|
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 ... |
14-494 |
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: 1036.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 14 QPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLAD 93
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 94 LIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLL 173
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 174 MQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVI 253
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 254 QVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGN 333
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 334 PFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTI 413
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 414 EEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
1O00_H 494 K 494
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
17-493 |
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: 935.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 17 VFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSpWRRMDASHRGRLLNRLADLIE 96
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 97 RDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQA 176
Cdd:cd07091 80 RDRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 177 WKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVA 256
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 257 AGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFD 336
Cdd:cd07091 240 AAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 337 SKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEV 416
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 417 VGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
20-491 |
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: 771.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 20 NQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGsPWRRMDASHRGRLLNRLADLIERDR 99
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 100 TYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGS 259
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 260 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKT 339
Cdd:cd07142 243 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 340 EQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGR 419
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1O00_H 420 ANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07142 403 ANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-499 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 753.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 3 AATQAVPAPNQQP-EVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGsPWRRMDA 81
Cdd:PLN02466 40 TAAAAVEEPITPPvQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 82 SHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGV 161
Cdd:PLN02466 119 YERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 162 CGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKV 241
Cdd:PLN02466 199 AGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 242 AFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVER 321
Cdd:PLN02466 279 AFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 322 SVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIF 401
Cdd:PLN02466 359 AKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIF 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 402 GPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYG 481
Cdd:PLN02466 439 GPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYS 518
|
490
....*....|....*...
1O00_H 482 LQAYTEVKTVTvkVPQKN 499
Cdd:PLN02466 519 LNNYLQVKAVV--TPLKN 534
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-495 |
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: 700.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 22 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgSPWRR-MDASHRGRLLNRLADLIERDRT 100
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 180
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 181 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSS 260
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 261 NLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTE 340
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 341 QGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRA 420
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1O00_H 421 NNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKV 495
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-493 |
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: 693.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 22 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgSPWRRMDASHRGRLLNRLADLIERDRTY 101
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 102 LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 181
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 182 ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsSN 261
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 262 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSR-VVGNPFDSKTE 340
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 341 QGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAAD---RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVV 417
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1O00_H 418 GRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
21-494 |
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: 678.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:COG1012 84 ELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGs 259
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 260 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKT 339
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 340 EQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAAD-RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVG 418
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 419 RANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-496 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 668.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 15 PEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGsPWRRMDASHRGRLLNRLADL 94
Cdd:PLN02766 16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 95 IERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLM 174
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 175 QAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQ 254
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 255 VAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNP 334
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 335 FDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIE 414
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 415 EVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
..
1O00_H 495 VP 496
Cdd:PLN02766 495 LY 496
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
28-491 |
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: 663.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 28 WHDAVSrKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALET 107
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 108 LDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGN 187
Cdd:pfam00171 77 LENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 188 VVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTL 267
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 268 ELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDE 347
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 348 TQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGL 427
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1O00_H 428 AAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-491 |
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: 636.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlGSPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 182
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 183 LATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSSNL 262
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAA-AGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 263 KRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQG 342
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 343 PQVDETQFKKILGYINTGKQEGAKLLCGG----GIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVG 418
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1O00_H 419 RANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-493 |
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: 631.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 60 DKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYViSYLVDLDMVLKCLRYYAGWADKY 139
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 140 HGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVV 218
Cdd:cd07078 77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 219 NIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQ 298
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 299 GQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGI-AADR 377
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 378 GYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYD 457
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
1O00_H 458 VFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07078 396 VGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
35-491 |
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: 623.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 35 KTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSpWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPY 114
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 115 VISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSP 274
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDA-DMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKI 353
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 354 LGYINTGKQEGAKLLCGGGI--AADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAV 431
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 432 FTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-495 |
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: 619.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISY 118
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 198
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 199 LTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVI-QVAAGssNLKRVTLELGGKSPNII 277
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKImQGAAG--NLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 278 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYI 357
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 358 NTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLD 437
Cdd:cd07115 316 DVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1O00_H 438 KANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKV 495
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-493 |
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: 608.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYV--- 115
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRetr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 116 --ISYLVDldmvlkCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMK 192
Cdd:cd07114 80 aqVRYLAE------WYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 193 VAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsSNLKRVTLELGGK 272
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 273 SPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKK 352
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 353 ILGYINTGKQEGAKLLCGGGIAA----DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLA 428
Cdd:cd07114 313 VERYVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1O00_H 429 AAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-493 |
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: 579.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISY 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 198
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 199 LTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQvAAGSSNLKRVTLELGGKSPNIIM 278
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIM-RAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 279 SDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYIN 358
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 359 TGKQEGAKLLCGGG----IAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTK 434
Cdd:cd07093 317 LARAEGATILTGGGrpelPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 435 DLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-493 |
0e+00 |
|
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: 577.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 180
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 181 PALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSS 260
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA-AE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 261 NLKRVTLELGGKSPNIIMSDA-----DMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPF 335
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 336 DSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAA----DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFK 411
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTlgglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 412 TIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
1O00_H 492 TV 493
Cdd:cd07559 477 LV 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
20-494 |
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: 555.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 20 NQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlGSPWRRMDASHRGRLLNRLADLIERDR 99
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 100 TYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPID----GDFFSYTRHEPVGVCGQIIPWNFPLLMQ 175
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 176 AWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQV 255
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 256 AAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPF 335
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 336 DSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKT--I 413
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 414 EEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
1O00_H 494 K 494
Cdd:cd07140 485 E 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-493 |
0e+00 |
|
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: 549.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISy 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 198
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 199 LTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIM 278
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAA-AKGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 279 SDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYIN 358
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 359 TGKQEGAKLLCGGGIAA-----DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFT 433
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 434 KDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-493 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 541.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLI-ERDR 99
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 100 TyLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:PRK13252 85 E-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEDVDKVAFTGSTEIGRVIQVAAGS 259
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 260 SnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKT 339
Cdd:PRK13252 243 S-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 340 EQGPQVDETQFKKILGYINTGKQEGAKLLCGG----GIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEE 415
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGerltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1O00_H 416 VVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-489 |
0e+00 |
|
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: 534.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ---GEWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 182
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 183 LATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIqVAAGSSNL 262
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKI-MAAAAGHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 263 KRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQG 342
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 343 PQVDETQFKKILGYINTGKQEGAKLLCGGGI----AADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVG 418
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRpenvGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1O00_H 419 RANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVK 489
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-493 |
0e+00 |
|
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: 527.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 180
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 181 PALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSS 260
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA-AK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 261 NLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTE 340
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 341 QGPQVDETQFKKILGYINTGKQEGAKLLCGG----GIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEV 416
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 417 VGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-493 |
0e+00 |
|
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: 526.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYl 119
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 199
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 200 TALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsSNLKRVTLELGGKSPNIIMS 279
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 280 DADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSkTEQGPQVDETQFKKILGYINT 359
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 360 GKQEGAKLLCGGGIAADR---GYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDL 436
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1O00_H 437 DKANYLSQALQAGTVWVNCY-DVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-492 |
0e+00 |
|
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: 524.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyVISY 118
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 LVDLDMVLKCLRYYAGWA---DKYHGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSP 274
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAA-AQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKIL 354
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 355 GYINTGKQEGAKLLCGGGIAA--DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVF 432
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 433 TKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVT 492
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-492 |
0e+00 |
|
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: 520.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 22 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTY 101
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 102 LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYH-----GKTIpidgdffsyTRHEPVGVCGQIIPWNFPLLMQA 176
Cdd:cd07138 78 LAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEfeerrGNSL---------VVREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 177 WKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIG-RVIQV 255
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGkRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 256 AAGSsnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPF 335
Cdd:cd07138 229 AADT--VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 336 DSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGG-----GIaaDRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKF 410
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpeGL--ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 411 KTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKT 490
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
..
1O00_H 491 VT 492
Cdd:cd07138 464 IQ 465
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
42-493 |
4.82e-180 |
|
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: 512.65 E-value: 4.82e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 42 PSTGEVICQVAEGDKEDVDKAVKAARAAFQLGsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISyLVD 121
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 122 LDMVLKCLRYYAGWADKYHGKTIPIDG-DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLT 200
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 201 ALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIqVAAGSSNLKRVTLELGGKSPNIIMSD 280
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAI-AAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 281 ADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTG 360
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 361 KQEGAKLLCGGGIAADR-GYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKA 439
Cdd:cd07118 321 RAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
1O00_H 440 NYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-492 |
1.37e-178 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 510.81 E-value: 1.37e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 7 AVPAPNQQpevfcnqIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAF--QLGSPWRRMDASHR 84
Cdd:PLN02467 2 AIPVPRRQ-------LFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 85 GRLLNRLADLIERDRTYLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGK-----TIPIDgDFFSYTRHEPV 159
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 160 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVD 239
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 240 KVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFV 319
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAA-AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 320 ERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAAD--RGYFIQPTVFGDVQDGMTIAK 397
Cdd:PLN02467 312 EKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 398 EEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGREL 477
Cdd:PLN02467 392 EEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGREL 471
|
490
....*....|....*
1O00_H 478 GEYGLQAYTEVKTVT 492
Cdd:PLN02467 472 GEWGLENYLSVKQVT 486
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-493 |
1.04e-176 |
|
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: 503.89 E-value: 1.04e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISyL 119
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 198
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 199 LTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGR-VIQVAAgsSNLKRVTLELGGKSPNII 277
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 278 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYI 357
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 358 NTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLD 437
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
1O00_H 438 KANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-493 |
6.47e-176 |
|
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: 498.68 E-value: 6.47e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 64 KAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKT 143
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 144 IP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVP 222
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 223 GFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCC 302
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 303 CAGSRTFVQEDIYDEFVERSVaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegakllcgggiaadrgyfiq 382
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 383 pTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVF-GA 461
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGP 335
|
410 420 430
....*....|....*....|....*....|..
1O00_H 462 QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
23-485 |
2.31e-173 |
|
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: 496.53 E-value: 2.31e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKyhgktipIDGDFfsyTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 182
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTEL---AGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 183 LATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVA-AGSSn 261
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 262 lKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQ 341
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 342 GPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRAN 421
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 422 NSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAY 485
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-491 |
5.08e-172 |
|
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: 492.53 E-value: 5.08e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlGSPWRrMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYL 119
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGK-TIPIDGDFFSYT----RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQvAAGSSNLKRVTLELGGKSP 274
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIM-AQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKIL 354
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 355 GYINTGKQEGAKLLCGGGIAA--DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVF 432
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 433 TKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-493 |
1.58e-171 |
|
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: 491.70 E-value: 1.58e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 22 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGsPWRRMDASHRGRLLNRLADLIERDRTY 101
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 102 LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTI---PIDGDffSYTRHEPVGVCGQIIPWNFPLLMQAWK 178
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERrpgSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 179 LGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAG 258
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 259 SsNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSK 338
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 339 TEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAA--DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEV 416
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 417 VGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVfGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-493 |
1.02e-168 |
|
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: 483.75 E-value: 1.02e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYL 119
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGktiPIDGDFF----SYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 195
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 196 QTPLTALYVANLIKEaGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPN 275
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAA-ADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 276 IIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILG 355
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 356 YInTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKD 435
Cdd:cd07092 314 FV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1O00_H 436 LDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
21-494 |
1.22e-166 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 479.41 E-value: 1.22e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWhDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGK-TIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKaAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGR-VIQVAAG 258
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKhVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 259 SsnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSK 338
Cdd:PRK13473 239 S--VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 339 TEQGPQVDETQFKKILGYINTGKQEG-AKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVV 417
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 418 GRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-493 |
3.70e-164 |
|
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: 472.01 E-value: 3.70e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYL 119
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 vDLDMVLKCLRYYAGWADKyhGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 199
Cdd:cd07106 79 -EVGGAVAWLRYTASLDLP--DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 200 TALYVANLIKEAgFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIqVAAGSSNLKRVTLELGGKSPNIIMS 279
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKV-MASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 280 DADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINT 359
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 360 GKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKA 439
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
1O00_H 440 NYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-493 |
9.59e-163 |
|
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: 468.76 E-value: 9.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGK------ 112
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNalrtqa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 113 -PYVISyLVDLdmvlkcLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 191
Cdd:cd07108 78 rPEAAV-LADL------FRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 192 KVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsSNLKRVTLELGG 271
Cdd:cd07108 151 KAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 272 KSPNIIMSDADMDWAVEQAHFAL-FFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQF 350
Cdd:cd07108 229 KSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 351 KKILGYINTGKQE-GAKLLCGG----GIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTY 425
Cdd:cd07108 309 AKVCGYIDLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 426 GLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELG-EYGLQAYTEVKTVTV 493
Cdd:cd07108 389 GLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
23-493 |
3.39e-162 |
|
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: 468.08 E-value: 3.39e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 182
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 183 LATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSSNL 262
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA-SENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 263 KRVTLELGGKSPNI----IMS--DADMDWAVEQahFALF-FNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPF 335
Cdd:cd07116 239 IPVTLELGGKSPNIffadVMDadDAFFDKALEG--FVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 336 DSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGG-----GIAADRGYFIQPTVFGDVQdgMTIAKEEIFGPVMQILKF 410
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGernelGGLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 411 KTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKT 490
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474
|
...
1O00_H 491 VTV 493
Cdd:cd07116 475 LLV 477
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
23-491 |
5.48e-162 |
|
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: 467.50 E-value: 5.48e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSrkTFPTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTY 101
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 102 LAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 180
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 181 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGsS 260
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 261 NLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTE 340
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 341 QGPQVDETQFKKILGYINTGKQEGAKLLCGGGI--AADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVG 418
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1O00_H 419 RANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNC----YDVfgaQSPFGGYKMSGSG-RELGEYGLQAYTEVKTV 491
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptagVDY---HVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
23-493 |
8.50e-162 |
|
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: 467.21 E-value: 8.50e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTG-EVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTY 101
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 102 LAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 180
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 181 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSS 260
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 261 NlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTE 340
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 341 QGPQVDETQFKKILGYINTGKQEGAKLLCGGGIA----ADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEV 416
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 417 VGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVfGA--QSPFGGYKMSGSG-RELGEYGLQAYTEVKTVTV 493
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTI-GAevHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-491 |
7.12e-161 |
|
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: 464.43 E-value: 7.12e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFS-YTRHEPVGVCGQIIPWNFPLLMQAWKLGP 181
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 182 ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIqVAAGSSN 261
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKI-MEAAAEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 262 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQ 341
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 342 GPQVDETQFKKILGYINTGKQEGAKLLCGGGIAA-DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRA 420
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1O00_H 421 NNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
20-491 |
1.03e-157 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 457.44 E-value: 1.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 20 NQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSpWRRMDASHRGRLLNRLADLIERDR 99
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 100 TYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGS 259
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 260 SNLKRVTLELGGKSPNIIMSDA-DMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSK 338
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 339 TEQGPQVDETQFKKILGYINTGKQEGAKLLcgGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVG 418
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLL--DGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1O00_H 419 RANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-493 |
5.51e-157 |
|
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: 454.14 E-value: 5.51e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYViSY 118
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 198
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 199 LTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSnLKRVTLELGGKSPNIIM 278
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 279 SDADMDWAVEQAHFALFFN-QGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYI 357
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 358 NTGKQEGAKLLCGGGIAAD----RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFT 433
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 434 KDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
23-494 |
3.27e-154 |
|
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: 447.66 E-value: 3.27e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgSPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTI------PIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQA 176
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 177 WKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEDVDKVAFTGSTEIGRVIQVA 256
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 257 AgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFD 336
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 337 SKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPT--VFGDVQDgmTIAKEEIFGPVMQILKFKTIE 414
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADS--RLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 415 EVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-493 |
5.02e-149 |
|
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: 433.68 E-value: 5.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 37 FPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYV- 115
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 116 ----ISYLVDLdmvlkcLRYYAGWADKYHGKTIPIDG-DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVV 190
Cdd:cd07150 78 awfeTTFTPEL------LRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 191 MKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELG 270
Cdd:cd07150 152 LKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 271 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQF 350
Cdd:cd07150 231 GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 351 KKILGYINTGKQEGAKLLCGGGIAadrGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAA 430
Cdd:cd07150 311 ERIKRQVEDAVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 431 VFTKDLDKANYLSQALQAGTVWVNCYDVFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1-491 |
2.23e-146 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 428.73 E-value: 2.23e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 1 SAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMD 80
Cdd:PLN02278 6 SSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 81 ASHRGRLLNRLADLIERDRTYLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWADKYHGKTIPI-DGDFFSYTRHEPV 159
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKP-LKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 160 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVD 239
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 240 KVAFTGSTEIGRVIQVAAGSSnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFV 319
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 320 ERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEE 399
Cdd:PLN02278 321 EAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 400 IFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGE 479
Cdd:PLN02278 401 VFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSK 480
|
490
....*....|..
1O00_H 480 YGLQAYTEVKTV 491
Cdd:PLN02278 481 YGIDEYLEIKYV 492
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
22-495 |
7.31e-145 |
|
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: 425.10 E-value: 7.31e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 22 IFINNEWHDavSRKTFPTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 180
Cdd:cd07124 110 ELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 181 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIG-----RVIQV 255
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriyeRAAKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 256 AAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPF 335
Cdd:cd07124 269 QPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 336 DSKTEQGPQVDETQFKKILGYINTGKQEGaKLLCGGGIAAD--RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTI 413
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 414 EEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGAQS---PFGGYKMSGSG-RELGEYGLQAYTEVK 489
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN-RKITGALVgrqPFGGFKMSGTGsKAGGPDYLLQFMQPK 506
|
....*.
1O00_H 490 TVTVKV 495
Cdd:cd07124 507 TVTENF 512
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-493 |
4.85e-142 |
|
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: 415.01 E-value: 4.85e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 58 DVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYlVDLDMVLKCLRYYAGWAD 137
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 138 KYHGKTIPIDGD-FFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLT-ALYVANLIKEAGFPP 215
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 216 GVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALF 295
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 296 FNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAa 375
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 376 drGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNC 455
Cdd:cd07104 315 --GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
1O00_H 456 YDVF-GAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-493 |
8.12e-141 |
|
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: 412.76 E-value: 8.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 37 FPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGspwRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyvI 116
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 117 SY-LVDLDMVLKCLRYYAGWADKYHGKTIPIDG-----DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVV 190
Cdd:cd07149 76 KDaRKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 191 MKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGssnLKRVTLELG 270
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 271 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQF 350
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 351 KKILGYINTGKQEGAKLLCGGGIaadRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAA 430
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 431 VFTKDLDKANYLSQALQAGTVWVNCYDVFGA-QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-493 |
1.26e-140 |
|
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: 413.11 E-value: 1.26e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAvSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPY------VISYLvdlDMVlkclrYYA-GWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLM 174
Cdd:cd07086 78 GRLVSLEMGKILpeglgeVQEMI---DIC-----DYAvGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 175 QAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEA----GFPPGVVNIVPGFGPtAGAAIASHEDVDKVAFTGSTEIG 250
Cdd:cd07086 150 PGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 251 RVIQVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRV 330
Cdd:cd07086 229 RRVGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 331 VGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIA--ADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQIL 408
Cdd:cd07086 308 IGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 409 KFKTIEEVVGRANNSTYGLAAAVFTKDLDKA-NYLSQA-LQAGTVWVNCyDVFGA--QSPFGGYKMSGSGRELGEYGLQA 484
Cdd:cd07086 388 KFDSLEEAIAINNDVPQGLSSSIFTEDLREAfRWLGPKgSDCGIVNVNI-PTSGAeiGGAFGGEKETGGGRESGSDAWKQ 466
|
....*....
1O00_H 485 YTEVKTVTV 493
Cdd:cd07086 467 YMRRSTCTI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-493 |
7.96e-137 |
|
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: 402.88 E-value: 7.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 37 FPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyVI 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKP-IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 117 SYLVDLDMVLKCLRYYAGWADKYHGKTIPIDG-----DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 191
Cdd:cd07145 77 QSRVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 192 KVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSnLKRVTLELGG 271
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 272 KSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFK 351
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 352 KILGYINTGKQEGAKLLCGGgiAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAV 431
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGG--KRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
1O00_H 432 FTKDLDKANYLSQALQAGTVWVNCYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
39-493 |
5.06e-136 |
|
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: 400.57 E-value: 5.06e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlGSPWRRmDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyVISY 118
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKI-LGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 198
Cdd:cd07120 78 RFEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 199 LTALYVANLIKEA-GFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQvAAGSSNLKRVTLELGGKSPNII 277
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIM-AAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 278 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYI 357
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 358 NTGKQEGAKLLCGGGIAAD---RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTK 434
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 435 DLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-493 |
3.91e-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: 382.19 E-value: 3.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 59 VDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISylvdLDMVLKC---LRYYAGW 135
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA----RAEVEKCawiCRYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 136 ADKY-HGKTIPIDGDFfSYTRHEPVGVCGQIIPWNFPLlmqaWK----LGPALATGNVVVMKVAEQTPLTALYVANLIKE 210
Cdd:cd07100 74 AEAFlADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 211 AGFPPGVVNIVPGFGPTAGAAIAsHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELGGKSPNIIMSDADMDWAVEQA 290
Cdd:cd07100 149 AGFPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 291 HFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCG 370
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 371 GGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGT 450
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
1O00_H 451 VWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-494 |
1.23e-125 |
|
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: 374.33 E-value: 1.23e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 26 NEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAfqlGSPWRRMDASHRGRLLNRLADLIERDRTYLAAL 105
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 106 ETLDNGKPYvISYLVDLDMVLKCLRYYAGWADKYHGKTIP--IDGDFfSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPAL 183
Cdd:cd07151 78 LIRESGSTR-IKANIEWGAAMAITREAATFPLRMEGRILPsdVPGKE-NRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 184 ATGNVVVMKVAEQTPLTA-LYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVI-QVAAGssN 261
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIgELAGR--H 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 262 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQ 341
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 342 GPQVDETQFKKILGYINTGKQEGAKLLCGGGIAadrGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRAN 421
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 422 NSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-493 |
1.31e-123 |
|
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: 368.86 E-value: 1.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYL 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 vDLDMVLKCLRYYAGWADKYHGKTIPIDGDFF----SYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 195
Cdd:cd07099 78 -EVLLALEAIDWAARNAPRVLAPRKVPTGLLMpnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 196 QTPLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEdVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPN 275
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAA-AERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 276 IIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILG 355
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 356 YINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKD 435
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 436 LDKANYLSQALQAGTVWVNCYDVFGAQS--PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPalPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
24-492 |
2.69e-123 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 370.03 E-value: 2.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 24 INNEWHDavSRKTFPTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:PRK03137 41 IGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYV-----ISYLVDLdmvlkcLRYYAGWADKY-HGKTI-PIDGDFFSYtRHEPVGVCGQIIPWNFPLLMQ 175
Cdd:PRK03137 116 SAWLVKEAGKPWAeadadTAEAIDF------LEYYARQMLKLaDGKPVeSRPGEHNRY-FYIPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 176 AWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIG----- 250
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlriye 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 251 RVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRV 330
Cdd:PRK03137 269 RAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 331 VGNPfDSKTEQGPQVDETQFKKILGYINTGKQEGaKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKF 410
Cdd:PRK03137 349 VGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 411 KTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVN--CYD-VFGAQsPFGGYKMSGSGRELG--EYgLQAY 485
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGaIVGYH-PFGGFNMSGTDSKAGgpDY-LLLF 504
|
....*..
1O00_H 486 TEVKTVT 492
Cdd:PRK03137 505 LQAKTVS 511
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-493 |
2.37e-122 |
|
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: 365.60 E-value: 2.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISyL 119
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGKTIPID-----GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGssnLKRVTLELGGKSP 274
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKIL 354
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 355 GYINTGKQEGAKLLCGGgiaADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTK 434
Cdd:cd07094 317 RWVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 435 DLDKANYLSQALQAGTVWVNCYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
30-493 |
2.83e-121 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 365.36 E-value: 2.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 30 DAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAfQLGspWRRMDASHRGRLLNRLADLIERDRTYLAALETLD 109
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 110 NGKPYVISYLVDLDMVLkCLRYYAGWADKY-----HGKTIPIDGDffSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALA 184
Cdd:PRK09407 104 TGKARRHAFEEVLDVAL-TARYYARRAPKLlaprrRAGALPVLTK--TTELRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 185 TGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIAshEDVDKVAFTGSTEIGRVIQVAAGSsNLKR 264
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGR-RLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 265 VTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQ 344
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 345 VDETQFKKILGYINTGKQEGAKLLCGGGIAADRG-YFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNS 423
Cdd:PRK09407 338 ISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDT 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1O00_H 424 TYGLAAAVFTKDLDKANYLSQALQAGTVWVNcyDVFGA-----QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:PRK09407 418 PYGLNASVWTGDTARGRAIAARIRAGTVNVN--EGYAAawgsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-494 |
9.63e-121 |
|
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: 362.22 E-value: 9.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:cd07085 79 ELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQvAAGS 259
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIY-ERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 260 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKT 339
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 340 EQGPQVDETQFKKILGYINTGKQEGAKLLCGG-GIAAD---RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEE 415
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGrGVKVPgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 416 VVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcydV--------FgaqsPFGGYKMSGSGrELGEYGLQA--- 484
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VpipvplafF----SFGGWKGSFFG-DLHFYGKDGvrf 467
|
490
....*....|
1O00_H 485 YTEVKTVTVK 494
Cdd:cd07085 468 YTQTKTVTSR 477
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
42-493 |
3.12e-120 |
|
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: 360.09 E-value: 3.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 42 PSTGEVICQVAEGDKEDVDKAVKAARAAfQLGspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVD 121
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 122 LDMVLKClRYYAGWADKY-----HGKTIPIdgdfFSYTR--HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07101 80 LDVAIVA-RYYARRAERLlkprrRRGAIPV----LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHedVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELGGKSP 274
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKIL 354
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 355 GYINTGKQEGAKLLCGGGIAADRG-YFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFT 433
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1O00_H 434 KDLDKANYLSQALQAGTVWVNcyDVFGA-----QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVN--EGYAAawasiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-491 |
4.04e-114 |
|
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: 344.61 E-value: 4.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyvISYL 119
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP--IAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 V-DLDMVLKCLRYYAGWADKY-HGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQT 197
Cdd:cd07102 76 GgEIRGMLERARYMISIAEEAlADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 198 PLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELGGKSPNII 277
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 278 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYI 357
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 358 NTGKQEGAKLLCGGG---IAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTK 434
Cdd:cd07102 314 ADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 435 DLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
21-494 |
1.57e-112 |
|
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: 1.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHDAvSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgSPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPY---------VISYLVDLDMVLKclryyagwadKYHGKTIPIDGDFFS-----YTRHEPVGVCGQII 166
Cdd:cd07082 80 EVANLLMWEIGKTLkdalkevdrTIDYIRDTIEELK----------RLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 167 PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS 246
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 247 TEIGRVIQVAAGssnLKRVTLELGGKSPNIIMSDADMDWAVEQ-AHFALFFNqGQCCCAGSRTFVQEDIYDEFVERSVAR 325
Cdd:cd07082 230 TEVGNRLKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEiVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 326 AKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIaaDRGYFIQPTVFGDVQDGMTIAKEEIFGPVM 405
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 406 QILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCY-----DVFgaqsPFGGYKMSGSGRELGEY 480
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQGIGD 459
|
490
....*....|....
1O00_H 481 GLQAYTEVKTVTVK 494
Cdd:cd07082 460 ALRSMTRRKGIVIN 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-489 |
1.05e-111 |
|
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: 338.07 E-value: 1.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 37 FPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVI 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 117 SYlVDLDMVLKCLRYYAGWADKYHGKTIPIDGD-----FFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 191
Cdd:cd07147 78 AR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 192 KVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfgPTAGAAI-ASHEDVDKVAFTGSTEIGRVIQVAAGSsnlKRVTLELG 270
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 271 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQF 350
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 351 KKILGYINTGKQEGAKLLCGGGIaadRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAA 430
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
1O00_H 431 VFTKDLDKANYLSQALQAGTVWVNcyDV--FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVK 489
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVIN--DVptFRVDHmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
40-493 |
3.60e-111 |
|
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: 337.02 E-value: 3.60e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAAraafqlGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISyL 119
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGKTIPID-----GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGssnLKRVTLELGGKSP 274
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKIL 354
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 355 GYINTGKQEGAKLLCGGGiaaDRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTK 434
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
1O00_H 435 DLDKANYLSQALQAGTVWVNcyDVFGAQ---SPFGGYKMSGSG-RELGEYGLQAYTEVKTVTV 493
Cdd:cd07146 391 DLDTIKRLVERLDVGTVNVN--EVPGFRselSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-493 |
7.33e-110 |
|
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: 332.62 E-value: 7.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 58 DVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWAD 137
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 138 KYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPG 216
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 217 VVNIV---PGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFA 293
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 294 LFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRvvgnpFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGI 373
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 374 AA-DRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVW 452
Cdd:cd07105 311 DEsPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
1O00_H 453 VN---CYDvfGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07105 391 INgmtVHD--EPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-493 |
1.50e-109 |
|
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: 332.34 E-value: 1.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 45 GEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNG----KPyvisyLV 120
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsirpKA-----GF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 121 DLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLT 200
Cdd:cd07152 73 EVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 201 ALYV-ANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSsNLKRVTLELGGKSPNIIMS 279
Cdd:cd07152 153 GGVViARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 280 DADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINT 359
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 360 GKQEGAKLLCGGGIaadRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKA 439
Cdd:cd07152 311 SVAAGARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
1O00_H 440 NYLSQALQAGTVWVNCYDVF-GAQSPFGGYKMSGSG-RELGEYGLQAYTEVKTVTV 493
Cdd:cd07152 388 MALADRLRTGMLHINDQTVNdEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
15-489 |
8.70e-109 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 331.87 E-value: 8.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 15 PEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADL 94
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 95 IERDRTYLAALETLDNGKPYV-----ISYLVDLdmvlkcLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPW 168
Cdd:PRK11241 83 MMEHQDDLARLMTLEQGKPLAeakgeISYAASF------IEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 169 NFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTE 248
Cdd:PRK11241 157 NFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 249 IGRVIqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKS 328
Cdd:PRK11241 237 IGRQL-MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 329 RVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQIL 408
Cdd:PRK11241 316 LHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 409 KFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEV 488
Cdd:PRK11241 396 RFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEI 475
|
.
1O00_H 489 K 489
Cdd:PRK11241 476 K 476
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
39-492 |
1.68e-107 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 329.52 E-value: 1.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVIS 117
Cdd:TIGR01237 50 SINPCdKSEVVGTVSKASQEHAEHALQAAAKAFE---AWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 118 YlVDLDMVLKCLRYYAGWADKY--HGKTIPIDGDFFSYTrHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 195
Cdd:TIGR01237 127 D-AEVAEAIDFMEYYARQMIELakGKPVNSREGETNQYV-YTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 196 QTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIG-RVIQVAA----GSSNLKRVTLELG 270
Cdd:TIGR01237 205 AAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGtRIFERAAkvqpGQKHLKRVIAEMG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 271 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQF 350
Cdd:TIGR01237 285 GKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 351 KKILGYINTGKQEGaKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAA 430
Cdd:TIGR01237 365 NKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGG 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1O00_H 431 VFTKDLDKANYLSQALQAGTVWVN--CYDVFGAQSPFGGYKMSGSGRELG--EYgLQAYTEVKTVT 492
Cdd:TIGR01237 444 VISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQAKTVT 508
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
88-491 |
7.16e-105 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 319.37 E-value: 7.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 88 LNRLADLIERDRTYLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPID---GDFFSYTRhePVGVCGQ 164
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 165 IIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFT 244
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 245 GSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVA 324
Cdd:PRK10090 158 GSVSAGEKIMAAA-AKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 325 RAKSRVVGNPFD-SKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP 403
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 404 VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQ 483
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
1O00_H 484 AYTEVKTV 491
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
39-491 |
2.48e-96 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 298.96 E-value: 2.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISY 118
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 lvdlDMVLKC---LRYYAGWADKYHGKTiPID----GDFFSYTRHEPVGVCGQIIPWNFPLlmqaWKL----GPALATGN 187
Cdd:PRK09406 82 ----AEALKCakgFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 188 VVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPgFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSnLKRVTL 267
Cdd:PRK09406 153 VGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 268 ELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDE 347
Cdd:PRK09406 231 ELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 348 TQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGL 427
Cdd:PRK09406 311 QGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 428 AAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-493 |
9.02e-94 |
|
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: 292.67 E-value: 9.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYL 119
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKyHGKTIPIDGDFF-----SYTRHEPVGVCGQIIPWNFPL--LmqawkLGPALA---TGNVV 189
Cdd:cd07098 78 GEILVTCEKIRWTLKHGEK-ALRPESRPGGLLmfykrARVEYEPLGVVGAIVSWNYPFhnL-----LGPIIAalfAGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 190 VMKVAEQTPLTALYVANLIKEA----GFPPGVVNIVPGFGPTaGAAIASHEDVDKVAFTGSTEIGRVIQVAAgSSNLKRV 265
Cdd:cd07098 152 VVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAA-AESLTPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 266 TLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQV 345
Cdd:cd07098 230 VLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 346 DETQFKKILGYINTGKQEGAKLLCGG----GIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRAN 421
Cdd:cd07098 310 SPARFDRLEELVADAVEKGARLLAGGkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 422 NSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDV-FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 493
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVnYYVQQlPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-492 |
5.86e-92 |
|
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: 289.09 E-value: 5.86e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 22 IFINNEWHDAVSRKTfpTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRT 100
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWADKYHGK---TIPIDGDFFSyTRHEPVGVCGQIIPWNFPLLMQAW 177
Cdd:cd07083 96 ELIATLTYEVGKN-WVEAIDDVAEAIDFIRYYARAALRLRYPaveVVPYPGEDNE-SFYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 178 KLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVI---- 253
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeaa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 254 -QVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVG 332
Cdd:cd07083 254 aRLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 333 NPFDSKTEQGPQVDETQFKKILGYINTGKQEGaKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKT 412
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 413 IE--EVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGA---QSPFGGYKMSGSGRELG--EYgLQAY 485
Cdd:cd07083 413 DDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN-RKITGAlvgVQPFGGFKLSGTNAKTGgpHY-LRRF 490
|
....*..
1O00_H 486 TEVKTVT 492
Cdd:cd07083 491 LEMKAVA 497
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-493 |
1.70e-87 |
|
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: 276.40 E-value: 1.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 25 NNEWhdAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAA 104
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 105 LETLDNGKPYV-----ISYLVDLdmvlkClRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWK 178
Cdd:cd07130 79 LVSLEMGKILPeglgeVQEMIDI-----C-DFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 179 LGPALATGNVVVMKVAEQTPLTALYVANLIKEA----GFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQ 254
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 255 VAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNP 334
Cdd:cd07130 232 QAV-AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 335 FDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPT-VFGDVQDGmtIAKEEIFGPVMQILKFKTI 413
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTiVEGLSDAP--IVKEETFAPILYVLKFDTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 414 EEVVGRANNSTYGLAAAVFTKDLDKA-NYLSQA-LQAGTVWVNC----YDVFGAqspFGGYKMSGSGRELGEYGLQAYTE 487
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAfRWLGPKgSDCGIVNVNIgtsgAEIGGA---FGGEKETGGGRESGSDAWKQYMR 465
|
....*.
1O00_H 488 VKTVTV 493
Cdd:cd07130 466 RSTCTI 471
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
20-498 |
6.05e-87 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 276.38 E-value: 6.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 20 NQIFINNEWHDAVSRktfptvnPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDR 99
Cdd:cd07125 39 GEETETGEGAPVIDP-------ADHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 100 ---TYLAALE---TLDNGKPYViSYLVDLdmvlkcLRYYAGWADKYHGKtiPIDGDFFSYTRH---EP--VGVCgqIIPW 168
Cdd:cd07125 109 gelIALAAAEagkTLADADAEV-REAIDF------CRYYAAQARELFSD--PELPGPTGELNGlelHGrgVFVC--ISPW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 169 NFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTE 248
Cdd:cd07125 178 NFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 249 IGRVIQVAAGSSNLKRVTL--ELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA 326
Cdd:cd07125 258 TAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 327 KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEgAKLLCGGGIAADRGYFIQPTVFGDVqdGMTIAKEEIFGPVMQ 406
Cdd:cd07125 338 ASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 407 ILKFK--TIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGA----QsPFGGYKMSGSGRELG-- 478
Cdd:cd07125 415 VIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFGGWGLSGTGPKAGgp 492
|
490 500
....*....|....*....|
1O00_H 479 EYgLQAYTEVKTVTVKVPQK 498
Cdd:cd07125 493 NY-LLRFGNEKTVSLNTTAA 511
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
23-494 |
1.38e-74 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 243.25 E-value: 1.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYViSYLVDLDMVLKCLRYYAGWADKYHGKTIP---IDGDFFSYTrhEPVGVCGQIIPWNFPLLMQAWKL 179
Cdd:TIGR01722 81 AELITAEHGKTHS-DALGDVARGLEVVEHACGVNSLLKGETSTqvaTRVDVYSIR--QPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQvAAGS 259
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIH-TTGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 260 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSrTFVQEDIYDEFVERSVARAKSRVVGNPFDSKT 339
Cdd:TIGR01722 236 AHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 340 EQGPQVDETQFKKILGYINTGKQEGAKLLCGG-GIAAD---RGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEE 415
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGrGYKVDgyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 416 VVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNC-YDVFGAQSPFGGYKMS--GSGRELGEYGLQAYTEVKTVT 492
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVpIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
..
1O00_H 493 VK 494
Cdd:TIGR01722 475 TR 476
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
76-491 |
4.58e-74 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 240.21 E-value: 4.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 76 WRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAG----W-ADKYHGKTIPIDGDF 150
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKhlkkWmKPKRVRTPLLLFGTK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 151 fSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGfgptaGA 230
Cdd:cd07134 94 -SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 231 AIASH---EDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSR 307
Cdd:cd07134 167 EVAQAlleLPFDHIFFTGSPAVGKIVMAAA-AKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 308 TFVQEDIYDEFVERSVARAKsRVVGNpfDSKTEQGPQ----VDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYfIQP 383
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIE-KFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRY-IAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 384 TVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcyDVFG--- 460
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN--DVVLhfl 399
|
410 420 430
....*....|....*....|....*....|..
1O00_H 461 -AQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07134 400 nPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
38-493 |
9.75e-74 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 251.66 E-value: 9.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 38 PTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGK--PY 114
Cdd:PRK11904 565 PVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAGKtlQD 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 115 VISYL---VDLdmvlkcLRYYAGWADKYHGKTIPIDGdffsytrhePVG-------------VCgqIIPWNFPLlmqAWK 178
Cdd:PRK11904 642 AIAEVreaVDF------CRYYAAQARRLFGAPEKLPG---------PTGesnelrlhgrgvfVC--ISPWNFPL---AIF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 179 LGP---ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQV 255
Cdd:PRK11904 702 LGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 256 AAGSSNLKRVTL--ELGGKSPNIIMSDA-------DmdwAVEQAhfalFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA 326
Cdd:PRK11904 782 TLAARDGPIVPLiaETGGQNAMIVDSTAlpeqvvdD---VVTSA----FRSAGQRCSALRVLFVQEDIADRVIEMLKGAM 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 327 KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEgAKLLCGG--GIAADRGYFIQPTVFGdvQDGMTIAKEEIFGPV 404
Cdd:PRK11904 855 AELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLplPAGTENGHFVAPTAFE--IDSISQLEREVFGPI 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 405 MQILKFKT--IEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGA----QsPFGGYKMSGSGRELG 478
Cdd:PRK11904 932 LHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ-PFGGQGLSGTGPKAG 1009
|
490
....*....|....*..
1O00_H 479 --EYgLQAYTEVKTVTV 493
Cdd:PRK11904 1010 gpHY-LLRFATEKTVTV 1025
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
40-474 |
2.85e-71 |
|
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: 233.85 E-value: 2.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWrrMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISyL 119
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 120 VDLDMVLKCLRYYAGWADKYHGKTIPID-----GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 194
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 195 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEdVDKVAFTGSTEIGRVI--QVAAGSsnlkRVTLELGGK 272
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLrsKLAPGT----RCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 273 SPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKK 352
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 353 ILGYINTGKQEGAKLLCGGGIAADRGYfiQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVF 432
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
1O00_H 433 TKDLDKANYLSQALQAGTVWVNCYDVFGAQ-SPFGGYKMSGSG 474
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
62-491 |
8.59e-71 |
|
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: 231.65 E-value: 8.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 62 AVKAARAAFQLGS----PWRRmdashrgRLLNRLADLI-ERDRTYLAALETlDNGKPYVISYLVDLDMVLKCLRYY---- 132
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRK-------AQLKALKRMLtENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHAlkhl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 133 AGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLIK 209
Cdd:cd07087 75 KKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 210 EAgFPPGVVNIVPGFGPTAGAAIAshEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQ 289
Cdd:cd07087 152 KY-FDPEAVAVVEGGVEVATALLA--EPFDHIFFTGSPAVGKIVMEAA-AKHLTPVTLELGGKSPCIVDKDANLEVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 290 AHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKtEQGPQVDETQFKKILGYINTGkqegaKLLC 369
Cdd:cd07087 228 IAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDG-----KVVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 370 GGGI-AADRgyFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQA 448
Cdd:cd07087 302 GGQVdKEER--YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
1O00_H 449 GTVWVNcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07087 380 GGVCVN--DVllhAAIPNlPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
39-491 |
1.80e-70 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 232.06 E-value: 1.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 39 TVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISY 118
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 119 lvdlDMVLKClryyAGWADKY--HG----KTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 191
Cdd:PRK13968 88 ----AEVAKS----ANLCDWYaeHGpamlKAEPtLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 192 KVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIaSHEDVDKVAFTGSTEIGRVIQVAAGSSnLKRVTLELGG 271
Cdd:PRK13968 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 272 KSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQV-----D 346
Cdd:PRK13968 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMArfdlrD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 347 E--TQFKKILGyintgkqEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNST 424
Cdd:PRK13968 318 ElhHQVEATLA-------EGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 425 YGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:PRK13968 391 FGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-475 |
1.45e-69 |
|
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: 228.70 E-value: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 58 DVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPY------VISYLVDLDMVLKCLRY 131
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 132 YAGwadkyhGKTIPIdGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEA 211
Cdd:cd07095 78 RTG------ERATPM-AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 212 GFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVI-QVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQA 290
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 291 HFALFFNQGQCCCAGSRTFVQEDIY-DEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLC 369
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 370 GGGIAADRGYFIQPTVFgDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAG 449
Cdd:cd07095 309 AMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420
....*....|....*....|....*...
1O00_H 450 TVWVNcYDVFGAQS--PFGGYKMSGSGR 475
Cdd:cd07095 388 IVNWN-RPTTGASStaPFGGVGLSGNHR 414
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
30-474 |
6.01e-68 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 236.37 E-value: 6.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 30 DAVSRKTFPTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAAL--- 105
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALlvr 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 106 E---TLDNGkpyvISYL---VDLdmvlkcLRYYAGWADKyhgktipidgDFFSYTRHEPVGVCGQIIPWNFPLlmqAWKL 179
Cdd:COG4230 642 EagkTLPDA----IAEVreaVDF------CRYYAAQARR----------LFAAPTVLRGRGVFVCISPWNFPL---AIFT 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 180 GP---ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVI--Q 254
Cdd:COG4230 699 GQvaaALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrT 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 255 VAAGSSNLkrVTL--ELGGKSPNIIMSDA-------DmdwAVEQAhfalFFNQGQCCCAGSRTFVQEDIYDEFVERSVAR 325
Cdd:COG4230 779 LAARDGPI--VPLiaETGGQNAMIVDSSAlpeqvvdD---VLASA----FDSAGQRCSALRVLCVQEDIADRVLEMLKGA 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 326 AKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGaKLL--CGGGIAADRGYFIQPTVF--GDVQDgmtiAKEEIF 401
Cdd:COG4230 850 MAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVhqLPLPEECANGTFVAPTLIeiDSISD----LEREVF 924
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 402 GPVMQILKFK--TIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGA----QsPFGGYKMSGSG 474
Cdd:COG4230 925 GPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
23-474 |
1.83e-67 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 235.14 E-value: 1.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWH-------DAVSRKTFPTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADL 94
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 95 IERDRTYLAALETLDNGK--PYVISYL---VDLdmvlkcLRYYAGWADkyhgktipidgDFFSYTRHEPVGVCGQIIPWN 169
Cdd:PRK11905 625 MEAHMPELFALAVREAGKtlANAIAEVreaVDF------LRYYAAQAR-----------RLLNGPGHKPLGPVVCISPWN 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 170 FPLlmqAWKLG---PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS 246
Cdd:PRK11905 688 FPL---AIFTGqiaAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGS 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 247 TEIGRVIQvAAGSSNLKR-VTL--ELGGKSPNIIMSDAdmdwAVEQAHFAL----FFNQGQCCCAGSRTFVQEDIYDEFV 319
Cdd:PRK11905 765 TEVARLIQ-RTLAKRSGPpVPLiaETGGQNAMIVDSSA----LPEQVVADViasaFDSAGQRCSALRVLCLQEDVADRVL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 320 ERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLL-CGGGIAADRGYFIQPTVFgDVqDGMTIAKE 398
Cdd:PRK11905 840 TMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVAPTLI-EI-DSISDLER 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 399 EIFGPVMQILKFKT--IEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVN---CYDVFGAQsPFGGYKMSGS 473
Cdd:PRK11905 918 EVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniIGAVVGVQ-PFGGEGLSGT 996
|
.
1O00_H 474 G 474
Cdd:PRK11905 997 G 997
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
38-489 |
4.43e-67 |
|
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: 224.02 E-value: 4.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 38 PTVNPSTGEVIC-QVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVI 116
Cdd:TIGR01238 54 PVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 117 SyLVDLDMVLKCLRYYAGWADkyhgktipidgDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQ 196
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 197 TPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTL--ELGGKSP 274
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 275 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKIL 354
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 355 GYINTGKQEG---AKLLCGGGIAADRGYFIQPTVFGdvQDGMTIAKEEIFGPVMQILKFKT--IEEVVGRANNSTYGLAA 429
Cdd:TIGR01238 359 AHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTM 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
1O00_H 430 AVFTKDLDKANYLSQALQAGTVWVNcYDVFGA---QSPFGGYKMSGSG-RELGEYGLQAYTEVK 489
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVN-RNQVGAvvgVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
57-491 |
1.38e-65 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 218.24 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 57 EDVDKAVKAARAAFQLGspwRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL-KCLRYYAG- 134
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKnDILHMLKNl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 135 --WA-DKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLI 208
Cdd:cd07135 82 kkWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 209 KEAgFPPGVVNIVPGFGPTAGAAIASHedVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVE 288
Cdd:cd07135 159 PKY-LDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAA-AKHLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 289 QAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSvARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKqeGAKLL 368
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK--GKVVI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 369 CGGGIAADRgyFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQA 448
Cdd:cd07135 312 GGEMDEATR--FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
1O00_H 449 GTVWVNcyDVFGA----QSPFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07135 390 GGVVIN--DTLIHvgvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
67-491 |
9.47e-63 |
|
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: 210.80 E-value: 9.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 67 RAAFQL-GSPwrrmDASHRGRLLNRLADLIERDRTYLA-ALETLDNGKPYVISYLVDLDMVLKCLRYY----AGWADKYH 140
Cdd:cd07133 8 KAAFLAnPPP----SLEERRDRLDRLKALLLDNQDALAeAISADFGHRSRHETLLAEILPSIAGIKHArkhlKKWMKPSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 141 GKTIPIdgdFF---SYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLIKEAgFP 214
Cdd:cd07133 84 RHVGLL---FLpakAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 215 PGVVNIVPGfGPTAGAAIaSHEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFAL 294
Cdd:cd07133 157 EDEVAVVTG-GADVAAAF-SSLPFDHLLFTGSTAVGRHVMRAA-AENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 295 FFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSR---VVGNPfdsktEQGPQVDETQFKKILGYINTGKQEGAKL--LC 369
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVieLN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 370 GGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAG 449
Cdd:cd07133 309 PAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
1O00_H 450 TVWVNcyDVF--GAQS--PFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07133 389 GVTIN--DTLlhVAQDdlPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
23-475 |
2.21e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 211.36 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHdAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFqlgSPWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPY------VISYLVDLDMVLKClryyagwadkYHGKTIPIDGDFFSYT---RHEPVGVCGQIIPWNFPLL 173
Cdd:PRK09457 80 AEVIARETGKPLweaateVTAMINKIAISIQA----------YHERTGEKRSEMADGAavlRHRPHGVVAVFGPYNFPGH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 174 MQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVI 253
Cdd:PRK09457 150 LPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 254 -QVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIY-DEFVERSVARAKSRVV 331
Cdd:PRK09457 229 hRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 332 GNPFDSKTE-QGPQVDETQFKKILgyintgkQEGAKLLCGGGIA--------ADRGyFIQPTVFgDVQDGMTIAKEEIFG 402
Cdd:PRK09457 308 GRWDAEPQPfMGAVISEQAAQGLV-------AAQAQLLALGGKSllemtqlqAGTG-LLTPGII-DVTGVAELPDEEYFG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1O00_H 403 PVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNcYDVFGAQS--PFGGYKMSGSGR 475
Cdd:PRK09457 379 PLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN-KPLTGASSaaPFGGVGASGNHR 452
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
80-491 |
6.13e-62 |
|
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: 208.90 E-value: 6.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 80 DASHRGRLLNRLADLI-ERDRTYLAALEtLDNGKPYVISYLVDLDMVLKCLRYY----AGWAdkyhgKTIPIDGDFF--- 151
Cdd:cd07136 18 DVEFRIEQLKKLKQAIkKYENEILEALK-KDLGKSEFEAYMTEIGFVLSEINYAikhlKKWM-----KPKRVKTPLLnfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 152 --SYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGfgp 226
Cdd:cd07136 92 skSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 227 taGAAIAS---HEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCC 303
Cdd:cd07136 165 --GVEENQellDQKFDYIFFTGSVRVGKIVMEAA-AKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 304 AGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKtEQGPQVDETQFKKILGYIntgkqEGAKLLCGGGIAADRGYfIQP 383
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETLY-IEP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 384 TVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS 463
Cdd:cd07136 315 TILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANP 394
|
410 420 430
....*....|....*....|....*....|
1O00_H 464 --PFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07136 395 ylPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-496 |
9.04e-60 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 204.60 E-value: 9.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 3 AATQAVPAPNQQPEVFcnQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDAS 82
Cdd:PLN00412 1 MAGTGFFAEILDGDVY--KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 83 HRGRLLNRLADLIERDRTYLAALETLDNGKPYVisylvdlDMVLKCLR------YYAGWADKYHGKTIPIDGDFFS---- 152
Cdd:PLN00412 76 KRAELLHKAAAILKEHKAPIAECLVKEIAKPAK-------DAVTEVVRsgdlisYTAEEGVRILGEGKFLVSDSFPgner 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 153 ----YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTA 228
Cdd:PLN00412 149 nkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 229 GAAIASHEDVDKVAFTGStEIGRVIQVAAGSSNLKrvtLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRT 308
Cdd:PLN00412 229 GDFLTMHPGVNCISFTGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 309 FVQEDIYDEFVERSVARAKSRVVGNPFDSkTEQGPQVDETQFKKILGYINTGKQEGAKLLCGggiAADRGYFIQPTVFGD 388
Cdd:PLN00412 305 LVMESVADALVEKVNAKVAKLTVGPPEDD-CDITPVVSESSANFIEGLVMDAKEKGATFCQE---WKREGNLIWPLLLDN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 389 VQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS-PFGG 467
Cdd:PLN00412 381 VRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQG 460
|
490 500
....*....|....*....|....*....
1O00_H 468 YKMSGSGRELGEYGLQAYTEVKTVTVKVP 496
Cdd:PLN00412 461 LKDSGIGSQGITNSINMMTKVKSTVINLP 489
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
23-492 |
3.11e-59 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 205.75 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 181
Cdd:PLN02419 194 AMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 182 ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGaAIASHEDVDKVAFTGSTEIGRVIQVAAGSSN 261
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 262 lKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIyDEFVERSVARAKSRVVGNPFDSKTEQ 341
Cdd:PLN02419 352 -KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLVERAKALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 342 GPQVDETQFKKILGYINTGKQEGAKLLCGGG----IAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVV 417
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1O00_H 418 GRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNC-YDVFGAQSPFGGYKMSGSG--RELGEYGLQAYTEVKTVT 492
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVpIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLVT 587
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
40-473 |
6.29e-58 |
|
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: 200.12 E-value: 6.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 40 VNPST-GEVICQVAEGDKEDVDKAVKAARAAfqlGSPWRRMDASHRGRLLNRLADLIE-RDRTYLAALETLDNGK-PY-- 114
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKnVWqa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 115 ---VISYLVDLdmvlkcLRYYAGWADK-YHGKTIPIDGDFFSYTRHEPV-GVCGQIIPWNFPLLMQAWKLGPALaTGNVV 189
Cdd:cd07123 128 eidAACELIDF------LRFNVKYAEElYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 190 VMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVI--QVAAGSSNLK---R 264
Cdd:cd07123 201 LWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLwkQIGENLDRYRtypR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 265 VTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQ 344
Cdd:cd07123 281 IVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 345 VDETQFKKILGYINTGKQE-GAKLLCGGGIAADRGYFIQPTVFgDVQDGM-TIAKEEIFGPVMQILKF--KTIEEVVGRA 420
Cdd:cd07123 361 IDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI-ETTDPKhKLMTEEIFGPVLTVYVYpdSDFEETLELV 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 421 NNST-YGLAAAVFTKDLDKANYLSQALQ--AGTVWVNCY---DVFGAQsPFGGYKMSGS 473
Cdd:cd07123 440 DTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINDKptgAVVGQQ-PFGGARASGT 497
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
33-473 |
3.81e-57 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 198.47 E-value: 3.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 33 SRKTFPTVNPST-GEVICQVAEGDKEDVDKAVKAARAAfqlGSPWRRMDASHRGRLLNRLADLIERDRTY-LAALETLDN 110
Cdd:TIGR01236 44 SNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDA---KKDWSNLPFYDRAAIFLKAADLLSGPYRYeILAATMLGQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 111 GK-PY-----VISYLVDLdmvlkcLRYYAGWADKYHGKTiPIDGD-FFSYTRHEPV-GVCGQIIPWNFPLLMQAWKLGPA 182
Cdd:TIGR01236 121 SKtVYqaeidAVAELIDF------FRFNVKYARELYAQQ-PISAPgEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 183 LaTGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEI-----GRVIQVAA 257
Cdd:TIGR01236 194 L-MGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTfkhlwKKVAQNLD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 258 GSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDS 337
Cdd:TIGR01236 273 RYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 338 KTEQGPQVDETQFKKILGYINTGKQEGAKL--LCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQIL-----KF 410
Cdd:TIGR01236 353 RGFMGAVIDEQSFDKIVKYIEDAKKDPEALtiLYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYvypddKY 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1O00_H 411 KTIEEVVGraNNSTYGLAAAVFTKDLDKANYLSQALQ--AGTVWVN--CYDVFGAQSPFGGYKMSGS 473
Cdd:TIGR01236 433 KEILDLVD--STSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSGT 497
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-493 |
1.96e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 193.13 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHdaVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYL 102
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 103 AALETLDNGKpYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 181
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 182 ALATGNVVVMKVAEQTPLTAL----YVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAA 257
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 258 gSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDS 337
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 338 KTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFgDVQDGMTIAKEEIFGPVMQILKFKTIEEVV 417
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 418 GRANNSTYGLAAAVFTKDLDKA-NYLS-QALQAGTVWVNC----YDVFGAqspFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIfKWIGpLGSDCGIVNVNIptngAEIGGA---FGGEKATGGGREAGSDSWKQYMRRSTC 491
|
..
1O00_H 492 TV 493
Cdd:PLN02315 492 TI 493
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
55-494 |
5.51e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 186.39 E-value: 5.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 55 DKEDVDKAVKAARAAFQLGS----PWRRMdashrgRLLNRLADLIERDRTYLAALEtLDNGKPYVISYLVDLDMVLKCLR 130
Cdd:PTZ00381 5 NPEIIPPIVKKLKESFLTGKtrplEFRKQ------QLRNLLRMLEENKQEFSEAVH-KDLGRHPFETKMTEVLLTVAEIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 131 YYAGWADKYhGKTIPIDGDFF-----SYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVA 205
Cdd:PTZ00381 78 HLLKHLDEY-LKPEKVDTVGVfgpgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 206 NLIKEAgFPPGVVNIVPGfGPTAGAAIASHEdVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDW 285
Cdd:PTZ00381 157 KLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAA-AENLTPCTLELGGKSPVIVDKSCNLKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 286 AVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVErSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYIntgKQEGA 365
Cdd:PTZ00381 233 AARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE-ALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 366 KLLCGGGI-AADRgyFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQ 444
Cdd:PTZ00381 309 KVVYGGEVdIENK--YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
1O00_H 445 ALQAGTVWVN-CYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:PTZ00381 387 NTSSGAVVINdCVFHLLNPNlPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
38-474 |
3.15e-51 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 187.87 E-value: 3.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 38 PTVNPS-TGEVICQVAEGDKEDVDKAVKAARAAFQLgspWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGK--PY 114
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI---WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKtfSN 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 115 VISYL---VDLdmvlkcLRYYAGWADkyhgktipidgDFFSYTRHEPVG--VCgqIIPWNFPLLMQAWKLGPALATGNVV 189
Cdd:PRK11809 739 AIAEVreaVDF------LRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSV 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 190 VMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQ--VAAGSSNLKRVT- 266
Cdd:PRK11809 800 LAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQrnLAGRLDPQGRPIp 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 267 --LELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVE--RSvARAKSRvVGNPFDSKTEQG 342
Cdd:PRK11809 880 liAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKmlRG-AMAECR-MGNPDRLSTDIG 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 343 PQVDETQFKKILGYINTGKQEGAK---LLCGGGIAADRGYFIQPTV--FGDVQDgmtiAKEEIFGPVMQILKFK--TIEE 415
Cdd:PRK11809 958 PVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrnQLDE 1033
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
1O00_H 416 VVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVN---CYDVFGAQsPFGGYKMSGSG 474
Cdd:PRK11809 1034 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmVGAVVGVQ-PFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
61-494 |
3.07e-48 |
|
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: 172.41 E-value: 3.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 61 KAVKAARAAFQLGspwRRMDASHRGRLLNRLADLIERDRT-YLAALEtLDNGKPYVISYLVDLDMVLKCLRY----YAGW 135
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEENEDeIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 136 A-DKYHGKTIP--IDGdffSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLI---- 208
Cdd:cd07132 78 MkPEPVKKNLAtlLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 209 -KEAgFPpgVVnivpgfgpTAGAAIAS---HEDVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNIIMSDADMD 284
Cdd:cd07132 155 dKEC-YP--VV--------LGGVEETTellKQRFDYIFYTGSTSVGKIVMQAA-AKHLTPVTLELGGKSPCYVDKSCDID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 285 WAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKtEQGPQVDETQFKKILGYIntgkqEG 364
Cdd:cd07132 223 VAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL-----SG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 365 AKLLCGG-GIAADRgyFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLS 443
Cdd:cd07132 297 GKVAIGGqTDEKER--YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKIL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
1O00_H 444 QALQAGTVWVNcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 494
Cdd:cd07132 375 SNTSSGGVCVN--DTimhYTLDSlPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
63-491 |
4.17e-48 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 171.83 E-value: 4.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 63 VKAARAAFQLGspwRRMDASHRGRLLNRLADLI-ERDRTYLAALETlDNGKPYVISYLVDLDMV-------LKCLRyyaG 134
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLvsscklaIKELK---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 135 WADKYHGK----TIPIDGDFFSytrhEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKE 210
Cdd:cd07137 78 WMAPEKVKtpltTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 211 AgFPPGVVNIVPGfGPTAGAAIASHEdVDKVAFTGSTEIGRVIqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQA 290
Cdd:cd07137 154 Y-LDTKAIKVIEG-GVPETTALLEQK-WDKIFFTGSPRVGRII-MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 291 HFALF-FNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQgpQVDETQFKKILGYINTGKQEGAKLLC 369
Cdd:cd07137 230 AGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS--RIVNSHHFQRLSRLLDDPSVADKIVH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 370 GGGIAADRGYfIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAG 449
Cdd:cd07137 308 GGERDEKNLY-IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
1O00_H 450 TVWVNcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTV 491
Cdd:cd07137 387 GVTFN--DTvvqYAIDTlPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
52-492 |
2.20e-37 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 143.33 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 52 AEGDKEDVDKAVKAARAAFQLGspwRRMDASHRGRLLNRLADLI-ERDRTYLAALETlDNGKPYVISYLVDLDMVLKCLR 130
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESG---RTRSLEWRKSQLKGLLRLLkDNEEAIFKALHQ-DLGKHRVEAYRDEVGVLTKSAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 131 Y----YAGWADKYHGK----TIPIDGDFFSytrhEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTAL 202
Cdd:PLN02203 77 LalsnLKKWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 203 YVANLIKeAGFPPGVVNIVPGfGPTAGAAIASHEdVDKVAFTGSTEIGRVIQVAAgSSNLKRVTLELGGKSPNI---IMS 279
Cdd:PLN02203 153 FLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAA-AKHLTPVALELGGKCPCIvdsLSS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 280 DADMDWAVEQAHFALFFN-QGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTeQGPQVDETQFKKILGYIN 358
Cdd:PLN02203 229 SRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 359 TgKQEGAKLLCGGGIAADRgYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLD- 437
Cdd:PLN02203 308 D-PRVAASIVHGGSIDEKK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKl 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1O00_H 438 KANYLSQAlQAGTVWVNcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVT 492
Cdd:PLN02203 386 KRRILSET-SSGSVTFN--DAiiqYACDSlPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
23-484 |
1.58e-32 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 130.21 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAVSRKTfPTVNPSTGEVICQVaegDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLI--ERDRT 100
Cdd:PRK11903 8 YVAGRWQAGSGAGT-PLFDPVTGEELVRV---SATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLqaNRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 101 YLAALEtldNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGD---------FFSytRHEPV---GVCGQIIPW 168
Cdd:PRK11903 84 YDIATA---NSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpaFQG--QHVLVptrGVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 169 NFPllmqAW----KLGPALATGNVVVMKVAEQTP-LTALYVANLIKEAGFPPGVVNIVPGfgpTAGAAIASHEDVDKVAF 243
Cdd:PRK11903 159 NFP----AWglweKAAPALLAGVPVIVKPATATAwLTQRMVKDVVAAGILPAGALSVVCG---SSAGLLDHLQPFDVVSF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 244 TGSTEIGRVIQ----VAAGSSnlkRVTLELGGKSPNIIMSDADMDwaveQAHFALFFNQ---------GQCCCAGSRTFV 310
Cdd:PRK11903 232 TGSAETAAVLRshpaVVQRSV---RVNVEADSLNSALLGPDAAPG----SEAFDLFVKEvvremtvksGQKCTAIRRIFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 311 QEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIA-----ADRGYFIQPTV 385
Cdd:PRK11903 305 PEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFAlvdadPAVAACVGPTL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 386 FG--DVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDldkANYLSQALQA-----GTVWVNCYDV 458
Cdd:PRK11903 385 LGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD---AAFLAAAALEladshGRVHVISPDV 461
|
490 500 510
....*....|....*....|....*....|....*
1O00_H 459 FGA---------QSPFGGYKMSGSGRELGeyGLQA 484
Cdd:PRK11903 462 AALhtghgnvmpQSLHGGPGRAGGGEELG--GLRA 494
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-478 |
1.13e-31 |
|
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: 126.58 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 59 VDKAVKAARAAfqlGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADK 138
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 139 YH---GKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAG-FP 214
Cdd:cd07084 78 IPhepGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 215 PGVVNIVPGFGPTaGAAIASHEDVDKVAFTGSTEIGRVIqvaagSSNLK--RVTLELGGKSPNIIMSDAD-MDWAVEQAH 291
Cdd:cd07084 158 PEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 292 FALFFNQGQCCCAGSRTFVQEDIYDE-FVERSVARAKSRVVGNpfdskTEQGPQVDETQFKKIlgyINTGKQEGAKLLCG 370
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQTFTTLAMI---AHMENLLGSVLLFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 371 G------GIAADRGYFIQPTVF--GDVQDGMTIA-KEEIFGPVMQILKFKTIEE--VVGRANNSTYGLAAAVFTKDLDKA 439
Cdd:cd07084 304 GkelknhSIPSIYGACVASALFvpIDEILKTYELvTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
1O00_H 440 NYLSQALQ-AGTVWVNCYD---VFGAQSPFGGYKMSGSGRELG 478
Cdd:cd07084 384 QELIGNLWvAGRTYAILRGrtgVAPNQNHGGGPAADPRGAGIG 426
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
100-491 |
2.08e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 126.70 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 100 TYLAALETlDNGKPYVISYLVDLDMVLK----CLRYYAGWADKYHGKT----IPIDGDFFSytrhEPVGVCGQIIPWNFP 171
Cdd:PLN02174 51 EIVAALRD-DLGKPELESSVYEVSLLRNsiklALKQLKNWMAPEKAKTslttFPASAEIVS----EPLGVVLVISAWNYP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 172 LLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIkEAGFPPGVVNIVPGFGPTAGAAIasHEDVDKVAFTGSTEIGR 251
Cdd:PLN02174 126 FLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 252 VIqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALF-FNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRV 330
Cdd:PLN02174 203 VI-MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 331 VGNPFDSKtEQGPQVDETQFKKILGYINTgKQEGAKLLCGGgiAADRGYF-IQPTVFGDVQDGMTIAKEEIFGPVMQILK 409
Cdd:PLN02174 282 GKNPMESK-DMSRIVNSTHFDRLSKLLDE-KEVSDKIVYGG--EKDRENLkIAPTILLDVPLDSLIMSEEIFGPLLPILT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 410 FKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS--PFGGYKMSGSGRELGEYGLQAYTE 487
Cdd:PLN02174 358 LNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtlPFGGVGESGMGAYHGKFSFDAFSH 437
|
....
1O00_H 488 VKTV 491
Cdd:PLN02174 438 KKAV 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-484 |
4.57e-29 |
|
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: 120.07 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 21 QIFINNEWHdAVSRKTFPTVNPSTGEVICQVAeGDKEDVDKAVKAARAAfqlGSP-WRRMDASHRGRLLNRLAD-LIERD 98
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREK---GGPaLRALTFHERAAMLKALAKyLMERK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 99 RTYlaaletldngkpYVISYL---------VDLDMVLKCLRYYAGWA------DKYH--GKTIPI--DGDFFSytRHEPV 159
Cdd:cd07128 77 EDL------------YALSAAtgatrrdswIDIDGGIGTLFAYASLGrrelpnAHFLveGDVEPLskDGTFVG--QHILT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 160 ---GVCGQIIPWNFPllmqAW----KLGPALATGNVVVMKVAEQTPLTALYVANLIKEAG-FPPGVVNIVPGfgpTAGAA 231
Cdd:cd07128 143 prrGVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 232 IASHEDVDKVAFTGSTEIGRVIQVAAG-SSNLKRVTLELGGKSPNIIMSDADMDwaveQAHFALFFNQ---------GQC 301
Cdd:cd07128 216 LDHLGEQDVVAFTGSAATAAKLRAHPNiVARSIRFNAEADSLNAAILGPDATPG----TPEFDLFVKEvaremtvkaGQK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 302 CCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEgAKLLCGG-------GIA 374
Cdd:cd07128 292 CTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfevvGAD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 375 ADRGYFIQPTVF-GDVQDGMTIAKE-EIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQA--GT 450
Cdd:cd07128 371 AEKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGR 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1O00_H 451 VWVNCYDVFGAQ----SPF-----GGYKMSGSGRELGeyGLQA 484
Cdd:cd07128 451 LLVLNRDSAKEStghgSPLpqlvhGGPGRAGGGEELG--GLRG 491
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-404 |
1.30e-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: 75.66 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 59 VDKAVKAARAAFQlgsPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWADK 138
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP-EARLQGELGRTTGQLRLFADLVRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 139 --YHGKTI-PIDGDFFSYTRHE---------PVGVCGqiiPWNFPLlmqAWKLG-----PALATGNVVVMKVAEQTPLTA 201
Cdd:cd07129 77 gsWLDARIdPADPDRQPLPRPDlrrmlvplgPVAVFG---ASNFPL---AFSVAggdtaSALAAGCPVVVKAHPAHPGTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 202 LYVANLI----KEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAgssnLKR-----VTLELGGK 272
Cdd:cd07129 151 ELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA----AARpepipFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 273 SPNIIMSDADMDWAVEQAH-FA--LFFNQGQ-CCCAGSRTFVQEDIYDEFVERSVARAKsrvvgnpfdsktEQGPQVDET 348
Cdd:cd07129 227 NPVFILPGALAERGEAIAQgFVgsLTLGAGQfCTNPGLVLVPAGPAGDAFIAALAEALA------------AAPAQTMLT 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1O00_H 349 QfkKILGYINTGKQE-----GAKLLCGGGiAADRGYFIQPTVFgdVQDGMTIAK-----EEIFGPV 404
Cdd:cd07129 295 P--GIAEAYRQGVEAlaaapGVRVLAGGA-AAEGGNQAAPTLF--KVDAAAFLAdpalqEEVFGPA 355
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
23-435 |
1.11e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 66.75 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 23 FINNEWHDAvsRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLG------SPWRRM---DASHRGRLLNRLAD 93
Cdd:cd07126 2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhnplkNPERYLlygDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 94 LierdRTYLAALETLDNGKPYvISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHE---PVGVCGQIIPWNF 170
Cdd:cd07126 80 V----EDFFARLIQRVAPKSD-AQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 171 PLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGaAIASHEDVDKVAFTGSTEIG 250
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 251 rviqvaagssnlKRVTLELGGKspnIIMSDADMDWAV------EQAHFALFFNQ------GQCCCAGSRTFVQEDIYDE- 317
Cdd:cd07126 234 ------------ERLALELHGK---VKLEDAGFDWKIlgpdvsDVDYVAWQCDQdayacsGQKCSAQSILFAHENWVQAg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 318 FVERSVARAKSRVVgnpfdSKTEQGPQVDETQfKKILGYINTGKQ-EGAKLLCGG------GIAADRGYfIQPT-VFGDV 389
Cdd:cd07126 299 ILDKLKALAEQRKL-----EDLTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGkpltnhSIPSIYGA-YEPTaVFVPL 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
1O00_H 390 QDGMT-----IAKEEIFGPvMQIL---KFKTIEEVVGRANNSTYGLAAAVFTKD 435
Cdd:cd07126 372 EEIAIeenfeLVTTEVFGP-FQVVteyKDEQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
84-467 |
2.36e-08 |
|
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: 56.08 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 84 RGRLLNRLADLIERDRTYLAALETLDNGKpYVISYLVDLDMVLKC-----------LRYYAGWADKYHGKTIPIDGDffS 152
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGA-YIRSLIANWIAMMGCsesklyknidtERGITASVGHIQDVLLPDNGE--T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 153 YTRHEPVGVCGQIIPWNFPLLMqAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEA---GFPPGVVNIVPGFGPTAG 229
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 230 AAIASHEDVDKVAFTGSTEigrVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCccagsrtF 309
Cdd:cd07077 174 EELLSHPKIDLIVATGGRD---AVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC-------A 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 310 VQEDIYdefversvaraksrVVGNPFDSKTEqgpqvdetQFKKILGYINTGKQEGAKLLcgggiaadrgyfiqptvFGDV 389
Cdd:cd07077 244 SEQNLY--------------VVDDVLDPLYE--------EFKLKLVVEGLKVPQETKPL-----------------SKET 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 390 QDGMTIAKEEIFGPVMQILKFKTIEEVVGRA----NNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPF 465
Cdd:cd07077 285 TPSFDDEALESMTPLECQFRVLDVISAVENAwmiiESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFA 364
|
..
1O00_H 466 GG 467
Cdd:cd07077 365 GK 366
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
162-334 |
3.19e-06 |
|
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: 49.78 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 162 CGQIIPWN-FPLLMQAwklgpaLATGNVVVMKvaeQTPLTALYVANLIK-------EAGFPPGVVNIVpGFGPTAGAA-- 231
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVK---PHPAAILPLAITVQvarevlaEAGFDPNLVTLA-ADTPEEPIAqt 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 232 IASHEDVDKVAFTGSTEIGRVIQVAAGSsnlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQ 311
Cdd:cd07127 272 LATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVP 348
|
170 180 190
....*....|....*....|....*....|..
1O00_H 312 ED---------IYDEfVERSVARAKSRVVGNP 334
Cdd:cd07127 349 RDgiqtddgrkSFDE-VAADLAAAIDGLLADP 379
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
147-454 |
2.33e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 46.88 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 147 DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM----KVAEQTPLTALYVANLIKEAGFPPGVVNIVP 222
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 223 GFGPTAGAAIASHEDVDKVAFTGSTEIgrviqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCC 302
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATGGPAV-----VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 303 CAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDskteqgpQVDETQFKKILGYINTGKQEGAKLLCGGGIAA---DRGY 379
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQ-------QVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVpqeTRIL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O00_H 380 FIQPTVFGDVQDGMTiakeEIFGPVMQILKFKTIEEVVGRA----NNSTYGLAAAVFT---KDLDKANYLSQALQAGTVW 452
Cdd:cd07081 312 IGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSdniKAIENMNQFANAMKTSRFV 387
|
..
1O00_H 453 VN 454
Cdd:cd07081 388 KN 389
|
|
| |
