|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
29-479 |
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: 822.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA 188
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDAD 268
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 269 LDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVK 348
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 349 KGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRV 428
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1801119160 429 AEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-480 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 795.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 1 MSLKDPSLLRQAALVGTRWIEAD-GSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWF 79
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 80 ELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPN 159
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 160 AMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAE 239
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 240 LYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGN 319
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 320 GFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDE 399
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 400 NDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
.
gi 1801119160 480 G 480
Cdd:PRK11241 481 G 481
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
3-483 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 774.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 3 LKDPSLLRQAALVGTRWIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFEL 81
Cdd:PLN02278 17 LRNAGLLRTQGLIGGKWTDAyDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 82 MIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAM 161
Cdd:PLN02278 97 IIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 162 ITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELY 241
Cdd:PLN02278 177 ITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 242 KQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGF 321
Cdd:PLN02278 257 AGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 322 EEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDEND 401
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 402 VIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCLGG 481
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLGN 496
|
..
gi 1801119160 482 IG 483
Cdd:PLN02278 497 MN 498
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
29-475 |
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: 723.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA 188
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIAILAERAGLPAGLFSVITGS-AREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAV 347
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 348 KKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFR 427
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1801119160 428 VAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-479 |
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: 653.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 7 SLLRQAALVGTRWIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIEN 85
Cdd:COG1012 2 TTPEYPLFIGGEWVAAaSGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 86 KDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRK 165
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 166 AGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCA 245
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 246 PTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGV 325
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 326 VLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHAL-GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIA 404
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 405 QANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIS-TAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-477 |
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: 601.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 19 WIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQG 98
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 99 KPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVL 178
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 179 KPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGN 258
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 259 APFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEK 338
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 339 VEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFY 418
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 419 AKDLSRVFRVAEALEYGMVGVNTGLISTAE-APFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
51-479 |
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: 531.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 51 EAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIV 130
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 131 PGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITG 210
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 211 SAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVC 290
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 291 ANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKR-HALGGTFYEA 369
Cdd:cd07078 242 ASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGKGYFVPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 370 TVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIST-AE 448
Cdd:cd07078 322 TVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAePS 401
|
410 420 430
....*....|....*....|....*....|.
gi 1801119160 449 APFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07078 402 APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
18-477 |
1.94e-180 |
|
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: 513.35 E-value: 1.94e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 18 RWIEADGSG-IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTME 96
Cdd:cd07088 5 EFVPSSSGEtIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 97 QGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAM 176
Cdd:cd07088 85 QGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 177 VLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELG 256
Cdd:cd07088 165 VIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 257 GNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAAL 336
Cdd:cd07088 245 GKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 337 EKVEEHVSDAVKKGGRVVQGGKRHALG-GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLAS 415
Cdd:cd07088 325 DKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 416 YFYAKDLSRVFRVAEALEYGMVGVNTGlisTAEAPFG---GVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07088 405 YIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
50-477 |
4.31e-158 |
|
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: 455.07 E-value: 4.31e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 50 KEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDI 129
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 130 VPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFS-AIAIAILAERAGLPAGLFSVI 208
Cdd:cd07104 83 LPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 209 TGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTC 288
Cdd:cd07104 163 PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 289 VCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHalgGTFYE 368
Cdd:cd07104 243 MAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 369 ATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIS-TA 447
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNdEP 399
|
410 420 430
....*....|....*....|....*....|
gi 1801119160 448 EAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
31-477 |
1.02e-157 |
|
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: 455.47 E-value: 1.02e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKG--WAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA 188
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDAD 268
Cdd:cd07114 163 LELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 269 LDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVK 348
Cdd:cd07114 243 LDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARARE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 349 KGGRVVQGGKRHAL----GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSR 424
Cdd:cd07114 323 EGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLAR 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 425 VFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07114 403 AHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
29-475 |
1.65e-157 |
|
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: 454.29 E-value: 1.65e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGasfVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA 188
Cdd:cd07106 81 GGA---VAWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIAILAERAgLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDAD 268
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 269 LDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVK 348
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 349 KGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRV 428
Cdd:cd07106 316 KGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1801119160 429 AEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07106 396 ARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-477 |
1.92e-157 |
|
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: 454.48 E-value: 1.92e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA 188
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDAD 268
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 269 LDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVK 348
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 349 KGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRV 428
Cdd:cd07150 323 KGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1801119160 429 AEALEYGMVGVN-TGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07150 400 AERLESGMVHINdPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
31-479 |
2.34e-155 |
|
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: 449.32 E-value: 2.34e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEA-TGEIV 109
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 110 YGASFVEWFAEEARRLYGDIVPgHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAI 189
Cdd:cd07093 83 RAAANFRFFADYILQLDGESYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 190 AIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADL 269
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 270 DAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKK 349
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 350 GGRVVQGGKRHAL----GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRV 425
Cdd:cd07093 322 GATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1801119160 426 FRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07093 402 HRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
27-479 |
1.19e-154 |
|
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: 447.43 E-value: 1.19e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATG 106
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 107 EIVYGASFVEWFAEEARRLYGDIVPGHQ----KDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPAS 182
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDAspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 183 QTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELyKQCAPtIKKLGLELGGNAPFI 262
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI-ARKAG-LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 263 VFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEH 342
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 343 VSDAVKKGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDL 422
Cdd:cd07149 319 VEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 423 SRVFRVAEALEYGMVGVNTglISTAEA---PFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07149 396 QKALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
27-479 |
6.63e-154 |
|
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: 445.64 E-value: 6.63e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATG 106
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 107 EIVYGASFVEWFAEEARRLYGDIVP--GHQKDKRILVM--KQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPAS 182
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPvdAYEYNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 183 QTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFI 262
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 263 VFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEH 342
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 343 VSDAVKKGGRVVQGGKRhaLGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDL 422
Cdd:cd07145 321 VNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 423 SRVFRVAEALEYGMVGVN-TGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07145 399 NRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
14-477 |
3.72e-148 |
|
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: 431.67 E-value: 3.72e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEAdGSGIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRI 92
Cdd:cd07097 4 YIDGEWVAG-GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 93 LTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAA 172
Cdd:cd07097 83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 173 GCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLG 252
Cdd:cd07097 163 GNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 253 LELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLID 332
Cdd:cd07097 243 LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 333 NAALEKVEEHVSDAVKKGGRVVQGGKRHALG--GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTE 410
Cdd:cd07097 323 ERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801119160 411 FGLASYFYAKDLSRVFRVAEALEYGMVGVNtglISTAE----APFGGVKLSGLG-REGSRYGIEEFTEIKYV 477
Cdd:cd07097 403 FGLSAGIVTTSLKHATHFKRRVEAGVVMVN---LPTAGvdyhVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
51-477 |
3.98e-146 |
|
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: 424.57 E-value: 3.98e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 51 EAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDiV 130
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 131 PGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITG 210
Cdd:cd07100 82 PIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 211 SAREIgAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVC 290
Cdd:cd07100 162 DSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 291 ANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEAT 370
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 371 VIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAP 450
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*..
gi 1801119160 451 FGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
18-477 |
3.13e-145 |
|
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: 424.42 E-value: 3.13e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 18 RWIEAD-GSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA--QKGWAARTAKERSGILRKWFELMIENKDDLGRILT 94
Cdd:cd07119 5 EWVEAAsGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 95 MEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPgHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGC 174
Cdd:cd07119 85 LNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 175 AMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLE 254
Cdd:cd07119 164 TVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 255 LGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNA 334
Cdd:cd07119 244 LGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 335 ALEKVEEHVSDAVKKGGRVVQGGKR----HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTE 410
Cdd:cd07119 324 HREKVLSYIQLGKEEGARLVCGGKRptgdELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTP 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 411 FGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07119 404 YGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
27-479 |
4.79e-143 |
|
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: 417.99 E-value: 4.79e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATG 106
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 107 EIVYGASFVEWFAEEARRLYGDIVPG----HQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPAS 182
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 183 QTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAptIKKLGLELGGNAPFI 262
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 263 VFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEH 342
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 343 VSDAVKKGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDL 422
Cdd:cd07094 319 VEEAVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 423 SRVFRVAEALEYGMVGVNTGLISTAEA-PFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
54-479 |
1.49e-142 |
|
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: 413.16 E-value: 1.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 54 DAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGH 133
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 134 QKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAR 213
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 214 EIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANR 293
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 294 LYVQDAVYDAFSAKLaaavgklktgngfeegvvlgplidnaalekveehvsdavkkggrvvqggkrhalggtfyeATVIA 373
Cdd:cd06534 241 LLVHESIYDEFVEKL------------------------------------------------------------VTVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 374 DVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLI-STAEAPFG 452
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFG 340
|
410 420
....*....|....*....|....*..
gi 1801119160 453 GVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-475 |
2.36e-141 |
|
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: 413.82 E-value: 2.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIEADGSG-IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRIL 93
Cdd:cd07138 3 IDGAWVAPAGTEtIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 94 TMEQGKPLAEATG-EIVYGASFVEWFAEEARRLYGDIVPGhqkdkRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAA 172
Cdd:cd07138 83 TLEMGAPITLARAaQVGLGIGHLRAAADALKDFEFEERRG-----NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 173 GCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLG 252
Cdd:cd07138 158 GCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 253 LELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLID 332
Cdd:cd07138 238 LELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 333 NAALEKVEEHVSDAVKKGGRVVQGGKRHALG---GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDT 409
Cdd:cd07138 318 AAQFDRVQGYIQKGIEEGARLVAGGPGRPEGlerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 410 EFGLASYFYAKDLSRVFRVAEALEYGMVGVNtGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07138 398 PYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
14-477 |
1.29e-140 |
|
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: 412.37 E-value: 1.29e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAAR--TAKERSGILRKWFELMIENKDDLG 90
Cdd:cd07091 7 FINNEFVDSvSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 91 RILTMEQGKPLAE-ATGEIVYGASFVEWFAEEARRLYGDIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPA 169
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPI-DGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 170 FAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-I 248
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 249 KKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLG 328
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 329 PLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAND 408
Cdd:cd07091 326 PQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAND 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801119160 409 TEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07091 406 TEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
14-477 |
2.17e-140 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 412.00 E-value: 2.17e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRIL 93
Cdd:PRK13473 6 LINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 94 TMEQGKPLAEATGEIVYGASFV-EWFAEEARRLYG----DIVPGHQKdkriLVMKQPIGVVAAITPWNFPNAMITRKAGP 168
Cdd:PRK13473 86 SLNCGKPLHLALNDEIPAIVDVfRFFAGAARCLEGkaagEYLEGHTS----MIRRDPVGVVASIAPWNYPLMMAAWKLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 169 AFAAGCAMVLKPASQTPFSAIAIAILAERAgLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTI 248
Cdd:PRK13473 162 ALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 249 KKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLG 328
Cdd:PRK13473 241 KRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 329 PLIDNAALEKVEEHVSDAVKKG-GRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAN 407
Cdd:PRK13473 321 PLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 408 DTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PRK13473 401 DSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
29-475 |
1.43e-138 |
|
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: 406.63 E-value: 1.43e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWA-ARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGE 107
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 108 IVYG-ASFVEWFAEEARRLYGDIVPGHQKDKRI----LVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPAS 182
Cdd:cd07089 81 QVDGpIGHLRYFADLADSFPWEFDLPVPALRGGpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 183 QTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFI 262
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 263 VFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEH 342
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 343 VSDAVKKGGRVVQGGKR--HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAK 420
Cdd:cd07089 321 IARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 421 DLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-477 |
4.02e-138 |
|
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: 405.18 E-value: 4.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 30 KNPATGELVGYVPKLGAKETKEAIDAAAEA-QKGWAAR-TAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGE 107
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfDKGPWPRmSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 108 IVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFS 187
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 188 AIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAV 347
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 348 KKGGRVVQGGKRHALG-GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVF 426
Cdd:cd07118 322 AEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1801119160 427 RVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
18-477 |
8.63e-138 |
|
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: 404.76 E-value: 8.63e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 18 RWIEADGSG-IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTME 96
Cdd:cd07151 2 EWRDGTSERtIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 97 QGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAM 176
Cdd:cd07151 82 SGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 177 VLKPASQTPFSA-IAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLEL 255
Cdd:cd07151 162 VLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 256 GGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAA 335
Cdd:cd07151 242 GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 336 LEKVEEHVSDAVKKGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLAS 415
Cdd:cd07151 322 VDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 416 YFYAKDLSRVFRVAEALEYGMVGVNTGLIS-TAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07151 399 AVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
14-477 |
1.27e-137 |
|
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: 404.81 E-value: 1.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSG-IAVKNPATG-ELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGR 91
Cdd:cd07131 2 YIGGEWVDSASGEtFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 92 ILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFA 171
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 172 AGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKL 251
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 252 GLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLI 331
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 332 DNAALEKVEEHVSDAVKKGGRVVQGGKR----HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAN 407
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 408 DTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIStAEA--PFGGVKLSGLG-REGSRYGIEEFTEIKYV 477
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIG-AEVhlPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
31-479 |
9.33e-136 |
|
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: 399.12 E-value: 9.33e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATG-EIV 109
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 110 YGASFVEWFAEEARRLYGDIVPghqKDKRIL--VMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFS 187
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP---VRGPFLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 188 AIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAV 347
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 348 KKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFR 427
Cdd:cd07115 320 EEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1801119160 428 VAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07115 400 VAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
29-477 |
1.23e-135 |
|
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: 398.62 E-value: 1.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAE-ATGE 107
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 108 IVYGASFVEWFAEEAR----RLYGDIVPGHQKdkriLVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQ 183
Cdd:cd07092 81 LPGAVDNFRFFAGAARtlegPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 184 TPFSAIAIAILAERaGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIV 263
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 264 FDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHV 343
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 344 SDAvKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLS 423
Cdd:cd07092 316 ERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1801119160 424 RVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
31-477 |
3.82e-135 |
|
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: 397.75 E-value: 3.82e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVY 110
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 111 GASFVEWFAEEARRLYGD-IVPGHQ--KDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFS 187
Cdd:cd07099 82 ALEAIDWAARNAPRVLAPrKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 188 AIAIAILAERAGLPAGLFSVITGSArEIGAEMTANPIiRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAGV-DKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAV 347
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 348 KKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFR 427
Cdd:cd07099 320 AKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1801119160 428 VAEALEYGMVGVNTGLISTA--EAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07099 400 IARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
14-475 |
7.87e-134 |
|
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: 395.01 E-value: 7.87e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRIL 93
Cdd:cd07086 2 VIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 94 TMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAG 173
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 174 CAMVLKPASQTPFSAIAIA-ILAE---RAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIK 249
Cdd:cd07086 162 NTVVWKPSETTPLTAIAVTkILAEvleKNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 250 KLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGP 329
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 330 LIDNAALEKVEEHVSDAVKKGGRVVQGGKR--HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAN 407
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801119160 408 DTEFGLASYFYAKDLSRVFRV--AEALEYGMVGVNTGlISTAEA--PFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIP-TSGAEIggAFGGEKETGGGRESGSDAWKQYMRRS 471
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
24-475 |
8.02e-134 |
|
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: 394.66 E-value: 8.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 24 GSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA-QKG-WAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPL 101
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAfESGvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 102 AEATGEIVYG-ASFVEWFAEEARRLYGDIVP-GHqkDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLK 179
Cdd:cd07112 81 SDALAVDVPSaANTFRWYAEAIDKVYGEVAPtGP--DALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 180 PASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-IKKLGLELGGN 258
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 259 APFIVFDDA-DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALE 337
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 338 KVEEHVSDAVKKGGRVVQGGKRH--ALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLAS 415
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 416 YFYAKDLSRVFRVAEALEYGMVGVNT---GLISTaeaPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCfdeGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
29-478 |
1.74e-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: 390.90 E-value: 1.74e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYGDIVPgHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA 188
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIA-ILAErAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:cd07090 160 LLLAeILTE-AGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAV 347
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 348 KKGGRVVQGGKRHAL-----GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDL 422
Cdd:cd07090 318 QEGAKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 423 SRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVC 478
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
27-475 |
2.71e-132 |
|
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: 390.45 E-value: 2.71e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATG 106
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 107 EIVYGASFVEWFAEEARRLYG-----DIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPA 181
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGevlplDISAR-GEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 182 SQTPFSAIAIAILAERAGLPAGLFSVITGSaREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPtiKKLGLELGGNAPF 261
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 262 IVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEE 341
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 342 HVSDAVKKGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKD 421
Cdd:cd07147 317 WVNEAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 422 LSRVFRVAEALEYGmvGVNTGLISTAEA---PFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07147 394 LEKALRAWDELEVG--GVVINDVPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-477 |
5.38e-132 |
|
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: 389.79 E-value: 5.38e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRL---YGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTP 185
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 186 FSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFD 265
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 266 DADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSD 345
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 346 AVKKGGRVVQGGKRHALG--GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLS 423
Cdd:cd07110 321 GKEEGARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1801119160 424 RVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
13-477 |
1.46e-131 |
|
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: 389.24 E-value: 1.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 13 ALVGTRWIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAAR-TAKERSGILRKWFELMIENKDDLGR 91
Cdd:cd07082 4 YLINGEWKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 92 ILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPG----HQKDKRILVMKQPIGVVAAITPWNFP-NAMITrKA 166
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGdwfpGTKGKIAQVRREPLGVVLAIGPFNYPlNLTVS-KL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 167 GPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQcAP 246
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ-HP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 247 tIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVV 326
Cdd:cd07082 242 -MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 327 LGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRhaLGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQA 406
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 407 NDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTgliSTAEA----PFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07082 399 NKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQRGpdhfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-482 |
1.60e-131 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 389.63 E-value: 1.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 6 PSLLRQAALVGTRWIEAD-GSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIE 84
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATsGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 85 NKDDLGRILTMEQGKPLAEA-TGEIVYGASFVEWFAEEARRLYGDIVPGHQKDkRILVMKQPIGVVAAITPWNFPNAMIT 163
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETsVVDIVTGADVLEYYAGLAPALEGEQIPLRGGS-FVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 164 RKAGPAFAAGCAMVLKPASQTPFSAIAIA-ILAErAGLPAGLFSVITGSAReIGAEMTANPIIRKLTFTGSTEIGAELYK 242
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAeIYTE-AGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 243 QCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFE 322
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 323 EGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKR----HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTD 398
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 399 ENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK--Y 476
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKsvQ 478
|
....*.
gi 1801119160 477 VCLGGI 482
Cdd:PRK13252 479 VEMGPF 484
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
5-473 |
7.28e-131 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 389.24 E-value: 7.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 5 DPSLLRQaaLVGTRWIEADGSgIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIE 84
Cdd:PRK09407 15 TFERLRR--LTARVDGAAGPT-REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 85 NKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGD-----IVPGHQKDKrilVMKQPIGVVAAITPWNFPN 159
Cdd:PRK09407 92 NREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPrrragALPVLTKTT---ELRQPKGVVGVISPWNYPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 160 AMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANpiIRKLTFTGSTEIGAE 239
Cdd:PRK09407 169 TLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 240 LYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGN 319
Cdd:PRK09407 247 LAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 320 GFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGK-RHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTD 398
Cdd:PRK09407 327 GYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVAD 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 399 ENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIST---AEAPFGGVKLSGLGREGSRYGIEEFTE 473
Cdd:PRK09407 407 VDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAwgsVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-475 |
3.65e-129 |
|
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: 383.08 E-value: 3.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIEADGSG-IAVKNPATGELVGYVPKLGAKETKEAIDAAAEA--QKGWAARTAKERSGILRKWFELMIENKDDLGR 91
Cdd:cd07139 3 IGGRWVAPSGSEtIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 92 ILTMEQGKPLAEATGEIVYGASFV-EWFAEEARRL-YGDIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPA 169
Cdd:cd07139 83 LWTAENGMPISWSRRAQGPGPAALlRYYAALARDFpFEERRPG-SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 170 FAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSaREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIK 249
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 250 KLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGP 329
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 330 LIDNAALEKVEEHVSDAVKKGGRVVQGGKR--HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAN 407
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 408 DTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNtGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07139 401 DSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
32-477 |
1.01e-127 |
|
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: 378.58 E-value: 1.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 32 PATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYG 111
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 112 ASFVEWFAEEARRLYGD-----IVPGHQkdkRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPF 186
Cdd:cd07101 83 AIVARYYARRAERLLKPrrrrgAIPVLT---RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 187 SAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANpiIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDD 266
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 267 ADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDA 346
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 347 VKKGGRVVQGGK-RHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRV 425
Cdd:cd07101 318 VAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 426 FRVAEALEYGMVGVNTGLIST---AEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07101 398 RRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
29-477 |
2.29e-127 |
|
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: 377.73 E-value: 2.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAAR-TAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGE 107
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 108 IVYGASFVEWFAEEARRLYGDIVPgHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFS 187
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 188 AIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGfEEGVVLGPLIDNAALEKVEEHVSDAV 347
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 348 KKGGRVVQGGKR---HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSR 424
Cdd:cd07109 319 ARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1801119160 425 VFRVAEALEYGMVGVNT-GLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07109 399 ALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
27-479 |
2.69e-126 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 375.16 E-value: 2.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKlgakETKEAIDAAAEAQKGWAAR-TAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEAT 105
Cdd:cd07146 1 LEVRNPYTGEVVGTVPA----GTEEALREALALAASYRSTlTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 106 GEIVYGASFVEWFAEEARRLYGDIVP----GHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPA 181
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdltANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 182 SQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELykQCAPTIKKLGLELGGNAPF 261
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 262 IVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEE 341
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 342 HVSDAVKKGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKD 421
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 422 LSRVFRVAEALEYGMVGVNTGL-ISTAEAPFGGVKLSGLG-REGSRYGIEEFTEIKYVCL 479
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
31-479 |
6.49e-125 |
|
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: 371.68 E-value: 6.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKG--WAaRTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYG---DIVPGhqkdKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTP 185
Cdd:cd07120 82 SGAISELRYYAGLARTEAGrmiEPEPG----SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 186 FSAIAIA-ILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVF 264
Cdd:cd07120 158 QINAAIIrILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 265 DDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVS 344
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 345 DAVKKGGRVVQGGKRHALG---GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKD 421
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 422 LSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-477 |
2.62e-124 |
|
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: 370.97 E-value: 2.62e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 19 WIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAAR-TAKERSGILRKWFELMIENKDDLGRILTME 96
Cdd:cd07144 16 FVKSsDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 97 QGKPL-AEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKdKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCA 175
Cdd:cd07144 96 SGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPN-KLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 176 MVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLEL 255
Cdd:cd07144 175 VVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLEC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 256 GGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGK-LKTGNGFEEGVVLGPLIDNA 334
Cdd:cd07144 255 GGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 335 ALEKVEEHVSDAVKKGGRVVQGGKRHALG---GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEF 411
Cdd:cd07144 335 QYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTY 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 412 GLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07144 415 GLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-477 |
7.79e-123 |
|
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: 366.30 E-value: 7.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPL-AEATGE 107
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 108 IVYGASFVEWFAEEARRLYGDIVPGHQkDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFS 187
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGP-DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 188 AIAIAILAERAgLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDA 267
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 268 DLDAAVEGALIA-KFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDA 346
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 347 VK-KGGRVVQGGKRHALG----GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKD 421
Cdd:cd07108 319 LStSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 422 LSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYG-IEEFTEIKYV 477
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
15-477 |
6.95e-122 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 365.59 E-value: 6.95e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIEAD-GSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA-----QKGWAARTAKERSGILRKWFELMIENKDD 88
Cdd:PLN02467 12 IGGEWREPVlGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 89 LGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRL----YGDI-VPGHQKDKRILvmKQPIGVVAAITPWNFPNAMIT 163
Cdd:PLN02467 92 LAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALdakqKAPVsLPMETFKGYVL--KEPLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 164 RKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQ 243
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 244 CAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEE 323
Cdd:PLN02467 250 AAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 324 GVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKR--HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDEND 401
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpeHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDE 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 402 VIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PLN02467 410 AIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
19-477 |
4.46e-121 |
|
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: 362.82 E-value: 4.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 19 WIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA-QKGWAART--AKERSGILRKWFELMIENKDDLGRILT 94
Cdd:cd07141 15 WHDSvSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAfKLGSPWRTmdASERGRLLNKLADLIERDRAYLASLET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 95 MEQGKPLAEA-TGEIVYGASFVEWFAEEARRLYGDIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAG 173
Cdd:cd07141 95 LDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPM-DGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 174 CAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGaELYKQCA--PTIKKL 251
Cdd:cd07141 174 NTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG-KLIQQAAgkSNLKRV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 252 GLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLI 331
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 332 DNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEF 411
Cdd:cd07141 333 DEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 412 GLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07141 413 GLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
48-477 |
1.99e-119 |
|
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: 356.89 E-value: 1.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 48 ETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYG 127
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 128 DIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSV 207
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 208 ITGS---AREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNN 284
Cdd:cd07105 161 VTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 285 GQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGngfeeGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGK-RHALG 363
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 364 GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGL 443
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1801119160 444 IST-AEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07105 396 VHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
23-477 |
2.62e-117 |
|
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: 352.99 E-value: 2.62e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 23 DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAAR--TAKERSGILRKWFELMIENKDDLGRILTMEQGKP 100
Cdd:cd07143 20 HGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLkvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 101 -LAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKdKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLK 179
Cdd:cd07143 100 fGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-KLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 180 PASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-IKKLGLELGGN 258
Cdd:cd07143 179 PSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnLKKVTLELGGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 259 APFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEK 338
Cdd:cd07143 259 SPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 339 VEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFY 418
Cdd:cd07143 339 IMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVF 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1801119160 419 AKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07143 419 TNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
75-479 |
5.24e-117 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 349.81 E-value: 5.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 75 LRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITP 154
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 155 WNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGST 234
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 235 EIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGK 314
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 315 LKTGNGFEEG-VVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPL 393
Cdd:PRK10090 241 VQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 394 FRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTE 473
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
....*.
gi 1801119160 474 IKYVCL 479
Cdd:PRK10090 401 TQVVYL 406
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
14-477 |
8.07e-117 |
|
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: 351.80 E-value: 8.07e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA--QKGWAARTAKERSGILRKWFELMIENKDDLG 90
Cdd:cd07142 7 FINGQFVDAaSGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 91 RILTMEQGKPLAEA-TGEIVYGASFVEWFAEEARRLYGDIVPGHQKdKRILVMKQPIGVVAAITPWNFPNAMITRKAGPA 169
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 170 FAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-I 248
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 249 KKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLG 328
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 329 PLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAND 408
Cdd:cd07142 326 PQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANN 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801119160 409 TEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07142 406 SKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
14-475 |
3.75e-116 |
|
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: 350.11 E-value: 3.75e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRI 92
Cdd:cd07559 4 FINGEWVAPsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 93 LTMEQGKPLAEATG-EIVYGASFVEWFAEEARRLYGDIVpghQKDKRIL--VMKQPIGVVAAITPWNFPNAMITRKAGPA 169
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLS---EIDEDTLsyHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 170 FAAGCAMVLKPASQTPFSaiaIAILAERAG--LPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT 247
Cdd:cd07559 161 LAAGNTVVLKPASQTPLS---ILVLMELIGdlLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 248 IKKLGLELGGNAPFIVFDDAD------LDAAVEGALIAKFrNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGF 321
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 322 EEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALG----GTFYEATVIADVTPDMAVAKEETFGPVAPLFRFT 397
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 398 DENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-475 |
1.64e-114 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 345.59 E-value: 1.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 19 WIEA-DGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQ 97
Cdd:cd07117 9 WVKGsSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 98 GKPLAEATG-EIVYGASFVEWFAEEARRLYGDIVpghQKDKRIL--VMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGC 174
Cdd:cd07117 89 GKPIRETRAvDIPLAADHFRYFAGVIRAEEGSAN---MIDEDTLsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 175 AMVLKPASQTPFSAIAIAILAERAgLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLE 254
Cdd:cd07117 166 TVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 255 LGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNA 334
Cdd:cd07117 245 LGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 335 ALEKVEEHVSDAVKKGGRVVQGGKR----HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTE 410
Cdd:cd07117 325 QLDKILSYVDIAKEEGAKILTGGHRltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 411 FGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07117 405 YGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-480 |
1.04e-113 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 342.87 E-value: 1.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATG 106
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 107 EIVYGASFVEWFAEEARRLYGDiVPGHQKD---KRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQ 183
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLAD-EPADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 184 TPFSAIAIAILAERAGLPAGLFSVITGSAREIGAeMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIV 263
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEA-ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 264 FDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHV 343
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 344 SDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLS 423
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 424 RVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCLG 480
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
35-477 |
2.13e-113 |
|
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: 341.58 E-value: 2.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 35 GELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASF 114
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 115 VEWFAEEARRLYGDIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSA-IAIAI 193
Cdd:cd07152 81 LHEAAGLPTQPQGEILPS-APGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 194 LAERAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAV 273
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 274 EGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRV 353
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 354 VQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALE 433
Cdd:cd07152 319 EAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1801119160 434 YGMVGVNTGLIS-TAEAPFGGVKLSGLG-REGSRYGIEEFTEIKYV 477
Cdd:cd07152 396 TGMLHINDQTVNdEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
31-475 |
2.28e-111 |
|
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: 336.91 E-value: 2.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVY 110
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 111 GASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFP-----NAMItrkagPAFAAGCAMVLKPASQTP 185
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPyltavNAVI-----PALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 186 FSAIAIAILAERAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFD 265
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 266 DADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSD 345
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 346 AVKKGGRVVQGGKRHAL---GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDL 422
Cdd:cd07102 316 AIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 423 SRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07102 396 ARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-478 |
2.67e-110 |
|
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: 336.12 E-value: 2.67e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSgIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRI 92
Cdd:cd07124 36 VIGGKEVRTEEK-IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 93 LTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKqPIGVVAAITPWNFPNAMITRKAGPAFAA 172
Cdd:cd07124 115 MVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 173 GCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT----- 247
Cdd:cd07124 194 GNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpgqk 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 248 -IKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVV 326
Cdd:cd07124 274 wLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 327 LGPLIDNAALEKVEEHVSDAvKKGGRVVQGGKR--HALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIA 404
Cdd:cd07124 354 MGPVIDKGARDRIRRYIEIG-KSEGRLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALE 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 405 QANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVN---TGLISTAEaPFGGVKLSGLG-REGSRYGIEEFTEIKYVC 478
Cdd:cd07124 433 IANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALVGRQ-PFGGFKMSGTGsKAGGPDYLLQFMQPKTVT 509
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-477 |
7.40e-110 |
|
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: 333.19 E-value: 7.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 29 VKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VYGASFVEWFAEEARRLYGDIVPghqKDKRILVM--KQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPF 186
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIP---VGGRNLHYtlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 187 SAIAIAILAeRAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDD 266
Cdd:cd07107 158 SALRLAELA-REVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 267 ADLDAAVEGALIA-KFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSD 345
Cdd:cd07107 237 ADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 346 AVKKGGRVVQGGKR---HALGGTFY-EATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKD 421
Cdd:cd07107 317 AKREGARLVTGGGRpegPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 422 LSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
31-477 |
2.27e-109 |
|
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: 332.92 E-value: 2.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKG--WAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEI 108
Cdd:cd07140 27 NPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 109 VyGASFVEW--FAEEARRLYGDIVPGHQ-KDKRILVM--KQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQ 183
Cdd:cd07140 107 V-GMSIQTFryFAGWCDKIQGKTIPINQaRPNRNLTLtkREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 184 TPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-IKKLGLELGGNAPFI 262
Cdd:cd07140 186 TPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSnLKKVSLELGGKSPLI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 263 VFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEH 342
Cdd:cd07140 266 IFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 343 VSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDEN--DVIAQANDTEFGLASYFYAK 420
Cdd:cd07140 346 CERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvdGVLQRANDTEYGLASGVFTK 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 421 DLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07140 426 DINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
31-478 |
4.44e-108 |
|
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: 328.88 E-value: 4.44e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEAT-GEIV 109
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 110 YGASFVEW--------FAEEARRlyGDIVPGHqkdKRILVMKQPIGVVAAITPWNFP--NAMitrkaGPAFAA---GCAM 176
Cdd:cd07098 82 VTCEKIRWtlkhgekaLRPESRP--GGLLMFY---KRARVEYEPLGVVGAIVSWNYPfhNLL-----GPIIAAlfaGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 177 VLKPASQT-----PFSAIAIAILAERaGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKL 251
Cdd:cd07098 152 VVKVSEQVawssgFFLSIIRECLAAC-GHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 252 GLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLI 331
Cdd:cd07098 230 VLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 332 DNAALEKVEEHVSDAVKKGGRVVQGGKRHAL----GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQAN 407
Cdd:cd07098 310 SPARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 408 DTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIST--AEAPFGGVKLSGLGREGSRYGIEEFTEIKYVC 478
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
27-479 |
3.07e-106 |
|
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: 324.39 E-value: 3.07e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKG-WAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEAT 105
Cdd:cd07113 17 LDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 106 G-EIVYGASFVEWFAEEARRLYGDI----VPGHQKDK-RILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLK 179
Cdd:cd07113 97 AfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 180 PASQTPFSAIAIAILAERAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNA 259
Cdd:cd07113 177 PSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 260 PFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKV 339
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 340 EEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYA 419
Cdd:cd07113 336 CSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 420 KDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYVCL 479
Cdd:cd07113 416 NNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
22-477 |
1.05e-103 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 318.69 E-value: 1.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA--QKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGK 99
Cdd:PLN02766 33 ASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 100 -PLAEATGEIVYGASFVEWFAEEARRLYGDIVpghqKDKRIL---VMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCA 175
Cdd:PLN02766 113 lFALGKAVDIPAAAGLLRYYAGAADKIHGETL----KMSRQLqgyTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 176 MVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-IKKLGLE 254
Cdd:PLN02766 189 MVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSnLKQVSLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 255 LGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNA 334
Cdd:PLN02766 269 LGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 335 ALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLA 414
Cdd:PLN02766 349 QFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 415 SYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PLN02766 429 AGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-477 |
1.35e-103 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 319.83 E-value: 1.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA--QKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGK 99
Cdd:PLN02466 70 ASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 100 PLAEATG-EIVYGASFVEWFAEEARRLYGDIVPG---HQkdkrILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCA 175
Cdd:PLN02466 150 PYEQSAKaELPMFARLFRYYAGWADKIHGLTVPAdgpHH----VQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 176 MVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-IKKLGLE 254
Cdd:PLN02466 226 IVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSnLKPVTLE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 255 LGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNA 334
Cdd:PLN02466 306 LGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 335 ALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLA 414
Cdd:PLN02466 386 QFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLA 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 415 SYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PLN02466 466 AGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
19-471 |
3.81e-99 |
|
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: 306.24 E-value: 3.81e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 19 WIEADG-SGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQ 97
Cdd:cd07111 30 WVKPENrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 98 GKPLAEA-TGEIVYGASFVEWFAEEARRLYGDIvPGHQkdkrilvmkqPIGVVAAITPWNFPNAMITRKAGPAFAAGCAM 176
Cdd:cd07111 110 GKPIRESrDCDIPLVARHFYHHAGWAQLLDTEL-AGWK----------PVGVVGQIVPWNFPLLMLAWKICPALAMGNTV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 177 VLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELG 256
Cdd:cd07111 179 VLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 257 GNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAAL 336
Cdd:cd07111 258 GKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 337 EKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPV--APLFRFTDEndVIAQANDTEFGLA 414
Cdd:cd07111 338 KRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVlvVLTFRTAKE--AVALANNTPYGLA 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 415 SYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEF 471
Cdd:cd07111 416 ASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
14-477 |
1.68e-95 |
|
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: 296.74 E-value: 1.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSG-IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRI 92
Cdd:cd07085 4 FINGEWVESKTTEwLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 93 LTMEQGKPLAEATGEIVYGASFVEwFAEEARRLY-GDIVPGHQKDKRILVMKQPIGVVAAITPWNFPnAMITR-KAGPAF 170
Cdd:cd07085 84 ITLEHGKTLADARGDVLRGLEVVE-FACSIPHLLkGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPMAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 171 AAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGsAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKK 250
Cdd:cd07085 162 ACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 251 LGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPL 330
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 331 IDNAALEKVEEHVSDAVKKGGRVVQGGKRHAL----GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQA 406
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 407 NDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGL-ISTAEAPFGGVKLSGLGrEGSRYG---IEEFTEIKYV 477
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSFFG-DLHFYGkdgVRFYTQTKTV 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-475 |
1.76e-94 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 294.88 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPATGELVGYVpklgAKETKEAIDAAAEAQKG------WAARTAKERSGILRKWFELMIENKDDLGRILTM 95
Cdd:PRK09847 32 AENETFETVDPVTQAPLAKI----ARGKSVDIDRAVSAARGvfergdWSLSSPAKRKAVLNKLADLMEAHAEELALLETL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 96 EQGKPLAEATGEIVYGAS-FVEWFAEEARRLYGDIVPGhQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGC 174
Cdd:PRK09847 108 DTGKPIRHSLRDDIPGAArAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 175 AMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT-IKKLGL 253
Cdd:PRK09847 187 SVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 254 ELGGNAPFIVFDDA-DLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLID 332
Cdd:PRK09847 267 EAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 333 NAALEKVEEHVSDAVKKGGRVVQGgkRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFG 412
Cdd:PRK09847 347 CAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYG 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 413 LASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:PRK09847 425 LGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
14-477 |
6.06e-94 |
|
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: 292.83 E-value: 6.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEA--QKGWAARTAKeRSGILRKWFELMIENKDDLGR 91
Cdd:TIGR04284 4 LIDGKLVAGSAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAfdETDWSRDTAL-RVRCLRQLRDALRAHVEELRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 92 ILTMEQGKPLAEATGEIVYG-ASFVEWFAEEA-----RRLYGDIVPGHQKDKRILVmKQPIGVVAAITPWNFPNAMITRK 165
Cdd:TIGR04284 83 LTIAEVGAPRMLTAGAQLEGpVDDLGFAADLAesyawTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQINLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 166 AGPAFAAGCAMVLKPASQTPFSAIAIA-ILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQC 244
Cdd:TIGR04284 162 LGPALAAGNTVVLKPAPDTPWCAAVLGeLIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 245 APTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEG 324
Cdd:TIGR04284 242 AATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 325 VVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHA--LGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDV 402
Cdd:TIGR04284 322 TVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRPAdrDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801119160 403 IAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:TIGR04284 402 VRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
31-477 |
6.79e-92 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 287.14 E-value: 6.79e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVY 110
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 111 GASFVEWFAEEARRLYgDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIA 190
Cdd:PRK13968 93 SANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 191 IAILAERAGLPAGLFSVITGSAREIgAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLD 270
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 271 AAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKG 350
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 351 GRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAE 430
Cdd:PRK13968 331 ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1801119160 431 ALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
14-464 |
3.59e-91 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 285.64 E-value: 3.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIeADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRIL 93
Cdd:cd07130 2 VYDGEWG-GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 94 TMEQGKPLAEATGEI---------VYGASfvewfaeeaRRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFP------ 158
Cdd:cd07130 81 SLEMGKILPEGLGEVqemidicdfAVGLS---------RQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPvavwgw 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 159 NAMItrkagpAFAAGCAMVLKPASQTPFSAIAI-AILA---ERAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGST 234
Cdd:cd07130 152 NAAI------ALVCGNVVVWKPSPTTPLTAIAVtKIVArvlEKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 235 EIGaelyKQCAPTI-KKLG---LELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAA 310
Cdd:cd07130 225 AVG----RQVGQAVaARFGrslLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 311 AVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATvIADVTPDMAVAKEETFGPV 390
Cdd:cd07130 301 AYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPT-IVEGLSDAPIVKEETFAPI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801119160 391 APLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEAL--EYGMVGVNTGlISTAE--APFGGVKLSGLGRE-GS 464
Cdd:cd07130 380 LYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG-TSGAEigGAFGGEKETGGGREsGS 457
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-458 |
2.02e-89 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 282.21 E-value: 2.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSgIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRI 92
Cdd:PRK03137 40 IIGGERITTEDK-IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 93 LTMEQGKPLAEATGEIVYGASFVEWFAEEARRLyGDIVPGHQK-DKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFA 171
Cdd:PRK03137 119 LVKEAGKPWAEADADTAEAIDFLEYYARQMLKL-ADGKPVESRpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 172 AGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT---- 247
Cdd:PRK03137 198 AGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVqpgq 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 248 --IKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGfEEGV 325
Cdd:PRK03137 278 iwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 326 VLGPLIDNAALEKVEEHVSDAvKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQ 405
Cdd:PRK03137 357 YMGPVINQASFDKIMSYIEIG-KEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEI 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 406 ANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVN---TGLISTAEaPFGGVKLSG 458
Cdd:PRK03137 436 ANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVGYH-PFGGFNMSG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
27-475 |
3.61e-87 |
|
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: 274.68 E-value: 3.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 27 IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQK---GWAArtAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAE 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 104 ATGEIVYGASFVEWFAEEARRLYGDIVP-GHQK--DKRI-LVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLK 179
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPmGLTPasAGRIaFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 180 PASQTPFSAIAIAILAERAGLPAGLFSVITgSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTiKKLGLELGGNA 259
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 260 PFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKV 339
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 340 EEHVSDAVKKGGRVVQGGKRhaLGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYA 419
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 420 KDLSRVFRVAEALEYGMVGVNTgliSTA----EAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVND---HTAfrvdWMPFAGRRQSGYGTGGIPYTMHDMTQEK 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-475 |
9.28e-84 |
|
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: 266.63 E-value: 9.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIE-ADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRIL 93
Cdd:cd07116 5 IGGEWVApVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 94 TMEQGKPLAEATG-EIVYGASFVEWFAEEARRLYGDIvpgHQKDKRILV--MKQPIGVVAAITPWNFPNAMITRKAGPAF 170
Cdd:cd07116 85 TWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI---SEIDENTVAyhFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 171 AAGCAMVLKPASQTPFSaiaIAILAERAG--LPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTI 248
Cdd:cd07116 162 AAGNCVVLKPAEQTPAS---ILVLMELIGdlLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 249 KKLGLELGGNAPFIVF------DDADLDAAVEGALIAKFrNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFE 322
Cdd:cd07116 239 IPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 323 EGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALG----GTFYEATVIADvTPDMAVAKEETFGPVAPLFRFTD 398
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 399 ENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
31-460 |
3.06e-80 |
|
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: 258.26 E-value: 3.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 31 NPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIV 109
Cdd:TIGR01237 52 NPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 110 YGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAI 189
Cdd:TIGR01237 132 EAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 190 AIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPT------IKKLGLELGGNAPFIV 263
Cdd:TIGR01237 212 KFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVqpgqkhLKRVIAEMGGKDTVIV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 264 FDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHV 343
Cdd:TIGR01237 292 DEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 344 SDAvKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLS 423
Cdd:TIGR01237 372 EIG-KAEGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRD 450
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1801119160 424 RVFRVAEALEYGMVGVN---TGLISTAEaPFGGVKLSGLG 460
Cdd:TIGR01237 451 HINRAKAEFEVGNLYFNrniTGAIVGYQ-PFGGFKMSGTD 489
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-475 |
3.03e-77 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 250.06 E-value: 3.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPL 101
Cdd:PLN00412 28 SSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 102 AEATGEIVYGASFVEWFAEEARRLYG-------DIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGC 174
Cdd:PLN00412 108 KDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 175 AMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGStEIGAELYKQCAptIKKLGLE 254
Cdd:PLN00412 188 AVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAG--MVPLQME 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 255 LGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGfEEGVVLGPLIDNA 334
Cdd:PLN00412 265 LGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSES 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 335 ALEKVEEHVSDAVKKGGRVVQGGKRHalgGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLA 414
Cdd:PLN00412 344 SANFIEGLVMDAKEKGATFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQ 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 415 SYFYAKDLSRVFRVAEALEYGMVGVNtglisTAEA------PFGGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:PLN00412 421 GCVFTRDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIGSQGITNSINMMTKVK 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
50-468 |
3.01e-74 |
|
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: 240.25 E-value: 3.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 50 KEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEwFAEEA------- 122
Cdd:cd07095 3 DAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAyhertge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 123 RRLYGDIVPGHQKDKrilvmkqPIGVVAAITPWNFP----NAMITrkagPAFAAGCAMVLKPASQTPFSAIAIAILAERA 198
Cdd:cd07095 82 RATPMAQGRAVLRHR-------PHGVMAVFGPFNFPghlpNGHIV----PALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 199 GLPAGLFSVITGsAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCA--PTiKKLGLELGGNAPFIVFDDADLDAAVEGA 276
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAgrPG-KILALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 277 LIAKFRNNGQTCVCANRLYV-QDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQ 355
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 356 GGKRHALGGTFYEATVIaDVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYG 435
Cdd:cd07095 309 AMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 1801119160 436 MVGVN---TGLISTaeAPFGGVKLSGLGREGSRYGI 468
Cdd:cd07095 388 IVNWNrptTGASST--APFGGVGLSGNHRPSAYYAA 421
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-477 |
1.63e-72 |
|
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: 237.86 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILT 94
Cdd:cd07083 23 IGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 95 MEQGKPLAEATGEIVYGASFVEWFAEEARRLYG--DIVPGHQKDKRILVMkQPIGVVAAITPWNFPNAMITRKAGPAFAA 172
Cdd:cd07083 103 YEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 173 GCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCA------P 246
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlapgqT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 247 TIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVV 326
Cdd:cd07083 262 WFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 327 LGPLIDNAALEKVEEHVsDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDEN--DVIA 404
Cdd:cd07083 342 LGPVIDAEQEAKVLSYI-EHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALE 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 405 QANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVN---TGLIsTAEAPFGGVKLSGLG-REGSRYGIEEFTEIKYV 477
Cdd:cd07083 421 VANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkiTGAL-VGVQPFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
19-458 |
7.05e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 227.92 E-value: 7.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 19 WIEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQG 98
Cdd:PRK09457 9 WIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 99 KPLAEATGEI--VYG------ASFVEWFAEEARRLygdivpghqKDKRILVMKQPIGVVAAITPWNFP----NAMITrka 166
Cdd:PRK09457 89 KPLWEAATEVtaMINkiaisiQAYHERTGEKRSEM---------ADGAAVLRHRPHGVVAVFGPYNFPghlpNGHIV--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 167 gPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGsAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAP 246
Cdd:PRK09457 157 -PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 247 TIKK-LGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYV-QDAVYDAFSAKLAAAVGKLKTGNGFEEG 324
Cdd:PRK09457 235 QPEKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVpQGAQGDAFLARLVAVAKRLTVGRWDAEP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 325 V-VLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIaDVTPDMAVAKEETFGPVAPLFRFTDENDVI 403
Cdd:PRK09457 315 QpFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAI 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 404 AQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVN---TGLISTaeAPFGGVKLSG 458
Cdd:PRK09457 394 RLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkplTGASSA--APFGGVGASG 449
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-460 |
2.82e-68 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 227.08 E-value: 2.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 21 EADGSGIAVKNPATGE-LVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGK 99
Cdd:cd07125 42 TETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 100 PLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLK 179
Cdd:cd07125 122 TLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 180 PASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAP---TIKKLGLELG 256
Cdd:cd07125 202 PAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgPILPLIAETG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 257 G-NApFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAA 335
Cdd:cd07125 282 GkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 336 LEKVEEHVsDAVKKGGRVVQGGKRHALGGTFYEATVIADVTPDmaVAKEETFGPVAPLFRFTDEN--DVIAQANDTEFGL 413
Cdd:cd07125 361 GKLLRAHT-ELMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEDldEAIEDINATGYGL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1801119160 414 ASYFYAKDLSRVFRVAEALEYGMVGVN---TGLISTAEaPFGGVKLSGLG 460
Cdd:cd07125 438 TLGIHSRDEREIEYWRERVEAGNLYINrniTGAIVGRQ-PFGGWGLSGTG 486
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-462 |
3.01e-67 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 224.33 E-value: 3.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 11 QAALVGTRWiEADGSGIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLG 90
Cdd:PLN02315 21 LGCYVGGEW-RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 91 RILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAF 170
Cdd:PLN02315 100 RLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 171 AAGCAMVLKPASQTPFSAIA----IAILAERAGLPAGLFSVITGSArEIGAEMTANPIIRKLTFTGSTEIGAELYKQCAP 246
Cdd:PLN02315 180 VCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 247 TIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVV 326
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 327 LGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHALGGTFYEATVIaDVTPDMAVAKEETFGPVAPLFRFTDENDVIAQA 406
Cdd:PLN02315 339 LGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEIN 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801119160 407 NDTEFGLASYFYAKDLSRVFRV--AEALEYGMVGVNtglISTAEA----PFGGVKLSGLGRE 462
Cdd:PLN02315 418 NSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVN---IPTNGAeiggAFGGEKATGGGRE 476
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
22-460 |
4.03e-59 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 210.49 E-value: 4.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKP 100
Cdd:PRK11905 564 VDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKT 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 101 LAEATGEIVYGASFVEWFAEEARRLYGDivPGHqkdkrilvmkQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP 180
Cdd:PRK11905 644 LANAIAEVREAVDFLRYYAAQARRLLNG--PGH----------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKP 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 181 ASQTPF-SAIAIAILAErAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAptiKKLG------L 253
Cdd:PRK11905 712 AEQTPLiAARAVRLLHE-AGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLA---KRSGppvpliA 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 254 ELGG-NApFIVFDDADLDAAVEGALIAKFRNNGQTCvCANR-LYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLI 331
Cdd:PRK11905 788 ETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRvLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVI 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 332 DNAALEKVEEHVsDAVKKGGRVVqggKRHAL-----GGTFYEATVIAdvTPDMAVAKEETFGPVAPLFRF--TDENDVIA 404
Cdd:PRK11905 866 DAEAQANIEAHI-EAMRAAGRLV---HQLPLpaeteKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFkaDELDRVID 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801119160 405 QANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIStaeA-----PFGGVKLSGLG 460
Cdd:PRK11905 940 DINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIG---AvvgvqPFGGEGLSGTG 997
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
10-477 |
5.65e-58 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 201.90 E-value: 5.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 10 RQAALVGTRWIEADGSG-IAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDD 88
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSfIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 89 LGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVPGHQKDKRILVMKQPIGVVAAITPWNFPnAMITRKAGP 168
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFP-AMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 169 -AFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAeMTANPIIRKLTFTGSTEIGAELYKQCAPT 247
Cdd:PLN02419 272 vAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 248 IKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVC-ANRLYVQDAvyDAFSAKLAAAVGKLKTGNGFEEGVV 326
Cdd:PLN02419 351 GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKLVERAKALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 327 LGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHAL----GGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDV 402
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVpgyeKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801119160 403 IAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGL-ISTAEAPFGGVKLSGLGREG--SRYGIEEFTEIKYV 477
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
66-478 |
1.02e-57 |
|
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: 196.59 E-value: 1.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 66 RTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEA--------TGEIVYG-ASFVEWFAEeaRRLYgdiVPGHQKD 136
Cdd:cd07087 17 RSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHAlKHLKKWMKP--RRVS---VPLLLQP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 137 KRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAgLPAGLFSVITGSAREIg 216
Cdd:cd07087 92 AKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 217 AEMTANP---IIrkltFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANR 293
Cdd:cd07087 170 TALLAEPfdhIF----FTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 294 LYVQDAVYDAFSAKLAAAVgKLKTGNGFEEGVVLGPLIDNAALEKVEEhvsdaVKKGGRVVQGGKRHAlGGTFYEATVIA 373
Cdd:cd07087 246 VLVHESIKDELIEELKKAI-KEFYGEDPKESPDYGRIINERHFDRLAS-----LLDDGKVVIGGQVDK-EERYIAPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 374 DVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLI--STAEAPF 451
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPF 398
|
410 420
....*....|....*....|....*..
gi 1801119160 452 GGVKLSGLGREGSRYGIEEFTEIKYVC 478
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
54-472 |
6.52e-57 |
|
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: 194.75 E-value: 6.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 54 DAAAEAQKG--WAAR--TAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGasfVEWFAEEARRlygdi 129
Cdd:cd07134 1 RRVFAAQQAhaLALRasTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILP---VLSEINHAIK----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 130 vpgH----QKDKRI-----------LVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAIL 194
Cdd:cd07134 73 ---HlkkwMKPKRVrtplllfgtksKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 195 AERAgLPAGLFSVITGSArEIGAEMTANP---IIrkltFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDA 271
Cdd:cd07134 150 IREA-FDEDEVAVFEGDA-EVAQALLELPfdhIF----FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 272 AVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGK-LKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKG 350
Cdd:cd07134 224 AAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 351 GRVVQGGKRHAlGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAE 430
Cdd:cd07134 304 AKVEFGGQFDA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1801119160 431 ALEYGMVGVNTGLISTAEA--PFGGVKLSGLGREGSRYGIEEFT 472
Cdd:cd07134 383 RTSSGGVVVNDVVLHFLNPnlPFGGVNNSGIGSYHGVYGFKAFS 426
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-472 |
2.12e-54 |
|
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: 188.20 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 75 LRKWFELMIENKDDLGRILTMEQGKPLAEAT--------GEIVYGASFVEWFAEEARRlyGDIVPGHQKDKrILVMKQPI 146
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETLltevsgvkNDILHMLKNLKKWAKDEKV--KDGPLAFMFGK-PRIRKEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 147 GVVAAITPWNFPnamITRKAGP---AFAAGCAMVLKPASQTPFSAIAIAILAERAgLPAGLFSVITGSAreigAEMTAnp 223
Cdd:cd07135 110 GVVLIIGPWNYP---VLLALSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGV----PETTA-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 224 IIR----KLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDA 299
Cdd:cd07135 180 LLEqkfdKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 300 VYDAFSAKLAAAVGKLkTGNGFEEGVVLGPLIDNAALEKVEEHVSDAvkkGGRVVQGGKRHAlGGTFYEATVIADVTPDM 379
Cdd:cd07135 260 VYDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEMDE-ATRFIPPTIVSDVSWDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 380 AVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTA--EAPFGGVKLS 457
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGvdNAPFGGVGDS 414
|
410
....*....|....*
gi 1801119160 458 GLGREGSRYGIEEFT 472
Cdd:cd07135 415 GYGAYHGKYGFDTFT 429
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
11-476 |
4.97e-54 |
|
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: 188.97 E-value: 4.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 11 QAALVGTRWIEADGSGIAVKNPAT-GELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDL 89
Cdd:TIGR01238 37 QAAPIIGHSYKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 90 GRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIVpghqkdkrilvmKQPIGVVAAITPWNFPNAMITRKAGPA 169
Cdd:TIGR01238 117 MALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFS------------VESRGVFVCISPWNFPLAIFTGQISAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 170 FAAGCAMVLKPASQTPF-SAIAIAILAErAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTI 248
Cdd:TIGR01238 185 LAAGNTVIAKPAEQTSLiAYRAVELMQE-AGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 249 KKLGL---ELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGV 325
Cdd:TIGR01238 264 DAPVPliaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 326 VLGPLIDNAALEKVEEHV---SDAVKKGGRVVQGGKRHALGGTFYEATVIAdvTPDMAVAKEETFGPVAPLFRF-TDEND 401
Cdd:TIGR01238 344 DVGPVIDAEAKQNLLAHIehmSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYkARELD 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801119160 402 -VIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEA--PFGGVKLSGLG-REGSRYGIEEFTEIKY 476
Cdd:TIGR01238 422 qIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTGpKAGGPHYLYRLTQVQY 500
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
141-477 |
1.78e-51 |
|
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: 180.37 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 141 VMKQPIGVVAAITPWNFP-----NAMITrkagpAFAAGCAMVLKPASQTP-FSAIAIAILAERagLPAGLFSVITGSArE 214
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPlylalGPLIA-----ALAAGNRVMIKPSEFTPrTSALLAELLAEY--FDEDEVAVVTGGA-D 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 215 IGAEMTANPIiRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRL 294
Cdd:cd07133 169 VAAAFSSLPF-DHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 295 YVQDAVYDAFSAKLAAAVGKL-KTGNGFEEgvvLGPLIDNAALEKVEEHVSDAVKKGGRVVQ---------GGKRHALgg 364
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAKMyPTLADNPD---YTSIINERHYARLQGLLEDARAKGARVIElnpagedfaATRKLPP-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 365 tfyeaTVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLI 444
Cdd:cd07133 323 -----TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
330 340 350
....*....|....*....|....*....|....*
gi 1801119160 445 STA--EAPFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07133 398 HVAqdDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-460 |
1.13e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 182.71 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 12 AALVGTRW-----IEADGSGIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIEN 85
Cdd:PRK11904 544 AAFLEKQWqagpiINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEAN 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 86 KDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLYGDIV--PGHQKDKRILvMKQPIGVVAAITPWNFPNAMIT 163
Cdd:PRK11904 624 RAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEklPGPTGESNEL-RLHGRGVFVCISPWNFPLAIFL 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 164 RKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQ 243
Cdd:PRK11904 703 GQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRT 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 244 CA-------PTIKklglELGG-NApFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKL 315
Cdd:PRK11904 783 LAardgpivPLIA----ETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAEL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 316 KTGNGFEEGVVLGPLIDNAALEKVEEHVsDAVKKGGRVVQGGK--RHALGGTFYEATVIAdvTPDMAVAKEETFGPVAPL 393
Cdd:PRK11904 858 KVGDPRLLSTDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPlpAGTENGHFVAPTAFE--IDSISQLEREVFGPILHV 934
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801119160 394 FRF--TDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLIStaeA-----PFGGVKLSGLG 460
Cdd:PRK11904 935 IRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIG---AvvgvqPFGGQGLSGTG 1005
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
64-478 |
6.84e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 172.14 E-value: 6.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 64 AARTAKERSGILRKWFELMIENKD--------DLGR----ILTMEQGKPLAEATGEIvygASFVEWFAEEARRLYGDIVP 131
Cdd:PTZ00381 24 KTRPLEFRKQQLRNLLRMLEENKQefseavhkDLGRhpfeTKMTEVLLTVAEIEHLL---KHLDEYLKPEKVDTVGVFGP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 132 GHQKdkrilVMKQPIGVVAAITPWNFP-NAMITRKAGpAFAAGCAMVLKPASQTPFSAIAIAILAERAgLPAGLFSVITG 210
Cdd:PTZ00381 101 GKSY-----IIPEPLGVVLVIGAWNYPlNLTLIPLAG-AIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 211 SAREIgAEMTANP---IIrkltFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQT 287
Cdd:PTZ00381 174 GVEVT-TELLKEPfdhIF----FTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 288 CVCANRLYVQDAVYDAFSAKLAAAVgKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDavkKGGRVVQGGKRHaLGGTFY 367
Cdd:PTZ00381 249 CVAPDYVLVHRSIKDKFIEALKEAI-KEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVD-IENKYV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 368 EATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTA 447
Cdd:PTZ00381 324 APTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLL 403
|
410 420 430
....*....|....*....|....*....|...
gi 1801119160 448 EA--PFGGVKLSGLGREGSRYGIEEFTEIKYVC 478
Cdd:PTZ00381 404 NPnlPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
22-460 |
1.80e-46 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 173.59 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKP 100
Cdd:COG4230 567 ASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 101 LAEATGEIVYGASFVEWFAEEARRLYGDIVPGHqkdkrilvmkqPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP 180
Cdd:COG4230 647 LPDAIAEVREAVDFCRYYAAQARRLFAAPTVLR-----------GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 181 ASQTPFSAI-AIAILAErAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAptiKKLGL------ 253
Cdd:COG4230 716 AEQTPLIAArAVRLLHE-AGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLA---ARDGPivplia 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 254 ELGG-NApFIVFDDADLDAAVEGALIAKFRNNGQTCvCANR-LYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLI 331
Cdd:COG4230 792 ETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRC-SALRvLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 332 DNAALEKVEEHVsDAVKKGGRVVQGGKR--HALGGTFYEATVIAdvTPDMAVAKEETFGPVAPLFRF--TDENDVIAQAN 407
Cdd:COG4230 870 DAEARANLEAHI-ERMRAEGRLVHQLPLpeECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVRYkaDELDKVIDAIN 946
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801119160 408 DTEFGLAsyfyakdL-------SRVFRVAEALEYG-----------MVGVNtglistaeaPFGGVKLSGLG 460
Cdd:COG4230 947 ATGYGLT-------LgvhsridETIDRVAARARVGnvyvnrniigaVVGVQ---------PFGGEGLSGTG 1001
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
22-460 |
8.09e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 171.70 E-value: 8.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 22 ADGSGIAVKNPA-TGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKP 100
Cdd:PRK11809 656 AAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 101 LAEATGEIVYGASFVEWFAEEARRLYGDivpghqkdkrilVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP 180
Cdd:PRK11809 736 FSNAIAEVREAVDFLRYYAGQVRDDFDN------------DTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKP 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 181 ASQTPF-SAIAIAILAErAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTE--------IGAELYKQCAPTikKL 251
Cdd:PRK11809 804 AEQTPLiAAQAVRILLE-AGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEvarllqrnLAGRLDPQGRPI--PL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 252 GLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLI 331
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 332 DNAALEKVEEHVSDAVKKGGRVVQGGKRHALG---GTFYEATVIA-DVTPDMavaKEETFGPVAPLFRFTDE--NDVIAQ 405
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSEDwqsGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNRNqlDELIEQ 1037
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801119160 406 ANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTAEA--PFGGVKLSGLG 460
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1094
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
141-475 |
1.31e-43 |
|
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: 159.59 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 141 VMKQPIGVVAAITPWNFP-----NAMItrkaGpAFAAGCAMVLKPASQTPF-SAIAIAILAERagLPAGLFSVITGsARE 214
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPfqlalAPLI----G-AIAAGNTAVLKPSELTPNtSKVIAKIIEET--FDEEYVAVVEG-GVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 215 IGAEMTANPIiRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRL 294
Cdd:cd07136 168 ENQELLDQKF-DYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 295 YVQDAVYDAFSAKLAAAVGKLKtGNGFEEGVVLGPLIDNAALEKVEEHVsdavkKGGRVVQGGKRHAlgGTFY-EATVIA 373
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFY-GEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDR--ETLYiEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 374 DVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLI--STAEAPF 451
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPF 398
|
330 340
....*....|....*....|....
gi 1801119160 452 GGVKLSGLGREGSRYGIEEFTEIK 475
Cdd:cd07136 399 GGVGNSGMGSYHGKYSFDTFSHKK 422
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
38-458 |
1.96e-41 |
|
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: 155.05 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 38 VGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTM-EQGKPLAEAtgEIVYGASFVE 116
Cdd:cd07123 60 LATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMlGQGKNVWQA--EIDAACELID 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 117 WF---AEEARRLYGDIVPGHQKDKRILVMKQPI-GVVAAITPWNFpnamiTRKAG-----PAFAaGCAMVLKPASQTPFS 187
Cdd:cd07123 138 FLrfnVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNF-----TAIGGnlagaPALM-GNVVLWKPSDTAVLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 188 AIAIAILAERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAP------TIKKLGLELGGNAPF 261
Cdd:cd07123 212 NYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnldryrTYPRIVGETGGKNFH 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 262 IVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEE 341
Cdd:cd07123 292 LVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 342 HVsDAVKK--GGRVVQGGKRHALGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDE--NDVIAQANDT-EFGLASY 416
Cdd:cd07123 372 YI-DHAKSdpEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDTTsPYALTGA 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1801119160 417 FYAKDLSRVFRVAEALEY--GMVGVN---TGLIsTAEAPFGGVKLSG 458
Cdd:cd07123 451 IFAQDRKAIREATDALRNaaGNFYINdkpTGAV-VGQQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
75-472 |
9.49e-36 |
|
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: 137.74 E-value: 9.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 75 LRKWFELMIENKDDLGRILTMEQGKPLAEAT--------GEIVYGASFV-EWFAEE--ARRLygdivpGHQKDkRILVMK 143
Cdd:cd07132 26 LEALLRMLEENEDEIVEALAKDLRKPKFEAVlseillvkNEIKYAISNLpEWMKPEpvKKNL------ATLLD-DVYIYK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 144 QPIGVVAAITPWNFP-NAMITRKAGpAFAAGCAMVLKPASQTPFSAIAIAILaeragLPAGL----FSVITGSAREIgAE 218
Cdd:cd07132 99 EPLGVVLIIGAWNYPlQLTLVPLVG-AIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLGGVEET-TE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 219 MTANpiiR--KLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRLYV 296
Cdd:cd07132 172 LLKQ---RfdYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 297 QDAVYDAFSAKLAAAVGKLkTGNGFEEGVVLGPLIDNAALEKVEEHVSdavkkGGRVVQGGkRHALGGTFYEATVIADVT 376
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKVAIGG-QTDEKERYIAPTVLTDVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 377 PDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGL--ISTAEAPFGGV 454
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImhYTLDSLPFGGV 401
|
410
....*....|....*...
gi 1801119160 455 KLSGLGREGSRYGIEEFT 472
Cdd:cd07132 402 GNSGMGAYHGKYSFDTFS 419
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
66-477 |
1.02e-29 |
|
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: 120.59 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 66 RTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEA----TGEIVYGA-----SFVEWFAEEARRLYGDIVPGHQKd 136
Cdd:cd07137 18 RSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfrdeVSVLVSSCklaikELKKWMAPEKVKTPLTTFPAKAE- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 137 krilVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAErAGLPAGLFSVITGSAREIG 216
Cdd:cd07137 97 ----IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIP-EYLDTKAIKVIEGGVPETT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 217 AEMTANpiIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKF-RNNGQTCVCANRLY 295
Cdd:cd07137 172 ALLEQK--WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 296 VQdavyDAFSAKLAAAVGK-LKT--GNGFEEGVVLGPLIDNAALEKVEEHVSDAvKKGGRVVQGGKRHAlGGTFYEATVI 372
Cdd:cd07137 250 VE----ESFAPTLIDALKNtLEKffGENPKESKDLSRIVNSHHFQRLSRLLDDP-SVADKIVHGGERDE-KNLYIEPTIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 373 ADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTA--EAP 450
Cdd:cd07137 324 LDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidTLP 403
|
410 420
....*....|....*....|....*..
gi 1801119160 451 FGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:cd07137 404 FGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
15-421 |
1.39e-26 |
|
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: 112.36 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIEADGSGIAVKNPATGELVGYVpklgakeTKEAID-AAAEA---QKGWAAR---TAKERSGILRKWFELMIENKD 87
Cdd:cd07128 5 VAGQWHAGTGDGRTLHDAVTGEVVARV-------SSEGLDfAAAVAyarEKGGPALralTFHERAAMLKALAKYLMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 88 DLGRILTmEQGKPLAEATGEIVYGASFVEWFAEEARRLY--------GDIVP----GHQKDKRILVMKQpiGVVAAITPW 155
Cdd:cd07128 78 DLYALSA-ATGATRRDSWIDIDGGIGTLFAYASLGRRELpnahflveGDVEPlskdGTFVGQHILTPRR--GVAVHINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 156 NFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIA-IAILAERAGLPAGLFSVITGSAREIGAEMTANPIIrklTFTGST 234
Cdd:cd07128 155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAvVKDIVESGLLPEGALQLICGSVGDLLDHLGEQDVV---AFTGSA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 235 EIGAELykQCAPTIkklgleLGGNAPFIVfdDAD-LDAAVEG----------ALIAK--FRN----NGQTCVCANRLYVQ 297
Cdd:cd07128 232 ATAAKL--RAHPNI------VARSIRFNA--EADsLNAAILGpdatpgtpefDLFVKevAREmtvkAGQKCTAIRRAFVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 298 DAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVsDAVKKGGRVVQGGK-------RHALGGTFYEAT 370
Cdd:cd07128 302 EARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPdrfevvgADAEKGAFFPPT 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 371 VIADVTPDMAVAKEET--FGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKD 421
Cdd:cd07128 381 LLLCDDPDAATAVHDVeaFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
15-432 |
3.94e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 111.33 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 15 VGTRWIEADGSGIAVKNPATGELVgyvpklgAKETKEAIDAA-----AEAQKGWAAR--TAKERSGILRKWFELMIENKD 87
Cdd:PRK11903 9 VAGRWQAGSGAGTPLFDPVTGEEL-------VRVSATGLDLAaafafAREQGGAALRalTYAQRAALLAAIVKVLQANRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 88 DLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLyGD---IVPGHQ----KDKRILVMKQPI---GVVAAITPWNF 157
Cdd:PRK11903 82 AYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL-GDarlLRDGEAvqlgKDPAFQGQHVLVptrGVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 158 PNAMITRKAGPAFAAGCAMVLKPASQTPFSAI-AIAILAERAGLPAGLFSVITGSAREIGAEMTANPIirkLTFTGSTEI 236
Cdd:PRK11903 161 PAWGLWEKAAPALLAGVPVIVKPATATAWLTQrMVKDVVAAGILPAGALSVVCGSSAGLLDHLQPFDV---VSFTGSAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 237 GAELykQCAPTIKKLGLELGGNA----PFIVFDDADLDAAVEGALIAKF-----RNNGQTCVCANRLYVQDAVYDAFSAK 307
Cdd:PRK11903 238 AAVL--RSHPAVVQRSVRVNVEAdslnSALLGPDAAPGSEAFDLFVKEVvremtVKSGQKCTAIRRIFVPEALYDAVAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 308 LAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVsDAVKKGGRVVQGGKRHAL------GGTFYEATVIADVTPDMA- 380
Cdd:PRK11903 316 LAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTLLGASDPDAAt 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1801119160 381 -VAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEAL 432
Cdd:PRK11903 395 aVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-477 |
3.72e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 108.21 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 141 VMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAgLPAGLFSVITGSAREIGAEMT 220
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 221 ANpiIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFR-NNGQTCVCANRLYVQD- 298
Cdd:PLN02174 187 QK--WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKe 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 299 ---AVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHAlggtfyeATVIADV 375
Cdd:PLN02174 265 yapKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIA-------PTILLDV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 376 TPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTA--EAPFGG 453
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGG 417
|
330 340
....*....|....*....|....
gi 1801119160 454 VKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PLN02174 418 VGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
66-477 |
1.24e-24 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 106.35 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 66 RTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEA--------TGEIVYGASFV-EWFAEEARRLYGDIVPGhqkd 136
Cdd:PLN02203 25 RSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdevgvlTKSANLALSNLkKWMAPKKAKLPLVAFPA---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 137 kRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAiaiAILAERAG--LPAGLFSVITGSArE 214
Cdd:PLN02203 101 -TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS---AFLAANIPkyLDSKAVKVIEGGP-A 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 215 IGAEMTANPiIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIV--FDDA-DLDAAVEGALIAKFRN-NGQTCVC 290
Cdd:PLN02203 176 VGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 291 ANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGvVLGPLIDNAALEKVEEHVSDAVKKGGrVVQGGKRHAlGGTFYEAT 370
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAAS-IVHGGSIDE-KKLFIEPT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 371 VIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNTGLISTA--E 448
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdS 411
|
410 420
....*....|....*....|....*....
gi 1801119160 449 APFGGVKLSGLGREGSRYGIEEFTEIKYV 477
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
52-450 |
1.06e-23 |
|
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: 103.09 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 52 AIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPlAEATGEIVYGASFVEWFAEEARRLYGDIVP 131
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYSYRIPHEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 132 GHQKDKRILVMKQ----PIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPF-SAIAIAILAERAGLPAGLFS 206
Cdd:cd07084 83 GNHLGQGLKQQSHgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIvMQIMVRLLHYAGLLPPEDVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 207 VITGSAReIGAEMTANPIIRKLTFTGSTEIGAELYKQcaPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAK-FRNNG 285
Cdd:cd07084 163 LINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALD--AKQARIYLELAGFNWKVLGPDAQAVDYVAWQCVQDmTACSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 286 QTCVCANRLYVQD-----AVYDAFSAKLAAAVgklktgngfEEGVVLGPLIDN---AALEKVEEHVSDAVKKGGRVVQGG 357
Cdd:cd07084 240 QKCTAQSMLFVPEnwsktPLVEKLKALLARRK---------LEDLLLGPVQTFttlAMIAHMENLLGSVLLFSGKELKNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 358 KRHALGGTFYEATVIADVTPDMAVAK---EETFGPVAPL--FRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEAL 432
Cdd:cd07084 311 SIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVveYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNL 390
|
410
....*....|....*...
gi 1801119160 433 EYGMVGVNTGLISTAEAP 450
Cdd:cd07084 391 WVAGRTYAILRGRTGVAP 408
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
51-407 |
5.07e-23 |
|
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: 101.46 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 51 EAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRlyG--- 127
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRE--Gswl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 128 ---------DIVPGHQKDKRIlvMKQPIGVVAAITPWNFPNAMITrkAG----PAFAAGCAMVLK--PA----SQTPFSA 188
Cdd:cd07129 81 daridpadpDRQPLPRPDLRR--MLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKahPAhpgtSELVARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 189 IAIAIlaERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCA--PTIKKLGLELGGNAPFIVFDD 266
Cdd:cd07129 157 IRAAL--RATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAarPEPIPFYAELGSVNPVFILPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 267 AdldAAVEGALIAK------FRNNGQTCVCANRLYVQD-AVYDAFSAKLAAAVGKlktgngFEEGVVLGPLIDNAALEKV 339
Cdd:cd07129 235 A---LAERGEAIAQgfvgslTLGAGQFCTNPGLVLVPAgPAGDAFIAALAEALAA------APAQTMLTPGIAEAYRQGV 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801119160 340 EEHVSDAvkkGGRVVQGGkrHALGGTFYEATVIADVTPDMAVAK----EETFGPVAPLFRFTDENDVIAQAN 407
Cdd:cd07129 306 EALAAAP---GVRVLAGG--AAAEGGNQAAPTLFKVDAAAFLADpalqEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
51-406 |
2.90e-14 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 74.61 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 51 EAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAE-------ATGEIVYGASFVEwfaEEAR 123
Cdd:cd07081 3 DAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDE---KTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 124 RLYGDIVPGhqkdkrILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP------ASQTPFSAIAIAILAer 197
Cdd:cd07081 80 VLTGDENGG------TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprakkVTQRAATLLLQAAVA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 198 AGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIKkLGlelGGNAPFIVFDDADLDAAVEGAL 277
Cdd:cd07081 152 AGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIG-VG---AGNTPVVIDETADIKRAVQSIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 278 IAKFRNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFE--EGVVLGPLIDNAAL-----EKVEEHVSDAVKKG 350
Cdd:cd07081 228 KSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQqvQPVILKNGDVNRDIvgqdaYKIAAAAGLKVPQE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1801119160 351 GRVVqggkrhalggtFYEATVIADVTPdmavAKEETFGPVAPLFRFTDENDVIAQA 406
Cdd:cd07081 308 TRIL-----------IGEVTSLAEHEP----FAHEKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
14-390 |
2.76e-10 |
|
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: 62.51 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 14 LVGTRWIEADGSgIAVKNPATGELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAK--ER----SGILRKWFELMI--EN 85
Cdd:cd07126 2 LVAGKWKGASNY-TTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERyllyGDVSHRVAHELRkpEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 86 KDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRLY--GDIVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMIT 163
Cdd:cd07126 81 EDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 164 RKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLFSVITGSAREIGAEMT-ANPiiRKLTFTGSTEIgAElyk 242
Cdd:cd07126 161 LQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP--RMTLFTGSSKV-AE--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 243 qcaptikKLGLELGGNapfIVFDDADLDAAVEGALIAKFRN------------NGQTCVCANRLYVQDAVYDA-FSAKLA 309
Cdd:cd07126 235 -------RLALELHGK---VKLEDAGFDWKILGPDVSDVDYvawqcdqdayacSGQKCSAQSILFAHENWVQAgILDKLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 310 AAVGKLKTgngfeEGVVLGPLIdNAALEKVEEHVSDAVK-KGGRVVQGGK---RHALGGTF--YEATVIadVTPDMAVAK 383
Cdd:cd07126 305 ALAEQRKL-----EDLTIGPVL-TWTTERILDHVDKLLAiPGAKVLFGGKpltNHSIPSIYgaYEPTAV--FVPLEEIAI 376
|
....*..
gi 1801119160 384 EETFGPV 390
Cdd:cd07126 377 EENFELV 383
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
51-433 |
3.15e-10 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 62.23 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 51 EAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAE-------ATGEIVYGasfVEWFAEEAr 123
Cdd:PRK15398 40 DAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEdkiaknvAAAEKTPG---VEDLTTEA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 124 rLYGDivpghqkDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP---ASQTpfSAIAIAIL---AER 197
Cdd:PRK15398 116 -LTGD-------NGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKV--SLRAIELLneaIVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 198 AGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKqcapTIKKLGLELGGNAPFIVFDDADLDAA----V 273
Cdd:PRK15398 186 AGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK----SGKKAIGAGAGNPPVVVDETADIEKAardiV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 274 EGaliAKFRNNgQTCVCANRLYVQDAVYDAFSAKLAAavgklktgngfeEGVVlgpLIDNAALEKVEEHVsdaVKKGGRV 353
Cdd:PRK15398 262 KG---ASFDNN-LPCIAEKEVIVVDSVADELMRLMEK------------NGAV---LLTAEQAEKLQKVV---LKNGGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 354 VQG--GKR-----HALGGTFYEAT--VIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGL--ASYFYAKDL 422
Cdd:PRK15398 320 NKKwvGKDaakilEAAGINVPKDTrlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNV 399
|
410
....*....|.
gi 1801119160 423 SRVFRVAEALE 433
Cdd:PRK15398 400 DNLNKMARAIQ 410
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
51-308 |
2.86e-09 |
|
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: 58.79 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 51 EAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAE-------ATGEIVYGasfVEWFAEEAR 123
Cdd:cd07121 8 DAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEdkiaknhLAAEKTPG---TEDLTTTAW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 124 RlyGDivpghqkDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP---ASQTpfSAIAIAILAE---R 197
Cdd:cd07121 85 S--GD-------NGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKV--SAYAVELINKaiaE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 198 AGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGsteiGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGAL 277
Cdd:cd07121 154 AGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIV 229
|
250 260 270
....*....|....*....|....*....|..
gi 1801119160 278 I-AKFRNNgQTCVCANRLYVQDAVYDAFSAKL 308
Cdd:cd07121 230 QgASFDNN-LPCIAEKEVIAVDSVADYLIAAM 260
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
135-310 |
2.95e-09 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 59.04 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 135 KDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKP---ASQTpfSAIAIAIL---AERAGLPAGLFSVI 208
Cdd:cd07122 85 EEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKC--SIEAAKIMreaAVAAGAPEGLIQWI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 209 TGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQCAPTIkklglelG---GNAPFIVFDDADLDAAVEGALIAKFRNNG 285
Cdd:cd07122 163 EEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAI-------GvgpGNVPAYIDETADIKRAVKDIILSKTFDNG 235
|
170 180
....*....|....*....|....*
gi 1801119160 286 QTCVCANRLYVQDAVYDAFSAKLAA 310
Cdd:cd07122 236 TICASEQSVIVDDEIYDEVRAELKR 260
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
46-467 |
8.43e-09 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 58.13 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 46 AKETKEAIDAAAEAQKGWAARTAKERSGILRKWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFVEWFAEEARRL 125
Cdd:COG0506 525 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAAR 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 126 YGDIVPGHqkdKRILVMKQPIGVVAAITPWNFPNAMITRKAGPAFAAGCAMVLKPASQTPFSAIAIAILAERAGLPAGLF 205
Cdd:COG0506 605 AAAPPPPP---PGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAG 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 206 SVITGSAREIGAEM----TANPIIRKLTFTGSTEIGAELYKQCAPTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKF 281
Cdd:COG0506 682 GGVLVLGAGGGAGGaaalTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAA 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 282 RNNGQTCVCANRLYVQDAVYDAFSAKLAAAVGKLKTGNGFEEGVVLGPLIDNAALEKVEEHVSDAVKKGGRVVQGGKRHA 361
Cdd:COG0506 762 ASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGP 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 362 LGGTFYEATVIADVTPDMAVAKEETFGPVAPLFRFTDENDVIAQANDTEFGLASYFYAKDLSRVFRVAEALEYGMVGVNT 441
Cdd:COG0506 842 LVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGG 921
|
410 420
....*....|....*....|....*.
gi 1801119160 442 GLISTAEAPFGGVKLSGLGREGSRYG 467
Cdd:COG0506 922 GGGGGGGGGGGGGGGGGGGGGGGGGG 947
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
36-303 |
9.04e-09 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 57.23 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 36 ELVGYVPKLGAKETKEAIDAAAEAQKGWAARTAKERSGILRK----WFELMIENKDDLGRILTMEQGKPLAEAtgeivyg 111
Cdd:cd07077 9 TLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSlianWIAMMGCSESKLYKNIDTERGITASVG------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 112 asfvewfaEEARRLYGDivpghqkDKRILVMKQPIGVVAAITPWNFPNAMITrKAGPAFAAGCAMVLKPASQTPFSAIAI 191
Cdd:cd07077 82 --------HIQDVLLPD-------NGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 192 AIL---AERAGLPAGLFSVITGSAREIGAEMTANPIIRKLTFTGSTEIGAELYKQcAPTIKKLGLElGGNAPFIVFDDAD 268
Cdd:cd07077 146 ALLfqaADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH-SPHIPVIGFG-AGNSPVVVDETAD 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1801119160 269 LDAAVEGALIAKFRNNgQTCVCANRLYVQDAVYDA 303
Cdd:cd07077 224 EERASGSVHDSKFFDQ-NACASEQNLYVVDDVLDP 257
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
136-391 |
6.08e-05 |
|
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: 45.55 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 136 DKRILVMKQPIGVV---AAITPWNFPNAMITrkagpAFAAGCAMVLKP--ASQTPFS---AIAIAILAErAGLPAGLFSV 207
Cdd:cd07127 186 EKTFTVVPRGVALVigcSTFPTWNGYPGLFA-----SLATGNPVIVKPhpAAILPLAitvQVAREVLAE-AGFDPNLVTL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 208 ITGSARE-IGAEMTANPIIRKLTFTGSTEIGAELYKQCapTIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQ 286
Cdd:cd07127 260 AADTPEEpIAQTLATRPEVRIIDFTGSNAFGDWLEANA--RQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801119160 287 TCVCANRLYV-QDAV--------YDAFSAKLAAAVGKLkTGNGFEEGVVLGPLIDNAALEKVEEhvsdaVKKGGRVVQGG 357
Cdd:cd07127 338 MCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAE-----ARQLGEVLLAS 411
|
250 260 270
....*....|....*....|....*....|....*....
gi 1801119160 358 KRHAlGGTFYEATV-----IADVTPDMAVAKEETFGPVA 391
Cdd:cd07127 412 EAVA-HPEFPDARVrtpllLKLDASDEAAYAEERFGPIA 449
|
|
| |
