|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
6-457 |
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: 724.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTT 165
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 166 IKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDAD 245
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 246 IEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQE 325
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 326 KGGQLSRSIEDIqALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLK 405
Cdd:cd07103 321 KGAKVLTGGKRL-GLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1564882272 406 LFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07103 400 VAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
4-458 |
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: 591.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:COG1012 23 FDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:COG1012 103 EVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:COG1012 183 SALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:COG1012 263 ADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLSRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTG 403
Cdd:COG1012 343 VAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARA 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 404 LKLFNELEYGVIGWNDGGPSA-AHAPFGGLKESGYGREGGVEGIEPYLETKYLSIQ 458
Cdd:COG1012 423 RRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-457 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 591.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PLN02278 42 FPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:PLN02278 282 ADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQL----SRsiediQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:PLN02278 362 VSKGAKVllggKR-----HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRD 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:PLN02278 437 LQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
6-453 |
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: 590.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTT 165
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 166 IKLVELAHQAGFPKDAISYIIAS-GKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQLSRSIEdIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGL 404
Cdd:TIGR01780 321 EKGAKVVTGGK-RHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1564882272 405 KLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:TIGR01780 400 RVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
3-453 |
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: 561.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:pfam00171 8 TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 GEVAYANSYVKWYAEEAKRVYGRTIPaNSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARRLDGETLP-SDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:pfam00171 167 LTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:pfam00171 247 DADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVED 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQL---SRSIEDiqalGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:pfam00171 327 AKEEGAKLltgGEAGLD----NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAA-HAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
30-453 |
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: 517.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 30 IKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRVYGRTIPA 109
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 110 NSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASG 189
Cdd:cd07078 84 PDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 190 KDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICAN 269
Cdd:cd07078 164 DEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 270 RIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEKGGQLSRSIEDIQALGGNFLKPVV 349
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 350 ITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSA-AHAP 428
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAePSAP 403
|
410 420
....*....|....*....|....*
gi 1564882272 429 FGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07078 404 FGGVKQSGIGREGGPYGLEEYTEPK 428
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
4-457 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 515.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PRK11241 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:PRK11241 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:PRK11241 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLSRSIEdIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTG 403
Cdd:PRK11241 348 LEKGARVVCGGK-AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRV 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 404 LKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:PRK11241 427 FRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
4-453 |
1.73e-154 |
|
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: 446.71 E-value: 1.73e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07088 15 IDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07088 95 EVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLSRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTG 403
Cdd:cd07088 335 VEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1564882272 404 LKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07088 415 MRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
6-453 |
9.68e-153 |
|
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: 441.60 E-value: 9.68e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQL---SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDY 400
Cdd:cd07114 321 REEGARVltgGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 401 RTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
4-457 |
8.31e-145 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 421.37 E-value: 8.31e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIP----ANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPvdayEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLI 239
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLSRSIEDIQalgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE---GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHA-PFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07145 398 INRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
2-453 |
1.20e-144 |
|
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: 421.62 E-value: 1.20e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 2 TKLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLA 79
Cdd:cd07091 19 KTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 80 E-AKGEVAYANSYVKWYAEEAKRVYGRTIPanSPSKKIVIDKF-PVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKP 157
Cdd:cd07091 99 EsAKGDVALSIKCLRYYAGWADKIQGKTIP--IDGNFLAYTRRePIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 158 AVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQ-VKNVTMELGGLA 236
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLKKVTLELGGKS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 237 PLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:cd07091 257 PNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQLsrsiediqALGGN-------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEF 389
Cdd:cd07091 337 LSYIESGKKEGATL--------LTGGErhgskgyFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEY 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 390 GLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07091 409 GLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
4-453 |
1.34e-144 |
|
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: 420.85 E-value: 1.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIP----ANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPfdasPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAqqVKNVTMELGGLAPLI 239
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLsrsiediqALG----GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:cd07149 319 VEEAVEGGARL--------LTGgkrdGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNDgGPS--AAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMIND-SSTfrVDHMPYGGVKESGTGREGPRYAIEEMTEIK 449
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
33-457 |
1.47e-141 |
|
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: 409.70 E-value: 1.47e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 33 AHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRVYGRTIPANSP 112
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 113 SKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDA 192
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 193 GDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIY 272
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 273 VHEDIAEaynekliekvhalsvgdglkeevkigplidnQAVEKVLThikdaqekggqlsrsiediqalggnflkpvVITN 352
Cdd:cd06534 243 VHESIYD-------------------------------EFVEKLVT------------------------------VLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 353 ANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSA-AHAPFGG 431
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 1564882272 432 LKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
4-457 |
4.29e-139 |
|
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: 406.82 E-value: 4.29e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIP----ANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPldatQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAqqVKNVTMELGGLAPLI 239
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLsrsiediqaLGGN-----FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASY 394
Cdd:cd07094 319 VEEAVEAGARL---------LCGGerdgaLFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 395 FFTNDYRTGLKLFNELEYGVIGWNDGGP-SAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSAfRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-457 |
1.99e-138 |
|
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: 404.99 E-value: 1.99e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYAnsyVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTT 165
Cdd:cd07106 81 GGA---VAWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 166 IKLVELAHQAgFPKDAISyIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDAD 245
Cdd:cd07106 158 LKLGELAQEV-LPPGVLN-VVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 246 IEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQE 325
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 326 KGGQLsrsiediqALGGN-------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTN 398
Cdd:cd07106 316 KGAKV--------LAGGEpldgpgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1564882272 399 DYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07106 388 DLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
5-457 |
2.19e-137 |
|
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: 403.62 E-value: 2.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:cd07119 16 DIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 GEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07119 96 IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTV-REPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07119 175 LTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07119 255 DADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQL---SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07119 335 GKEEGARLvcgGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07119 415 IARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
4-457 |
3.42e-136 |
|
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: 399.40 E-value: 3.42e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLsrsiediqALG----GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07150 321 VAKGAKL--------LTGgkydGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDggPS---AAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07150 393 LQRAFKLAERLESGMVHIND--PTildEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
5-453 |
2.05e-134 |
|
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: 395.46 E-value: 2.05e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07097 17 ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07097 97 EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:cd07097 177 SAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07097 257 ADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLSRSIEDIQ-ALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRT 402
Cdd:cd07097 337 RSEGAKLVYGGERLKrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKH 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 403 GLKLFNELEYGVIGWNDggPSAA---HAPFGGLKESGYG-REGGVEGIEPYLETK 453
Cdd:cd07097 417 ATHFKRRVEAGVVMVNL--PTAGvdyHVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
30-457 |
3.21e-134 |
|
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: 393.43 E-value: 3.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 30 IKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRVYGRTIPA 109
Cdd:cd07104 6 YAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 110 NSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTT-IKLVELAHQAGFPKDAISYIIAS 188
Cdd:cd07104 86 DVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVPGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 189 GKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICA 268
Cdd:cd07104 166 GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 269 NRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEKGGQLsrsiediQALG---GNFL 345
Cdd:cd07104 246 GRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL-------LTGGtyeGLFY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 346 KPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDggPSA- 424
Cdd:cd07104 319 QPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND--QTVn 396
|
410 420 430
....*....|....*....|....*....|....*
gi 1564882272 425 --AHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07104 397 dePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
6-457 |
4.14e-134 |
|
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: 394.24 E-value: 4.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK-GE 84
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVL-RQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQL---SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYR 401
Cdd:cd07093 320 AEGATIltgGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 402 TGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
4-453 |
5.98e-132 |
|
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: 389.40 E-value: 5.98e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:cd07131 16 FDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 GEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07131 96 GDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07131 176 ACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07131 256 DADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQLS---RSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07131 336 GKEEGATLLlggERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTED 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1564882272 400 YRTGLKLFNELEYGVIGWNdgGPS---AAHAPFGGLKESGYG-REGGVEGIEPYLETK 453
Cdd:cd07131 416 VNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
4-457 |
2.74e-131 |
|
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: 386.99 E-value: 2.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIP----ANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAgDIFTNHSLISKVTFTGSTAVGKSLIESSAQqvKNVTMELGGLAPLI 239
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQL----SRSiediqalgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:cd07147 318 VNEAVDAGAKLltggKRD--------GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNDgGPS--AAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVIND-VPTfrVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
3-453 |
1.41e-130 |
|
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: 385.42 E-value: 1.41e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAE 80
Cdd:cd07112 3 TFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 81 A-KGEVAYANSYVKWYAEEAKRVYGRTIPAnSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07112 83 AlAVDVPSAANTFRWYAEAIDKVYGEVAPT-GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTMELGGLAPL 238
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDA-DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVL 317
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 318 THIKDAQEKGGQL----SRsieDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLAS 393
Cdd:cd07112 322 GYIESGKAEGARLvaggKR---VLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 394 YFFTNDYRTGLKLFNELEYGVI---GWNDGGPSaahAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVwvnCFDEGDIT---TPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
6-455 |
4.33e-130 |
|
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: 384.01 E-value: 4.33e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYANSYVKWYAEEAKRV---YGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQLSRSIEDIQALG-GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYR 401
Cdd:cd07110 321 GKEEGARLLCGGRRPAHLEkGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 402 TGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYL 455
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
7-457 |
1.89e-129 |
|
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: 382.07 E-value: 1.89e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGE 84
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQLSRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGL 404
Cdd:cd07118 322 AEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 405 KLFNELEYG---VIGWNDGGPsaaHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07118 402 TVARRIRAGtvwVNTFLDGSP---ELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
6-453 |
4.42e-127 |
|
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: 376.01 E-value: 4.42e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG-E 84
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVRE-PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQLSRSIEDIQAlGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGL 404
Cdd:cd07115 320 EEGARLLTGGKRPGA-RGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1564882272 405 KLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVK 447
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
26-446 |
6.44e-127 |
|
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: 374.87 E-value: 6.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 26 INHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRvYGR 105
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEA-FLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 106 TIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISYI 185
Cdd:cd07100 80 DEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 186 IASGKDAGDIFtNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTC 265
Cdd:cd07100 160 LIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 266 ICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEKGGQLsrsiediqALG---- 341
Cdd:cd07100 239 IAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATL--------LLGgkrp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 342 ---GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWN 418
Cdd:cd07100 311 dgpGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420
....*....|....*....|....*...
gi 1564882272 419 DGGPSAAHAPFGGLKESGYGREGGVEGI 446
Cdd:cd07100 391 GMVKSDPRLPFGGVKRSGYGRELGRFGI 418
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
7-455 |
1.20e-126 |
|
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: 375.02 E-value: 1.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVA 86
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKWYAEEAKRVYG-RTIPANS--PSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07099 81 LALEAIDWAARNAPRVLApRKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKdagdifTNHSLIS----KVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLI 239
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGA------TGAALIDagvdKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLSRSIEDIQaLGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07099 315 VDDAVAKGAKALTGGARSN-GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAA--HAPFGGLKESGYGREGGVEGIEPYLETKYL 455
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
6-457 |
2.02e-126 |
|
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: 374.65 E-value: 2.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQ-NWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGE 84
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPANsPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLkEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQL--SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRT 402
Cdd:cd07109 319 ARGARIvaGGRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 403 GLKLFNELEYGVIGWNDGGPSAA-HAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-457 |
8.47e-126 |
|
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: 373.99 E-value: 8.47e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQ---NWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLA 79
Cdd:cd07141 23 TFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 80 EAK-GEVAYANSYVKWYAEEAKRVYGRTIPANSpskkiviDKF------PVGVVGAITPWNFPAAMITRKMAPALAAGCT 152
Cdd:cd07141 103 KSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDG-------DFFtytrhePVGVCGQIIPWNFPLLMAAWKLAPALACGNT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 153 IICKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTME 231
Cdd:cd07141 176 VVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 232 LGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQ 311
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 312 AVEKVLTHIKDAQEKGGQLsrsiediqALGGN-------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIA 384
Cdd:cd07141 336 QFKKILELIESGKKEGAKL--------ECGGKrhgdkgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 385 NDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07141 408 NNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
6-453 |
1.69e-123 |
|
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: 367.01 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYANSYVKWYAEEAKRVYGRTIPAnsPSKKIVIDK-FPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPL--PGGSFAYTRrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPkDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07090 159 ALLLAEILTEAGLP-DGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQL----SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDY 400
Cdd:cd07090 318 QEGAKVlcggERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 401 RTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLK 450
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
4-451 |
1.11e-122 |
|
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: 365.73 E-value: 1.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07086 95 EVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQA----GFPkDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLI 239
Cdd:cd07086 175 TAIAVTKILAEVleknGLP-PGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAII 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07086 254 VMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLSRSIEDIQ-ALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTN 398
Cdd:cd07086 334 IEIAKSQGGTVLTGGKRIDgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTE 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 399 DYRTGLKLF--NELEYGVIGWNdGGPSAA--HAPFGGLKESGYGREGGVEGIEPYLE 451
Cdd:cd07086 414 DLREAFRWLgpKGSDCGIVNVN-IPTSGAeiGGAFGGEKETGGGRESGSDAWKQYMR 469
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
3-453 |
1.78e-122 |
|
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: 365.58 E-value: 1.78e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWK-KVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPL-AE 80
Cdd:cd07144 24 TIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWsKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 81 AKGEVAYANSYVKWYAEEAKRVYGRTIPaNSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVK 160
Cdd:cd07144 104 ALGDLDEIIAVIRYYAGWADKIQGKTIP-TSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAEN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 161 TPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIV 240
Cdd:cd07144 183 TPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 241 HNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKV-HALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07144 263 FEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSY 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLSRSIE-DIQALG-GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFT 397
Cdd:cd07144 343 IEKGKKEGAKLVYGGEkAPEGLGkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFT 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 398 NDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07144 423 KDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
6-457 |
2.17e-122 |
|
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: 364.37 E-value: 2.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPL-AEAKGE 84
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPANsPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAgFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIAS-KFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEK-------GGQLSRSIEDIQalgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFF 396
Cdd:cd07108 319 LSTsgatvlrGGPLPGEGPLAD---GFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564882272 397 TNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEG-IEPYLETKYLSI 457
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
4-453 |
4.06e-122 |
|
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: 364.20 E-value: 4.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA 81
Cdd:cd07139 16 IDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 82 K-GEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVK 160
Cdd:cd07139 96 RrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 161 TPLTTIKLVELAHQAGFPKDAISyIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIV 240
Cdd:cd07139 176 TPLDAYLLAEAAEEAGLPPGVVN-VVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 241 HNDADIEAAVDGTIASKFRNAGQTCICANRIYV----HEDIAEAynekLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:cd07139 255 LDDADLDAAVPGLVPASLMNNGQVCVALTRILVprsrYDEVVEA----LAAAVAALKVGDPLDPATQIGPLASARQRERV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQLSRSIEDIQALG-GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:cd07139 331 EGYIAKGRAEGARLVTGGGRPAGLDrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSV 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNdGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07139 411 WTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
4-458 |
6.69e-122 |
|
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: 363.36 E-value: 6.69e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07138 16 IDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 -EVAYANSYVKWYAEEAKrvygrTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07138 96 aQVGLGIGHLRAAADALK-----DFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07138 171 LSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07138 251 DADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQLsrsiediqALG----------GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLA 392
Cdd:cd07138 331 GIEEGARL--------VAGgpgrpeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 393 SYFFTNDYRTGLKLFNELEYGVIGWNdGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKylSIQ 458
Cdd:cd07138 403 GYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK--SIQ 465
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
4-457 |
4.44e-121 |
|
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: 360.91 E-value: 4.44e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINhQIKQAHQAFQnwKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALR-EALALAASYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIP----ANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFScdltANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAqqVKNVTMELGGLAPLI 239
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLsrsiediqALG----GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:cd07146 316 VEEAIAQGARV--------LLGnqrqGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNDG-GPSAAHAPFGGLKESGYG-REGGVEGIEPYLETKYLSI 457
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNEVpGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
6-454 |
5.07e-119 |
|
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: 355.48 E-value: 5.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK-GE 84
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAhQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 -----EKGGqlsRSIEDiqalGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07092 320 aharvLTGG---RRAEG----PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKY 454
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
4-459 |
3.21e-117 |
|
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: 351.22 E-value: 3.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07151 92 EWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TT-IKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07151 172 TGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07151 252 DADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGG--QLSRSIEdiqalgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDY 400
Cdd:cd07151 332 AVEEGAtlLVGGEAE------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDL 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 401 RTGLKLFNELEYGVIGWNDGGPS-AAHAPFGGLKESGYGREGGVEGIEPYLETKYLSIQE 459
Cdd:cd07151 406 ERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-453 |
5.08e-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: 351.41 E-value: 5.08e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA 81
Cdd:cd07142 21 FPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 82 K-GEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVK 160
Cdd:cd07142 101 RyAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHE-PIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 161 TPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTMELGGLAPLI 239
Cdd:cd07142 180 TPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07142 260 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLSRSIEDIQAlGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07142 340 IEHGKEEGATLITGGDRIGS-KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKN 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07142 419 IDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
25-457 |
9.81e-117 |
|
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: 348.80 E-value: 9.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 25 QINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRVYG 104
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 105 RTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISY 184
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 185 IIASGKDAGDIFT---NHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNA 261
Cdd:cd07105 161 VTHSPEDAPEVVEaliAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 262 GQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDglkeeVKIGPLIDNQAVEKVLTHIKDAQEKGGQLSRSIEDIQALG 341
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 342 GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNdgG 421
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN--G 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 1564882272 422 PSA---AHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07105 394 MTVhdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
6-453 |
6.63e-116 |
|
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: 347.69 E-value: 6.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWK-KVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG- 83
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYG-RTIPANSPSKKI---VIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLI 239
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQLsrsiediqALGGN---------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFG 390
Cdd:cd07089 321 IARGRDEGARL--------VTGGGrpagldkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 391 LASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
7-455 |
2.02e-115 |
|
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: 346.25 E-value: 2.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKkVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGE 84
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGRTIPAnSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEP-EPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQA-GFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQ----LSRSIEDIQAlgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07120 320 IAAGAEvvlrGGPVTEGLAK--GAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYL 455
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
3-453 |
2.05e-115 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 346.90 E-value: 2.05e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:PRK13473 18 KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 G-EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKT 161
Cdd:PRK13473 98 NdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEIT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 162 PLTTIKLVELAHQAgFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVH 241
Cdd:PRK13473 178 PLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 242 NDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIK 321
Cdd:PRK13473 257 DDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 322 DAQEKGGqlSRSIEDIQALGGN--FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:PRK13473 337 RAKALGH--IRVVTGGEAPDGKgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:PRK13473 415 VGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
3-456 |
1.45e-113 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 343.25 E-value: 1.45e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPATNEVLERLDYATHEQINHQIKQAHQAF-----QNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKP 77
Cdd:PLN02467 24 RIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 78 LAEAKGEVAYANSYVKWYAEEAKRVYGR-TIPANSP--SKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTII 154
Cdd:PLN02467 104 LDEAAWDMDDVAGCFEYYADLAEALDAKqKAPVSLPmeTFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 155 CKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGG 234
Cdd:PLN02467 184 LKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 235 LAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVE 314
Cdd:PLN02467 264 KSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 315 KVLTHIKDAQEKGGQLSRSIEDIQALG-GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLAS 393
Cdd:PLN02467 344 KVLKFISTAKSEGATILCGGKRPEHLKkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 394 YFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLE----TKYLS 456
Cdd:PLN02467 424 AVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSvkqvTKYIS 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-447 |
2.89e-113 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 341.47 E-value: 2.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKK-VDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:cd07082 18 IEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 GEVAYANSYVKWYAEEAKRVYGRTIP---ANSPSKKI-VIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPA 158
Cdd:cd07082 98 KEVDRTIDYIRDTIEELKRLDGDSLPgdwFPGTKGKIaQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 159 VKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAqqVKNVTMELGGLAPL 238
Cdd:cd07082 178 TQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLT 318
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 319 HIKDAQEKGGQLsrsIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTN 398
Cdd:cd07082 336 LIDDAVAKGATV---LNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTK 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1564882272 399 DYRTGLKLFNELEYGVIGWNDG---GPSaaHAPFGGLKESGYGREGGVEGIE 447
Cdd:cd07082 413 DINKARKLADALEVGTVNINSKcqrGPD--HFPFLGRKDSGIGTQGIGDALR 462
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
4-458 |
2.16e-112 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 339.55 E-value: 2.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK- 82
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 GEVAYANSYVKWYAEEAKRVYGRTIPANSPSkkividkF------PVGVVGAITPWNFPAAMITRKMAPALAAGCTIICK 156
Cdd:PRK13252 104 VDIVTGADVLEYYAGLAPALEGEQIPLRGGS-------FvytrrePLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 157 PAVKTPLTTIKLVELAHQAGFPKDAISYIIASGkDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLA 236
Cdd:PRK13252 177 PSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 237 PLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQL---SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLAS 393
Cdd:PRK13252 336 LGYIEKGKAEGARLlcgGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 394 YFFTNDYRTGLKLFNELEYGvIGW-NDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKylSIQ 458
Cdd:PRK13252 416 GVFTADLSRAHRVIHQLEAG-ICWiNTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK--SVQ 478
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-457 |
2.25e-110 |
|
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: 334.41 E-value: 2.25e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 2 TKLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN-WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAE 80
Cdd:cd07113 15 KRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 81 AKG-EVAYANSYVKWYAEEAKRVYGRTIPANSPSKK-----IVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTII 154
Cdd:cd07113 95 SRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQgerytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 155 CKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASGkDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGG 234
Cdd:cd07113 175 IKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 235 LAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVE 314
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 315 KVLTHIKDAQEKGGQLSRSIEDIqALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASY 394
Cdd:cd07113 334 KVCSYLDDARAEGDEIVRGGEAL-AGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTAS 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 395 FFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07113 413 VWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-457 |
1.32e-109 |
|
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: 332.57 E-value: 1.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 2 TKLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN-W-KKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKP-L 78
Cdd:cd07143 22 GTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTfG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 79 AEAKGEVAYANSYVKWYAEEAKRVYGRTIPANsPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPA 158
Cdd:cd07143 102 TAKRVDVQASADTFRYYGGWADKIHGQVIETD-IKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 159 VKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTMELGGLAP 237
Cdd:cd07143 181 ELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 238 LIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVL 317
Cdd:cd07143 261 NIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 318 THIKDAQEKGGQLsrsiediqALGGN-------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFG 390
Cdd:cd07143 341 SYIESGKAEGATV--------ETGGKrhgnegyFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYG 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 391 LASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07143 413 LAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
3-442 |
1.34e-106 |
|
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: 325.72 E-value: 1.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA 81
Cdd:cd07124 47 KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 82 KGEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKT 161
Cdd:cd07124 127 DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 162 PLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ------QVKNVTMELGGL 235
Cdd:cd07124 206 PVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 236 APLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEK 315
Cdd:cd07124 286 NAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 316 VLTHIKDAQEKGGQLSRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:cd07124 366 IRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNDGGPSA---AHaPFGGLKESGYGREGG 442
Cdd:cd07124 446 FSRSPEHLERARREFEVGNLYANRKITGAlvgRQ-PFGGFKMSGTGSKAG 494
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
4-457 |
1.42e-106 |
|
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: 324.68 E-value: 1.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07559 18 FDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 -EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07559 98 aDIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHE-PLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAgFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07559 177 LSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DA-----DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVL 317
Cdd:cd07559 256 DAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKIL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 318 THIKDAQEKGGQL----SRSIEDiQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLAS 393
Cdd:cd07559 336 SYVDIGKEEGAEVltggERLTLG-GLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGG 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 394 YFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07559 415 GVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
4-458 |
1.65e-106 |
|
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: 324.45 E-value: 1.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA 81
Cdd:cd07140 23 YNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 82 -KGEVAYANSYVKWYAEEAKRVYGRTIPANS--PSKKIVIDKF-PVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKP 157
Cdd:cd07140 103 lKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarPNRNLTLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 158 AVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSA-QQVKNVTMELGGLA 236
Cdd:cd07140 183 AQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKKVSLELGGKS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 237 PLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:cd07140 263 PLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQL---SRSIEdiqaLGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTY--SDLDEVINIANDTEFGL 391
Cdd:cd07140 343 VEYCERGVKEGATLvygGKQVD----RPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFddGDVDGVLQRANDTEYGL 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 392 ASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSIQ 458
Cdd:cd07140 419 ASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
7-453 |
5.98e-106 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 324.84 E-value: 5.98e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAE-AKG 83
Cdd:PLN02466 78 LDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQsAKA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:PLN02466 158 ELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHE-PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTMELGGLAPLIVHN 242
Cdd:PLN02466 237 SALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKliEKVHALS--VGDGLKEEVKIGPLIDNQAVEKVLTHI 320
Cdd:PLN02466 317 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrvVGDPFKKGVEQGPQIDSEQFEKILRYI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 321 KDAQEKGGQLSRSIEDIQAlGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDY 400
Cdd:PLN02466 395 KSGVESGATLECGGDRFGS-KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNL 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 401 RTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:PLN02466 474 DTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
5-453 |
3.38e-105 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 321.77 E-value: 3.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:PLN02766 39 ETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 G-EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKT 161
Cdd:PLN02766 119 AvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTL-KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 162 PLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTMELGGLAPLIV 240
Cdd:PLN02766 198 PLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 241 HNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHI 320
Cdd:PLN02766 278 FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 321 KDAQEKGGQLsrsIEDIQALG--GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTN 398
Cdd:PLN02766 358 EHGKREGATL---LTGGKPCGdkGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTK 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 399 DYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:PLN02766 435 DLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
56-458 |
4.42e-105 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 318.22 E-value: 4.42e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 56 AQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFP 135
Cdd:PRK10090 5 AAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 136 AAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGK 215
Cdd:PRK10090 85 FFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 216 SLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVG 295
Cdd:PRK10090 165 KIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 296 DGLKEE-VKIGPLIDNQAVEKVLTHIKDAQEKGGQLsrsiediqALGGN-------FLKPVVITNANLDMKAMHEETFGP 367
Cdd:PRK10090 245 NPAERNdIAMGPLINAAALERVEQKVARAVEEGARV--------ALGGKavegkgyYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 368 VAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIE 447
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
410
....*....|.
gi 1564882272 448 PYLETKYLSIQ 458
Cdd:PRK10090 397 EYLQTQVVYLQ 407
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
4-457 |
9.16e-105 |
|
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: 319.79 E-value: 9.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07117 18 IDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 -EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07117 98 vDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVL-REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAgFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07117 177 LSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07117 256 DANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQL----SRSIEDiQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTN 398
Cdd:cd07117 336 AKEEGAKIltggHRLTEN-GLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTK 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1564882272 399 DYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:cd07117 415 DINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
6-458 |
2.47e-101 |
|
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: 310.46 E-value: 2.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYANSYVKWYAEEAKRVYGRTIPAnSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTT 165
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPV-GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 166 IKLVELAHQAgFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDAD 245
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 246 IEAAVDGTIAS-KFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQL---SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYR 401
Cdd:cd07107 319 REGARLvtgGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 402 TGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLSIQ 458
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-456 |
3.22e-101 |
|
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: 310.87 E-value: 3.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK-G 83
Cdd:cd07111 40 PTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKrvygrTIPANSPSKKividkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07111 120 DIPLVARHFYHHAGWAQ-----LLDTELAGWK------PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKdAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:cd07111 189 TALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:cd07111 268 ADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLSRSIEDIQAlGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTG 403
Cdd:cd07111 348 RAEGADVFQPGADLPS-KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLA 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 404 LKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYLS 456
Cdd:cd07111 427 LEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEP 479
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
7-452 |
3.51e-101 |
|
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: 310.01 E-value: 3.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVA 86
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKWYAEEAKRVYG--RTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07101 81 DVAIVARYYARRAERLLKprRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSliSKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDA 244
Cdd:cd07101 161 ALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNA--DYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 245 DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQL---SRSIEDiqaLGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYR 401
Cdd:cd07101 319 AKGATVlagGRARPD---LGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 402 TGLKLFNELEYGVIGWNDGGPSA---AHAPFGGLKESGYGREGGVEGIEPYLET 452
Cdd:cd07101 396 RGRRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGRRHGAEGLLKYTET 449
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
13-457 |
4.66e-101 |
|
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: 309.22 E-value: 4.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 13 EVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYV 92
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 93 KWYAEEAKRVYGRTIPaNSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTT-IKLVEL 171
Cdd:cd07152 82 HEAAGLPTQPQGEILP-SAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 172 AHQAGFPKdAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVD 251
Cdd:cd07152 161 FEEAGLPA-GVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 252 GTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEKGGQLs 331
Cdd:cd07152 240 NGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 332 rsiediqALGGN----FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLF 407
Cdd:cd07152 319 -------EAGGTydglFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1564882272 408 NELEYGVIGWNDGGPS-AAHAPFGGLKESGYG-REGGVEGIEPYLETKYLSI 457
Cdd:cd07152 392 DRLRTGMLHINDQTVNdEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-453 |
6.26e-100 |
|
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: 307.52 E-value: 6.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07085 18 LDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAaMITRKMAP-ALAAGCTIICKPAVKTP 162
Cdd:cd07085 98 DVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPA-MIPLWMFPmAIACGNTFVLKPSERVP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISyIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:cd07085 177 GAAMRLAELLQEAGLPDGVLN-VVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:cd07085 256 DADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIES 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQL---SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:cd07085 336 GVEEGAKLvldGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRS 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 400 YRTGLKLFNELEYGVIGWNDGGP-SAAHAPFGGLKESGYGREG--GVEGIEPYLETK 453
Cdd:cd07085 416 GAAARKFQREVDAGMVGINVPIPvPLAFFSFGGWKGSFFGDLHfyGKDGVRFYTQTK 472
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
4-458 |
1.32e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 307.96 E-value: 1.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEA------KRVYGrTIPANSpskKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKP 157
Cdd:PRK09407 114 EVLDVALTARYYARRApkllapRRRAG-ALPVLT---KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 158 AVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSliSKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAP 237
Cdd:PRK09407 190 DSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNA--DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 238 LIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVL 317
Cdd:PRK09407 268 MIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 318 THIKDAQEKGGQL---SRSIEDiqaLGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASY 394
Cdd:PRK09407 348 AHVDDAVAKGATVlagGKARPD---LGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNAS 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 395 FFTNDYRTGLKLFNELEYGVIGWNDG-GPSAAH--APFGGLKESGYGREGGVEGIEPYLETKYLSIQ 458
Cdd:PRK09407 425 VWTGDTARGRAIAARIRAGTVNVNEGyAAAWGSvdAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
7-453 |
7.25e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 303.97 E-value: 7.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVA 86
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKWYAEEAKRVYGRTiPANSPS---KKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIAsGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHND 243
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLV-GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 244 ADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDA 323
Cdd:PRK09406 244 ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 324 QEKGGQLSRSIEDIQAlGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTG 403
Cdd:PRK09406 324 VAAGATILCGGKRPDG-PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQ 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1564882272 404 LKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:PRK09406 403 ERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-447 |
9.23e-98 |
|
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: 301.09 E-value: 9.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVA 86
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTI 166
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 167 KLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSlISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADI 246
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPR-IDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 247 EAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEK 326
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 327 GGQLS--RSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGL 404
Cdd:cd07102 320 GARALidGALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1564882272 405 KLFNELEYGVIGWNDGG-PSAAhAPFGGLKESGYGREGGVEGIE 447
Cdd:cd07102 400 ALGEQLETGTVFMNRCDyLDPA-LAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
8-446 |
5.08e-92 |
|
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: 286.50 E-value: 5.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 8 NPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK-GEVA 86
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKW---YAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:cd07098 82 VTCEKIRWtlkHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQA----GFPKDAISYIIASGkDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLI 239
Cdd:cd07098 162 SSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTH 319
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 320 IKDAQEKGGQL----SRSIEDIQAlGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:cd07098 321 VADAVEKGARLlaggKRYPHPEYP-QGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNDGGPS--AAHAPFGGLKESGYGREGGVEGI 446
Cdd:cd07098 400 FGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
7-440 |
6.26e-88 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 275.97 E-value: 6.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVA 86
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKWYAEEAKRVYgRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTI 166
Cdd:PRK13968 92 KSANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 167 KLVELAHQAGFPKDAISYIIASgKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADI 246
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNAD-NDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 247 EAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEK 326
Cdd:PRK13968 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 327 GGQLSRSIEDIqALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKL 406
Cdd:PRK13968 330 GARLLLGGEKI-AGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQM 408
|
410 420 430
....*....|....*....|....*....|....
gi 1564882272 407 FNELEYGVIGWNDGGPSAAHAPFGGLKESGYGRE 440
Cdd:PRK13968 409 AARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
4-443 |
1.25e-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: 275.07 E-value: 1.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN---WkkVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAE 80
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrnnW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 81 AKGEVAYANSYVKWYAEEAKRVYGRTIP----ANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICK 156
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 157 PAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSlISKVTFTGSTAVGKSLiESSAQQVKNVTMELGGLA 236
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWML-RSKLAPGTRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 237 PLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQLsrsIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFF 396
Cdd:cd07148 317 EEWVNEAVAAGARL---LCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1564882272 397 TNDYRTGLKLFNELEYGVIGWNDggPSAAHA---PFGGLKESGYGrEGGV 443
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVND--HTAFRVdwmPFAGRRQSGYG-TGGI 440
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
2-457 |
5.66e-87 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 274.47 E-value: 5.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 2 TKLEVINPATNEVLERLDYATHEQINHQIKQAHQAFQN--WKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLA 79
Cdd:PRK09847 35 ETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 80 EA-KGEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPA 158
Cdd:PRK09847 115 HSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVRE-PVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 159 VKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ-QVKNVTMELGGLAP 237
Cdd:PRK09847 194 EKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 238 LIVHNDA-DIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:PRK09847 274 NIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQL--SRSIEDIQALGgnflkPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASY 394
Cdd:PRK09847 354 HSFIREGESKGQLLldGRNAGLAAAIG-----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 395 FFTNDYRTGLKLFNELEYG---VIGWNDGGPSaahAPFGGLKESGYGREGGVEGIEPYLETKYLSI 457
Cdd:PRK09847 429 VWTRDLSRAHRMSRRLKAGsvfVNNYNDGDMT---VPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-436 |
6.56e-87 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 274.89 E-value: 6.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA 81
Cdd:PRK03137 51 KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 82 KGEVAYANSYVKWYAEEAKRvYGRTIPANS-PSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVK 160
Cdd:PRK03137 131 DADTAEAIDFLEYYARQMLK-LADGKPVESrPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 161 TPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSA-----QQ-VKNVTMELGG 234
Cdd:PRK03137 210 TPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqpgQIwLKRVIAEMGG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 235 LAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGlKEEVKIGPLIDNQAVE 314
Cdd:PRK03137 290 KDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 315 KVLTHIKDAQEKGGQLSRSIEDiqALGGNFLKPVVItnANLDMKA--MHEETFGPVAPVMTYSDLDEVINIANDTEFGLA 392
Cdd:PRK03137 369 KIMSYIEIGKEEGRLVLGGEGD--DSKGYFIQPTIF--ADVDPKAriMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLT 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1564882272 393 SYFFTNDYRTGLKLFNELEYGVIGWNDGGPSA---AHaPFGGLKESG 436
Cdd:PRK03137 445 GAVISNNREHLEKARREFHVGNLYFNRGCTGAivgYH-PFGGFNMSG 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
25-442 |
9.14e-87 |
|
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: 271.84 E-value: 9.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 25 QINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV----AYANSYVKWYAEeak 100
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVaamaGKIDISIKAYHE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 101 RVYGRTIPAnsPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKD 180
Cdd:cd07095 78 RTGERATPM--AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 181 AISyIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQV-KNVTMELGGLAPLIVHNDADIEAAVDGTIASKFR 259
Cdd:cd07095 156 VLN-LVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 260 NAGQTCICANRIYVHED-IAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEKGGQLSRSIEDIQ 338
Cdd:cd07095 235 TAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 339 AlGGNFLKPVVItnanlDMKAM----HEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGV 414
Cdd:cd07095 315 A-GTAFLSPGII-----DVTDAadvpDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420 430
....*....|....*....|....*....|.
gi 1564882272 415 IGWN---DGGPSAahAPFGGLKESGYGREGG 442
Cdd:cd07095 389 VNWNrptTGASST--APFGGVGLSGNHRPSA 417
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-442 |
3.68e-85 |
|
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: 270.61 E-value: 3.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK 82
Cdd:cd07125 48 APVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 83 GEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:cd07125 128 AEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGK----SLIESSAQQVKnVTMELGGLAPL 238
Cdd:cd07125 208 LIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKlinrALAERDGPILP-LIAETGGKNAM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLT 318
Cdd:cd07125 287 IVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 319 HIkdaQEKGGQlSRSIE--DIQALGGNFLKPVVITNANLDmkAMHEETFGPVAPVMTY--SDLDEVINIANDTEFGLASY 394
Cdd:cd07125 367 HT---ELMRGE-AWLIApaPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFkaEDLDEAIEDINATGYGLTLG 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1564882272 395 FFTNDYRTGLKLFNELEYGVIGWNDG--GPSAAHAPFGGLKESGYGREGG 442
Cdd:cd07125 441 IHSRDEREIEYWRERVEAGNLYINRNitGAIVGRQPFGGWGLSGTGPKAG 490
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
3-456 |
3.43e-84 |
|
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: 267.89 E-value: 3.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 3 KLEVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA 81
Cdd:TIGR01237 47 KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 82 KGEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKT 161
Cdd:TIGR01237 127 DAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 162 PLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSA------QQVKNVTMELGGL 235
Cdd:TIGR01237 207 PVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqKHLKRVIAEMGGK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 236 APLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEK 315
Cdd:TIGR01237 287 DTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNK 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 316 VLTHIKDAQEKGGQLSRSIEDIQAlgGNFLKPVVItnANLDMKA--MHEETFGPVAPVMTYSDLDEVINIANDTEFGLAS 393
Cdd:TIGR01237 367 IMEYIEIGKAEGRLVSGGCGDDSK--GYFIGPTIF--ADVDRKArlAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTG 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 394 YFFTNDYRTGLKLFNELEYGVIGWNDG--GPSAAHAPFGGLKESGYG-REGGVEGIEPYLETKYLS 456
Cdd:TIGR01237 443 GVISNNRDHINRAKAEFEVGNLYFNRNitGAIVGYQPFGGFKMSGTDsKAGGPDYLALFMQAKTVT 508
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
4-442 |
7.32e-84 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 265.61 E-value: 7.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVayaNSYVKW--YAEEAKR-VYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVK 160
Cdd:cd07130 94 EV---QEMIDIcdFAVGLSRqLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 161 TPLTTI---KLV-ELAHQAGFPKdAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLA 236
Cdd:cd07130 171 TPLTAIavtKIVaRVLEKNGLPG-AIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 237 PLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKV 316
Cdd:cd07130 250 AIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQLSRSIEDIQAlGGNFLKPVVITNANlDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFF 396
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGKVIDG-PGNYVEPTIVEGLS-DAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIF 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 397 TNDYRtglKLFNELeyGVIGWNDG------GPSAAH--APFGGLKESGYGREGG 442
Cdd:cd07130 408 TTDLR---NAFRWL--GPKGSDCGivnvniGTSGAEigGAFGGEKETGGGRESG 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-455 |
2.88e-79 |
|
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: 253.91 E-value: 2.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG- 83
Cdd:cd07116 19 DNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYG--RTIPANSPSKKIvidKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKT 161
Cdd:cd07116 99 DIPLAIDHFRYFAGCIRAQEGsiSEIDENTVAYHF---HEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 162 PLTTIKLVELAHQAgFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIV- 240
Cdd:cd07116 176 PASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFf 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 241 -----HNDADIEAAVDGTIASKFrNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEK 315
Cdd:cd07116 255 advmdADDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 316 VLTHIKDAQEKGGQL----SRSIEDIQALGGNFLKPVVITNANldMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGL 391
Cdd:cd07116 334 ILSYIDIGKEEGAEVltggERNELGGLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGL 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564882272 392 ASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETKYL 455
Cdd:cd07116 412 GAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
4-436 |
7.07e-77 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 247.95 E-value: 7.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PRK09457 17 FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EV-AYANSY---VKWYAEeakRVYGRTIPAnsPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAV 159
Cdd:PRK09457 97 EVtAMINKIaisIQAYHE---RTGEKRSEM--ADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 160 KTPLTTIKLVELAHQAGFPKDAISYIIAsGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQV-KNVTMELGGLAPL 238
Cdd:PRK09457 172 LTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPeKILALEMGGNNPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDI-AEAYNEKLIEKVHALSVGDGLKEEVK-IGPLIDNQAVEKV 316
Cdd:PRK09457 251 VIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 317 LTHIKDAQEKGGQLSRSIEDIQAlGGNFLKPVVItnanlDMKAM----HEETFGPVAPVMTYSDLDEVINIANDTEFGLA 392
Cdd:PRK09457 331 VAAQAQLLALGGKSLLEMTQLQA-GTGLLTPGII-----DVTGVaelpDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1564882272 393 SYFFTNDYRTGLKLFNELEYGVIGWN---DGGPSAahAPFGGLKESG 436
Cdd:PRK09457 405 AGLLSDDREDYDQFLLEIRAGIVNWNkplTGASSA--APFGGVGASG 449
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
5-453 |
7.21e-72 |
|
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: 234.66 E-value: 7.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPATNEVLERLDYATHEQINHQIKQAHQAFQ--NWKKvDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPL---- 78
Cdd:TIGR04284 18 PTVNPATEEVLGVAADATAADMDAAIAAARRAFDetDWSR-DTALRVRCLRQLRDALRAHVEELRELTIAEVGAPRmlta 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 79 -AEAKGEVA-------YANSYvKWyaeeaKRVYGRTIPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAG 150
Cdd:TIGR04284 97 gAQLEGPVDdlgfaadLAESY-AW-----TTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQINLAKLGPALAAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 151 CTIICKPAVKTPLTTIKLVEL-AHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVT 229
Cdd:TIGR04284 170 NTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 230 MELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLID 309
Cdd:TIGR04284 250 LELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGPVIS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 310 NQAVEKVLTHIKDAQEKGGQLsrsiediqALGGN---------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEV 380
Cdd:TIGR04284 330 ARQRDRVQSYLDLAVAEGGRF--------ACGGGrpadrdrgfFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564882272 381 INIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPSAAHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:TIGR04284 402 VRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
23-445 |
1.02e-71 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 232.89 E-value: 1.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 23 HEQINHQIKQAHQafqnWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK--------GEVAYANSYVK- 93
Cdd:cd07134 1 RRVFAAQQAHALA----LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 94 WYAeeAKRVygRTIPANSPSKKIVIDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAH 173
Cdd:cd07134 77 WMK--PKRV--RTPLLLFGTKSKIRYE-PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 174 QAgFPKDAISYIiasgkdAGDIFTNHSLISK----VTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAA 249
Cdd:cd07134 152 EA-FDEDEVAVF------EGDAEVAQALLELpfdhIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 250 VDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHA-LSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEKGG 328
Cdd:cd07134 225 AKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 329 QLsrsiediqALGG------NFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRT 402
Cdd:cd07134 305 KV--------EFGGqfdaaqRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKAN 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1564882272 403 GLKLFNELEYGVIGWNDggpSAAHA-----PFGGLKESGYGREGGVEG 445
Cdd:cd07134 377 VNKVLARTSSGGVVVND---VVLHFlnpnlPFGGVNNSGIGSYHGVYG 421
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
7-453 |
1.30e-71 |
|
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: 234.78 E-value: 1.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INP-ATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEV 85
Cdd:cd07083 37 VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 86 AYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKF-PVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:cd07083 117 AEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYvGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQ------VKNVTMELGGLAPL 238
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLapgqtwFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLT 318
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 319 HIKDAQE-----KGGQLSRSIediqalgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTY--SDLDEVINIANDTEFGL 391
Cdd:cd07083 357 YIEHGKNegqlvLGGKRLEGE-------GYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGL 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 392 ASYFFTNDYRTGLKLFNELEYGVIGWNDG--GPSAAHAPFGGLKESGYG-REGGVEGIEPYLETK 453
Cdd:cd07083 430 TGGVYSRKREHLEEARREFHVGNLYINRKitGALVGVQPFGGFKLSGTNaKTGGPHYLRRFLEMK 494
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-453 |
3.37e-69 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 228.10 E-value: 3.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PLN00412 33 VAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGR-------TIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICK 156
Cdd:PLN00412 113 EVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 157 PAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFT-GSTAVGkslIESSAQQVKnVTMELGGL 235
Cdd:PLN00412 193 PPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA---ISKKAGMVP-LQMELGGK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 236 APLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGlKEEVKIGPLIDNQAVEK 315
Cdd:PLN00412 269 DACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 316 VLTHIKDAQEKGGQLSRSIEDiqalGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYF 395
Cdd:PLN00412 348 IEGLVMDAKEKGATFCQEWKR----EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCV 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564882272 396 FTNDYRTGLKLFNELEYGVIGWNDG---GPSaaHAPFGGLKESGYGREGGVEGIEPYLETK 453
Cdd:PLN00412 424 FTRDINKAILISDAMETGTVQINSAparGPD--HFPFQGLKDSGIGSQGITNSINMMTKVK 482
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
48-447 |
1.52e-68 |
|
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: 224.33 E-value: 1.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 48 RSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA--------KGEVAYANSYVKWYAEEaKRVygRTIPANSPSKKIVId 119
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLKKWMKP-RRV--SVPLLLQPAKAYVI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 120 KFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAgFPKDAISYIiasgkdAGDIFTNH 199
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVV------EGGVEVAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 200 SLIS----KVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHE 275
Cdd:cd07087 171 ALLAepfdHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 276 DIAEAYNEKLIEKVHALsVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ-EKGGQLSRSiediqalgGNFLKPVVITNAN 354
Cdd:cd07087 251 SIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGKvVIGGQVDKE--------ERYIAPTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 355 LDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDggpSAAHA-----PF 429
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVND---VLLHAaipnlPF 398
|
410
....*....|....*...
gi 1564882272 430 GGLKESGYGREGGVEGIE 447
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFD 416
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
5-391 |
3.82e-68 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 235.60 E-value: 3.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:COG4230 573 PVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIA 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANspskkividkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:COG4230 653 EVREAVDFCRYYAAQARRLFAAPTVLR-----------GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPL 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGK----SLIESSAQQVKNVTmELGGLAPLI 239
Cdd:COG4230 722 IAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinrTLAARDGPIVPLIA-ETGGQNAMI 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCiCANRI-YVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLT 318
Cdd:COG4230 801 VDSSALPEQVVDDVLASAFDSAGQRC-SALRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEA 879
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 319 HIKDAQEKGGQLSRSIEDIQALGGNFLKPVVITNANLDmkAMHEETFGPVAPVMTY--SDLDEVINIANDTEFGL 391
Cdd:COG4230 880 HIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSIS--DLEREVFGPVLHVVRYkaDELDKVIDAINATGYGL 952
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
5-391 |
6.35e-68 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 235.14 E-value: 6.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PRK11905 570 PVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAkrvygRTIPANSPSKkividkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPL 163
Cdd:PRK11905 650 EVREAVDFLRYYAAQA-----RRLLNGPGHK-------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPL 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 164 TTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVG----KSLIESSAQQVKNVTmELGGLAPLI 239
Cdd:PRK11905 718 IAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVArliqRTLAKRSGPPVPLIA-ETGGQNAMI 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 240 VHNDADIEAAVDGTIASKFRNAGQTCiCANRI-YVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLT 318
Cdd:PRK11905 797 VDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEA 875
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 319 HIKDAQEKGGQLSRSIEDIQALGGNFLKPVVITNANLDmkAMHEETFGPVAPVMTY--SDLDEVINIANDTEFGL 391
Cdd:PRK11905 876 HIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSIS--DLEREVFGPVLHVVRFkaDELDRVIDDINATGYGL 948
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
5-391 |
3.74e-67 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 232.01 E-value: 3.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 5 EVINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PRK11904 565 PVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIA 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKF-PVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTP 162
Cdd:PRK11904 645 EVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLhGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTP 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKsLIessaqqvkNVTM------------ 230
Cdd:PRK11904 725 LIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETAR-II--------NRTLaardgpivplia 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 231 ELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCiCANRI-YVHEDIAeaynEKLIEKVH----ALSVGDGLKEEVKIG 305
Cdd:PRK11904 796 ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRC-SALRVlFVQEDIA----DRVIEMLKgamaELKVGDPRLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 306 PLIDNQAVEKVLTHIKDAQEKGGQLSRSIEDIQALGGNFLKPVVITNANLDmkAMHEETFGPVAPVMTY--SDLDEVINI 383
Cdd:PRK11904 871 PVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSIS--QLEREVFGPILHVIRYkaSDLDKVIDA 948
|
....*...
gi 1564882272 384 ANDTEFGL 391
Cdd:PRK11904 949 INATGYGL 956
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
28-445 |
1.84e-64 |
|
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: 213.89 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 28 HQIKQAHQAFQNwkkVDAHERSAKLAQWAQLIDDHQDELARLITLE-GGKP-----LAE---AKGEVAYANSYVKWYAEE 98
Cdd:cd07133 5 ERQKAAFLANPP---PSLEERRDRLDRLKALLLDNQDALAEAISADfGHRSrhetlLAEilpSIAGIKHARKHLKKWMKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 99 AKRvygRTIPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAgFP 178
Cdd:cd07133 82 SRR---HVGLLFLPAKAEVE-YQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 179 KDAISyIIASGKDAGDIFT----NHSLiskvtFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTI 254
Cdd:cd07133 157 EDEVA-VVTGGADVAAAFSslpfDHLL-----FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 255 ASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALsVGDGLKEEvKIGPLIDNQAVEKVLTHIKDAQEKGGQLSRSI 334
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIELN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 335 EDIQALGGN-FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYG 413
Cdd:cd07133 309 PAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSG 388
|
410 420 430
....*....|....*....|....*....|....
gi 1564882272 414 VIGWNDGGPSAA--HAPFGGLKESGYGREGGVEG 445
Cdd:cd07133 389 GVTINDTLLHVAqdDLPFGGVGASGMGAYHGKEG 422
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
20-447 |
7.50e-63 |
|
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: 209.77 E-value: 7.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 20 YATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKP-----LAE---AKGEVAYANSY 91
Cdd:cd07135 1 YTPLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDILHMLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 92 VKWYAEEAKRvyGRTIPANSPSKkIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVEL 171
Cdd:cd07135 81 LKKWAKDEKV--KDGPLAFMFGK-PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 172 AHQAgFPKDAISYIIASGKDAGDIFTNHslISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVD 251
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 252 GTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLiEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEK---GG 328
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGKvviGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 329 QLSRsiediqalGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFN 408
Cdd:cd07135 314 EMDE--------ATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1564882272 409 ELEYGVIGWNDggpSAAH-----APFGGLKESGYGREGGVEGIE 447
Cdd:cd07135 386 RTRSGGVVIND---TLIHvgvdnAPFGGVGDSGYGAYHGKYGFD 426
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-459 |
7.38e-62 |
|
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: 209.00 E-value: 7.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPAT-NEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGE 84
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYGrtipaNSPSKkividkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:TIGR01238 135 VREAVDFCRYYAKQVRDVLG-----EFSVE-------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKN---VTMELGGLAPLIVH 241
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDApvpLIAETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 242 NDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHI- 320
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIe 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 321 --KDAQEKGGQLSRSiEDIQALGGNFLKPVVITNANLDmkAMHEETFGPVAPVMTYS--DLDEVINIANDTEFGLASYFF 396
Cdd:TIGR01238 363 hmSQTQKKIAQLTLD-DSRACQHGTFVAPTLFELDDIA--ELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVH 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 397 TNDYRTGLKLFNELEYG--VIGWNDGGPSAAHAPFGGLKESGYGREGGvegiEPYLETKYLSIQE 459
Cdd:TIGR01238 440 SRIETTYRWIEKHARVGncYVNRNQVGAVVGVQPFGGQGLSGTGPKAG----GPHYLYRLTQVQY 500
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-418 |
4.35e-61 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 209.60 E-value: 4.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 4 LEVINPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKG 83
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 84 EVAYANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPaAMITRKMAP-ALAAGCTIICKPAVKTP 162
Cdd:PLN02419 211 DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFP-AMIPLWMFPvAVTCGNTFILKPSEKDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 163 LTTIKLVELAHQAGFPkDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:PLN02419 290 GASVILAELAMEAGLP-DGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLP 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDiAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:PLN02419 369 DANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQLSRSIEDIQALG---GNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:PLN02419 448 GVDDGAKLLLDGRDIVVPGyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410
....*....|....*....
gi 1564882272 400 YRTGLKLFNELEYGVIGWN 418
Cdd:PLN02419 528 GAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
48-439 |
2.92e-59 |
|
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: 200.81 E-value: 2.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 48 RSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA--------KGEVAYANSYVKWYAEEaKRVygRTIPANSPSKKIVId 119
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAymteigfvLSEINYAIKHLKKWMKP-KRV--KTPLLNFPSKSYIY- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 120 KFPVGVVGAITPWNFPAAMItrkMAP---ALAAGCTIICKPAVKTPLTTIKLVELAHQAgFPKDAISYIiasgkdAGDIF 196
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVV------EGGVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 197 TNHSLIS----KVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRNAGQTCICANRIY 272
Cdd:cd07136 168 ENQELLDqkfdYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 273 VHEDIAEAYNEKLIEKVHALSVGDGLKEE--VKIgplIDNQAVEKVLTHIKDAQ-EKGGQLSRsiediqalGGNFLKPVV 349
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESPdyGRI---INEKHFDRLAGLLDNGKiVFGGNTDR--------ETLYIEPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 350 ITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYG--VIgwND-----GGP 422
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggCI--NDtimhlANP 394
|
410
....*....|....*..
gi 1564882272 423 saaHAPFGGLKESGYGR 439
Cdd:cd07136 395 ---YLPFGGVGNSGMGS 408
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
35-447 |
5.57e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 185.23 E-value: 5.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 35 QAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK--------GEVAYANSYVKWYAeeaKRVYGRT 106
Cdd:PTZ00381 18 ESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLLKHLDEYL---KPEKVDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 107 IPANSPSKKIVIdKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELahqagFPK---DAIS 183
Cdd:PTZ00381 95 VGVFGPGKSYII-PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-----LTKyldPSYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 184 YIIASGKDAgdifTNHSLISK---VTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRN 260
Cdd:PTZ00381 169 RVIEGGVEV----TTELLKEPfdhIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 261 AGQTCICANRIYVHEDIAEAYNEKLIEKVHALsVGDGLKEEVKIGPLIDNQAVEKVLTHIKDaqeKGGQLsrsiediqAL 340
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKV--------VY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 341 GGNF------LKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGV 414
Cdd:PTZ00381 313 GGEVdienkyVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGA 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 1564882272 415 IGWND-----GGPsaaHAPFGGLKESGYGREGGVEGIE 447
Cdd:PTZ00381 393 VVINDcvfhlLNP---NLPFGGVGNSGMGAYHGKYGFD 427
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
7-450 |
3.02e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.10 E-value: 3.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 7 INPATNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVA 86
Cdd:PLN02315 39 VNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 YANSYVKWYAEEAKRVYGRTIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTI 166
Cdd:PLN02315 119 EIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 167 ---KLV-ELAHQAGFPkDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHN 242
Cdd:PLN02315 199 amtKLVaEVLEKNNLP-GAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 243 DADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKD 322
Cdd:PLN02315 278 DADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 323 AQEKGGQLSRSIEDIQAlGGNFLKPVVItNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRT 402
Cdd:PLN02315 358 IKSQGGKILTGGSAIES-EGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPET 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1564882272 403 GLKLFNEL--EYGVIGWN--DGGPSAAHApFGGLKESGYGREGGVEGIEPYL 450
Cdd:PLN02315 436 IFKWIGPLgsDCGIVNVNipTNGAEIGGA-FGGEKATGGGREAGSDSWKQYM 486
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
6-391 |
7.58e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 179.78 E-value: 7.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 6 VINPA-TNEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGE 84
Cdd:PRK11809 663 VINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 85 VAYANSYVKWYAEEAKRVYgrtipANSPSKkividkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLT 164
Cdd:PRK11809 743 VREAVDFLRYYAGQVRDDF-----DNDTHR-------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKN------VTMELGGLAPL 238
Cdd:PRK11809 811 AAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAM 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDADIEAAVDGTIASKFRNAGQTCiCANRIY-VHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVL 317
Cdd:PRK11809 891 IVDSSALTEQVVADVLASAFDSAGQRC-SALRVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIE 969
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1564882272 318 THIKDAQEKGG---QLSRSIEDIQALgGNFLKPVVITNANLDmkAMHEETFGPVAPVMTY--SDLDEVINIANDTEFGL 391
Cdd:PRK11809 970 RHIQAMRAKGRpvfQAARENSEDWQS-GTFVPPTLIELDSFD--ELKREVFGPVLHVVRYnrNQLDELIEQINASGYGL 1045
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
30-439 |
1.08e-41 |
|
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: 153.53 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 30 IKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA--------KGEVAYANSYV-KWYAEEAk 100
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpEWMKPEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 101 rvygrtiPANSPSKK---IVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELahqagF 177
Cdd:cd07132 83 -------VKKNLATLlddVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----I 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 178 PK--DAISYIIASG--KDAGDIFTNHslISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGT 253
Cdd:cd07132 151 PKylDKECYPVVLGgvEETTELLKQR--FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 254 IASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALsVGDGLKEEVKIGPLIDN---QAVEKVLthikdaqeKGGQL 330
Cdd:cd07132 229 AWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDrhfQRLKKLL--------SGGKV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 331 srsiediqALGG------NFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGL 404
Cdd:cd07132 300 --------AIGGqtdekeRYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVIN 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1564882272 405 KLFNELEYGVIGWNDggpSAAHA-----PFGGLKESGYGR 439
Cdd:cd07132 372 KILSNTSSGGVCVND---TIMHYtldslPFGGVGNSGMGA 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
36-442 |
8.83e-41 |
|
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: 151.02 E-value: 8.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 36 AFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA-KGEVAYANSYV--------KWYAEEAKRVYGRT 106
Cdd:cd07137 11 TFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKWMAPEKVKTPLTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 107 IPANSpskKIVIDkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAgFPKDAISyII 186
Cdd:cd07137 91 FPAKA---EIVSE--PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIK-VI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 187 ASGKDAGDIFTNHSLiSKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKF-RNAGQTC 265
Cdd:cd07137 164 EGGVPETTALLEQKW-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 266 ICANRIYVHEDIAeaynEKLIekvhalsvgDGLKEEVK--IGPlidNQAVEKVLTHIKDAQEKgGQLSRSIED--IQA-- 339
Cdd:cd07137 243 IAPDYVLVEESFA----PTLI---------DALKNTLEkfFGE---NPKESKDLSRIVNSHHF-QRLSRLLDDpsVADki 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 340 -LGGN------FLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEY 412
Cdd:cd07137 306 vHGGErdeknlYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSS 385
|
410 420 430
....*....|....*....|....*....|..
gi 1564882272 413 GVIGWNDGGPSAA--HAPFGGLKESGYGREGG 442
Cdd:cd07137 386 GGVTFNDTVVQYAidTLPFGGVGESGFGAYHG 417
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-436 |
1.38e-37 |
|
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: 143.88 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 12 NEVLERLDYATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDD-HQDELARLITLEGGKPLAEAKGEVA---- 86
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGkYRYELNAATMLGQGKNVWQAEIDAAceli 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 87 -YANSYVKwYAEEakrVYGRTIPANSPSKKIVIDKFPV-GVVGAITPWNFPAAMITRKMAPALAaGCTIICKPAVKTPLT 164
Cdd:cd07123 137 dFLRFNVK-YAEE---LYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 165 TIKLVELAHQAGFPKDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQQVKN------VTMELGGLAPL 238
Cdd:cd07123 212 NYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRyrtyprIVGETGGKNFH 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 239 IVHNDADIEAAVDGTIASKFRNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLT 318
Cdd:cd07123 292 LVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 319 HIKDAQEK-------GGQLSRSIediqalgGNFLKPVVITNANLDMKAMHEETFGPVAPVMTY--SDLDEVINIANDT-E 388
Cdd:cd07123 372 YIDHAKSDpeaeiiaGGKCDDSV-------GYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsP 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1564882272 389 FGLASYFFTNDYRTGLKLFNELEY--GVIGWNDG--GPSAAHAPFGGLKESG 436
Cdd:cd07123 445 YALTGAIFAQDRKAIREATDALRNaaGNFYINDKptGAVVGQQPFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
21-442 |
3.81e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 133.70 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 21 ATHEQINHQIKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEA--------KGEVAYANSYV 92
Cdd:PLN02203 3 APGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdevgvlTKSANLALSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 93 -KWYAEEAKRVYGRTIPANSpskKIVIDkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVel 171
Cdd:PLN02203 83 kKWMAPKKAKLPLVAFPATA---EVVPE--PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 172 ahqAGFPK--DAISY-IIASGKDAGDIFTNHSLiSKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVH---NDAD 245
Cdd:PLN02203 156 ---ANIPKylDSKAVkVIEGGPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 246 IEAAVDGTIASKFRN-AGQTCICANRIYVHEDIAEAYNEkLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQ 324
Cdd:PLN02203 232 TKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIE-LLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 325 EKGGQLSRSIEDIQALggnFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGL 404
Cdd:PLN02203 311 VAASIVHGGSIDEKKL---FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKR 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1564882272 405 KLFNELEYGVIGWNDG--GPSAAHAPFGGLKESGYGREGG 442
Cdd:PLN02203 388 RILSETSSGSVTFNDAiiQYACDSLPFGGVGESGFGRYHG 427
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
33-450 |
5.01e-33 |
|
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: 129.67 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 33 AHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAkGEVAYANSYVKWYAEEAKRVYGRTIPANSP 112
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIPHEPGNHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 113 SKKIVIDK----FPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISYIIAS 188
Cdd:cd07084 87 GQGLKQQShgyrWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLING 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 189 GKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQqvKNVTMELGGLAPLIVHNDADIEAAV-DGTIASKFRNAGQTCIC 267
Cdd:cd07084 167 DGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAVDYVaWQCVQDMTACSGQKCTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 268 ANRIYVHEDIA-EAYNEKLIEKVHALSVGDGLkeevkIGPLIdnqaVEKVLTHIKDAQEKGGQ---LSRSIE---DIQAL 340
Cdd:cd07084 245 QSMLFVPENWSkTPLVEKLKALLARRKLEDLL-----LGPVQ----TFTTLAMIAHMENLLGSvllFSGKELknhSIPSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 341 GGNFLKP---VVITNANLDMKAMHEETFGPVAPVMTYSDLDE--VINIANDTEFGLASYFFTNDYRTGLKLFNELE-YGV 414
Cdd:cd07084 316 YGACVASalfVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1564882272 415 ---IGWNDGG--PSAAHApfGGLKESGYGRE-GGVEGIEPYL 450
Cdd:cd07084 396 tyaILRGRTGvaPNQNHG--GGPAADPRGAGiGGPEAIKLVW 435
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
46-444 |
4.60e-32 |
|
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: 128.16 E-value: 4.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 46 HERSAKLAQWAQLIDDHQDELARLITLEGGKpLAEAKGEVAYANSYVKWYAEEAKRVygrtipanSPSKKIVIDKFPV-- 123
Cdd:cd07128 59 HERAAMLKALAKYLMERKEDLYALSAATGAT-RRDSWIDIDGGIGTLFAYASLGRRE--------LPNAHFLVEGDVEpl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 124 ----------------GVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAG-FPKDAISYII 186
Cdd:cd07128 130 skdgtfvgqhiltprrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLIC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 187 ASGKDAGDIFTNHSLiskVTFTGSTAVGKSLIESSAQQVKNV--TMELGGLAPLIVHNDA-------DI---EAAVDGTI 254
Cdd:cd07128 210 GSVGDLLDHLGEQDV---VAFTGSAATAAKLRAHPNIVARSIrfNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 255 askfrNAGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEK-----GGQ 329
Cdd:cd07128 287 -----KAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEaevvfGGP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 330 LSRSIEDIQALGGNFLKPVVITNAN-LDMKAMHE-ETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYrtglKLF 407
Cdd:cd07128 362 DRFEVVGADAEKGAFFPPTLLLCDDpDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDP----AFA 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1564882272 408 NELEYGVIGWN---------DGGPSAAH-APFGGLKESGYGREGGVE 444
Cdd:cd07128 438 RELVLGAAPYHgrllvlnrdSAKESTGHgSPLPQLVHGGPGRAGGGE 484
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
48-438 |
4.41e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.52 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 48 RSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK-GEVAYANSYVK--------WYAEEAKRVYGRTIPAnspSKKIVI 118
Cdd:PLN02174 34 RVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSvYEVSLLRNSIKlalkqlknWMAPEKAKTSLTTFPA---SAEIVS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 119 DkfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAgfpKDAISYIIASGKDAGDIFTN 198
Cdd:PLN02174 111 E--PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY---LDSSAVRVVEGAVTETTALL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 199 HSLISKVTFTGSTAVGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFR-NAGQTCICANRIYVHEDI 277
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 278 AEAYNEKLIEKVHALsVGDGLKEEVKIGPLIDNQAVEKvLTHIKDAQE------KGGQLSRsiEDIQalggnfLKPVVIT 351
Cdd:PLN02174 266 APKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDR-LSKLLDEKEvsdkivYGGEKDR--ENLK------IAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 352 NANLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTNDYRTGLKLFNELEYGVIGWNDGGPS-AAHA-PF 429
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHlALHTlPF 415
|
....*....
gi 1564882272 430 GGLKESGYG 438
Cdd:PLN02174 416 GGVGESGMG 424
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
33-385 |
7.45e-22 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 97.61 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 33 AHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKR--VYGRTI--- 107
Cdd:cd07129 8 AAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWLDARIdpa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 108 -PANSPSKKIVIDKF--PVGVVGAITPWNFPAAMITR--KMAPALAAGCTIICKPAVKTPLTTIKLVELAHQA----GFP 178
Cdd:cd07129 88 dPDRQPLPRPDLRRMlvPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 179 KDAISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSAQ--QVKNVTMELGGLAPLIVHNDA---DIEAAVDGT 253
Cdd:cd07129 168 AGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGAlaeRGEAIAQGF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 254 IASKFRNAGQTCICANRIYVHEDIA-EAYNEKLIEKVHALSVGDGLKEEVKigplidnQAVEKVLTHIKDAqeKGGQLSr 332
Cdd:cd07129 248 VGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLTPGIA-------EAYRQGVEALAAA--PGVRVL- 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564882272 333 sIEDIQALGGNFLKPVVIT---NANLDMKAMHEETFGPVAPVMTYSDLDEVINIAN 385
Cdd:cd07129 318 -AGGAAAEGGNQAAPTLFKvdaAAFLADPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
47-399 |
5.70e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.54 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 47 ERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAK----GEVAYANSYVKWYAEEAKRVYGRTIPANSPSKKiviDKFP 122
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAvdidGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKD---PAFQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 123 V--------GVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAG-FPKDAISYIIASGKD-- 191
Cdd:PRK11903 141 GqhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGll 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 192 ----AGDIftnhsliskVTFTGSTAVGkSLIESSAQQVKN---VTMELGGLAPLIVHNDADIE-AAVDGTIASKFRN--- 260
Cdd:PRK11903 221 dhlqPFDV---------VSFTGSAETA-AVLRSHPAVVQRsvrVNVEADSLNSALLGPDAAPGsEAFDLFVKEVVREmtv 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 261 -AGQTCICANRIYVHEDIAEAYNEKLIEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHIKDAQEK-----GGQLSRSI 334
Cdd:PRK11903 291 kSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQaevlfDGGGFALV 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564882272 335 eDIQALGGNFLKPVVI-TNANLDMKAMHE-ETFGPVAPVMTYSDLDEVINIANDTEFGLASYFFTND 399
Cdd:PRK11903 371 -DADPAVAACVGPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
63-401 |
1.35e-11 |
|
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: 66.37 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 63 QDELARLITLEGGKPLAEAKGEVAYANSYVKWYAEEAKRVYGR--TIPANSPSKKIVIDKFPVGVVGAITPWNFPAAMIT 140
Cdd:cd07126 81 EDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARsfNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 141 RKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQAGFPKDAISYIIASGKDAGDIF--TNHSLIskvTFTGSTAVGKSLI 218
Cdd:cd07126 161 LQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILleANPRMT---LFTGSSKVAERLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 219 ESSAQQVKnvtMELGG-----LAPLIvhNDADIEAAVDGTIASKFrnAGQTCICANRIYVHEDIAEAyneKLIEKVHALS 293
Cdd:cd07126 238 LELHGKVK---LEDAGfdwkiLGPDV--SDVDYVAWQCDQDAYAC--SGQKCSAQSILFAHENWVQA---GILDKLKALA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 294 VGDGLkEEVKIGPLIdNQAVEKVLTHIKD-AQEKGGQLsrsiediqALGGNFLK------------------PVVITNAN 354
Cdd:cd07126 308 EQRKL-EDLTIGPVL-TWTTERILDHVDKlLAIPGAKV--------LFGGKPLTnhsipsiygayeptavfvPLEEIAIE 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1564882272 355 LDMKAMHEETFGPVAPVMTYSD--LDEVINIANDTEFGLASYFFTNDYR 401
Cdd:cd07126 378 ENFELVTTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAVVSNDIR 426
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
31-287 |
1.53e-11 |
|
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: 65.98 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 31 KQAHQAFQNW--KKVDAHERSAKLAqwaqlIDDHQDELARLITLEGGKPLAEAKgeVA---YANSYVkWYAEEAKRVYGr 105
Cdd:cd07122 9 RKAQREFATFsqEQVDKIVEAVAWA-----AADAAEELAKMAVEETGMGVVEDK--VIknhFASEYV-YNDIKDMKTVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 106 tIPANSPSKKIV-IDKfPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVEL----AHQAGFPKD 180
Cdd:cd07122 80 -VIEEDEEKGIVeIAE-PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 181 AISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSaqqvknvTMELG---GLAPLIVHNDADIEAAVDGTIASK 257
Cdd:cd07122 158 LIQWIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSG-------KPAIGvgpGNVPAYIDETADIKRAVKDIILSK 230
|
250 260 270
....*....|....*....|....*....|...
gi 1564882272 258 -FRNAgqtCICA--NRIYVHEDIAEAYNEKLIE 287
Cdd:cd07122 231 tFDNG---TICAseQSVIVDDEIYDEVRAELKR 260
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
30-288 |
4.96e-10 |
|
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: 61.13 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 30 IKQAHQAFQNWKK--VDAHERSAKLAQwaqliDDHQDELARLITLEGGKPLAE---AKGEVAYANSYVKWYAEEAKRVYG 104
Cdd:cd07081 8 AKVAQQGLSCKSQemVDLIFRAAAEAA-----EDARIDLAKLAVSETGMGRVEdkvIKNHFAAEYIYNVYKDEKTCGVLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 105 RTIPANspskkIVIDKFPVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKPAVKTPLTTIKLVELAHQA----GFPKD 180
Cdd:cd07081 83 GDENGG-----TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 181 AISYIIASGKDAGDIFTNHSLISKVTFTGstavGKSLIESSAQQVKNVTMELGGLAPLIVHNDADIEAAVDGTIASKFRN 260
Cdd:cd07081 158 LIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFD 233
|
250 260
....*....|....*....|....*...
gi 1564882272 261 AGQTCICANRIYVHEDIAEAYNEKLIEK 288
Cdd:cd07081 234 NGVICASEQSVIVVDSVYDEVMRLFEGQ 261
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
19-426 |
5.84e-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: 57.62 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 19 DYATHEQINHQIKQAHQAFQNWKKVDAHERSAK----LAQWAQLIDDHQDELARLITLEGGKPLAEAkgevayansyvkw 94
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYirslIANWIAMMGCSESKLYKNIDTERGITASVG------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 95 yaeeakRVYGRTIPANSpskKIVIDKFPVGVVGAITPWNFPAAMITrKMAPALAAGCTIICKPAVKTPLTTiKLVELAHQ 174
Cdd:cd07077 82 ------HIQDVLLPDNG---ETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTN-RALALLFQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 175 A----GFPKDAISYI-IASGKDAGDIFtNHSLISKVTFTGSTAVGKSLIESSAQqvKNVTMELGGLAPLIVHNDADIEAA 249
Cdd:cd07077 151 AadaaHGPKILVLYVpHPSDELAEELL-SHPKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 250 VDGTIASKFRNaGQTCICANRIYVHEDIAEAYNEKLieKVHALSVGDGLKEEVKIgplidnQAVEKVLTHIKDAQEKGGQ 329
Cdd:cd07077 228 SGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEF--KLKLVVEGLKVPQETKP------LSKETTPSFDDEALESMTP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 330 LSRSIEdiqalGGNFLKPVVItnaNLDMKAMHEetfGPVAPVMTYSDLDEVINIANDTE----FGLASYFFTNDYRTGLK 405
Cdd:cd07077 299 LECQFR-----VLDVISAVEN---AWMIIESGG---GPHTRCVYTHKINKVDDFVQYIDtasfYPNESSKKGRGAFAGKG 367
|
410 420
....*....|....*....|.
gi 1564882272 406 LFNELEYGVIGWNDGGPSAAH 426
Cdd:cd07077 368 VERIVTSGMNNIFGAGVGHDA 388
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
30-384 |
1.46e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 56.72 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 30 IKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELAR----------LITLEGGKPLAEAKG--EVAYAnsyvkwyAE 97
Cdd:cd07127 90 LAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavmhttgqafMMAFQAGGPHAQDRGleAVAYA-------WR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 98 EAKRVYGRTIPANSPSKK--IVIDK----FPVG---VVGAIT--PWN-FPAamitrkMAPALAAGCTIICKPAVKTPLTT 165
Cdd:cd07127 163 EMSRIPPTAEWEKPQGKHdpLAMEKtftvVPRGvalVIGCSTfpTWNgYPG------LFASLATGNPVIVKPHPAAILPL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 166 IKLVELAH----QAGFPKDAISYIIAS-GKDAGDIFTNHSLISKVTFTGSTAVGKSLiESSAQQvKNVTMELGGLAPLIV 240
Cdd:cd07127 237 AITVQVARevlaEAGFDPNLVTLAADTpEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANARQ-AQVYTEKAGVNTVVV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 241 HNDADIEAAVDGTIASKFRNAGQTCICANRIYV------HEDIAEAYNE---KLIEKVHALsVGDGLKEEVKIGPlIDNQ 311
Cdd:cd07127 315 DSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqTDDGRKSFDEvaaDLAAAIDGL-LADPARAAALLGA-IQSP 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564882272 312 AVekvLTHIKDAQEKGGQL--SRSIEDIQALGGNFLKPVVITNANLDMKAMHEETFGPVAPVMTYSDLDEVINIA 384
Cdd:cd07127 393 DT---LARIAEARQLGEVLlaSEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
122-391 |
7.02e-06 |
|
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: 48.00 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 122 PVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKP---AVKTPLTTIKLVELA-HQAGFPKDAISYIIASGKDAGDIFT 197
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELINKAiAEAGGPDNLVVTVEEPTIETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 198 NHSLISKVTFTGSTAVGKSLIESSaqqvKNVTMELGGLAPLIVHNDADIE-AAVDGTIASKFRNaGQTCICANRIYVHED 276
Cdd:cd07121 177 AHPDINLLVVTGGPAVVKAALSSG----KKAIGAGAGNPPVVVDETADIEkAARDIVQGASFDN-NLPCIAEKEVIAVDS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 277 IAEAYNEKLiEKVHALSVGDglKEEVKIGPLIDNQAVEKVL--THI-KDAQEKGGQLSRSIEDIqalggnflKPVVITNA 353
Cdd:cd07121 252 VADYLIAAM-QRNGAYVLND--EQAEQLLEVVLLTNKGATPnkKWVgKDASKILKAAGIEVPAD--------IRLIIVET 320
|
250 260 270
....*....|....*....|....*....|....*...
gi 1564882272 354 NLDMKAMHEETFGPVAPVMTYSDLDEVINIANDTEFGL 391
Cdd:cd07121 321 DKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGN 358
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
30-391 |
1.21e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.12 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 30 IKQAHQAFQNWKKVDAHERSAKLAQWAQLIDDHQDELARLITLEGGKPLAEAKGE----VAYANSYVKWYAEEAKR-VYG 104
Cdd:PRK15398 42 VAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAknvaAAEKTPGVEDLTTEALTgDNG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 105 RTIPANSPskkividkfpVGVVGAITPWNFPAAMITRKMAPALAAGCTIICKP---AVKTPLTTIKLV-ELAHQAGFPKD 180
Cdd:PRK15398 122 LTLIEYAP----------FGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKVSLRAIELLnEAIVAAGGPEN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 181 AISYIIASGKDAGDIFTNHSLISKVTFTGSTAVGKSLIESSaqqvKNVTMELGGLAPLIVHNDADIEAA----VDGtiAS 256
Cdd:PRK15398 192 LVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSG----KKAIGAGAGNPPVVVDETADIEKAardiVKG--AS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 257 kFRNaGQTCICANRIYVHEDIAEAYNEKLiEKVHALSVGDGLKEEVKIGPLIDNQAVEKVLTHiKDA----QEKGGQLSR 332
Cdd:PRK15398 266 -FDN-NLPCIAEKEVIVVDSVADELMRLM-EKNGAVLLTAEQAEKLQKVVLKNGGTVNKKWVG-KDAakilEAAGINVPK 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1564882272 333 SIEDIqalggnflkpVVITNANlDMKAMHEETFgPVAPVMTYSDLDEVINIANDTEFGL 391
Cdd:PRK15398 342 DTRLL----------IVETDAN-HPFVVTELMM-PVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
122-287 |
3.06e-04 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 43.25 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 122 PVGVVGAITPWNFPA------AMItrkmapALAAGCTIICKP---AVKTPLTTIKLV-ELAHQAGFPKDAISYIIASGKD 191
Cdd:PRK13805 108 PVGVIAGITPTTNPTstaifkALI------ALKTRNPIIFSFhprAQKSSIAAAKIVlDAAVAAGAPKDIIQWIEEPSVE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564882272 192 AGDIFTNHSLISKVTFTGSTAVGKSLIESS--AqqvknvtmeLG---GLAPLIVHNDADIEAAVDGTIASK-FRNAgqtC 265
Cdd:PRK13805 182 LTNALMNHPGIALILATGGPGMVKAAYSSGkpA---------LGvgaGNVPAYIDKTADIKRAVNDILLSKtFDNG---M 249
|
170 180
....*....|....*....|....
gi 1564882272 266 ICA--NRIYVHEDIAEAYNEKLIE 287
Cdd:PRK13805 250 ICAseQAVIVDDEIYDEVKEEFAS 273
|
|
| |
