPGAdKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAG 174
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRApkllapRRRAGAL---PVL-TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 175 CTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgdERVRKLSFTGSTEVGRVLMRQCAESIKKLSL 254
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 255 ELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINA 334
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 335 DAGRKVQSLLDDALTRGATLLTGGKAHP-LGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYG 413
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKARPdLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYG 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180169 414 LASYFYSNDAARIWRVSEQLEYGMVGINTGLIS---NEVAPFGGVKQSGLGREGSEHGIEDYLE 474
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-479 |
6.41e-128 |
|
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: 379.86 E-value: 6.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAAL-PAWRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEI----IPSPGADK-RLMVIRQGVGVCAAITPWNFPAAMITRKA 167
Cdd:cd07113 84 ETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 168 GPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE 247
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 248 SIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 328 IGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
14-478 |
2.46e-127 |
|
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: 378.61 E-value: 2.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPLAEAEG-EIAYAASFIEWFAeqgkranGEIIPSPGA----DKRLM--VIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFA-------GVIRAQEGSlseiDEDTLsyHFHEPLGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 247 ESIKKLSLELGGNAPFIVFDDA-----DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDG 321
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 322 SESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLG----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKF 397
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 398 EDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKY 477
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKN 475
|
.
gi 505180169 478 L 478
Cdd:cd07559 476 I 476
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
49-476 |
2.93e-127 |
|
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: 376.53 E-value: 2.93e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 49 EAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANG 128
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 129 EIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINV 208
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 209 VTgQSREIGAVFT----GDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRN 284
Cdd:cd07105 161 VT-HSPEDAPEVVealiAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 285 AGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGdgsesDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKA-HPL 363
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAdESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 364 GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTG 443
Cdd:cd07105 315 SGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGM 394
|
410 420 430
....*....|....*....|....*....|....
gi 505180169 444 LISNE-VAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07105 395 TVHDEpTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-476 |
5.14e-127 |
|
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: 378.02 E-value: 5.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAAL--PAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKP-LAEAEGEIAYAASFIEWFAEQGKRANGEIIPSpgADKRLMVIR-QGVGVCAAITPWNFPAAMITRKAGPA 170
Cdd:cd07143 91 IEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIET--DIKKLTYTRhEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 171 LAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-I 249
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 250 KKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 330 PLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANN 409
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAND 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07143 409 STYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
33-474 |
8.57e-126 |
|
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: 373.57 E-value: 8.57e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 33 PSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYA 112
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 113 ASFIEWFAEQG------KRANGEIipsPGAdKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETP 186
Cdd:cd07101 83 AIVARYYARRAerllkpRRRRGAI---PVL-TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 187 FTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgdERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFD 266
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 267 DADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDD 346
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 347 ALTRGATLLTGGKAHP-LGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07101 317 AVAKGATVLAGGRARPdLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 505180169 426 IWRVSEQLEYGMVGINTGLIS---NEVAPFGGVKQSGLGREGSEHGIEDYLE 474
Cdd:cd07101 397 GRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
12-476 |
9.54e-126 |
|
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: 374.52 E-value: 9.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALP--AWRALTAAQRAALLKNWHHLILENKTA 89
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 90 LAQIMTAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGAdKRLMVIRQGVGVCAAITPWNFPAAMITRKAG 168
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 169 PALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES 248
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 -IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:cd07142 244 nLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 328 IGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180169 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-475 |
6.26e-120 |
|
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: 359.58 E-value: 6.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRDAaDGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAW-RALTAAQRAALLKNWHHLILENKTAL 90
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 91 AQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIP---SPGADKRLMVIRQG-VGVCAAITPWNFPAAMITRK 166
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgdwFPGTKGKIAQVRREpLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQca 246
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:cd07082 240 HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 327 QIGPLINADAGRKVQSLLDDALTRGATLLTGGKAhpLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQ 406
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 407 ANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT----GLisnEVAPFGGVKQSGLGREgsehGIEDYLEM 475
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrGP---DHFPFLGRKDSGIGTQ----GIGDALRS 463
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
30-476 |
9.10e-120 |
|
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: 358.61 E-value: 9.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 30 VSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 110 AYAASFIEWFAEQGKRANGEIIPSPGADkRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRN-LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 190 LAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 270 IDKAVEGALIA-KFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAL 348
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 349 TRGATLLTGGKaHPLG-----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDA 423
Cdd:cd07107 319 REGARLVTGGG-RPEGpalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 505180169 424 ARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEK 450
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-476 |
2.20e-119 |
|
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: 357.44 E-value: 2.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 28 LAVSNPSTGATLGQIPnmgrAEAQQAVDAATAALPAWRA-LTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE 106
Cdd:cd07146 1 LEVRNPYTGEVVGTVP----AGTEEALREALALAASYRStLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 107 GEIAYAASFIEWFAEQGKRANGEIIP---SPGADKRLMV-IRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPA 182
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdlTANGKARKIFtLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 183 NETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLmrQCAESIKKLSLELGGNAPF 262
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 263 IVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQS 342
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 343 LLDDALTRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSND 422
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 423 AARIWRVSEQLEYGMVGINTGL-ISNEVAPFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
14-476 |
2.66e-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: 357.92 E-value: 2.66e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPLAEAEG-EIAYAASFIEWFAeqgkranGEIIPSPGA----DKRLM--VIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFA-------GVIRAEEGSanmiDEDTLsiVLREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 327 QIGPLINADAGRKVQSLLDDALTRGATLLTGGK----AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQE 402
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180169 403 VIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-476 |
9.48e-118 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 354.90 E-value: 9.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALP--AWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEIIPSPGADKRlMVIRQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQG-YTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-IK 250
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSnLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 251 KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGP 330
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 331 LINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNT 410
Cdd:PLN02766 344 QVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PLN02766 424 KYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-473 |
4.38e-117 |
|
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: 353.45 E-value: 4.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADgtSLAVSNPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:cd07124 36 VIGGKEVRTEE--KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPS-PGADKRLMVIRQGVGVcaAITPWNFPAAMITRKAGPAL 171
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMvPGEDNRYVYRPLGVGA--VISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES--- 248
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 ---IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 326 VQIGPLINADAGRKVQSLLDDALtRGATLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEV 403
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEA 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISnEVAPFGGVKQSGLgreGSEHGIEDYL 473
Cdd:cd07124 431 LEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALV-GRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
83-478 |
8.81e-117 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 349.03 E-value: 8.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 83 ILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAM 162
Cdd:PRK10090 8 IRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 163 ITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLM 242
Cdd:PRK10090 88 IARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 243 RQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGD-G 321
Cdd:PRK10090 168 AAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNpA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 322 SESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQ 401
Cdd:PRK10090 248 ERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 402 EVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTgliSNEVAPFG---GVKQSGLGREGSEHGIEDYLEMK-- 476
Cdd:PRK10090 328 EAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR---ENFEAMQGfhaGWRKSGIGGADGKHGLHEYLQTQvv 404
|
..
gi 505180169 477 YL 478
Cdd:PRK10090 405 YL 406
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-478 |
9.66e-115 |
|
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: 346.31 E-value: 9.66e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIipsPGadkrlmviRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07111 106 SLDNGKPIRESrDCDIPLVARHFYHHAGWAQLLDTEL---AG--------WKPVGVVGQIVPWNFPLLMLAWKICPALAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 174 GCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLS 253
Cdd:cd07111 175 GNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 254 LELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLIN 333
Cdd:cd07111 254 LELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 334 ADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYG 413
Cdd:cd07111 334 PAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180169 414 LASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07111 414 LAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWE 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-476 |
1.06e-110 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 335.17 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 27 SLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE 106
Cdd:PRK09406 2 PIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 107 GEIAYAASFIEWFAEQGKrangEIIPSPGAD------KRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIK 180
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAE----ALLADEPADaaavgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 181 PANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNA 260
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILR-DPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 261 PFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKV 340
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 341 QSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYS 420
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 421 NDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK09406 397 RDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-476 |
1.48e-110 |
|
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: 336.00 E-value: 1.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA--WRALTAAQRAALLKNWHHLILENKTA 89
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 90 LAQIMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSPGA--DKRL-MVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:cd07140 87 LATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 246 AES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:cd07140 247 AVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 325 DVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDE--QE 402
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180169 403 VIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
12-476 |
2.48e-110 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 337.16 E-value: 2.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALP--AWRALTAAQRAALLKNWHHLILENKTA 89
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 90 LAQIMTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFPAAMITRKAG 168
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADG-PHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 169 PALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES 248
Cdd:PLN02466 218 PALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 -IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:PLN02466 298 nLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 328 IGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRA 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180169 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PLN02466 458 NNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
36-474 |
1.06e-108 |
|
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: 329.64 E-value: 1.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 36 GATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASF 115
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 116 IEWFAEQGKRANGEIIPSpgADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA-LAMA 193
Cdd:cd07152 81 LHEAAGLPTQPQGEILPS--APGRLsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 194 ELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKA 273
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 274 VEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRGAT 353
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 354 LLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQL 433
Cdd:cd07152 318 LEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 505180169 434 EYGMVGINTGLISNE-VAPFGGVKQSGLG-REGSEHGIEDYLE 474
Cdd:cd07152 395 RTGMLHINDQTVNDEpHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
32-470 |
1.11e-107 |
|
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: 327.28 E-value: 1.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAY 111
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 112 AASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALA 191
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 192 MAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADID 271
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 272 KAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRG 351
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 352 ATLLTGGKAHPL---GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWR 428
Cdd:cd07102 321 ARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 505180169 429 VSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIE 470
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-473 |
7.12e-103 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 316.88 E-value: 7.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADgtSLAVSNPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:PRK03137 40 IIGGERITTED--KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQG-KRANGE-IIPSPGADKRLMVIRQGVGVcaAITPWNFPAAMITRKAGPA 170
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYYARQMlKLADGKpVESRPGEHNRYFYIPLGVGV--VISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 171 LAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-- 248
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 ----IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:PRK03137 276 gqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 325 DVqIGPLINADAGRKVQSLLDDALTRGaTLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVI 404
Cdd:PRK03137 356 AY-MGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHAL 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 405 EQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNeVAPFGGVKQSGlgrEGSEHGIEDYL 473
Cdd:PRK03137 434 EIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVG-YHPFGGFNMSG---TDSKAGGPDYL 501
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
32-469 |
7.59e-102 |
|
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: 312.70 E-value: 7.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE-GEIA 110
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 111 YAASFIEWFAEQGKRAngeIIPSPGADKRLMVIRQG------VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANE 184
Cdd:cd07098 82 VTCEKIRWTLKHGEKA---LRPESRPGGLLMFYKRArveyepLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 185 T-----PFTALAMAELANqAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGN 259
Cdd:cd07098 159 VawssgFFLSIIRECLAA-CGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 260 APFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRK 339
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 340 VQSLLDDALTRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLA 415
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 416 SYFYSNDAARIWRVSEQLEYGMVGINTGLIS--NEVAPFGGVKQSGLGREGSEHGI 469
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-461 |
2.64e-101 |
|
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: 311.76 E-value: 2.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALA 91
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 92 QIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPaAMITR-KAGPA 170
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 171 LAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIK 250
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 251 KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTC------VCVNrfyihrAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCmalsvaVAVG------DEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 325 DVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDE 400
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180169 401 QEVIEQANNTIYGLASYFYSND--AARiwRVSEQLEYGMVGINTGlISNEVA--PFGGVKQSGLG 461
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSgaAAR--KFQREVDAGMVGINVP-IPVPLAffSFGGWKGSFFG 455
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-476 |
6.69e-99 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 306.05 E-value: 6.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPA--WRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:PRK09847 24 INGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:PRK09847 104 LETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-IK 250
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 251 KLSLELGGNAPFIVFDDA-DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:PRK09847 263 RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 330 PLINADAGRKVQSLLDDALTRGaTLLTGGKAHPLGGnFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANN 409
Cdd:PRK09847 343 TLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAND 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK09847 421 SQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
12-476 |
2.58e-97 |
|
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: 301.69 E-value: 2.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRDAADGTsLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAAL--PAWRALTAAqRAALLKNWHHLILENKTA 89
Cdd:TIGR04284 2 RLLIDGKLVAGSAGT-FPTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 90 LAQIMTAEQGKPL-----AEAEGEI---AYAASFIEWFAeqGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAA 161
Cdd:TIGR04284 80 LRELTIAEVGAPRmltagAQLEGPVddlGFAADLAESYA--WTTDLGVASPM-GIPTRRTLRREAVGVVGAITPWNFPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 162 MITRKAGPALAAGCTMVIKPANETPFTALAMAEL-ANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRV 240
Cdd:TIGR04284 157 INLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 241 LMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGD 320
Cdd:TIGR04284 237 VMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 321 GSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGG--KAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFE 398
Cdd:TIGR04284 317 PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGgrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180169 399 DEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:TIGR04284 397 GDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-478 |
3.28e-96 |
|
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: 298.60 E-value: 3.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEAEG-EIAYAASFIEWFAeQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07116 85 TWDNGKPVRETLAaDIPLAIDHFRYFA-GCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 174 GCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLS 253
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 254 LELGGNAPFIVF------DDADIDKAVEGALIAKFrNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:cd07116 243 LELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 328 IGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGN----FFTPTVIGDVQPGSlLLQEEIFGPVAALVKFEDEQEV 403
Cdd:cd07116 322 IGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180169 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07116 401 LEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
32-473 |
9.51e-94 |
|
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: 293.31 E-value: 9.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 32 NPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIA 110
Cdd:TIGR01237 52 NPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 111 YAASFIEWFAEQGKR--ANGEIIPSPGADKRLMVIRQGVGVcaAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:TIGR01237 132 EAIDFMEYYARQMIElaKGKPVNSREGETNQYVYTPTGVTV--VISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 189 ALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA------ESIKKLSLELGGNAPF 262
Cdd:TIGR01237 210 AAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqKHLKRVIAEMGGKDTV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 263 IVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQS 342
Cdd:TIGR01237 290 IVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIME 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 343 LLDDALTRGaTLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSND 422
Cdd:TIGR01237 370 YIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNN 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505180169 423 AARIWRVSEQLEYGMVGIN---TGLISNeVAPFGGVKQSGLgreGSEHGIEDYL 473
Cdd:TIGR01237 449 RDHINRAKAEFEVGNLYFNrniTGAIVG-YQPFGGFKMSGT---DSKAGGPDYL 498
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
29-472 |
8.57e-93 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 289.45 E-value: 8.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 29 AVS-NPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:PRK13968 9 AISvNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 108 EIAYAASFIEWFAEQGKrANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPF 187
Cdd:PRK13968 89 EVAKSANLCDWYAEHGP-AMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 188 TALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDD 267
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 268 ADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDA 347
Cdd:PRK13968 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 348 LTRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIW 427
Cdd:PRK13968 327 LAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQAR 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 505180169 428 RVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDY 472
Cdd:PRK13968 407 QMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
16-465 |
1.92e-84 |
|
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: 267.92 E-value: 1.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 16 AGSWRdaADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMT 95
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 96 AEQGKPLAEAEGEIAyaasfiEW-----FA-EQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGP 169
Cdd:cd07130 82 LEMGKILPEGLGEVQ------EMidicdFAvGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 170 ALAAGCTMVIKPANETPFTALAMAELANQA----GIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 246 AESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:cd07130 235 AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 326 VQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQEVIE 405
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180169 406 QANNTIYGLASYFYSNDAARIWRVSEQL--EYGMVGINTGLISNEV-APFGGVKQSGLGRE-GS 465
Cdd:cd07130 394 WNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
20-461 |
3.04e-84 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 268.68 E-value: 3.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 20 RDAADGTSLAVSNPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQ 98
Cdd:cd07125 40 EETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 99 GKPLAEAEGEIAYAASFIEWFAEQGKRANGE-IIPSP-GADKRLMVIRQGVGVCaaITPWNFPAAMITRKAGPALAAGCT 176
Cdd:cd07125 120 GKTLADADAEVREAIDFCRYYAAQARELFSDpELPGPtGELNGLELHGRGVFVC--ISPWNFPLAIFTGQIAAALAAGNT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 177 MVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE---SIKKLS 253
Cdd:cd07125 198 VIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgPILPLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 254 LELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07125 278 AETGGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 333 NADAGRKVQSlLDDALTRGATLLTGGKAHPLGGNFFTPTVIGDVqpGSLLLQEEIFGPVAALVKFEDEQ--EVIEQANNT 410
Cdd:cd07125 357 DKPAGKLLRA-HTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAEDldEAIEDINAT 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505180169 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISnEVAPFGGVKQSGLG 461
Cdd:cd07125 434 GYGLTLGIHSRDEREIEYWRERVEAGNLYINrniTGAIV-GRQPFGGWGLSGTG 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-476 |
5.05e-83 |
|
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: 265.21 E-value: 5.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAADgTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:cd07083 23 IGGEWVDTKE-RMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANG---EIIPSPGADKRLMVirQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpavEVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE---- 247
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 248 --SIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:cd07083 260 qtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 326 VQIGPLINADAGRKVQSLLDDALTRGaTLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQ--EV 403
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180169 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNeVAPFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07083 419 LEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkiTGALVG-VQPFGGFKLSGTNaKTGGPHYLRRFLEMK 494
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
52-472 |
5.99e-81 |
|
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: 257.59 E-value: 5.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 52 QAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEiI 131
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGE-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 132 PSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTG 211
Cdd:cd07095 83 ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 212 qSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKK-LSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCV 290
Cdd:cd07095 163 -GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 291 CVNRFYIHR-AVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFT 369
Cdd:cd07095 242 CARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 370 PTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLIS 446
Cdd:cd07095 322 PGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrptTGASS 400
|
410 420
....*....|....*....|....*.
gi 505180169 447 NevAPFGGVKQSGLGREgSEHGIEDY 472
Cdd:cd07095 401 T--APFGGVGLSGNHRP-SAYYAADY 423
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-464 |
3.71e-77 |
|
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: 248.49 E-value: 3.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAATAA-LPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE 106
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALfLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 107 GEIAYAASFIEWFAEQGKRANGEIIP----SPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPA 182
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 183 NETPFTALAMAELANQAGIPQGVINVVTgQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESiKKLSLELGGNAPF 262
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 263 IVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQS 342
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 343 LLDDALTRGATLLTGGKahPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSND 422
Cdd:cd07148 319 WVNEAVAAGARLLCGGK--RLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 505180169 423 AARIWRVSEQLEYGMVGINtglisNEVA------PFGGVKQSGLGREG 464
Cdd:cd07148 397 LDVALKAVRRLDATAVMVN-----DHTAfrvdwmPFAGRRQSGYGTGG 439
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-470 |
1.12e-74 |
|
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: 241.28 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 70 AQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIEWFAEQgKRANGEIIPSPGadkRLM 141
Cdd:cd07087 20 EWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiavvlGEIDHALKHLKKWMKP-RRVSVPLLLQPA---KAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 142 VIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFt 221
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 222 gDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:cd07087 174 -AEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 302 YDQFCDKFVARVAALKVGDGSESDvQIGPLINADAGRKVQSLLDDaltrgATLLTGGKAHPlGGNFFTPTVIGDVQPGSL 381
Cdd:cd07087 253 KDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDD-----GKVVIGGQVDK-EERYIAPTILDDVSPDSP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 382 LLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI--SNEVAPFGGVKQSG 459
Cdd:cd07087 326 LMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGNSG 405
|
410
....*....|.
gi 505180169 460 LGREGSEHGIE 470
Cdd:cd07087 406 MGAYHGKAGFD 416
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
14-476 |
2.26e-74 |
|
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: 242.09 E-value: 2.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPaAMITRKAGP-ALA 172
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFP-AMIPLWMFPiAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDErVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPD-VKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVyDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 333 NADAGRKVQSLLDDALTRGATLLTGG-----KAHPlGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGrgykvDGYE-EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL-ISNEVAPFGGVKQSGLGREG--SEHGIEDYLEMK 476
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIpVPLPYFSFTGWKDSFFGDHHiyGKQGTHFYTRGK 471
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
49-468 |
6.18e-74 |
|
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: 239.44 E-value: 6.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 49 EAQQAVDAAtaalpaWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIE-WF 119
Cdd:cd07134 5 AAQQAHALA------LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 120 AEQGKRAngeiiPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQA 199
Cdd:cd07134 79 KPKRVRT-----PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 200 GIPQGVinvvtgqsreigAVFTGDERVRK--LS-------FTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADI 270
Cdd:cd07134 154 FDEDEV------------AVFEGDAEVAQalLElpfdhifFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 271 DKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFvarVAALKVGDGSESDVQIGP----LINADAGRKVQSLLDD 346
Cdd:cd07134 222 KKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHL---KAEIEKFYGKDAARKASPdlarIVNDRHFDRLKGLLDD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 347 ALTRGATLLTGGKAHPlGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARI 426
Cdd:cd07134 299 AVAKGAKVEFGGQFDA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANV 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 505180169 427 WRVSEQLEYGMVGINTGLI--SNEVAPFGGVKQSGLGREGSEHG 468
Cdd:cd07134 378 NKVLARTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYG 421
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
14-470 |
1.87e-70 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 232.34 E-value: 1.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQI 93
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 94 MTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGE-------IIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGStEVGRVLMRQCa 246
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKA- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 247 eSIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDgSESDV 326
Cdd:PLN00412 257 -GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP-PEDDC 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 327 QIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQ 406
Cdd:PLN00412 335 DITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHH 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180169 407 ANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISN-EVAPFGGVKQSGLGREGSEHGIE 470
Cdd:PLN00412 412 CNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGpDHFPFQGLKDSGIGSQGITNSIN 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
15-459 |
2.34e-70 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 231.77 E-value: 2.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRdAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:PRK09457 5 INGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIpSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAG 174
Cdd:PRK09457 84 ARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKR-SEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 175 CTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKK-LS 253
Cdd:PRK09457 163 NTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKiLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 254 LELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY-DQFCDKFVARVAALKVGDgSESDVQ--IGP 330
Cdd:PRK09457 242 LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR-WDAEPQpfMGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 331 LINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNT 410
Cdd:PRK09457 321 VISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 505180169 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNevAPFGGVKQSG 459
Cdd:PRK09457 400 RFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkplTGASSA--APFGGVGASG 449
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-475 |
7.82e-68 |
|
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: 223.52 E-value: 7.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 68 TAAQRAALLKNWHHLILENKTALAQIMTAEQG-KPLAE---AE-----GEIAYAASFI-EWFAEQgKRANGeiIPSPGAd 137
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHEtllAEilpsiAGIKHARKHLkKWMKPS-RRHVG--LLFLPA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 138 kRLMVIRQGVGVCAAITPWNFP-----AAMITrkagpALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGq 212
Cdd:cd07133 94 -KAEVEYQPLGVVGIIVPWNYPlylalGPLIA-----ALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 213 SREIGAVFTG---DervrKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTC 289
Cdd:cd07133 166 GADVAAAFSSlpfD----HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 290 VCVNRFYIHRAVYDQFCDKFVARVAALkVGDGSESDvQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPL--GGNF 367
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDfaATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 368 FTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL--I 445
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhV 399
|
410 420 430
....*....|....*....|....*....|
gi 505180169 446 SNEVAPFGGVKQSGLGRegsEHGIEDYLEM 475
Cdd:cd07133 400 AQDDLPFGGVGASGMGA---YHGKEGFLTF 426
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
10-441 |
8.58e-68 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 228.09 E-value: 8.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 10 RQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTA 89
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 90 LAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGP 169
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 170 ALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVfTGDERVRKLSFTGSTEVGRVLMRQCAESI 249
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAI-CDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 250 KKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFyIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 330 PLINADAGRKVQSLLDDALTRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIE 405
Cdd:PLN02419 431 PVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVpgyeKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAIS 510
|
410 420 430
....*....|....*....|....*....|....*.
gi 505180169 406 QANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN 441
Cdd:PLN02419 511 IINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
76-472 |
2.73e-65 |
|
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: 217.09 E-value: 2.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 76 LKNWHHLILENKTALAQIMTAEQGKP-----LAE---AEGEIAYAASFIEwfaeqgKRANGEIIPSPGADKRLMVIR--- 144
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDILHMLKNLK------KWAKDEKVKDGPLAFMFGKPRirk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 145 QGVGVCAAITPWNFPaamITRKAGP---ALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFt 221
Cdd:cd07135 107 EPLGVVLIIGPWNYP---VLLALSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 222 gDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:cd07135 182 -EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 302 YDQFcdkfvarVAALK------VGDGSESDVQIGPLINADAGRKVQSLLDDalTRGaTLLTGGKAHPlGGNFFTPTVIGD 375
Cdd:cd07135 261 YDEF-------VEELKkvldefYPGGANASPDYTRIVNPRHFNRLKSLLDT--TKG-KVVIGGEMDE-ATRFIPPTIVSD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 376 VQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI--SNEVAPFG 453
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFG 409
|
410
....*....|....*....
gi 505180169 454 GVKQSGLGREGSEHGIEDY 472
Cdd:cd07135 410 GVGDSGYGAYHGKYGFDTF 428
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
7-461 |
1.84e-61 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 216.60 E-value: 1.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 7 DLFRQQALIAGSWRDAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILEN 86
Cdd:PRK11904 544 AAFLEKQWQAGPIINGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEAN 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 87 KTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPSP-GADKRLMviRQGVGVCAAITPWNFPAAMI 163
Cdd:PRK11904 624 RAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRlfGAPEKLPGPtGESNELR--LHGRGVFVCISPWNFPLAIF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 164 TRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMR 243
Cdd:PRK11904 702 LGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 244 QCAE---SIKKLSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVG 319
Cdd:PRK11904 782 TLAArdgPIVPLIAETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVG 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 320 DGSESDVQIGPLINADAGRKvqsLLD--DALTRGATLLTGGKAHPLG--GNFFTPTV--IGDVQpgslLLQEEIFGPVAA 393
Cdd:PRK11904 861 DPRLLSTDVGPVIDAEAKAN---LDAhiERMKREARLLAQLPLPAGTenGHFVAPTAfeIDSIS----QLEREVFGPILH 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 394 LVKFEDEQ--EVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISN--EVAPFGGVKQSGLG 461
Cdd:PRK11904 934 VIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAvvGVQPFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-473 |
2.70e-60 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 205.84 E-value: 2.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 13 ALIAGSWRdaADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQ 92
Cdd:PLN02315 23 CYVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 173 AGCTMVIKPANETPFTALAM----AELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES 248
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQI 328
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 329 GPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQAN 408
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180169 409 NTIYGLASYFYSNDAARI--WRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGREGSEHGIEDYL 473
Cdd:PLN02315 419 SVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
70-469 |
5.59e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 201.80 E-value: 5.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 70 AQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIEWFAEQgKRANGEIIPSPGADKrlm 141
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLLKHLDEYLKP-EKVDTVGVFGPGKSY--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 142 VIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFT 221
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 222 gdERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:PTZ00381 184 --EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 302 YDQFCDKFvARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDaltRGATLLTGGKAHpLGGNFFTPTVIGDVQPGSL 381
Cdd:PTZ00381 262 KDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVD-IENKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 382 LLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL--ISNEVAPFGGVKQSG 459
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNSG 416
|
410
....*....|
gi 505180169 460 LgreGSEHGI 469
Cdd:PTZ00381 417 M---GAYHGK 423
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
9-477 |
5.78e-56 |
|
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: 193.97 E-value: 5.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 9 FRQQALIAGSWRdaADGTSLAVSNPST-GATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENK 87
Cdd:TIGR01238 36 WQAAPIIGHSYK--ADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 88 TALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPgadkrlmvirqgVGVCAAITPWNFPAAMITRKA 167
Cdd:TIGR01238 114 PELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES------------RGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 168 GPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE 247
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 248 SIK---KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:TIGR01238 262 REDapvPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 325 DVQIGPLINADAGRKVQSLLDDALTRGAT---LLTGGKAHPLGGNFFTPTV--IGDVQPgsllLQEEIFGPVAALVKFED 399
Cdd:TIGR01238 342 TTDVGPVIDAEAKQNLLAHIEHMSQTQKKiaqLTLDDSRACQHGTFVAPTLfeLDDIAE----LSEEVFGPVLHVVRYKA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 400 EQ--EVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVA--PFGGVKQSGLG-REGSEHGIEDYLE 474
Cdd:TIGR01238 418 REldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTGpKAGGPHYLYRLTQ 497
|
...
gi 505180169 475 MKY 477
Cdd:TIGR01238 498 VQY 500
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
148-468 |
1.96e-55 |
|
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: 191.18 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 148 GVCAAITPWNFP-----AAMItrkaGpALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFtg 222
Cdd:cd07136 102 GVVLIIAPWNYPfqlalAPLI----G-AIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 223 DERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY 302
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 303 DQFCDKFVARVAALKVGDGSESDvQIGPLINADAGRKVQSLLDDaltrgATLLTGGKAHPlGGNFFTPTVIGDVQPGSLL 382
Cdd:cd07136 254 EKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDN-----GKIVFGGNTDR-ETLYIEPTILDNVTWDDPV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 383 LQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI--SNEVAPFGGVKQSGL 460
Cdd:cd07136 327 MQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGNSGM 406
|
....*...
gi 505180169 461 greGSEHG 468
Cdd:cd07136 407 ---GSYHG 411
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
4-461 |
6.98e-55 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.17 E-value: 6.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 4 FHSDLFRQQALIAGswrDAADGTSLAVSNPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHL 82
Cdd:PRK11905 548 FAAKTWHAAPLLAG---GDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 83 ILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPgadkrlmvirQGVGVCaaITPWNFPAAM 162
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKP----------LGPVVC--ISPWNFPLAI 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 163 ITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLM 242
Cdd:PRK11905 693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQ 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 243 RQCAESIKK---LSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKV 318
Cdd:PRK11905 773 RTLAKRSGPpvpLIAETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRI 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 319 GDGSESDVQIGPLINADAGRKVQSLLDDALTRGATLltggKAHPL-----GGNFFTPTVIgdvQPGSL-LLQEEIFGPVA 392
Cdd:PRK11905 852 GDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpaeteKGTFVAPTLI---EIDSIsDLEREVFGPVL 924
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180169 393 ALVKFEDEQ--EVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVA--PFGGVKQSGLG 461
Cdd:PRK11905 925 HVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-461 |
5.06e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 189.76 E-value: 5.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 13 ALIAGswrDAADGTSLAVSNPSTGA-TLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALA 91
Cdd:COG4230 560 PLIAG---EAASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 92 QIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRangeiipSPGADKRLmvirQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCRYYAAQARR-------LFAAPTVL----RGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE---S 248
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAArdgP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 249 IKKLSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTC-----VCVNrfyihRAVYDQFCDKFVARVAALKVGDGS 322
Cdd:COG4230 786 IVPLIAETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRCsalrvLCVQ-----EDIADRVLEMLKGAMAELRVGDPA 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 323 ESDVQIGPLINADAgrkVQSLLD--DALTRGATLLTGGK--AHPLGGNFFTPTVIgdvQPGSL-LLQEEIFGPVAALVKF 397
Cdd:COG4230 860 DLSTDVGPVIDAEA---RANLEAhiERMRAEGRLVHQLPlpEECANGTFVAPTLI---EIDSIsDLEREVFGPVLHVVRY 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180169 398 EDEQ--EVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINtgliSNEVA------PFGGVKQSGLG 461
Cdd:COG4230 934 KADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN----RNIIGavvgvqPFGGEGLSGTG 1001
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
9-461 |
9.18e-50 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 183.25 E-value: 9.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 9 FRQQALIAGSwrdAADGTSLAVSNPS-TGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENK 87
Cdd:PRK11809 645 WQAAPMLEDP---VAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQM 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 88 TALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPspgadkrlmvirQGVGVCaaITPWNFPAAMITR 165
Cdd:PRK11809 722 QTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDdfDNDTHRP------------LGPVVC--ISPWNFPLAIFTG 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:PRK11809 788 QVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 246 AESIKK------LSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVG 319
Cdd:PRK11809 868 AGRLDPqgrpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMG 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 320 DGSESDVQIGPLINADAGRKVQSLLDDALTRGATLLTGGKAHPLG---GNFFTPTVI--GDVQPgsllLQEEIFGPVAAL 394
Cdd:PRK11809 948 NPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqsGTFVPPTLIelDSFDE----LKREVFGPVLHV 1023
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 395 VKFEDEQ--EVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYG-------MVGINTGlisneVAPFGGVKQSGLG 461
Cdd:PRK11809 1024 VRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGnlyvnrnMVGAVVG-----VQPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
25-459 |
1.05e-48 |
|
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: 175.08 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 25 GTSLAVSNPST-GATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENK--TALAQIMTAeQGKP 101
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYryELNAATMLG-QGKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 102 LAEAEgeIAYAASFIEWF------AEQgKRANGEIIPSPGADKRlMVIRQGVGVCAAITPWNFPAAMITRKAGPALAaGC 175
Cdd:cd07123 124 VWQAE--IDAACELIDFLrfnvkyAEE-LYAQQPLSSPAGVWNR-LEYRPLEGFVYAVSPFNFTAIGGNLAGAPALM-GN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 176 TMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIK----- 250
Cdd:cd07123 199 VVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrty 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 251 -KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:cd07123 279 pRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 330 PLINADAGRKVQSLLDDALT-RGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQ--EVIEQ 406
Cdd:cd07123 359 AVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeETLEL 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 505180169 407 ANNT-IYGLASYFYSNDAARIWRVSEQLEY--GMVGIN---TGLISNEvAPFGGVKQSG 459
Cdd:cd07123 439 VDTTsPYALTGAIFAQDRKAIREATDALRNaaGNFYINdkpTGAVVGQ-QPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
51-462 |
4.18e-46 |
|
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: 166.24 E-value: 4.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 51 QQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIEWFAEq 122
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlseillvkNEIKYAISNLPEWMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 123 gkrangeiiPSPgADKRLMVIRQGV-------GVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAEL 195
Cdd:cd07132 80 ---------PEP-VKKNLATLLDDVyiykeplGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 196 anqagIPQGVIN----VVTGQSREIGAVFtgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADID 271
Cdd:cd07132 150 -----IPKYLDKecypVVLGGVEETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 272 KAVEGALIAKFRNAGQTCVCVNrfYI--HRAVYDQFCDKfvARvAALK--VGDGSESDVQIGPLINADAGRKVQSLLDda 347
Cdd:cd07132 223 VAARRIAWGKFINAGQTCIAPD--YVlcTPEVQEKFVEA--LK-KTLKefYGEDPKESPDYGRIINDRHFQRLKKLLS-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 348 ltrGATLLTGGKAHPlGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIW 427
Cdd:cd07132 296 ---GGKVAIGGQTDE-KERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVIN 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 505180169 428 RVSEQLEYGMVGINTGL--ISNEVAPFGGVKQSGLGR 462
Cdd:cd07132 372 KILSNTSSGGVCVNDTImhYTLDSLPFGGVGNSGMGA 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
50-462 |
1.02e-36 |
|
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: 140.24 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 50 AQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEA-EGEIAYAASFI--------EWFA 120
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 121 EQGKR-------ANGEIIPSPgadkrlmvirqgVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMA 193
Cdd:cd07137 81 PEKVKtplttfpAKAEIVSEP------------LGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 194 ELanqagIPQ----GVINVVTGQSREIGAVFtgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07137 149 KL-----IPEyldtKAIKVIEGGVPETTALL--EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 270 IDKAVEGALIAKF-RNAGQTCVCVNrfYIhrAVYDQFCDKFvarVAALK------VGDGSESDVQIGPLINADAGRKVQS 342
Cdd:cd07137 222 LKVAVRRIAGGKWgCNNGQACIAPD--YV--LVEESFAPTL---IDALKntlekfFGENPKESKDLSRIVNSHHFQRLSR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 343 LLDDALTRGATLLTGGK-AHPLggnFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSN 421
Cdd:cd07137 295 LLDDPSVADKIVHGGERdEKNL---YIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 505180169 422 DAARIWRVSEQLEYGMVGINTGLI--SNEVAPFGGVKQSGLGR 462
Cdd:cd07137 372 NKELKRRIVAETSSGGVTFNDTVVqyAIDTLPFGGVGESGFGA 414
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
15-424 |
1.43e-36 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 141.38 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 15 IAGSWRDAAdGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIM 94
Cdd:PRK11903 9 VAGRWQAGS-GAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 95 TAEQGKPLAEA----EGEIAYAASFIEWFAEQGKR---ANGEIIpSPGADKR-----LMVIRQGVGVcaAITPWNFPAAM 162
Cdd:PRK11903 88 TANSGTTRNDSavdiDGGIFTLGYYAKLGAALGDArllRDGEAV-QLGKDPAfqgqhVLVPTRGVAL--FINAFNFPAWG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 163 ITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGI-PQGVINVVTGQSREIGAVFTGDERVrklSFTGSTEVGRVL 241
Cdd:PRK11903 165 LWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFTGSAETAAVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 242 -------MRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVA 314
Cdd:PRK11903 242 rshpavvQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 315 ALKVGDGSESDVQIGPLINADAGRKVQSLLdDALTRGATLLTGGKAHPL------GGNFFTPTVIG--DVQPGSLLLQEE 386
Cdd:PRK11903 322 KTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTLLGasDPDAATAVHDVE 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 505180169 387 IFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAA 424
Cdd:PRK11903 401 VFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAA 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
12-424 |
1.62e-33 |
|
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: 132.78 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 12 QALIAGSWRdAADGTSLAVSNPSTGATLGQIPNMGRAEAQQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALA 91
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 92 QIMT---AEQGKPLAEAEGEIAYAASFIEWFAEQGKRAN----GEIIP-SPG---ADKRLMVIRQGVGVcaAITPWNFPA 160
Cdd:cd07128 81 ALSAatgATRRDSWIDIDGGIGTLFAYASLGRRELPNAHflveGDVEPlSKDgtfVGQHILTPRRGVAV--HINAFNFPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 161 AMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGI-PQGVINVVTGQSREIGAVFTGDERVrklSFTGSTEVGR 239
Cdd:cd07128 159 WGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 240 VLMRQ---CAESIK----KLSLELGGNAPFIVFDDADID---KAVEGALIAKfrnAGQTCVCVNRFYIHRAVYDQFCDKF 309
Cdd:cd07128 236 KLRAHpniVARSIRfnaeADSLNAAILGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRAFVPEARVDAVIEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 310 VARVAALKVGDGSESDVQIGPLINADAGRKVQSLLdDALTRGATLLTGGK-------AHPLGGNFFTPTVIGDVQP--GS 380
Cdd:cd07128 313 KARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLLCDDPdaAT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 505180169 381 LLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07128 392 AVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA 435
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
52-408 |
4.96e-33 |
|
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: 130.35 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 52 QAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFA---EQGK---- 124
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlvREGSwlda 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 125 ---RANGEIIPSPGADKRLMviRQGVGVCAAITPWNFPAAMITrkAG----PALAAGCTMVIKPANETPFTALAMAELAN 197
Cdd:cd07129 83 ridPADPDRQPLPRPDLRRM--LVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 198 QA----GIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESI--KKLSLELGGNAPFIVFDDADID 271
Cdd:cd07129 159 AAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVFILPGALAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 272 KAVE--GALIAKFR-NAGQTCVC---VnrFYIHRAVYDQFCDKFVARVAAlkvgdgSESDVQIGPLINADAGRKVQSLLD 345
Cdd:cd07129 239 RGEAiaQGFVGSLTlGAGQFCTNpglV--LVPAGPAGDAFIAALAEALAA------APAQTMLTPGIAEAYRQGVEALAA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180169 346 DAltrGATLLTGGKAHPlGGNFFTPTVI---GDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQAN 408
Cdd:cd07129 311 AP---GVRVLAGGAAAE-GGNQAAPTLFkvdAAAFLADPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
51-451 |
1.40e-30 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 123.12 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 51 QQAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEgEIAYAASFIEWFAEQGK--RANG 128
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYsyRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 129 EIIPSPGADKRLMVIRQ--GVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGI-PQGV 205
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 206 INVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESikKLSLELGGNAPFIVFDDADIDKAVEGALIAK-FRN 284
Cdd:cd07084 161 VTLINGDGKTMQALLL-HPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDmTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 285 AGQTCVCVNRFYIH-----RAVYDQFCDKFVARvaalkvgdgSESDVQIGPLINADAGRKVQSLLDDAltrGATLLTGGK 359
Cdd:cd07084 238 SGQKCTAQSMLFVPenwskTPLVEKLKALLARR---------KLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 360 AHPlggNFFTPTVIGDVQPGSLLL------------QEEIFGPVAALVKFEDEQE--VIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07084 306 ELK---NHSIPSIYGACVASALFVpideilktyelvTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIF 382
|
410 420
....*....|....*....|....*.
gi 505180169 426 IWRVSEQLEYGMVGINTGLISNEVAP 451
Cdd:cd07084 383 LQELIGNLWVAGRTYAILRGRTGVAP 408
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
65-462 |
2.96e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 114.05 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 65 RALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEA--------EGEIAYAASFI-EWFAEqgKRANGEIIPSPG 135
Cdd:PLN02203 23 RTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdevgvlTKSANLALSNLkKWMAP--KKAKLPLVAFPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 136 adkRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAelanqAGIPQ----GVINVVTG 211
Cdd:PLN02203 101 ---TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPKyldsKAVKVIEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 212 QSrEIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIV--FDDA-DIDKAVEGALIAKFRN-AGQ 287
Cdd:PLN02203 173 GP-AVGEQLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 288 TCVCVNrfYIhrAVYDQFCDKFvarVAALKV------GDGSESDVQIGPLINADAGRKVQSLLDDALTRgATLLTGGKAH 361
Cdd:PLN02203 251 ACIAID--YV--LVEERFAPIL---IELLKStikkffGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSID 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 362 PlGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN 441
Cdd:PLN02203 323 E-KKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN 401
|
410 420
....*....|....*....|...
gi 505180169 442 TGLISN--EVAPFGGVKQSGLGR 462
Cdd:PLN02203 402 DAIIQYacDSLPFGGVGESGFGR 424
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
118-461 |
1.65e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 112.06 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 118 WFAEQGKRANGEIIPSPGAdkrlmVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELAN 197
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 198 QAgIPQGVINVVTGQSREIGAVFtgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGA 277
Cdd:PLN02174 164 QY-LDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 278 LIAKFR-NAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDvQIGPLINADAGRKVQSLLDDALTRGATLLT 356
Cdd:PLN02174 241 IAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKEVSDKIVYG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 357 GGKAHPlggNF-FTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQANNTIYGLASYFYSNDAARIWRVSEQLEY 435
Cdd:PLN02174 320 GEKDRE---NLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSA 396
|
330 340 350
....*....|....*....|....*....|....
gi 505180169 436 GmvgintGLISNEVA--------PFGGVKQSGLG 461
Cdd:PLN02174 397 G------GIVVNDIAvhlalhtlPFGGVGESGMG 424
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
47-431 |
4.98e-15 |
|
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: 77.52 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 47 RAEAQQAVDAATAALPAWRALTAAQRAAL----LKNWHHLILE------NKTALAQIMTAEQGKPLAEAEG--EIAYAA- 113
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVcleiLQRLNARSFEmahavmHTTGQAFMMAFQAGGPHAQDRGleAVAYAWr 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 114 --SFI----EWFAEQGKRangeiiPSPGADKRLMVIRQGVGV---CAAITPWNFPAAMITrkagpALAAGCTMVIKPAne 184
Cdd:cd07127 163 emSRIpptaEWEKPQGKH------DPLAMEKTFTVVPRGVALvigCSTFPTWNGYPGLFA-----SLATGNPVIVKPH-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 185 tPFTALAMA-------ELANQAGI-PQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAEsiKKLSLEL 256
Cdd:cd07127 230 -PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 257 GGNAPFIVfDDADIDKAVEGALIAKFR-NAGQTCVCVNRFYIHR---------AVYDQFCDKFVARVAALkVGDGSESDV 326
Cdd:cd07127 307 AGVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAADLAAAIDGL-LADPARAAA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 327 QIGPLINADAGRKVQslldDALTRGATLLTGGK-AHP--LGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEV 403
Cdd:cd07127 385 LLGAIQSPDTLARIA----EARQLGEVLLASEAvAHPefPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHS 460
|
410 420 430
....*....|....*....|....*....|.
gi 505180169 404 IEQANNTIY---GLASYFYSNDAARIWRVSE 431
Cdd:cd07127 461 IELARESVRehgAMTVGVYSTDPEVVERVQE 491
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
14-422 |
4.07e-14 |
|
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: 74.45 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 14 LIAGSWRDAADGTSLAvsNPSTGATLGQIPNMGRAEAQQAVDAAtAALPA---WRALTAAQRAALLKNWHHLILEN---- 86
Cdd:cd07126 2 LVAGKWKGASNYTTLL--DPLNGDKFISVPDTDEDEINEFVDSL-RQCPKsglHNPLKNPERYLLYGDVSHRVAHElrkp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 87 --KTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAM 162
Cdd:cd07126 79 evEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRflARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 163 ITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVgrvlm 242
Cdd:cd07126 159 PALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL-EANPRMTLFTGSSKV----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 243 rqcAEsikKLSLELGGNapfIVFDDADIDKAVEGALIAKF--------RNA----GQTCVCVNRFYIHRAVYDQfcdKFV 310
Cdd:cd07126 233 ---AE---RLALELHGK---VKLEDAGFDWKILGPDVSDVdyvawqcdQDAyacsGQKCSAQSILFAHENWVQA---GIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 311 ARVAALkVGDGSESDVQIGPLINADAgRKVQSLLDDALT-RGATLLTGGKahPLGgNFFTPTVIGDVQPGSL-------- 381
Cdd:cd07126 301 DKLKAL-AEQRKLEDLTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGK--PLT-NHSIPSIYGAYEPTAVfvpleeia 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 505180169 382 ------LLQEEIFGPVAALVKFEDEQE--VIEQANNTIYGLASYFYSND 422
Cdd:cd07126 376 ieenfeLVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSND 424
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
52-277 |
1.42e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 50.67 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 52 QAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGkpLAEAEGEIAyaasfiewfaeqgK-RANGEI 130
Cdd:PRK15398 40 DAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG--MGRVEDKIA-------------KnVAAAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 131 IPSP---------GADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKP----ANETPFTALAMAELAN 197
Cdd:PRK15398 105 TPGVedlttealtGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 198 QAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRqcaeSIKKLSLELGGNAPFIVFDDADIDKA---- 273
Cdd:PRK15398 185 AAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK----SGKKAIGAGAGNPPVVVDETADIEKAardi 260
|
....
gi 505180169 274 VEGA 277
Cdd:PRK15398 261 VKGA 264
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
52-407 |
1.42e-05 |
|
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: 47.23 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 52 QAVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGkpLAEAEGEIA---YAAsfiewfaeqgKRANG 128
Cdd:cd07121 8 DAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG--MGRVEDKIAknhLAA----------EKTPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 129 EIIPSPGA---DKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQA----G 200
Cdd:cd07121 76 TEDLTTTAwsgDNGLtLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 201 IPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRqcaeSIKKLSLELGGNAPFIVFDDADIDKAVEGALI- 279
Cdd:cd07121 156 GPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALS----SGKKAIGAGAGNPPVVVDETADIEKAARDIVQg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 280 AKFRNaGQTCVCVNRFYIHRAVYDQFCDKFVaRVAALKVGDgsESDVQIGPLInadagrkvqsLLDDALTRGATLLTGGK 359
Cdd:cd07121 232 ASFDN-NLPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLND--EQAEQLLEVV----------LLTNKGATPNKKWVGKD 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 505180169 360 AHPL----GGN--FFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEVIEQA 407
Cdd:cd07121 298 ASKIlkaaGIEvpADIRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
53-316 |
3.79e-05 |
|
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: 46.10 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 53 AVDAATAALPAWRALTAAQRAALLKNWHHLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGeiIP 132
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCG--VL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 133 SPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQA----GIPQGVINV 208
Cdd:cd07081 82 TGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180169 209 VTGQSREIGAVFTGDERVRKLSFTGstevGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQT 288
Cdd:cd07081 162 IDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVI 237
|
250 260
....*....|....*....|....*...
gi 505180169 289 CVCVNRFYIHRAVYDQFCDKFVARVAAL 316
Cdd:cd07081 238 CASEQSVIVVDSVYDEVMRLFEGQGAYK 265
|
|
| |
