|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
1-416 |
0e+00 |
|
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: 880.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07141 66 MDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07141 146 VGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07141 226 DKVAFTGSTEVGKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:cd07141 306 VKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:cd07141 386 EIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELG 465
|
410
....*....|....*.
gi 25777728 401 EFGLREYSEVKTVTVK 416
Cdd:cd07141 466 EYGLQEYTEVKTVTIK 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-415 |
0e+00 |
|
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: 787.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07091 62 MDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07091 142 IGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07091 222 DKIAFTGSTAVGRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:cd07091 302 VEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:cd07091 382 EIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELG 461
|
410
....*....|....*
gi 25777728 401 EFGLREYSEVKTVTV 415
Cdd:cd07091 462 EEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
1-413 |
0e+00 |
|
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: 665.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07142 62 MTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07142 142 IGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07142 222 DKVAFTGSTEVGKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:cd07142 302 VEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARD 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:cd07142 382 EIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKG 461
|
410
....*....|...
gi 25777728 401 EFGLREYSEVKTV 413
Cdd:cd07142 462 IYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1-421 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 655.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:PLN02466 116 MTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:PLN02466 196 IGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:PLN02466 276 DKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEF 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:PLN02466 356 VEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:PLN02466 436 EIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKG 515
|
410 420
....*....|....*....|.
gi 25777728 401 EFGLREYSEVKTVTVkiPQKN 421
Cdd:PLN02466 516 IYSLNNYLQVKAVVT--PLKN 534
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-417 |
0e+00 |
|
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: 648.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGV 83
Cdd:cd07143 68 SKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 84 CGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKI 163
Cdd:cd07143 148 CGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 164 AFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRR 243
Cdd:cd07143 228 AFTGSTLVGRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 244 SVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIF 323
Cdd:cd07143 308 FKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIF 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 324 GPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFG 403
Cdd:cd07143 388 GPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYA 467
|
410
....*....|....
gi 25777728 404 LREYSEVKTVTVKI 417
Cdd:cd07143 468 LENYTQIKAVHINL 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-413 |
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: 627.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:pfam00171 48 TPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:pfam00171 127 LGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:pfam00171 207 RKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:pfam00171 286 VEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREM 399
Cdd:pfam00171 366 EIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREG 445
|
410
....*....|....
gi 25777728 400 GEFGLREYSEVKTV 413
Cdd:pfam00171 446 GPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-416 |
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: 622.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHE 79
Cdd:COG1012 62 TPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRRE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:COG1012 141 PLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:COG1012 221 VDKISFTGSTAVGRRIAAAAAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIA 318
Cdd:COG1012 300 FVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNGR 397
Cdd:COG1012 380 REEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGR 459
|
410
....*....|....*....
gi 25777728 398 EMGEFGLREYSEVKTVTVK 416
Cdd:COG1012 460 EGGREGLEEYTETKTVTIR 478
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-415 |
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: 609.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHE 79
Cdd:cd07078 17 LPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRLHGEVIPsPDPGELAIVRRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd07078 96 PLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07078 176 VDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR-KGFFIEPTVFSNVTDDMRIA 318
Cdd:cd07078 255 FVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVDPDMPIA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNGR 397
Cdd:cd07078 335 QEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGGVKQSGIGR 414
|
410
....*....|....*...
gi 25777728 398 EMGEFGLREYSEVKTVTV 415
Cdd:cd07078 415 EGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
3-415 |
0e+00 |
|
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: 604.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIG 82
Cdd:cd07144 67 GEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 83 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDK 162
Cdd:cd07144 147 VCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 163 IAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVR 242
Cdd:cd07144 227 IAFTGSTATGRLVMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 243 RSVERAKRR-VVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIA 318
Cdd:cd07144 306 KFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGRE 398
Cdd:cd07144 386 KEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRE 465
|
410
....*....|....*..
gi 25777728 399 MGEFGLREYSEVKTVTV 415
Cdd:cd07144 466 LGEYGLETYTQTKAVHI 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-418 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 581.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:PLN02766 79 MSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:PLN02766 159 IGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:PLN02766 239 DKVSFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:PLN02766 319 VKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:PLN02766 399 EIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQG 478
|
410
....*....|....*...
gi 25777728 401 EFGLREYSEVKTVTVKIP 418
Cdd:PLN02766 479 MDALDKYLQVKSVVTPLY 496
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
1-413 |
0e+00 |
|
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: 581.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07119 56 LPAQERAALLFRIADKIREDAEELARLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07119 135 VGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07119 215 DLVSFTGGTATGRSIMRAAAG-NVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMR 316
Cdd:cd07119 294 VAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMR 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNG 396
Cdd:cd07119 374 IVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIG 453
|
410
....*....|....*..
gi 25777728 397 REMGEFGLREYSEVKTV 413
Cdd:cd07119 454 RELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1-413 |
0e+00 |
|
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: 573.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07112 45 LSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07112 125 LGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07112 205 DALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRI 317
Cdd:cd07112 285 FLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRI 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGR 397
Cdd:cd07112 365 AREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGR 444
|
410
....*....|....*.
gi 25777728 398 EMGEFGLREYSEVKTV 413
Cdd:cd07112 445 DKSLHALDKYTELKTT 460
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-417 |
0e+00 |
|
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: 570.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07115 38 MDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07115 118 VGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07115 198 DKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:cd07115 277 LERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:cd07115 357 EIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMG 436
|
410
....*....|....*..
gi 25777728 401 EFGLREYSEVKTVTVKI 417
Cdd:cd07115 437 REALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
1-415 |
0e+00 |
|
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: 570.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPF----LQAFYVdlqgvIKTFRYYAGWADKIHGMTIPVD-GDYFTF 75
Cdd:cd07114 40 LTPTERGKLLRRLADLIEANAEELAELETRDNGKLIretrAQVRYL-----AEWYRYYAGLADKIEGAVIPVDkGDYLNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 76 TRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07114 115 TRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07114 195 EHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNV 311
Cdd:cd07114 274 IYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGErpsgADLGAGYFFEPTILADV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 312 TDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFK 391
Cdd:cd07114 354 TNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFK 433
|
410 420
....*....|....*....|....
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07114 434 DSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
1-415 |
0e+00 |
|
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: 542.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07093 38 MSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07093 118 VGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07093 198 DLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMR 316
Cdd:cd07093 277 LERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNG 396
Cdd:cd07093 357 VAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIG 436
|
410
....*....|....*....
gi 25777728 397 REMGEFGLREYSEVKTVTV 415
Cdd:cd07093 437 REGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-416 |
0e+00 |
|
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: 525.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD----GDYFTFT 76
Cdd:cd07140 64 MNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIAS 156
Cdd:cd07140 144 KREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:cd07140 224 HPDVRKLGFTGSTPIGKHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMR 316
Cdd:cd07140 304 HDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMF 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSG 394
Cdd:cd07140 384 IAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSG 463
|
410 420
....*....|....*....|..
gi 25777728 395 NGREMGEFGLREYSEVKTVTVK 416
Cdd:cd07140 464 FGKDLGEEALNEYLKTKTVTIE 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-415 |
6.69e-176 |
|
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: 499.14 E-value: 6.69e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07090 38 TSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGI 160
Cdd:cd07090 117 LGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07090 196 AKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG-----RKGFFIEPTVFSNVTDDM 315
Cdd:cd07090 275 TERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGN 395
Cdd:cd07090 355 TIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGF 434
|
410 420
....*....|....*....|
gi 25777728 396 GREMGEFGLREYSEVKTVTV 415
Cdd:cd07090 435 GRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
2-415 |
7.24e-176 |
|
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: 499.95 E-value: 7.24e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI 81
Cdd:cd07559 58 SVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07559 138 GVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADA-----DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:cd07559 217 KLAFTGSTTVGRLIMQYAAE-NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVT 312
Cdd:cd07559 296 YDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlGGLDKGYFYEPTLIKGGN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 313 DDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKM 392
Cdd:cd07559 376 NDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKK 455
|
410 420
....*....|....*....|...
gi 25777728 393 SGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07559 456 SGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-415 |
1.24e-175 |
|
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: 498.30 E-value: 1.24e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:cd07109 39 LSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07109 118 HGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07109 198 DHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVG-SPFDPttEQGPQIDKKQYNKILELIQSGVAEGAKLECGG---KGLGRKGFFIEPTVFSNVTDDMR 316
Cdd:cd07109 277 LERLVERFRALRVGpGLEDP--DLGPLISAKQLDRVEGFVARARARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGN 395
Cdd:cd07109 355 LAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGH 434
|
410 420
....*....|....*....|
gi 25777728 396 GREMGEFGLREYSEVKTVTV 415
Cdd:cd07109 435 GREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
3-415 |
1.88e-172 |
|
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: 490.02 E-value: 1.88e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPI 81
Cdd:cd07103 40 ARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07103 119 GVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGK-LIQEAAgrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07103 199 KISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:cd07103 277 VEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:cd07103 357 ETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGG 436
|
410
....*....|....*
gi 25777728 401 EFGLREYSEVKTVTV 415
Cdd:cd07103 437 KEGLEEYLETKYVSL 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-415 |
1.48e-171 |
|
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: 488.00 E-value: 1.48e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHE 79
Cdd:cd07118 40 MSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd07118 119 PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07118 199 VDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIA 318
Cdd:cd07118 278 FVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGRE 398
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRE 437
|
410
....*....|....*..
gi 25777728 399 MGEFGLREYSEVKTVTV 415
Cdd:cd07118 438 LGRYGVEEYTELKTVHL 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1-415 |
3.93e-171 |
|
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: 483.66 E-value: 3.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHE 79
Cdd:cd06534 13 LPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPELPsPDPGGEAYVRRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd06534 92 PLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd06534 172 VDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVerakrrvvgspfdptteqgpqidkkqynkileliqsgvaegaklecggkglgrkgffiepTVFSNVTDDMRIAK 319
Cdd:cd06534 251 FVEKLV------------------------------------------------------------TVLVDVDPDMPIAQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 320 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMSGNGRE 398
Cdd:cd06534 271 EEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKNSGIGRE 350
|
410
....*....|....*..
gi 25777728 399 MGEFGLREYSEVKTVTV 415
Cdd:cd06534 351 GGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-414 |
2.97e-170 |
|
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: 485.08 E-value: 2.97e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLA---TMESlngGKPFLQAFYVDLQGVIKTFRYYAGWADKIHgMTIPVDGdyfTFTRHEPI 81
Cdd:cd07138 59 ERAALLERIAEAYEARADELAqaiTLEM---GAPITLARAAQVGLGIGHLRAAADALKDFE-FEERRGN---SLVVREPI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07138 132 GVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 241
Cdd:cd07138 212 MVSFTGSTRAGKRVAEAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIA 318
Cdd:cd07138 291 EIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNAQSPFGGFKMSGNGRE 398
Cdd:cd07138 371 REEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGRE 449
|
410
....*....|....*.
gi 25777728 399 MGEFGLREYSEVKTVT 414
Cdd:cd07138 450 WGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
3-414 |
1.17e-169 |
|
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: 483.01 E-value: 1.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIH---GMTIPVDGDYFT-FTRH 78
Cdd:cd07110 40 GAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHI 158
Cdd:cd07110 119 EPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 238
Cdd:cd07110 199 GIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIAD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 239 EFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMR 316
Cdd:cd07110 278 AFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNG 396
Cdd:cd07110 358 IWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIG 437
|
410
....*....|....*...
gi 25777728 397 REMGEFGLREYSEVKTVT 414
Cdd:cd07110 438 RELGEWGLDNYLEVKQIT 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
1-411 |
1.25e-168 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 480.85 E-value: 1.25e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEP 80
Cdd:TIGR01804 54 MSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:TIGR01804 134 LGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:TIGR01804 214 AKVSFTGGVPTGKKIMAAAA-GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERF 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMR 316
Cdd:TIGR01804 293 LARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNG 396
Cdd:TIGR01804 373 IVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIG 452
|
410
....*....|....*
gi 25777728 397 REMGEFGLREYSEVK 411
Cdd:TIGR01804 453 RENGKAALAHYTEVK 467
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-415 |
4.46e-168 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 480.53 E-value: 4.46e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLV-ERDRAvLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHE 79
Cdd:PRK13252 63 MTAMERSRILRRAVDILrERNDE-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIG 159
Cdd:PRK13252 142 PLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:PRK13252 221 IAKVSFTGGVPTGKKVMAAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDM 315
Cdd:PRK13252 300 FEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDM 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGN 395
Cdd:PRK13252 380 TIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGI 459
|
410 420
....*....|....*....|
gi 25777728 396 GREMGEFGLREYSEVKTVTV 415
Cdd:PRK13252 460 GRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-415 |
2.58e-163 |
|
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: 467.70 E-value: 2.58e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI 81
Cdd:cd07117 58 TVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07117 138 GVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 241
Cdd:cd07117 217 KLAFTGSTEVGRDVAIAAAK-KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRI 317
Cdd:cd07117 296 AKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGR 397
Cdd:cd07117 376 AQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGR 455
|
410
....*....|....*...
gi 25777728 398 EMGEFGLREYSEVKTVTV 415
Cdd:cd07117 456 ETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
4-415 |
7.67e-161 |
|
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: 460.64 E-value: 7.67e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGmtiPVDGDYF----TFTRHE 79
Cdd:cd07092 41 AERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRRE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEaGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd07092 118 PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07092 197 VRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIqSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAK 319
Cdd:cd07092 276 FVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 320 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREM 399
Cdd:cd07092 355 EEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDL 434
|
410
....*....|....*.
gi 25777728 400 GEFGLREYSEVKTVTV 415
Cdd:cd07092 435 SIYALEDYTRIKHVMV 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-413 |
3.95e-159 |
|
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: 456.70 E-value: 3.95e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHG-MTIPVDGDYFTFT--- 76
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 -RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07089 119 vRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07089 199 TDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK---GLGrKGFFIEPTVFSNVT 312
Cdd:cd07089 278 RYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGrpaGLD-KGFYVEPTLFADVD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 313 DDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKM 392
Cdd:cd07089 357 NDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQ 436
|
410 420
....*....|....*....|.
gi 25777728 393 SGNGREMGEFGLREYSEVKTV 413
Cdd:cd07089 437 SGLGRENGIEGLEEFLETKSI 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
4-417 |
1.24e-157 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 453.21 E-value: 1.24e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGmtiPVDGDY---FT-FTRHE 79
Cdd:PRK13473 61 KERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGEYlegHTsMIRRD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:PRK13473 138 PVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:PRK13473 217 VRMVSLTGSIATGKHVLSAAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEG-AKLECGGKGLGRKGFFIEPTVFSNVTDDMRIA 318
Cdd:PRK13473 296 LVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGRE 398
Cdd:PRK13473 376 QREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKD 455
|
410
....*....|....*....
gi 25777728 399 MGEFGLREYSEVKTVTVKI 417
Cdd:PRK13473 456 MSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-415 |
5.74e-156 |
|
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: 448.13 E-value: 5.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGwadkihgMTIPV-----DGDYFTFT 76
Cdd:cd07106 39 PLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTAS-------LDLPDeviedDDTRRVEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAAIAS 156
Cdd:cd07106 111 RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:cd07106 189 HPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMR 316
Cdd:cd07106 268 YDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNG 396
Cdd:cd07106 348 IVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIG 427
|
410
....*....|....*....
gi 25777728 397 REMGEFGLREYSEVKTVTV 415
Cdd:cd07106 428 VEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
1-413 |
4.74e-154 |
|
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: 444.00 E-value: 4.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHE 79
Cdd:cd07097 56 TSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTRE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd07097 135 PLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07097 215 VDAVSFTGSTAVGRRIAAAAA-ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRI 317
Cdd:cd07097 294 FVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRI 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNG 396
Cdd:cd07097 374 AREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYG 453
|
410
....*....|....*...
gi 25777728 397 -REMGEFGLREYSEVKTV 413
Cdd:cd07097 454 pREQGEAALEFYTTIKTV 471
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
1-409 |
5.01e-154 |
|
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: 444.53 E-value: 5.01e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIhgmtipvdgDYfTFTRHEP 80
Cdd:cd07111 78 LPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLL---------DT-ELAGWKP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGI 160
Cdd:cd07111 148 VGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEA-AGRSnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07111 227 DKVAFTGSTEVGRALRRAtAGTG--KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAK 319
Cdd:cd07111 305 LIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 320 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREM 399
Cdd:cd07111 385 EEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREG 464
|
410
....*....|
gi 25777728 400 GEFGLREYSE 409
Cdd:cd07111 465 GKEGLYEYLR 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
4-414 |
1.12e-150 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 436.86 E-value: 1.12e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHG-----MTIPVDgDYFTFTRH 78
Cdd:PLN02467 72 AVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAkqkapVSLPME-TFKGYVLK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHI 158
Cdd:PLN02467 150 EPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 238
Cdd:PLN02467 230 GVDKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIAS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 239 EFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMR 316
Cdd:PLN02467 309 EFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNG 396
Cdd:PLN02467 389 IWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFG 468
|
410
....*....|....*...
gi 25777728 397 REMGEFGLREYSEVKTVT 414
Cdd:PLN02467 469 RELGEWGLENYLSVKQVT 486
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
5-417 |
5.89e-149 |
|
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: 430.64 E-value: 5.89e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVC 84
Cdd:cd07107 42 ERARMLRELATRLREHAEELALIDALDCGNP-VSAMLGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 85 GQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIA 164
Cdd:cd07107 121 ARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 165 FTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEESIYEEFVRR 243
Cdd:cd07107 200 LIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLAR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 244 SVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAK 319
Cdd:cd07107 279 VVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 320 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREM 399
Cdd:cd07107 359 EEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREE 438
|
410
....*....|....*...
gi 25777728 400 GEFGLREYSEVKTVTVKI 417
Cdd:cd07107 439 CLEELLSYTQEKNVNVRL 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-415 |
1.37e-148 |
|
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: 430.07 E-value: 1.37e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG------WADKIHGMTIpvdGDyfT 74
Cdd:cd07139 57 LSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAAlardfpFEERRPGSGG---GH--V 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 75 FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAI 154
Cdd:cd07139 132 LVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 234
Cdd:cd07139 211 VRHPGVDKVSFTGSTAAGRRIAAVCGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK---GLGRkGFFIEPTVFSNV 311
Cdd:cd07139 290 SRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpaGLDR-GWFVEPTLFADV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 312 TDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYnALNAQSPFGGFK 391
Cdd:cd07139 369 DNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFK 447
|
410 420
....*....|....*....|....
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07139 448 QSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
1-415 |
8.80e-148 |
|
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: 427.40 E-value: 8.80e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-----DYFTF 75
Cdd:cd07149 40 LPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 76 TRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07149 119 TIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07149 199 TDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHED 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDM 315
Cdd:cd07149 276 IYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSG 394
Cdd:cd07149 353 KVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESG 432
|
410 420
....*....|....*....|.
gi 25777728 395 NGREMGEFGLREYSEVKTVTV 415
Cdd:cd07149 433 TGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
3-415 |
4.59e-147 |
|
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: 425.62 E-value: 4.59e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIG 82
Cdd:cd07108 40 ARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 83 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDK 162
Cdd:cd07108 120 VVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 163 IAFTGSTEVGKLI-QEAAGRsnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGV-FFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07108 199 VTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAE-GAKLECGGK----GLGRKGFFIEPTVFSNVTDDM 315
Cdd:cd07108 277 LEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEW 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN-CYNALNAQSpFGGFKMSG 394
Cdd:cd07108 357 RLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNqGGGQQPGQS-YGGFKQSG 435
|
410 420
....*....|....*....|..
gi 25777728 395 NGREMG-EFGLREYSEVKTVTV 415
Cdd:cd07108 436 LGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1-415 |
4.74e-147 |
|
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: 426.38 E-value: 4.74e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHE 79
Cdd:cd07131 56 VPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07131 215 VDVVSFTGSTEVGERIGETCARPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDM 315
Cdd:cd07131 294 FLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDM 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNAlNAQSPFGGFKMS 393
Cdd:cd07131 374 RIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKS 452
|
410 420
....*....|....*....|...
gi 25777728 394 GNG-REMGEFGLREYSEVKTVTV 415
Cdd:cd07131 453 GNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
1-415 |
4.32e-146 |
|
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: 422.32 E-value: 4.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGD-YFTFTRHE 79
Cdd:cd07104 19 TPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPRRPEGEILPSDVPgKESMVRRV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI-KEAGFPPGVINILPGYGPTAGAAIASHI 158
Cdd:cd07104 98 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIfEEAGLPKGVLNVVPGGGSEIGDALVEHP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 238
Cdd:cd07104 178 RVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 239 EFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIA 318
Cdd:cd07104 257 EFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT---YEGLFYQPTVLSDVTPDMPIF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMSGNGR 397
Cdd:cd07104 334 REEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHVPFGGVKASGGGR 413
|
410
....*....|....*...
gi 25777728 398 EMGEFGLREYSEVKTVTV 415
Cdd:cd07104 414 FGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
3-413 |
5.45e-145 |
|
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: 420.90 E-value: 5.45e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFT-FTRHEPI 81
Cdd:cd07088 56 AIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07088 135 GVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 241
Cdd:cd07088 215 MISLTGSTEAGQKIMEAAAE-NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFM 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKE 320
Cdd:cd07088 294 EKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 321 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 400
Cdd:cd07088 374 EIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADG 453
|
410
....*....|...
gi 25777728 401 EFGLREYSEVKTV 413
Cdd:cd07088 454 KHGLEEYLQTKVV 466
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
1-419 |
3.86e-143 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 416.90 E-value: 3.86e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWA-DKIHGMTIPVDgDYFTFT 76
Cdd:TIGR02299 57 LKAAERKRYLHKIADLIEQHADEIAVLECLDCGQPLRQT----RQQVIRAaenFRFFADKCeEAMDGRTYPVD-THLNYT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIAS 156
Cdd:TIGR02299 132 VRVPVGPVGLITPWNAPFMLSTWKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLIQeAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:TIGR02299 212 HPDVKAVSFTGETATGSIIM-RNGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG-------RKGFFIEPTVFS 309
Cdd:TIGR02299 291 AEDFVEKLVERVRAIRVGHPLDPETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 310 NVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGG 389
Cdd:TIGR02299 371 GADNHMRIAQEEIFGPVLTVIPFKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGG 450
|
410 420 430
....*....|....*....|....*....|....*
gi 25777728 390 FKMSGNGREMGEFGLREYSEVKTVTV-----KIPQ 419
Cdd:TIGR02299 451 VKASGIGREGGTYSFDFYTETKNVALalgphHIPK 485
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
3-415 |
3.47e-142 |
|
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: 413.26 E-value: 3.47e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPI 81
Cdd:cd07150 42 PSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07150 121 GVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 241
Cdd:cd07150 201 MVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRkgfFIEPTVFSNVTDDMRIAKEE 321
Cdd:cd07150 280 KKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 322 IFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNAL-NAQSPFGGFKMSGNGREMG 400
Cdd:cd07150 357 TFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGG 436
|
410
....*....|....*
gi 25777728 401 EFGLREYSEVKTVTV 415
Cdd:cd07150 437 EWSMEEFTELKWITV 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
1-415 |
2.15e-140 |
|
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: 408.66 E-value: 2.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-DY----FTF 75
Cdd:cd07145 40 LPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyEYnerrIAF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 76 TRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07145 119 TVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07145 199 TNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDM 315
Cdd:cd07145 278 VYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDM 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSG 394
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSG 435
|
410 420
....*....|....*....|.
gi 25777728 395 NGREMGEFGLREYSEVKTVTV 415
Cdd:cd07145 436 IGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
1-416 |
1.89e-137 |
|
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: 402.20 E-value: 1.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTI------PVDGDYFT 74
Cdd:cd07113 57 TTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 75 FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAI 154
Cdd:cd07113 137 FTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 234
Cdd:cd07113 216 ISHPDVAKVSFTGSVATGKKIGRQAA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDD 314
Cdd:cd07113 295 SKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSAD 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSG 394
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSG 454
|
410 420
....*....|....*....|..
gi 25777728 395 NGREMGEFGLREYSEVKTVTVK 416
Cdd:cd07113 455 IGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
4-413 |
4.77e-136 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 399.27 E-value: 4.77e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGV 83
Cdd:PRK09847 81 AKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 84 CGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKI 163
Cdd:PRK09847 161 IAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 164 AFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVR 242
Cdd:PRK09847 241 AFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 243 RSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGfFIEPTVFSNVTDDMRIAKEEI 322
Cdd:PRK09847 321 LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 323 FGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEF 402
Cdd:PRK09847 399 FGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLH 478
|
410
....*....|.
gi 25777728 403 GLREYSEVKTV 413
Cdd:PRK09847 479 ALEKFTELKTI 489
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
3-413 |
3.51e-135 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 397.14 E-value: 3.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPI 81
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 241
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEE 321
Cdd:PLN02278 321 EAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 322 IFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGE 401
Cdd:PLN02278 401 VFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSK 480
|
410
....*....|..
gi 25777728 402 FGLREYSEVKTV 413
Cdd:PLN02278 481 YGIDEYLEIKYV 492
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
3-415 |
5.00e-135 |
|
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: 396.05 E-value: 5.00e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIG 82
Cdd:cd07116 59 VAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 83 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDK 162
Cdd:cd07116 139 VVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 163 IAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFA------DADLDYAVEQAhqGVF-FNQGQCCTAGSRIFVEES 235
Cdd:cd07116 218 VAFTGETTTGRLIMQYASE-NIIPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQES 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNv 311
Cdd:cd07116 295 IYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnelGGLLGGGYYVPTTFKG- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 312 TDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFK 391
Cdd:cd07116 374 GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYK 453
|
410 420
....*....|....*....|....
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07116 454 QSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
4-415 |
2.46e-129 |
|
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: 379.50 E-value: 2.46e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY-VDLQGVIktFRYYAgwaDKIHGM----TIPVDGDYfTFTRH 78
Cdd:cd07100 21 AERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKCAWI--CRYYA---ENAEAFladePIETDAGK-AYVRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07100 95 EPLGVVLGIMPWNFPFwqvFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAIIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIgIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07100 172 DPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHED 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDM 315
Cdd:cd07100 250 VYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGN 395
Cdd:cd07100 330 PAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGY 409
|
410 420
....*....|....*....|
gi 25777728 396 GREMGEFGLREYSEVKTVTV 415
Cdd:cd07100 410 GRELGRFGIREFVNIKTVWV 429
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
1-417 |
4.97e-128 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 378.30 E-value: 4.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHG----MTIPVDGDYFTFT 76
Cdd:TIGR03216 56 MTVAERADLLYAVADEIERRFDDFLAAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTecfeMATPDGKGALNYA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGP-TAGAAIA 155
Cdd:TIGR03216 136 VRKPLGVVGVISPWNLPLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:TIGR03216 216 RHPGVDAITFTGETRTGSAIMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGG-----KGLGRKGFFIEPTVFSN 310
Cdd:TIGR03216 295 IFDRFVAALKARAESLKIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 311 VTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGF 390
Cdd:TIGR03216 375 LPDSARVVTEEIFGPCCHIAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGS 454
|
410 420
....*....|....*....|....*..
gi 25777728 391 KMSGNGREMGEFGLREYSEVKTVTVKI 417
Cdd:TIGR03216 455 KLSGIGREGGVHSLEFYTELTNVCIKL 481
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
2-415 |
1.51e-126 |
|
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: 373.60 E-value: 1.51e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI 81
Cdd:cd07120 40 DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEA-GFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07120 119 GVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEF 240
Cdd:cd07120 199 DVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 241 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAK-LECGGKGLGR--KGFFIEPTVFSNVTDDMRI 317
Cdd:cd07120 278 RDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGR 397
Cdd:cd07120 358 VQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGR 437
|
410
....*....|....*...
gi 25777728 398 EMGEFGLREYSEVKTVTV 415
Cdd:cd07120 438 LHGVAALEDFIEYKHIYL 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-417 |
4.72e-126 |
|
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: 374.25 E-value: 4.72e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI 81
Cdd:cd07124 89 PPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGID 161
Cdd:cd07124 168 GVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 162 KIAFTGSTEVGKLIQEAAGR-----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:cd07124 248 FIAFTGSREVGLRIYERAAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGK--GLGRKGFFIEPTVFSNVTDD 314
Cdd:cd07124 328 YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKM 392
Cdd:cd07124 407 HRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKM 486
|
410 420
....*....|....*....|....*.
gi 25777728 393 SG-NGREMGEFGLREYSEVKTVTVKI 417
Cdd:cd07124 487 SGtGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-415 |
2.78e-124 |
|
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: 368.43 E-value: 2.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPI 81
Cdd:cd07086 56 APRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGYGPtAGAAIASH 157
Cdd:cd07086 135 GVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGKLIQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY 237
Cdd:cd07086 214 PRVPLVSFTGSTEVGRRVGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDM 315
Cdd:cd07086 293 DEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAM--QAGTVWIN--CYNAlNAQSPFGGFK 391
Cdd:cd07086 373 RIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNipTSGA-EIGGAFGGEK 451
|
410 420
....*....|....*....|....
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07086 452 ETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
5-415 |
2.20e-121 |
|
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: 360.21 E-value: 2.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHE 79
Cdd:cd07094 44 ERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:cd07094 123 PVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADER 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:cd07094 203 VAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAK 319
Cdd:cd07094 280 FIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLST 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 320 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGRE 398
Cdd:cd07094 357 EETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGRE 436
|
410
....*....|....*..
gi 25777728 399 MGEFGLREYSEVKTVTV 415
Cdd:cd07094 437 GVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
4-415 |
3.43e-119 |
|
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: 354.61 E-value: 3.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKI-------HGMTIPVdgdyFTFT 76
Cdd:cd07099 40 EGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEVLLALEAIDWAARNAPRVlaprkvpTGLLMPN----KKAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 -RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07099 115 vEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALID 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 ShiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07099 195 A--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDM 315
Cdd:cd07099 272 VYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINC--YNALNAQSPFGGFKMS 393
Cdd:cd07099 352 DVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDS 431
|
410 420
....*....|....*....|..
gi 25777728 394 GNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07099 432 GGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
1-411 |
2.34e-116 |
|
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: 347.31 E-value: 2.34e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGD-----YFTF 75
Cdd:cd07147 40 LPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RGEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 76 TRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGygPTAGAAI- 154
Cdd:cd07147 119 VRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 234
Cdd:cd07147 197 VTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDD 314
Cdd:cd07147 274 SVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMS 393
Cdd:cd07147 351 MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDHmPYGGVKDS 430
|
410
....*....|....*...
gi 25777728 394 GNGREMGEFGLREYSEVK 411
Cdd:cd07147 431 GIGREGVRYAIEEMTEPR 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-415 |
6.93e-116 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 348.41 E-value: 6.93e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKI-----HGMTIPVDGDyfTFTR 77
Cdd:PRK09407 75 VRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE-EVLDVALTARYYARRAPKLlaprrRAGALPVLTK--TTEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASH 157
Cdd:PRK09407 152 RQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 igIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY 237
Cdd:PRK09407 232 --ADYLMFTGSTATGRVLAEQAGR-RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKG---LGrkGFFIEPTVFSNVTDD 314
Cdd:PRK09407 309 DEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKArpdLG--PLFYEPTVLTGVTPD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN-CYNALNA--QSPFGGFK 391
Cdd:PRK09407 387 MELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMK 466
|
410 420
....*....|....*....|....
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTV 415
Cdd:PRK09407 467 DSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
1-415 |
1.57e-115 |
|
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: 345.05 E-value: 1.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATM---ESlnGGKPFLQAFYVDLqgVIKTFRYYAGWADKIHGMTIPVDGDYFTFTR 77
Cdd:cd07152 32 TPPRERAAVLRRAADLLEEHADEIADWivrES--GSIRPKAGFEVGA--AIGELHEAAGLPTQPQGEILPSAPGRLSLAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI-KEAGFPPGVINILPGyGPTAGAAIAS 156
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLfEEAGLPAGVLHVLPG-GADAGEALVE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:cd07152 187 DPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMR 316
Cdd:cd07152 266 ADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTVLSGVKPGMP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMSGN 395
Cdd:cd07152 343 AFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGMGASGN 422
|
410 420
....*....|....*....|.
gi 25777728 396 G-REMGEFGLREYSEVKTVTV 415
Cdd:cd07152 423 GsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
1-416 |
1.95e-115 |
|
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: 345.44 E-value: 1.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP--VDGDYFTFTRh 78
Cdd:cd07151 51 TLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPsdVPGKENRVYR- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSA-LYMGALIKEAGFPPGVINILPGYGPTAGAAIASH 157
Cdd:cd07151 129 EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY 237
Cdd:cd07151 209 PVPRLISFTGSTPVGRHIGELAGR-HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVY 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRI 317
Cdd:cd07151 288 DEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGE---AEGNVLEPTVLSDVTNDMEI 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALN--AQSPFGGFKMSGN 395
Cdd:cd07151 365 AREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNdePHVPFGGEKNSGL 443
|
410 420
....*....|....*....|.
gi 25777728 396 GREMGEFGLREYSEVKTVTVK 416
Cdd:cd07151 444 GRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
1-415 |
3.13e-115 |
|
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: 343.79 E-value: 3.13e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVL-ATMESLNGGKPFLQAFYVDLqgVIKTFRYYAGWADKIHGMTIPVD--GDYfTFTR 77
Cdd:cd07105 19 TPPSERRDILLKAADLLESRRDEFiEAMMEETGATAAWAGFNVDL--AAGMLREAASLITQIIGGSIPSDkpGTL-AMVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINIL---PGYGPTAGAAI 154
Cdd:cd07105 96 KEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVEAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 234
Cdd:cd07105 176 IAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 SIYEEFVrrsvERAKRRVVGSPFDPTTEqGPQIDKKQYNKILELIQSGVAEGAKLECGGKG-LGRKGFFIEPTVFSNVTD 313
Cdd:cd07105 255 SIADEFV----EKLKAAAEKLFAGPVVL-GSLVSAAAADRVKELVDDALSKGAKLVVGGLAdESPSGTSMPPTILDNVTP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 314 DMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKM 392
Cdd:cd07105 330 DMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDePTLPHGGVKS 409
|
410 420
....*....|....*....|...
gi 25777728 393 SGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07105 410 SGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
1-416 |
1.34e-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: 341.09 E-value: 1.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWADKIHGMTIPVDGDYFT--- 74
Cdd:cd07082 58 MPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA----LKEVDRTidyIRDTIEELKRLDGDSLPGDWFPGTkgk 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 75 --FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGA 152
Cdd:cd07082 134 iaQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 153 AIASHIGIDKIAFTGSTEVGKLIQEAAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 232
Cdd:cd07082 214 PLVTHGRIDVISFTGSTEVGNRLKKQHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 233 EESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVT 312
Cdd:cd07082 291 HESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 313 DDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFK 391
Cdd:cd07082 369 PDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRK 448
|
410 420
....*....|....*....|....*
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTVK 416
Cdd:cd07082 449 DSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
4-415 |
2.52e-112 |
|
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: 336.97 E-value: 2.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKI-----HGMTIPVdgdyFTFTR- 77
Cdd:cd07101 40 AERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-EVLDVAIVARYYARRAERLlkprrRRGAIPV----LTRTTv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 -HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIAS 156
Cdd:cd07101 115 nRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 236
Cdd:cd07101 195 NA--DYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKG---LGRkgFFIEPTVFSNVTD 313
Cdd:cd07101 272 YDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRArpdLGP--YFYEPTVLTGVTE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 314 DMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN-CYNAL--NAQSPFGGF 390
Cdd:cd07101 350 DMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGM 429
|
410 420
....*....|....*....|....*
gi 25777728 391 KMSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07101 430 KDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-415 |
1.30e-109 |
|
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: 330.09 E-value: 1.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTR 77
Cdd:cd07146 39 RYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASH 157
Cdd:cd07146 118 REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY 237
Cdd:cd07146 198 PDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGkglGRKGFFIEPTVFSNVTDDMRI 317
Cdd:cd07146 275 DEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAEL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG 396
Cdd:cd07146 352 VTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLG 431
|
410 420
....*....|....*....|
gi 25777728 397 -REMGEFGLREYSEVKTVTV 415
Cdd:cd07146 432 gKEGVREAMKEMTNVKTYSL 451
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-394 |
3.37e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 331.13 E-value: 3.37e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYA----GWADKIHgmTIPVDGDYFTFtR 77
Cdd:PRK03137 93 SPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYArqmlKLADGKP--VESRPGEHNRY-F 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASH 157
Cdd:PRK03137 169 YIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDH 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGKLIQEAAGRSN-----LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 232
Cdd:PRK03137 249 PKTRFITFTGSREVGLRIYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 233 EESIYEEFVRRSVERAKRRVVGSPFDPtTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVT 312
Cdd:PRK03137 329 HEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 313 DDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGF 390
Cdd:PRK03137 407 PKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGF 486
|
....
gi 25777728 391 KMSG 394
Cdd:PRK03137 487 NMSG 490
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
10-413 |
2.27e-105 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 317.83 E-value: 2.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 10 LDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD---GDYFTFTRhePIGVCGQ 86
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 87 IIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFT 166
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 167 GSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVE 246
Cdd:PRK10090 158 GSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 247 RAKRRVVGSPFD-PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGP 325
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 326 VQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLR 405
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 25777728 406 EYSEVKTV 413
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
4-413 |
1.31e-102 |
|
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: 312.26 E-value: 1.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfyvdlQGVIKTF----RYYAGWADKIHGMTIPVDGDYFT-FTRH 78
Cdd:cd07102 40 EERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-----GGEIRGMleraRYMISIAEEALADIRVPEKDGFErYIRR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHI 158
Cdd:cd07102 115 EPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 gIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 238
Cdd:cd07102 195 -IDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 239 EFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDM 315
Cdd:cd07102 273 AFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGN 395
Cdd:cd07102 353 RVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGR 432
|
410
....*....|....*...
gi 25777728 396 GREMGEFGLREYSEVKTV 413
Cdd:cd07102 433 GVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-416 |
6.30e-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: 305.98 E-value: 6.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIG 82
Cdd:cd07085 60 LKRQQVMFKFRQLLEENLDELARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 83 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDK 162
Cdd:cd07085 139 VVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 163 IAFTGSTEVGKLIQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVR 242
Cdd:cd07085 218 VSFVGSTPVGEYIYERAAANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 243 RSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIA 318
Cdd:cd07085 297 KLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIY 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 319 KEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMS--GN 395
Cdd:cd07085 377 KEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPlAFFSFGGWKGSffGD 456
|
410 420
....*....|....*....|.
gi 25777728 396 GREMGEFGLREYSEVKTVTVK 416
Cdd:cd07085 457 LHFYGKDGVRFYTQTKTVTSR 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-417 |
3.80e-99 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 304.14 E-value: 3.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfyvdlQGVIKTFRYYAGW----ADKIHGMTIP-VDGDYFTF 75
Cdd:PRK11241 67 LTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeGKRIYGDTIPgHQADKRLI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 76 TRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIA 155
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:PRK11241 222 SNPLVRKLSFTGSTEIGRQLMEQCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDM 315
Cdd:PRK11241 301 VYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGN 395
Cdd:PRK11241 381 KVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGL 460
|
410 420
....*....|....*....|..
gi 25777728 396 GREMGEFGLREYSEVKTVTVKI 417
Cdd:PRK11241 461 GREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
4-415 |
5.68e-97 |
|
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: 298.06 E-value: 5.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvdlqGVIKTFryyagwADKI-----HG----MTIPVDGDYFT 74
Cdd:cd07098 40 AERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL----GEILVT------CEKIrwtlkHGekalRPESRPGGLLM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 75 FTR-----HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPG 145
Cdd:cd07098 110 FYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 146 YGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCT 225
Cdd:cd07098 190 LPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 226 AGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGF 301
Cdd:cd07098 268 GIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 302 FIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCY--N 379
Cdd:cd07098 348 YFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvN 427
|
410 420 430
....*....|....*....|....*....|....*.
gi 25777728 380 ALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07098 428 YYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
4-413 |
3.87e-92 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 285.48 E-value: 3.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAgwaDKIHGMTIPVDGDYFT------FTR 77
Cdd:PRK09406 45 AQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KAEALKCAKGFRYYA---EHAEALLADEPADAAAvgasraYVR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPgYGPTAGAAI 154
Cdd:PRK09406 121 YQPLGVVLAVMPWNFPLwqvVRFA---APALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 234
Cdd:PRK09406 197 LRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDD 314
Cdd:PRK09406 276 DVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSG 394
Cdd:PRK09406 356 MRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSG 435
|
410
....*....|....*....
gi 25777728 395 NGREMGEFGLREYSEVKTV 413
Cdd:PRK09406 436 YGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-414 |
1.03e-83 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 264.83 E-value: 1.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADKIHG---MTIPVDG-DYFTFTRheP 80
Cdd:cd07083 78 DRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYpavEVVPYPGeDNESFYV--G 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:cd07083 155 LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGR-----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07083 235 RGINFTGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDM 315
Cdd:cd07083 315 AYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMD--EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFK 391
Cdd:cd07083 394 RIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFK 473
|
410 420
....*....|....*....|....
gi 25777728 392 MSGNGREMGEFG-LREYSEVKTVT 414
Cdd:cd07083 474 LSGTNAKTGGPHyLRRFLEMKAVA 497
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
77-413 |
6.34e-80 |
|
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: 252.92 E-value: 6.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPL-LMFAwKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGygptaGAAIA 155
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFnLAFG-PLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 232
Cdd:cd07134 170 QALlelPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 233 EESIYEEFVRRsVERAKRRVVGSpfDPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKLECGGKgLGRKGFFIEPTVF 308
Cdd:cd07134 249 HESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 309 SNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKALTVSSamqAGTVWIN--CYNALNA 383
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDkanVNKVLARTS---SGGVVVNdvVLHFLNP 401
|
330 340 350
....*....|....*....|....*....|
gi 25777728 384 QSPFGGFKMSGNGREMGEFGLREYSEVKTV 413
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
78-413 |
3.08e-76 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 244.39 E-value: 3.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVInilpGYGPTAGAAIASH 157
Cdd:PRK13968 124 YRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVY----GWLNADNDGVSQM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIA---FTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 234
Cdd:PRK13968 200 INDSRIAavtVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDD 314
Cdd:PRK13968 279 GIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSG 394
Cdd:PRK13968 359 MTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSG 438
|
330
....*....|....*....
gi 25777728 395 NGREMGEFGLREYSEVKTV 413
Cdd:PRK13968 439 FGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
3-396 |
2.70e-75 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 241.94 E-value: 2.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTR 77
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPLVDA-KVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASH 157
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 igidKIA---FTGSTEVGKLIqeaagRSNLK---RVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIF 231
Cdd:cd07148 202 ----RVAffsFIGSARVGWML-----RSKLApgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 232 VEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFfiEPTVFSNV 311
Cdd:cd07148 273 VPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 312 TDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGF 390
Cdd:cd07148 351 PRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGR 430
|
....*.
gi 25777728 391 KMSGNG 396
Cdd:cd07148 431 RQSGYG 436
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
3-415 |
2.35e-73 |
|
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: 237.10 E-value: 2.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPI 81
Cdd:cd07130 55 APKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGyGPTAGAAIASH 157
Cdd:cd07130 134 GVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGKLI-QEAAGRsnLKRVTLELGGKSPNIIFADADLDYAVeqahQGVFF----NQGQCCTAGSRIFV 232
Cdd:cd07130 213 PRVPLVSFTGSTAVGRQVgQAVAAR--FGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 233 EESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSnVT 312
Cdd:cd07130 287 HESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 313 DDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINC-YNALNAQSPFGG 389
Cdd:cd07130 366 SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIgTSGAEIGGAFGG 445
|
410 420
....*....|....*....|....*.
gi 25777728 390 FKMSGNGREMGEFGLREYSEVKTVTV 415
Cdd:cd07130 446 EKETGGGRESGSDAWKQYMRRSTCTI 471
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
16-413 |
6.94e-73 |
|
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: 234.73 E-value: 6.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 16 LVERDRAVLATMES-LngGKPFLQAFYVDLQGVIKTFRYY----AGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPW 90
Cdd:cd07087 33 LTENEEEIAAALYAdL--GKPPAEAYLTEIAVVLGEIDHAlkhlKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 91 NFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGygptaGAAIASHI---GIDKIA 164
Cdd:cd07087 111 NYPLQL---ALAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-----GVEVATALlaePFDHIF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 165 FTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFvrrs 244
Cdd:cd07087 182 FTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDEL---- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 245 VERAKRRVV---GSPFDPTTEQGPQIDKKQYNKILELIQSGvaegaKLECGGkGLGRKGFFIEPTVFSNVTDDMRIAKEE 321
Cdd:cd07087 257 IEELKKAIKefyGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEERYIAPTILDDVSPDSPLMQEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 322 IFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREM 399
Cdd:cd07087 331 IFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLPFGGVGNSGMGAYH 410
|
410
....*....|....
gi 25777728 400 GEFGLREYSEVKTV 413
Cdd:cd07087 411 GKAGFDTFSHLKSV 424
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-420 |
1.97e-72 |
|
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: 235.94 E-value: 1.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADK-IHGMTIPVDGDYFTFTRHEPIGV 83
Cdd:cd07125 92 ERAEILEKAADLLEANRGELIALAAAEAGKTLADAD-AEVREAIDFCRYYAAQARElFSDPELPGPTGELNGLELHGRGV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 84 CGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKI 163
Cdd:cd07125 171 FVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 164 AFTGSTEVGKLIQEAagRSNLKRVTL----ELGGKspNIIFAD--ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY 237
Cdd:cd07125 251 IFTGSTETAKLINRA--LAERDGPILpliaETGGK--NAMIVDstALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEgAKLECGGKGLGRKGFFIEPTVFSNVTDDMRi 317
Cdd:cd07125 327 ERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 aKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFGGFK 391
Cdd:cd07125 405 -TTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFGGWG 481
|
410 420 430
....*....|....*....|....*....|..
gi 25777728 392 MSGNGREMGefG---LREYSEVKTVTVKIPQK 420
Cdd:cd07125 482 LSGTGPKAG--GpnyLLRFGNEKTVSLNTTAA 511
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
5-397 |
2.73e-70 |
|
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: 227.92 E-value: 2.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY--------VDLQgvIKTFRYYAGwaDKIHGMtipvdGDYFTFT 76
Cdd:cd07095 23 ERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAYHERTG--ERATPM-----AQGRAVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIAS 156
Cdd:cd07095 94 RHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETGEALAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLI-QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IY-EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFsNVTDD 314
Cdd:cd07095 252 AVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGII-DVTDA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcyNALNAQS---PFGGFK 391
Cdd:cd07095 331 ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN--RPTTGASstaPFGGVG 408
|
....*.
gi 25777728 392 MSGNGR 397
Cdd:cd07095 409 LSGNHR 414
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
2-413 |
2.47e-67 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 220.43 E-value: 2.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 2 DASERGRLLDKLADLVERDRAVLAtmESLN---GGKPFLQAFYVDLQGVIKTFRYY----AGW--ADKIHGMtipvdgdy 72
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALA--EAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWmkPSRRHVG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 73 FTFT------RHEPIGVCGQIIPWNFPL-LMFAWKIApALCCGNTVVIKPAEQTP-LSALyMGALIKEAgFPPGVINILP 144
Cdd:cd07133 88 LLFLpakaevEYQPLGVVGIIVPWNYPLyLALGPLIA-ALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 145 GyGPTAGAAIaSHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 224
Cdd:cd07133 165 G-GADVAAAF-SSLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 225 TAGSRIFVEESIYEEFVRRSVERAKRRVvgspfdPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKL-ECGGKG---- 295
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMY------PTLADNPDytsiINERHYARLQGLLEDARAKGARViELNPAGedfa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 296 LGRKgffIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKAL--TVSsamqa 370
Cdd:cd07133 316 ATRK---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDkaeQDRVLrrTHS----- 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 25777728 371 GTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 413
Cdd:cd07133 388 GGVTINdtLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
80-396 |
8.78e-67 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 220.78 E-value: 8.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIG 159
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGStEVGKLIQEAAGRSNLKrvtLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEE 239
Cdd:PLN00412 238 VNCISFTGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 240 FVRRSVERAKRRVVGSPFDpTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAK 319
Cdd:PLN00412 314 LVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAW 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777728 320 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNG 396
Cdd:PLN00412 390 EEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIG 467
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
74-413 |
1.06e-66 |
|
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: 218.63 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 74 TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAA 153
Cdd:cd07135 102 PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 154 IASHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVE 233
Cdd:cd07135 181 LEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 234 ESIYEEFVRRSvERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKLECGGKgLGRKGFFIEPTVFSNVTD 313
Cdd:cd07135 258 PSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGE-MDEATRFIPPTIVSDVSW 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 314 DMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN-------CYNAlnaqsP 386
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtlihvgVDNA-----P 407
|
330 340
....*....|....*....|....*..
gi 25777728 387 FGGFKMSGNGREMGEFGLREYSEVKTV 413
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
79-413 |
1.48e-65 |
|
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: 216.22 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIA 155
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 156 SHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:cd07136 175 QKF--DYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IYEEFVRRSVERAKRRVVGSPFDpTTEQGPQIDKKQYNKILELIQSGvaegaKLECGGKGlGRKGFFIEPTVFSNVTDDM 315
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDNG-----KIVFGGNT-DRETLYIEPTILDNVTWDD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcyNAL----NAQSPFGGFK 391
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTImhlaNPYLPFGGVG 402
|
330 340
....*....|....*....|..
gi 25777728 392 MSGNGREMGEFGLREYSEVKTV 413
Cdd:cd07136 403 NSGMGSYHGKYSFDTFSHKKSI 424
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
1-400 |
1.34e-64 |
|
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: 215.16 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADkihgmtipvdgDYFTFTRHEP 80
Cdd:TIGR01238 93 TPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI-AEVREAVDFCRYYAKQVR-----------DVLGEFSVES 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 81 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 160
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 161 DKIAFTGSTEVGKLIQEAAGRSNLKRVTL--ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 238
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVAD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 239 EFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEG---AKLECGGKGLGRKGFFIEPTVFSnvTDDM 315
Cdd:TIGR01238 321 RVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 316 RIAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFK 391
Cdd:TIGR01238 399 AELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQG 478
|
....*....
gi 25777728 392 MSGNGREMG 400
Cdd:TIGR01238 479 LSGTGPKAG 487
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-416 |
1.55e-62 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 208.97 E-value: 1.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGvIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIG 82
Cdd:TIGR01722 60 AQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARG-LEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 83 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDK 162
Cdd:TIGR01722 139 VCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 163 IAFTGSTEVGKLIQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFV 241
Cdd:TIGR01722 218 VSFVGSTPIGRYIHTTGSAHG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAaVLVGAA--DEWV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGF----FIEPTVFSNVTDDMRI 317
Cdd:TIGR01722 295 PEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSP---FGGFKMS- 393
Cdd:TIGR01722 375 YQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSf 452
|
410 420
....*....|....*....|....
gi 25777728 394 -GNGREMGEFGLREYSEVKTVTVK 416
Cdd:TIGR01722 453 fGDHHIYGKQGTHFYTRGKTVTTR 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-397 |
1.16e-59 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 201.73 E-value: 1.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY--------VDLQgvIKTFRYYAGwaDKIHGMtipvdGDYFTFT 76
Cdd:PRK09457 60 ERQAIVERFAALLEENKEELAEVIARETGKPLWEAATevtaminkIAIS--IQAYHERTG--EKRSEM-----ADGAAVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIAS 156
Cdd:PRK09457 131 RHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLI-QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 235
Cdd:PRK09457 210 HPDIDGLLFTGSANTGYLLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 236 IY-EEFVRRSVERAKRRVVGSPF-DPTTEQGPQIDKKQYNKILELIQSGVAEGAK----LECGGKGLGrkgfFIEPTVFs 309
Cdd:PRK09457 289 AQgDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKslleMTQLQAGTG----LLTPGII- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 310 NVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTV-WINCYNALNAQSPFG 388
Cdd:PRK09457 364 DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFG 443
|
....*....
gi 25777728 389 GFKMSGNGR 397
Cdd:PRK09457 444 GVGASGNHR 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-417 |
6.67e-58 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 204.66 E-value: 6.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQ--------AfyVDlqgviktF-RYYAGWADKIHGMTIPVDGdyf 73
Cdd:PRK11904 606 VEERAAILERAADLLEANRAELIALCVREAGKT-LQdaiaevreA--VD-------FcRYYAAQARRLFGAPEKLPG--- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 74 tFT------RHEPIGV--CgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPG 145
Cdd:PRK11904 673 -PTgesnelRLHGRGVfvC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPG 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 146 YGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGRSNlKRVTL--ELGGKspNIIFADAD------LDYAVEQAhqgv 216
Cdd:PRK11904 750 DGATVGAALTADPRIAGVAFTGSTETARIINRTlAARDG-PIVPLiaETGGQ--NAMIVDSTalpeqvVDDVVTSA---- 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 217 FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEG---AKLECGg 293
Cdd:PRK11904 823 FRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP- 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 294 kGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAG 371
Cdd:PRK11904 902 -AGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVG 978
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 25777728 372 TVWINcYNALNA----QsPFGGFKMSGNGREMGefG---LREYSEVKTVTVKI 417
Cdd:PRK11904 979 NVYVN-RNQIGAvvgvQ-PFGGQGLSGTGPKAG--GphyLLRFATEKTVTVNT 1027
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
1-394 |
1.43e-57 |
|
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: 197.04 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVE---RDRAVLATMesLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTiPVDGDYFTFTR 77
Cdd:cd07123 88 MPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 78 --HEPI-GVCGQIIPWNFPLLMFAWKIAPALCcGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAI 154
Cdd:cd07123 165 leYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGRS-----NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR 229
Cdd:cd07123 244 LASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 230 IFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAE-GAKLECGGKGLGRKGFFIEPTVF 308
Cdd:cd07123 324 AYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 309 snVTDD--MRIAKEEIFGPVQEILRFKTMD--EVIERANN-SDFGLVAAVFTND---INKALTVSSaMQAGTVWIN--CY 378
Cdd:cd07123 404 --ETTDpkHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTtSPYALTGAIFAQDrkaIREATDALR-NAAGNFYINdkPT 480
|
410
....*....|....*.
gi 25777728 379 NALNAQSPFGGFKMSG 394
Cdd:cd07123 481 GAVVGQQPFGGARASG 496
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-414 |
3.99e-57 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 197.66 E-value: 3.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIG 82
Cdd:PLN02419 173 TTRQRVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 83 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGaAIASHIGIDK 162
Cdd:PLN02419 252 VCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 163 IAFTGSTEVGKLIQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFV 241
Cdd:PLN02419 331 VSFVGSNTAGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 242 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRI 317
Cdd:PLN02419 408 DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMEC 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 318 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSPFGGF-----KM 392
Cdd:PLN02419 488 YKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgnkaSF 565
|
410 420
....*....|....*....|..
gi 25777728 393 SGNGREMGEFGLREYSEVKTVT 414
Cdd:PLN02419 566 AGDLNFYGKAGVDFFTQIKLVT 587
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
3-396 |
5.44e-57 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 202.09 E-value: 5.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFL-------QAfyVDlqgviktF-RYYAGWADKIHGMTipvdgdyft 74
Cdd:COG4230 614 VEERAAILERAADLLEAHRAELMALLVREAGKTLPdaiaevrEA--VD-------FcRYYAAQARRLFAAP--------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 75 fTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAI 154
Cdd:COG4230 676 -TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAAL 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEA-AGRSNlKRVTL--ELGGKspNIIFADADldyA-VEQAHQGV----FFNQGQCCTA 226
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLINRTlAARDG-PIVPLiaETGGQ--NAMIVDSS---AlPEQVVDDVlasaFDSAGQRCSA 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 227 gSRI-FVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIE 304
Cdd:COG4230 829 -LRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVA 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 305 PTVFSnvTDDMRIAKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFT-NDiNKALTVSSAMQAGTVWINcYNAL 381
Cdd:COG4230 908 PTLIE--IDSISDLEREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSrID-ETIDRVAARARVGNVYVN-RNII 983
|
410
....*....|....*....
gi 25777728 382 NA----QsPFGGFKMSGNG 396
Cdd:COG4230 984 GAvvgvQ-PFGGEGLSGTG 1001
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
74-416 |
4.07e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 192.55 E-value: 4.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 74 TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAA 153
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 154 IASHiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVE 233
Cdd:PTZ00381 181 LLKE-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 234 ESIYEEFVrRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKLECGGKgLGRKGFFIEPTVFSNVTD 313
Cdd:PTZ00381 259 RSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 314 DMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFK 391
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVG 413
|
330 340
....*....|....*....|....*
gi 25777728 392 MSGNGREMGEFGLREYSEVKTVTVK 416
Cdd:PTZ00381 414 NSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
3-396 |
1.41e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 192.39 E-value: 1.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF-----YVDlqgviktF-RYYAGWADkihgmtipvdgDYFTFT 76
Cdd:PRK11905 611 AAERAAILERAADLMEAHMPELFALAVREAGKTLANAIaevreAVD-------FlRYYAAQAR-----------RLLNGP 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 77 RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIAS 156
Cdd:PRK11905 673 GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGKLIQEA-AGRSNlKRVTL--ELGGKSPNIIFADAdldyAVEQAHQGV----FFNQGQCCTAGSR 229
Cdd:PRK11905 753 DPRIAGVMFTGSTEVARLIQRTlAKRSG-PPVPLiaETGGQNAMIVDSSA----LPEQVVADViasaFDSAGQRCSALRV 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 230 IFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVF 308
Cdd:PRK11905 828 LCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLI 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 309 SnvTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA--- 383
Cdd:PRK11905 908 E--IDSISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvg 984
|
410
....*....|....
gi 25777728 384 -QsPFGGFKMSGNG 396
Cdd:PRK11905 985 vQ-PFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
3-415 |
1.44e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.10 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKpFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPI 81
Cdd:PLN02315 77 APKRGEIVRQIGDALRAKLDYLGRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 GVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGyGPTAGAAIASH 157
Cdd:PLN02315 156 GIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGKLIQEAAgRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY 237
Cdd:PLN02315 235 TRIPLVSFTGSSKVGLMVQQTV-NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGP---QIDKKQYNKILELIQSgvaEGAKLECGGKGLGRKGFFIEPTVFSnVTDD 314
Cdd:PLN02315 314 DDVLEQLLTVYKQVKIGDPLEKGTLLGPlhtPESKKNFEKGIEIIKS---QGGKILTGGSAIESEGNFVQPTIVE-ISPD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKALTVSSAmQAGTVWINC-YNALNAQSPFGGF 390
Cdd:PLN02315 390 ADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNpetIFKWIGPLGS-DCGIVNVNIpTNGAEIGGAFGGE 468
|
410 420
....*....|....*....|....*
gi 25777728 391 KMSGNGREMGEFGLREYSEVKTVTV 415
Cdd:PLN02315 469 KATGGGREAGSDSWKQYMRRSTCTI 493
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
4-396 |
2.41e-48 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 177.09 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 4 SERGRLLDKLADLVErdravlATMESLNG------GKPFLQAF-----YVDLqgviktFRYYAGWADkihgmtipvdgDY 72
Cdd:PRK11809 704 AERAAILERAADLME------AQMQTLMGllvreaGKTFSNAIaevreAVDF------LRYYAGQVR-----------DD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 73 FTFTRHEPIG--VCgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTA 150
Cdd:PRK11809 761 FDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETV 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 151 GAAIASHIGIDKIAFTGSTEVGKLIQEA-AGR-SNLKRVT---LELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCT 225
Cdd:PRK11809 839 GAALVADARVRGVMFTGSTEVARLLQRNlAGRlDPQGRPIpliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCS 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 226 AGSRIFVEESIYEefvrRSVERAK----RRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAK---LECGGKGLGR 298
Cdd:PRK11809 919 ALRVLCLQDDVAD----RTLKMLRgamaECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQ 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 299 KGFFIEPTVFS-NVTDDMriaKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTN-DINKALTVSSAmQAGTVW 374
Cdd:PRK11809 995 SGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRiDETIAQVTGSA-HVGNLY 1070
|
410 420
....*....|....*....|....*.
gi 25777728 375 INcYNALNA----QsPFGGFKMSGNG 396
Cdd:PRK11809 1071 VN-RNMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
75-416 |
1.92e-46 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 165.47 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 75 FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI-----KEAgFPpgVInilpgygpT 149
Cdd:cd07132 95 YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC-YP--VV--------L 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 150 AGAAIASHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTA 226
Cdd:cd07132 164 GGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 227 GSRIFVEESIYEEFvrrsVERAKRRVV---GSpfDPTTEQ--GPQIDKKQYNKILELIQSG-VA---EGAKLECggkglg 297
Cdd:cd07132 243 PDYVLCTPEVQEKF----VEALKKTLKefyGE--DPKESPdyGRIINDRHFQRLKKLLSGGkVAiggQTDEKER------ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 298 rkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKALTVSSamqAGTVw 374
Cdd:cd07132 311 ----YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNkkvINKILSNTS---SGGV- 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 25777728 375 inCYNALNAQS-----PFGGFKMSGNGREMGEFGLREYSEVKTVTVK 416
Cdd:cd07132 383 --CVNDTIMHYtldslPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
79-413 |
1.99e-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: 151.79 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAAIASHi 158
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF-FNQGQCCTAGSRIFVEESIY 237
Cdd:cd07137 177 KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRrsverAKRRVVGSPF--DP-TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGkGLGRKGFFIEPTVFSNVTDD 314
Cdd:cd07137 256 PTLID-----ALKNTLEKFFgeNPkESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG-ERDEKNLYIEPTILLDPPLD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 315 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNdiNKALT--VSSAMQAGTVWIN--CYNALNAQSPFGGF 390
Cdd:cd07137 330 SSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK--NKELKrrIVAETSSGGVTFNdtVVQYAIDTLPFGGV 407
|
330 340
....*....|....*....|...
gi 25777728 391 KMSGNGREMGEFGLREYSEVKTV 413
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
3-396 |
3.04e-34 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 132.36 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 3 ASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyvDLQGVIKTFRYYA--GWADKIHGMTIPVDGDYFTFTRHE- 79
Cdd:cd07084 20 LPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPHEPGNHLGQGLKQQSHGy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 --PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILPGYGPTaGAAIAS 156
Cdd:cd07084 98 rwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-MQALLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 157 HIGIDKIAFTGSTEVGkliqeAAGRSNLK--RVTLELGGKSPNIIFADAD-LDYAVEQAHQGVFFNQGQCCTAGSRIFVE 233
Cdd:cd07084 177 HPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 234 ESIY-EEFVRRSVERAKRRVVGspfdpTTEQGPQidkkQYNKILELIQSGVAE-GAKLECGGKGLGRK------GFFIEP 305
Cdd:cd07084 252 ENWSkTPLVEKLKALLARRKLE-----DLLLGPV----QTFTTLAMIAHMENLlGSVLLFSGKELKNHsipsiyGACVAS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 306 TVFSNVTDDMRIAK---EEIFGPVQEILRFK-----TMDEVIERANNSdfgLVAAVFTNDInkalTVSSAMqAGTVWINC 377
Cdd:cd07084 323 ALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSNDP----IFLQEL-IGNLWVAG 394
|
410
....*....|....*....
gi 25777728 378 YNALNAQSPFGGFKMSGNG 396
Cdd:cd07084 395 RTYAILRGRTGVAPNQNHG 413
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
5-405 |
2.38e-32 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 128.28 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 5 ERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI--- 81
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 82 -------GVCGQIIPWNFPllmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILPGygpt 149
Cdd:PRK11903 143 hvlvptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 150 AGAAIASHIG-IDKIAFTGSTEVGKLIQE--AAGRSNLkRVTLELGGKSPNIIFADAD-----LDYAVEQAHQGVFFNQG 221
Cdd:PRK11903 215 SSAGLLDHLQpFDVVSFTGSAETAAVLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 222 QCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQsGVAEGAKLECGGKGLG---- 297
Cdd:PRK11903 294 QKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvda 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 298 --RKGFFIEPTVF-SNVTDDMRIAKE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI--------------N 359
Cdd:PRK11903 373 dpAVAACVGPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshG 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 25777728 360 KALTVSSAMQA-----GTVWincynalnAQSPFGGFKMSGNGREMGefGLR 405
Cdd:PRK11903 453 RVHVISPDVAAlhtghGNVM--------PQSLHGGPGRAGGGEELG--GLR 493
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
79-414 |
2.30e-30 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 122.14 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKeAGFPPGVINILPGyGPTAGAAIASHi 158
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNI---IFADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEE 234
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 235 siyeEFVRRSVERAK---RRVVGSPFDPTTEQGPQIDKKQYNKILEL-----IQSGVAEGAKLEcggkglgRKGFFIEPT 306
Cdd:PLN02203 263 ----RFAPILIELLKstiKKFFGENPRESKSMARILNKKHFQRLSNLlkdprVAASIVHGGSID-------EKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 307 VFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNA 383
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaiIQYACDS 411
|
330 340 350
....*....|....*....|....*....|.
gi 25777728 384 qSPFGGFKMSGNGREMGEFGLREYSEVKTVT 414
Cdd:PLN02203 412 -LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
79-413 |
5.85e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 118.22 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIkEAGFPPGVINILPGYGPTAGAAIASHi 158
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQK- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 159 gIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF-FNQGQCCTAGSRIFVEESiY 237
Cdd:PLN02174 189 -WDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKE-Y 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 238 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI-QSGVAEgaKLECGGKGlGRKGFFIEPTVFSNVTDDMR 316
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLdEKEVSD--KIVYGGEK-DRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 317 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNAQsPFGGFKMS 393
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHTL-PFGGVGES 421
|
330 340
....*....|....*....|
gi 25777728 394 GNGREMGEFGLREYSEVKTV 413
Cdd:PLN02174 422 GMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
1-405 |
2.61e-26 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 110.82 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 1 MDASERGRLLDKLADLVERDRAVLATMESLNGGKpfLQAFYVDLQGVIKTFRYYAGWADK--------IHGMTIPVDGDY 72
Cdd:cd07128 56 LTFHERAAMLKALAKYLMERKEDLYALSAATGAT--RRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 73 FTFTRH--EPI-GVCGQIIPWNFPllmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILP 144
Cdd:cd07128 134 TFVGQHilTPRrGVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLIC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 145 GygptAGAAIASHIGI-DKIAFTGSTEVG-KL-----IQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF 217
Cdd:cd07128 210 G----SVGDLLDHLGEqDVVAFTGSAATAaKLrahpnIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 218 FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN----KILELIQSG-VAEGAKLECG 292
Cdd:cd07128 286 VKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREdvraAVATLLAEAeVVFGGPDRFE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 293 GKGLGR-KGFFIEPTVF-SNVTDDMRIAKE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQ 369
Cdd:cd07128 366 VVGADAeKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAA 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 25777728 370 A--GTVWINcyNALNAQ------SPF-----GGFKMSGNGREMGefGLR 405
Cdd:cd07128 446 PyhGRLLVL--NRDSAKestghgSPLpqlvhGGPGRAGGGEELG--GLR 490
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
80-359 |
2.80e-16 |
|
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: 80.62 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 80 PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGaAIASHIG 159
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 160 IDKIAFTGSTEVG-KLIQEAAGrsnlkRVTLELGGKSPNIIFAD-ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES-I 236
Cdd:cd07126 221 PRMTLFTGSSKVAeRLALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 237 YEEFVRRSVERAKRR-----VVGSPFDPTTEqgpqidkkqynKILELIQSGVA-EGAKLECGGKGLGRKGF-----FIEP 305
Cdd:cd07126 296 QAGILDKLKALAEQRkledlTIGPVLTWTTE-----------RILDHVDKLLAiPGAKVLFGGKPLTNHSIpsiygAYEP 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25777728 306 T-VF-----SNVTDDMRIAKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDIN 359
Cdd:cd07126 365 TaVFvpleeIAIEENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIR 426
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
91-343 |
4.63e-14 |
|
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: 73.73 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 91 NFPllmFAWKI-----APALCCGNTVVIK-----PAeqtpLSALYMGAL---IKEAGFPPGVINILPGYGPTAGAAIASH 157
Cdd:cd07129 116 NFP---LAFSVaggdtASALAAGCPVVVKahpahPG----TSELVARAIraaLRATGLPAGVFSLLQGGGREVGVALVKH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 158 IGIDKIAFTGSTEVGK-LIQEAAGRSNLKRVTLELGGKSPNIIFADAdLDYAVEQAHQG----VFFNQGQCCTAGSRIFV 232
Cdd:cd07129 189 PAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGSVNPVFILPGA-LAERGEAIAQGfvgsLTLGAGQFCTNPGLVLV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 233 EESiyEEFvRRSVERAKRRVVGSPFDPTTEQGpqidkkqynkILELIQSGVAE----GAKLECGGKGLGRKGFFIEPTVF 308
Cdd:cd07129 268 PAG--PAG-DAFIAALAEALAAAPAQTMLTPG----------IAEAYRQGVEAlaaaPGVRVLAGGAAAEGGNQAAPTLF 334
|
250 260 270
....*....|....*....|....*....|....*...
gi 25777728 309 SNVTDDMR---IAKEEIFGPVQEILRFKTMDEVIERAN 343
Cdd:cd07129 335 KVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
48-376 |
5.00e-12 |
|
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: 67.25 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 48 IKTFRYYAGWADKIHGMTIPVDGDyfTFTRHEPIGVCGQIIPWNFPLLMFAwKIAPALCCGNTVVIKPAEQTPLSALYMg 127
Cdd:cd07077 70 IDTERGITASVGHIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 128 ALIKEAGFPPGVINILPGYGPTAGAAIA----SHIGIDKIAFTGSTEVGKLIQEAagrSNLKRVTLELGGKSPNIIFADA 203
Cdd:cd07077 146 ALLFQAADAAHGPKILVLYVPHPSDELAeellSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 204 DLDYAVEQAHQGVFFNQGQCctagsriFVEESIYeefvrrsverakrrVVGSPFDPTTEQgpqidkkqynkileLIQSGV 283
Cdd:cd07077 223 DEERASGSVHDSKFFDQNAC-------ASEQNLY--------------VVDDVLDPLYEE--------------FKLKLV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 284 AEGAKLECGGKGLgrkgffieptvFSNVTDDMRIAKEEIFGPVQeiLRFKTMDEVIERANNSDF------GLVAAVFTND 357
Cdd:cd07077 268 VEGLKVPQETKPL-----------SKETTPSFDDEALESMTPLE--CQFRVLDVISAVENAWMIiesgggPHTRCVYTHK 334
|
330
....*....|....*....
gi 25777728 358 INKALTVSSAMQAGTVWIN 376
Cdd:cd07077 335 INKVDDFVQYIDTASFYPN 353
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
69-376 |
1.65e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 56.12 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 69 DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP----AEQTPLSALYMGALIKEAGFPPGVINILP 144
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 145 GYGPTAGAAIASHIGIDKIAFTGSTEVGKliqeaAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 224
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 225 TAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE-------QGPQIDKKQYNKILELIQSGVAEGAKLecggkglg 297
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPvilkngdVNRDIVGQDAYKIAAAAGLKVPQETRI-------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 298 rkgFFIEPTVFsnvtDDMRIAKEEIFGPVQEILRFKTMDEVIERA----NNSDFGLVAAVFTNDINKALTV---SSAMQA 370
Cdd:cd07081 311 ---LIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENMnqfANAMKT 383
|
....*.
gi 25777728 371 GTVWIN 376
Cdd:cd07081 384 SRFVKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
79-377 |
8.69e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.95 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 79 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP---AEQTPLSAL-YMGALIKEAGFPPGVINILPGygPT--AGA 152
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEE--PSieLTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 153 AIASHIGIDKIAFTGSTEVGKliqeAAGRSNlkrvTLELG---GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR 229
Cdd:cd07122 172 ELMKHPDVDLILATGGPGMVK----AAYSSG----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 230 IFVEESIYEEFVRRSVER--------AKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL---ECGGKGLGr 298
Cdd:cd07122 244 VIVDDEIYDEVRAELKRRgayflneeEKEKLEKALFDDGGTLNPDIVGKSAQKIAELAGIEVPEDTKVlvaEETGVGPE- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 299 kgffiEPtvFSNvtddmriakeEIFGPVQEILRFKTMDEVIERA----NNSDFGLVAAVFTNDINKALTVSSAMQAGTVW 374
Cdd:cd07122 323 -----EP--LSR----------EKLSPVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSRIL 385
|
...
gi 25777728 375 INC 377
Cdd:cd07122 386 VNT 388
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
65-342 |
1.51e-05 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 46.85 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 65 TIPVDGDY-FTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP---AEQTPLSALYM-GALIKEAGFPPGV 139
Cdd:cd07121 81 TTAWSGDNgLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELiNKAIAEAGGPDNL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 140 INILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKliqeaAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFN 219
Cdd:cd07121 161 VVTVEEPTIETTNELMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 220 QGQCCTAGSRIFVEESIYEEFVRR------------SVERAKRRVVgspfdpTTEQGPQIDK----KQYNKILELIqsGV 283
Cdd:cd07121 236 NNLPCIAEKEVIAVDSVADYLIAAmqrngayvlndeQAEQLLEVVL------LTNKGATPNKkwvgKDASKILKAA--GI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777728 284 AEGAKLECggkglgrkgffieptVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERA 342
Cdd:cd07121 308 EVPADIRL---------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
84-232 |
6.59e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 45.16 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777728 84 CGQIIPWNFPLLMFAwkiapALCCGNTVVIKPAeqtPLSALYMG-------ALIKEAGFPPGVInILPGYGPTAGAA--I 154
Cdd:cd07127 202 CSTFPTWNGYPGLFA-----SLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFDPNLV-TLAADTPEEPIAqtL 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777728 155 ASHIGIDKIAFTGSTEVGKLIQEAAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 232
Cdd:cd07127 273 ATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV 347
|
|
| |
