|
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 ... |
33-513 |
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: 1032.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 33 QPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLYRLAD 112
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 113 LIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLL 192
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 193 MQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 273 QVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 353 PFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTI 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 433 EEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 13529509 513 K 513
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
36-512 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 36 VFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSpWRRMDASDRGRLLYRLADLIE 115
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 116 RDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQA 195
Cdd:cd07091 80 RDRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 196 WKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVA 275
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 276 AGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFD 355
Cdd:cd07091 240 AAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 356 SRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEV 435
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 436 VGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
39-510 |
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: 768.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 39 NQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGsPWRRMDASDRGRLLYRLADLIERDR 118
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 119 TYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGS 278
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRT 358
Cdd:cd07142 243 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 359 EQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGR 438
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13529509 439 ANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07142 403 ANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-518 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 758.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 3 RAALTTVRRGPRLSRLLS--AAATSAVPAPNHQP-EVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVD 79
Cdd:PLN02466 19 SALLRSRGRNGGRGRGIRrfSTAAAAVEEPITPPvQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 80 KAVKAARAAFQLGsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYH 159
Cdd:PLN02466 99 RAVAAARKAFDEG-PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 160 GKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNI 239
Cdd:PLN02466 178 GLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 240 VPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQ 319
Cdd:PLN02466 258 VSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 320 CCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYF 399
Cdd:PLN02466 338 CCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 400 IQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFG 479
Cdd:PLN02466 418 IQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFD 497
|
490 500 510
....*....|....*....|....*....|....*....
gi 13529509 480 AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTvkVPQKN 518
Cdd:PLN02466 498 AAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV--TPLKN 534
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
41-512 |
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: 696.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 41 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgSPWRRMDASDRGRLLYRLADLIERDRTY 120
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 121 LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 200
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 201 ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGsSN 280
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 281 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSR-VVGNPFDSRTE 359
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 360 QGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAAD---RGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVV 436
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13529509 437 GRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
41-514 |
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: 695.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 41 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgSPWRR-MDASDRGRLLYRLADLIERDRT 119
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 199
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 200 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSS 279
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 280 NLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTE 359
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 360 QGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRA 439
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13529509 440 NDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKV 514
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
40-513 |
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: 680.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:COG1012 84 ELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGs 278
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRT 358
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 359 EQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAAD-RGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVG 437
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 438 RANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
47-510 |
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: 666.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 47 WHDAVSrKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALET 126
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 127 LDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGN 206
Cdd:pfam00171 77 LENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 207 VVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 287 ELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDE 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 367 TQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGL 446
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13529509 447 AAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
34-515 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 664.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 34 PEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGsPWRRMDASDRGRLLYRLADL 113
Cdd:PLN02766 16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 114 IERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLM 193
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 194 QAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQ 273
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 274 VAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNP 353
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 354 FDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIE 433
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 434 EVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
..
gi 13529509 514 VP 515
Cdd:PLN02766 495 LY 496
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
42-510 |
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: 641.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlGSPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 201
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 202 LATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQVAAGssN 280
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGrSIMRAAAG--N 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 281 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQ 360
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 361 GPQVDETQFKKILGYIKSGQQEGAKLLCGG----GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVV 436
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 437 GRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
79-512 |
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: 630.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 79 DKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYViSYLVDLDMVLKCLRYYAGWADKY 158
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 159 HGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVV 237
Cdd:cd07078 77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 238 NIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGsSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQ 317
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 318 GQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGA-AADR 396
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 397 GYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYD 476
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 13529509 477 VFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07078 396 VGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
58-514 |
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: 616.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISY 137
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 217
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 218 LTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGH-LIQVAAGssNLKRVTLELGGKSPNII 296
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAG--NLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 297 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYI 376
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 377 KSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLD 456
Cdd:cd07115 316 DVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 13529509 457 KANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKV 514
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-510 |
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: 614.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 54 KTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSpWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPY 133
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 134 VISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSP 293
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDA-DMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKI 372
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 373 LGYIKSGQQEGAKLLCGGGA--AADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAV 450
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 451 FTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
58-512 |
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: 609.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYV--- 134
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRetr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 135 --ISYLVDldmvlkCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMK 211
Cdd:cd07114 80 aqVRYLAE------WYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 212 VAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQVAAgsSNLKRVTLELGG 290
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGrHIARAAA--ENLAPVTLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 291 KSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFK 370
Cdd:cd07114 232 KSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 371 KILGYIKSGQQEGAKLLCGG----GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGL 446
Cdd:cd07114 312 KVERYVARAREEGARVLTGGerpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGL 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13529509 447 AAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07114 392 AAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
58-512 |
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: 576.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISY 137
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 217
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 218 LTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQvAAGSSNLKRVTLELGGKSPNIIM 297
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIM-RAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 298 SDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIK 377
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 378 SGQQEGAKLLCGGG----AAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTK 453
Cdd:cd07093 317 LARAEGATILTGGGrpelPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 13529509 454 DLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
40-512 |
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: 576.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 199
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 200 PALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSS 279
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA-AE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 280 NLKRVTLELGGKSPNIIMSDA-----DMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPF 354
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 355 DSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAA----DRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFK 430
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTlgglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 431 TIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 13529509 511 TV 512
Cdd:cd07559 477 LV 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
39-513 |
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: 557.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 39 NQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlGSPWRRMDASDRGRLLYRLADLIERDR 118
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 119 TYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPID----GDFFSYTRHEPVGVCGQIIPWNFPLLMQ 194
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 195 AWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQV 274
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 275 AAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPF 354
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 355 DSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKT--I 432
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 433 EEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 13529509 513 K 513
Cdd:cd07140 485 E 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
58-512 |
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: 548.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISy 137
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 217
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 218 LTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIM 297
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAA-AKGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 298 SDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIK 377
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 378 SGQQEGAKLLCGGGAAA-----DRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFT 452
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 453 KDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
40-512 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 539.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLI-ERDR 118
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 119 TyLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:PRK13252 85 E-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEGVDKVAFTGSTEVGHLIQVAAGS 278
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 SnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRT 358
Cdd:PRK13252 243 S-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 359 EQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGA----AADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEE 434
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13529509 435 VVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
42-508 |
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: 532.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ---GEWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 201
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 202 LATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIqVAAGSSNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKI-MAAAAGHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 282 KRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 362 PQVDETQFKKILGYIKSGQQEGAKLLCGGG----AAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVG 437
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGrpenVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13529509 438 RANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVK 508
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
40-512 |
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: 529.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 199
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 200 PALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSS 279
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA-AK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 280 NLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTE 359
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 360 QGPQVDETQFKKILGYIKSGQQEGAKLLCGG----GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEV 435
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 436 VGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-512 |
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: 524.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYl 138
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 218
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 219 TALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGsSNLKRVTLELGGKSPNIIMS 298
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 299 DADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDsRTEQGPQVDETQFKKILGYIKS 378
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 379 GQQEGAKLLCGGGAAADR---GYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDL 455
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 13529509 456 DKANYLSQALQAGTVWINCY-DVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-511 |
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: 524.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 41 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTY 120
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 121 LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYH-----GKTIpidgdffsyTRHEPVGVCGQIIPWNFPLLMQA 195
Cdd:cd07138 78 LAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEfeerrGNSL---------VVREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 196 WKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVA 275
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 276 AGSSnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFD 355
Cdd:cd07138 229 AADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 356 SRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGG---GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTI 432
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13529509 433 EEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVT 511
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
58-511 |
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: 523.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyVISY 137
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 LVDLDMVLKCLRYYAGWA---DKYHGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSP 293
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAA-AQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKIL 373
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 374 GYIKSGQQEGAKLLCGGGAAA--DRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVF 451
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 452 TKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVT 511
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
61-512 |
1.30e-179 |
|
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: 512.27 E-value: 1.30e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 61 PSTGEVICQVAEGNKEDVDKAVKAARAAFQLGsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISyLVD 140
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 141 LDMVLKCLRYYAGWADKYHGKTIPIDG-DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLT 219
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 220 ALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIqVAAGSSNLKRVTLELGGKSPNIIMSD 299
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAI-AAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 300 ADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSG 379
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 380 QQEGAKLLCGGGAAADR-GYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKA 458
Cdd:cd07118 321 RAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 13529509 459 NYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
59-512 |
1.46e-177 |
|
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: 506.97 E-value: 1.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISyL 138
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 217
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 218 LTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQVAAgsSNLKRVTLELGGKSPNII 296
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGkLLMAQAA--DTVKRVSLELGGNAPFIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 297 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYI 376
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 377 KSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLD 456
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 13529509 457 KANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
26-511 |
5.04e-177 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 507.73 E-value: 5.04e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 26 AVPAPnhqpevfCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAF--QLGSPWRRMDASDR 103
Cdd:PLN02467 2 AIPVP-------RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 104 GRLLYRLADLIERDRTYLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGK-----TIPIDgDFFSYTRHEPV 178
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 179 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVD 258
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 259 KVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFV 338
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAA-AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 339 ERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAAD--RGYFIQPTVFGDVKDGMTIAK 416
Cdd:PLN02467 312 EKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 417 EEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGREL 496
Cdd:PLN02467 392 EEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGREL 471
|
490
....*....|....*
gi 13529509 497 GEYGLQAYTEVKTVT 511
Cdd:PLN02467 472 GEWGLENYLSVKQVT 486
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
83-512 |
8.93e-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: 499.06 E-value: 8.93e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 83 KAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKT 162
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 163 IP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVP 241
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 242 GFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGsSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCC 321
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 322 CAGSRTFVQENVYDEFVERSVaraksrvvgnpfdsrteqgpqvdetqfkkilgyiksgqqegakllcgggaaadrgyfiq 401
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 402 pTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVF-GA 480
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 13529509 481 QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
42-504 |
2.09e-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: 497.69 E-value: 2.09e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKyhgktipIDGDFfsyTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 201
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTEL---AGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 202 LATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVA-AGSSn 280
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 281 lKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQ 360
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 361 GPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRAN 440
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 441 DSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAY 504
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-510 |
2.41e-170 |
|
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: 489.06 E-value: 2.41e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlGSPWRrMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYL 138
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGK-TIPIDGDFFSYT----RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQvAAGSSNLKRVTLELGGKSP 293
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIM-AQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKIL 373
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 374 GYIKSGQQEGAKLLCGGGAAA--DRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVF 451
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 13529509 452 TKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
41-512 |
4.31e-170 |
|
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: 488.62 E-value: 4.31e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 41 IFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGsPWRRMDASDRGRLLYRLADLIERDRTY 120
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 121 LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTI---PIDGDffSYTRHEPVGVCGQIIPWNFPLLMQAWK 197
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERrpgSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 198 LGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAG 277
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 278 SsNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSR 357
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 358 TEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGG--AAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEV 435
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 436 VGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVfGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-512 |
3.85e-169 |
|
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: 485.68 E-value: 3.85e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYL 138
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGktiPIDGDFF----SYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 214
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 215 QTPLTALYVANLIKEaGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPN 294
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAA-ADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 295 IIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILG 374
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 375 YIkSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKD 454
Cdd:cd07092 314 FV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 13529509 455 LDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
40-513 |
1.18e-167 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 482.87 E-value: 1.18e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWhDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGK-TIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKaAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQVAAG 277
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGkHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 278 SsnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSR 357
Cdd:PRK13473 239 S--VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 358 TEQGPQVDETQFKKILGYIKSGQQEG-AKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVV 436
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 437 GRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-512 |
1.99e-162 |
|
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: 468.16 E-value: 1.99e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYL 138
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 vDLDMVLKCLRYYAGWADKyhGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 218
Cdd:cd07106 79 -EVGGAVAWLRYTASLDLP--DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 219 TALYVANLIKEAgFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIqVAAGSSNLKRVTLELGGKSPNIIMS 298
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKV-MASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 299 DADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKS 378
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 379 GQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKA 458
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 13529509 459 NYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
42-510 |
2.18e-161 |
|
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: 466.73 E-value: 2.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSrkTFPTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTY 120
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 121 LAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 199
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 200 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGsS 279
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 280 NLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTE 359
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 360 QGPQVDETQFKKILGYIKSGQQEGAKLLCGGGA--AADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVG 437
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13529509 438 RANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINC----YDVfgaQSPFGGYKMSGSG-RELGEYGLQAYTEVKTV 510
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptagVDY---HVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
42-512 |
3.09e-161 |
|
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: 466.44 E-value: 3.09e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTG-EVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTY 120
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 121 LAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 199
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 200 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSS 279
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 280 NlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTE 359
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 360 QGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAA----ADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEV 435
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 436 VGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVfGA--QSPFGGYKMSGSG-RELGEYGLQAYTEVKTVTV 512
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTI-GAevHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
58-512 |
5.60e-161 |
|
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: 464.91 E-value: 5.60e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGK------ 131
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNalrtqa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 132 -PYVISyLVDLdmvlkcLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 210
Cdd:cd07108 78 rPEAAV-LADL------FRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 211 KVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGsSNLKRVTLELGG 290
Cdd:cd07108 151 KAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 291 KSPNIIMSDADMDWAVEQAHFAL-FFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQF 369
Cdd:cd07108 229 KSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 370 KKILGYIKSGQQE-GAKLLCGG----GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKY 444
Cdd:cd07108 309 AKVCGYIDLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13529509 445 GLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELG-EYGLQAYTEVKTVTV 512
Cdd:cd07108 389 GLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
42-510 |
1.05e-160 |
|
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: 464.82 E-value: 1.05e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFS-YTRHEPVGVCGQIIPWNFPLLMQAWKLGP 200
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 201 ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIqVAAGSSN 280
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKI-MEAAAEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 281 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQ 360
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 361 GPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAA-DRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRA 439
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13529509 440 NDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
42-512 |
2.11e-160 |
|
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: 464.23 E-value: 2.11e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 201
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 202 LATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSSNL 281
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA-SENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 282 KRVTLELGGKSPNI----IMS--DADMDWAVEQahFALF-FNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPF 354
Cdd:cd07116 239 IPVTLELGGKSPNIffadVMDadDAFFDKALEG--FVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 355 DSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAA-----ADRGYFIQPTVFGDVKdgMTIAKEEIFGPVMQILKF 429
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelgglLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 430 KTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKT 509
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474
|
...
gi 13529509 510 VTV 512
Cdd:cd07116 475 LLV 477
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-510 |
5.60e-156 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 453.58 E-value: 5.60e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 39 NQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSpWRRMDASDRGRLLYRLADLIERDR 118
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 119 TYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGS 278
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 SNLKRVTLELGGKSPNIIMSDA-DMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSR 357
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 358 TEQGPQVDETQFKKILGYIKSGQQEGaKLLCGGGAAADRGYfIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVG 437
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13529509 438 RANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
58-512 |
8.98e-155 |
|
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: 449.13 E-value: 8.98e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYViSY 137
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 217
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 218 LTALYVANLIKEAgFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSnLKRVTLELGGKSPNIIM 297
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 298 SDADMDWAVEQAHFALFFN-QGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYI 376
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 377 KSGQQEGAKLLCGGGAAAD----RGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFT 452
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 453 KDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
42-513 |
1.29e-152 |
|
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: 444.58 E-value: 1.29e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgSPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTI------PIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQA 195
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 196 WKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEGVDKVAFTGSTEVGHLIQVA 275
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 276 AgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFD 355
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 356 SRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPT--VFGDVKDgmTIAKEEIFGPVMQILKFKTIE 433
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADS--RLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 434 EVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
56-512 |
1.26e-148 |
|
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: 433.29 E-value: 1.26e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 56 FPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYV- 134
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 135 ----ISYLVDLdmvlkcLRYYAGWADKYHGKTIPIDG-DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVV 209
Cdd:cd07150 78 awfeTTFTPEL------LRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 210 MKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELG 289
Cdd:cd07150 152 LKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 290 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQF 369
Cdd:cd07150 231 GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 370 KKILGYIKSGQQEGAKLLCGGGAAadrGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAA 449
Cdd:cd07150 311 ERIKRQVEDAVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 450 VFTKDLDKANYLSQALQAGTVWINCYDVFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
36-510 |
9.60e-146 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 427.57 E-value: 9.60e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 36 VFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIE 115
Cdd:PLN02278 22 LLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 116 RDRTYLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWADKYHGKTIPI-DGDFFSYTRHEPVGVCGQIIPWNFPLLMQ 194
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKP-LKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 195 AWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQV 274
Cdd:PLN02278 178 TRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 275 AAGSSnLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPF 354
Cdd:PLN02278 258 GAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 355 DSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEE 434
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13529509 435 VVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
41-514 |
3.85e-144 |
|
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: 423.94 E-value: 3.85e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 41 IFINNEWHDavSRKTFPTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLG 199
Cdd:cd07124 110 ELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 200 PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLI-----QV 274
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIyeraaKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 275 AAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPF 354
Cdd:cd07124 269 QPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 355 DSRTEQGPQVDETQFKKILGYIKSGQQEGaKLLCGGGAAAD--RGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTI 432
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 433 EEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcYDVFGAQS---PFGGYKMSGSG-RELGEYGLQAYTEVK 508
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN-RKITGALVgrqPFGGFKMSGTGsKAGGPDYLLQFMQPK 506
|
....*.
gi 13529509 509 TVTVKV 514
Cdd:cd07124 507 TVTENF 512
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
77-512 |
4.83e-143 |
|
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: 418.47 E-value: 4.83e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 77 DVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYlVDLDMVLKCLRYYAGWAD 156
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 157 KYHGKTIPIDGD-FFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLT-ALYVANLIKEAGFPP 234
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 235 GVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALF 314
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 315 FNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAa 394
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 395 drGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINC 474
Cdd:cd07104 315 --GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 13529509 475 YDVF-GAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
56-512 |
5.12e-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: 413.92 E-value: 5.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 56 FPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGspwRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyvI 135
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 136 SY-LVDLDMVLKCLRYYAGWADKYHGKTIPIDG-----DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVV 209
Cdd:cd07149 76 KDaRKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 210 MKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGssnLKRVTLELG 289
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 290 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQF 369
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 370 KKILGYIKSGQQEGAKLLCGGGAaadRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAA 449
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 450 VFTKDLDKANYLSQALQAGTVWINCYDVFGA-QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
42-512 |
1.63e-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: 413.50 E-value: 1.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAvSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPY------VISYLvdlDMVlkclrYYA-GWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLM 193
Cdd:cd07086 78 GRLVSLEMGKILpeglgeVQEMI---DIC-----DYAvGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 194 QAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEA----GFPPGVVNIVPGFGPtAGAAIASHEGVDKVAFTGSTEVG 269
Cdd:cd07086 150 PGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 270 HLIQVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRV 349
Cdd:cd07086 229 RRVGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 350 VGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAA--ADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQIL 427
Cdd:cd07086 308 IGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 428 KFKTIEEVVGRANDSKYGLAAAVFTKDLDKA-NYLSQA-LQAGTVWINCyDVFGA--QSPFGGYKMSGSGRELGEYGLQA 503
Cdd:cd07086 388 KFDSLEEAIAINNDVPQGLSSSIFTEDLREAfRWLGPKgSDCGIVNVNI-PTSGAeiGGAFGGEKETGGGRESGSDAWKQ 466
|
....*....
gi 13529509 504 YTEVKTVTV 512
Cdd:cd07086 467 YMRRSTCTI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
56-512 |
2.17e-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: 404.81 E-value: 2.17e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 56 FPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyVI 135
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKP-IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 136 SYLVDLDMVLKCLRYYAGWADKYHGKTIPIDG-----DFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 210
Cdd:cd07145 77 QSRVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 211 KVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSnLKRVTLELGG 290
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 291 KSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFK 370
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 371 KILGYIKSGQQEGAKLLCGGgaAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAV 450
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGG--KRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13529509 451 FTKDLDKANYLSQALQAGTVWINCYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
58-512 |
4.06e-135 |
|
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: 399.03 E-value: 4.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlGSPWRRmDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyVISY 137
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKI-LGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 LVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 217
Cdd:cd07120 78 RFEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 218 LTALYVANLIKEA-GFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQvAAGSSNLKRVTLELGGKSPNII 296
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIM-AAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 297 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYI 376
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 377 KSGQQEGAKLLCGGGAAAD---RGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTK 453
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 13529509 454 DLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
45-513 |
1.88e-127 |
|
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: 379.73 E-value: 1.88e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 45 NEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAfqlGSPWRRMDASDRGRLLYRLADLIERDRTYLAAL 124
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 125 ETLDNGKPYvISYLVDLDMVLKCLRYYAGWADKYHGKTIP--IDGDFfSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPAL 202
Cdd:cd07151 78 LIRESGSTR-IKANIEWGAAMAITREAATFPLRMEGRILPsdVPGKE-NRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 203 ATGNVVVMKVAEQTPLTA-LYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQVAAGssN 280
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGrHIGELAGR--H 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 281 LKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQ 360
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 361 GPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAadrGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRAN 440
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 441 DSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFG-AQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
78-512 |
3.38e-127 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 377.57 E-value: 3.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 78 VDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISylvdLDMVLKC---LRYYAGW 154
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA----RAEVEKCawiCRYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 155 ADKY-HGKTIPIDGDFfSYTRHEPVGVCGQIIPWNFPLlmqaWK----LGPALATGNVVVMKVAEQTPLTALYVANLIKE 229
Cdd:cd07100 74 AEAFlADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 230 AGFPPGVVNIVPGFGPTAGAAIAsHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELGGKSPNIIMSDADMDWAVEQA 309
Cdd:cd07100 149 AGFPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 310 HFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCG 389
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 390 GGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGT 469
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 13529509 470 VWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
43-511 |
2.10e-123 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 371.19 E-value: 2.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 43 INNEWHDavSRKTFPTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:PRK03137 41 IGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYV-----ISYLVDLdmvlkcLRYYAGWADKY-HGKTI-PIDGDFFSYtRHEPVGVCGQIIPWNFPLLMQ 194
Cdd:PRK03137 116 SAWLVKEAGKPWAeadadTAEAIDF------LEYYARQMLKLaDGKPVeSRPGEHNRY-FYIPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 195 AWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQ 273
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 274 VAA----GSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRV 349
Cdd:PRK03137 269 RAAkvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 350 VGNPfDSRTEQGPQVDETQFKKILGYIKSGQQEGaKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKF 429
Cdd:PRK03137 349 VGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 430 KTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWIN--CYD-VFGAQsPFGGYKMSGSGRELG--EYgLQAY 504
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGaIVGYH-PFGGFNMSGTDSKAGgpDY-LLLF 504
|
....*..
gi 13529509 505 TEVKTVT 511
Cdd:PRK03137 505 LQAKTVS 511
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
59-512 |
4.68e-122 |
|
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: 365.39 E-value: 4.68e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYL 138
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 vDLDMVLKCLRYYAGWADKYHGKTIPIDGDFF----SYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 214
Cdd:cd07099 78 -EVLLALEAIDWAARNAPRVLAPRKVPTGLLMpnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 215 QTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASheGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPN 294
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAA-AERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 295 IIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILG 374
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 375 YIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKD 454
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 455 LDKANYLSQALQAGTVWINCYDVFGAQS--PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPalPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
40-513 |
1.61e-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: 364.92 E-value: 1.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:cd07085 79 ELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQvAAGS 278
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIY-ERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRT 358
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 359 EQGPQVDETQFKKILGYIKSGQQEGAKLLCGG----GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEE 434
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 435 VVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcydV--------FgaqsPFGGYKMSGSGrELGEYGLQA--- 503
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VpipvplafF----SFGGWKGSFFG-DLHFYGKDGvrf 467
|
490
....*....|
gi 13529509 504 YTEVKTVTVK 513
Cdd:cd07085 468 YTQTKTVTSR 477
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
59-512 |
2.05e-121 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 364.06 E-value: 2.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISyL 138
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGKTIPID-----GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGssnLKRVTLELGGKSP 293
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKIL 373
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 374 GYIKSGQQEGAKLLCGGgaaADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTK 453
Cdd:cd07094 317 RWVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 454 DLDKANYLSQALQAGTVWINCYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-512 |
8.32e-119 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 359.58 E-value: 8.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 49 DAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAfQLGspWRRMDASDRGRLLYRLADLIERDRTYLAALETLD 128
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 129 NGKPYVISYLVDLDMVLkCLRYYAGWADKY-----HGKTIPIDGDffSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALA 203
Cdd:PRK09407 104 TGKARRHAFEEVLDVAL-TARYYARRAPKLlaprrRAGALPVLTK--TTELRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 204 TGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIAshEGVDKVAFTGSTEVGHLIQVAAGSsNLKR 283
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGR-RLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 284 VTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQ 363
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 364 VDETQFKKILGYIKSGQQEGAKLLCGGGAAADRG-YFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDS 442
Cdd:PRK09407 338 ISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDT 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13529509 443 KYGLAAAVFTKDLDKANYLSQALQAGTVWINcyDVFGA-----QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:PRK09407 418 PYGLNASVWTGDTARGRAIAARIRAGTVNVN--EGYAAawgsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
61-512 |
3.30e-117 |
|
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: 353.15 E-value: 3.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 61 PSTGEVICQVAEGNKEDVDKAVKAARAAfQLGspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVD 140
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 141 LDMVLKClRYYAGWADKY-----HGKTIPIdgdfFSYTR--HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07101 80 LDVAIVA-RYYARRAERLlkprrRRGAIPV----LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHegVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELGGKSP 293
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKIL 373
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 374 GYIKSGQQEGAKLLCGGGAAADRG-YFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFT 452
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13529509 453 KDLDKANYLSQALQAGTVWINcyDVFGA-----QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVN--EGYAAawasiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
40-513 |
1.17e-114 |
|
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: 347.25 E-value: 1.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHDAvSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgSPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPY---------VISYLVDLDMVLKclryyagwadKYHGKTIPIDGDFFS-----YTRHEPVGVCGQII 185
Cdd:cd07082 80 EVANLLMWEIGKTLkdalkevdrTIDYIRDTIEELK----------RLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 186 PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGS 265
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 266 TEVGHLIQVAAGssnLKRVTLELGGKSPNIIMSDADMDWAVEQ-AHFALFFNqGQCCCAGSRTFVQENVYDEFVERSVAR 344
Cdd:cd07082 230 TEVGNRLKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEiVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 345 AKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGaaADRGYFIQPTVFGDVKDGMTIAKEEIFGPVM 424
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 425 QILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCY-----DVFgaqsPFGGYKMSGSGRELGEY 499
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQGIGD 459
|
490
....*....|....
gi 13529509 500 GLQAYTEVKTVTVK 513
Cdd:cd07082 460 ALRSMTRRKGIVIN 473
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
59-510 |
1.65e-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: 346.16 E-value: 1.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyvISYL 138
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP--IAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 V-DLDMVLKCLRYYAGWADKY-HGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQT 216
Cdd:cd07102 76 GgEIRGMLERARYMISIAEEAlADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 217 PLTALYVANLIKEAGFPPGVVNIVPGFGPTaGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELGGKSPNII 296
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 297 MSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYI 376
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 377 KSGQQEGAKLLCGGG---AAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTK 453
Cdd:cd07102 314 ADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 454 DLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
56-508 |
7.81e-113 |
|
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: 341.92 E-value: 7.81e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 56 FPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVI 135
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 136 SYlVDLDMVLKCLRYYAGWADKYHGKTIPIDGD-----FFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 210
Cdd:cd07147 78 AR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 211 KVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfgPTAGAAI-ASHEGVDKVAFTGSTEVGHLIQVAAGSsnlKRVTLELG 289
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 290 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQF 369
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 370 KKILGYIKSGQQEGAKLLCGGGAaadRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAA 449
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13529509 450 VFTKDLDKANYLSQALQAGTVWINcyDV--FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVK 508
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVIN--DVptFRVDHmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
77-512 |
2.21e-112 |
|
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: 339.94 E-value: 2.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 77 DVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWAD 156
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 157 KYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPG 235
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 236 VVNIV---PGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFA 312
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 313 LFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNpfdsrTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGA 392
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 393 AA-DRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVW 471
Cdd:cd07105 311 DEsPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 13529509 472 IN---CYDvfGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07105 391 INgmtVHD--EPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
64-512 |
8.91e-111 |
|
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: 336.19 E-value: 8.91e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 64 GEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNG----KPyvisyLV 139
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsirpKA-----GF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 140 DLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLT 219
Cdd:cd07152 73 EVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 220 ALYV-ANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSsNLKRVTLELGGKSPNIIMS 298
Cdd:cd07152 153 GGVViARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 299 DADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKS 378
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 379 GQQEGAKLLCGGGAaadRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKA 458
Cdd:cd07152 311 SVAAGARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 13529509 459 NYLSQALQAGTVWINCYDVF-GAQSPFGGYKMSGSG-RELGEYGLQAYTEVKTVTV 512
Cdd:cd07152 388 MALADRLRTGMLHINDQTVNdEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
34-508 |
7.26e-110 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 335.34 E-value: 7.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 34 PEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADL 113
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 114 IERDRTYLAALETLDNGKPYV-----ISYLVDLdmvlkcLRYYAGWADKYHGKTIP-IDGDFFSYTRHEPVGVCGQIIPW 187
Cdd:PRK11241 83 MMEHQDDLARLMTLEQGKPLAeakgeISYAASF------IEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 188 NFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTE 267
Cdd:PRK11241 157 NFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 268 VGHLIqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKS 347
Cdd:PRK11241 237 IGRQL-MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 348 RVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQIL 427
Cdd:PRK11241 316 LHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 428 KFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEV 507
Cdd:PRK11241 396 RFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEI 475
|
.
gi 13529509 508 K 508
Cdd:PRK11241 476 K 476
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
59-512 |
8.04e-110 |
|
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: 333.94 E-value: 8.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAAraafqlGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISyL 138
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGKTIPID-----GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGssnLKRVTLELGGKSP 293
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKIL 373
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 374 GYIKSGQQEGAKLLCGGGAaadRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTK 453
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13529509 454 DLDKANYLSQALQAGTVwiNCYDVFGAQ---SPFGGYKMSGSG-RELGEYGLQAYTEVKTVTV 512
Cdd:cd07146 391 DLDTIKRLVERLDVGTV--NVNEVPGFRselSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
58-511 |
1.32e-108 |
|
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: 332.99 E-value: 1.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVIS 136
Cdd:TIGR01237 50 SINPCdKSEVVGTVSKASQEHAEHALQAAAKAFE---AWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 137 YlVDLDMVLKCLRYYAGWADKY--HGKTIPIDGDFFSYTrHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 214
Cdd:TIGR01237 127 D-AEVAEAIDFMEYYARQMIELakGKPVNSREGETNQYV-YTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 215 QTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVG-HLIQVAA----GSSNLKRVTLELG 289
Cdd:TIGR01237 205 AAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGtRIFERAAkvqpGQKHLKRVIAEMG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 290 GKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQF 369
Cdd:TIGR01237 285 GKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 370 KKILGYIKSGQQEGaKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAA 449
Cdd:TIGR01237 365 NKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGG 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13529509 450 VFTKDLDKANYLSQALQAGTVWIN--CYDVFGAQSPFGGYKMSGSGRELG--EYgLQAYTEVKTVT 511
Cdd:TIGR01237 444 VISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQAKTVT 508
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
107-510 |
2.50e-105 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 320.92 E-value: 2.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 107 LYRLADLIERDRTYLAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPID---GDFFSYTRhePVGVCGQ 183
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 184 IIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFT 263
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 264 GSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVA 343
Cdd:PRK10090 158 GSVSAGEKIMAAA-AKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 344 RAKSRVVGNPFD-SRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGP 422
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 423 VMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQ 502
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 13529509 503 AYTEVKTV 510
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
59-512 |
7.29e-98 |
|
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: 303.84 E-value: 7.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYL 138
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKyHGKTIPIDGDFF-----SYTRHEPVGVCGQIIPWNFPL--LmqawkLGPALA---TGNVV 208
Cdd:cd07098 78 GEILVTCEKIRWTLKHGEK-ALRPESRPGGLLmfykrARVEYEPLGVVGAIVSWNYPFhnL-----LGPIIAalfAGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 209 VMKVAEQTPLTALYVANLIKEA----GFPPGVVNIVPGFGPTaGAAIASHEGVDKVAFTGSTEVGHLIQVAAgSSNLKRV 284
Cdd:cd07098 152 VVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAA-AESLTPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 285 TLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQV 364
Cdd:cd07098 230 VLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 365 DETQFKKILGYIKSGQQEGAKLLCGG----GAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRAN 440
Cdd:cd07098 310 SPARFDRLEELVADAVEKGARLLAGGkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 441 DSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDV-FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTV 512
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVnYYVQQlPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
58-510 |
2.41e-93 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 291.64 E-value: 2.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISY 137
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 lvdlDMVLKC---LRYYAGWADKYHGKTiPID----GDFFSYTRHEPVGVCGQIIPWNFPLlmqaWKL----GPALATGN 206
Cdd:PRK09406 82 ----AEALKCakgFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 207 VVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPgFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSnLKRVTL 286
Cdd:PRK09406 153 VGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 287 ELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDE 366
Cdd:PRK09406 231 ELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 367 TQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGL 446
Cdd:PRK09406 311 QGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 447 AAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
41-511 |
8.80e-91 |
|
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: 286.78 E-value: 8.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 41 IFINNEWHDAVSRKTfpTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRT 119
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 120 YLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWADKYHGK---TIPIDGDFFSyTRHEPVGVCGQIIPWNFPLLMQAW 196
Cdd:cd07083 96 ELIATLTYEVGKN-WVEAIDDVAEAIDFIRYYARAALRLRYPaveVVPYPGEDNE-SFYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 197 KLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLI---- 272
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeaa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 273 -QVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVG 351
Cdd:cd07083 254 aRLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 352 NPFDSRTEQGPQVDETQFKKILGYIKSGQQEGaKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKT 431
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 432 IE--EVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcYDVFGA---QSPFGGYKMSGSGRELG--EYgLQAY 504
Cdd:cd07083 413 DDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN-RKITGAlvgVQPFGGFKLSGTNAKTGgpHY-LRRF 490
|
....*..
gi 13529509 505 TEVKTVT 511
Cdd:cd07083 491 LEMKAVA 497
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
44-512 |
4.91e-86 |
|
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: 273.31 E-value: 4.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 44 NNEWhdAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAA 123
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 124 LETLDNGKPYV-----ISYLVDLdmvlkClRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWK 197
Cdd:cd07130 79 LVSLEMGKILPeglgeVQEMIDI-----C-DFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 198 LGPALATGNVVVMKVAEQTPLTALYVANLIKEA----GFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQ 273
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 274 VAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNP 353
Cdd:cd07130 232 QAV-AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 354 FDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDgMTIAKEEIFGPVMQILKFKTIE 433
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 434 EVVGRANDSKYGLAAAVFTKDLDKA-NYLSQA-LQAGTVWINC----YDVFGAqspFGGYKMSGSGRELGEYGLQAYTEV 507
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAfRWLGPKgSDCGIVNVNIgtsgAEIGGA---FGGEKETGGGRESGSDAWKQYMRR 466
|
....*
gi 13529509 508 KTVTV 512
Cdd:cd07130 467 STCTI 471
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
39-517 |
3.09e-85 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 272.53 E-value: 3.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 39 NQIFINNEWHDAVSRktfptvnPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDR 118
Cdd:cd07125 39 GEETETGEGAPVIDP-------ADHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 119 ---TYLAALE---TLDNGKPYViSYLVDLdmvlkcLRYYAGWADKYHGKtiPIDGDFFSYTRH---EP--VGVCgqIIPW 187
Cdd:cd07125 109 gelIALAAAEagkTLADADAEV-REAIDF------CRYYAAQARELFSD--PELPGPTGELNGlelHGrgVFVC--ISPW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 188 NFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTE 267
Cdd:cd07125 178 NFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 268 VGHLIQVAAGSSNLKRVTL--ELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARA 345
Cdd:cd07125 258 TAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 346 KSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEgAKLLCGGGAAADRGYFIQPTVFGDVKDGmTIaKEEIFGPVMQ 425
Cdd:cd07125 338 ASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF-DL-TTEVFGPILH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 426 ILKFK--TIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcYDVFGA----QsPFGGYKMSGSGRELG-- 497
Cdd:cd07125 415 VIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFGGWGLSGTGPKAGgp 492
|
490 500
....*....|....*....|
gi 13529509 498 EYgLQAYTEVKTVTVKVPQK 517
Cdd:cd07125 493 NY-LLRFGNEKTVSLNTTAA 511
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
42-513 |
4.53e-75 |
|
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: 244.79 E-value: 4.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPYViSYLVDLDMVLKCLRYYAGWADKYHGKTIP---IDGDFFSYTrhEPVGVCGQIIPWNFPLLMQAWKL 198
Cdd:TIGR01722 81 AELITAEHGKTHS-DALGDVARGLEVVEHACGVNSLLKGETSTqvaTRVDVYSIR--QPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQvAAGS 278
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIH-TTGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSrTFVQENVYDEFVERSVARAKSRVVGNPFDSRT 358
Cdd:TIGR01722 236 AHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 359 EQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGY----FIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEE 434
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 435 VVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINC-YDVFGAQSPFGGYKMS--GSGRELGEYGLQAYTEVKTVT 511
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVpIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
..
gi 13529509 512 VK 513
Cdd:TIGR01722 475 TR 476
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
95-510 |
3.45e-73 |
|
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: 238.67 E-value: 3.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 95 WRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAG----W-ADKYHGKTIPIDGDF 169
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKhlkkWmKPKRVRTPLLLFGTK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 170 fSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGfgptaGA 249
Cdd:cd07134 94 -SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 250 AIASH---EGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSR 326
Cdd:cd07134 167 EVAQAlleLPFDHIFFTGSPAVGKIVMAAA-AKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 327 TFVQENVYDEFVERSVARAKsRVVGNpfDSRTEQGPQ----VDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYfIQP 402
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIE-KFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRY-IAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 403 TVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcyDVFG--- 479
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN--DVVLhfl 399
|
410 420 430
....*....|....*....|....*....|..
gi 13529509 480 -AQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07134 400 nPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
77-494 |
1.63e-71 |
|
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: 234.09 E-value: 1.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 77 DVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPY------VISYLVDLDMVLKCLRY 150
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 151 YAGwadkyhGKTIPIdGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEA 230
Cdd:cd07095 78 RTG------ERATPM-AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 231 GFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLI-QVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQA 309
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 310 HFALFFNQGQCCCAGSRTFVQEN-VYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKilgYIKSGQQ---EGAK 385
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR---YLLAQQDllaLGGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 386 LLCGGGAAADRGYFIQPTVFgDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQAL 465
Cdd:cd07095 306 PLLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420 430
....*....|....*....|....*....|.
gi 13529509 466 QAGTVWINcYDVFGAQS--PFGGYKMSGSGR 494
Cdd:cd07095 385 RAGIVNWN-RPTTGASStaPFGGVGLSGNHR 414
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
58-510 |
2.35e-71 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 234.76 E-value: 2.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 58 TVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISY 137
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 138 lvdlDMVLKClryyAGWADKY--HG----KTIP-IDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 210
Cdd:PRK13968 88 ----AEVAKS----ANLCDWYaeHGpamlKAEPtLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 211 KVAEQTPLTALYVANLIKEAGFPPGVVNIVPgfgptagaaiASHEGVDK---------VAFTGSTEVGHLIQVAAGSSnL 281
Cdd:PRK13968 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLN----------ADNDGVSQmindsriaaVTVTGSVRAGAAIGAQAGAA-L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 282 KRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQG 361
Cdd:PRK13968 229 KKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 362 PQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRAND 441
Cdd:PRK13968 309 PMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELAND 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13529509 442 SKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:PRK13968 389 SEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
81-510 |
2.03e-70 |
|
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: 231.26 E-value: 2.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 81 AVKAARAAFQLGS----PWRRmdasDRGRLLYRLadLIERDRTYLAALETlDNGKPYVISYLVDLDMVLKCLRYY----A 152
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRK----AQLKALKRM--LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHAlkhlK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 153 GWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLIKE 229
Cdd:cd07087 76 KWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 230 AgFPPGVVNIVPGFGPTAGAAIAshEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQA 309
Cdd:cd07087 153 Y-FDPEAVAVVEGGVEVATALLA--EPFDHIFFTGSPAVGKIVMEAA-AKHLTPVTLELGGKSPCIVDKDANLEVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 310 HFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRtEQGPQVDETQFKKILGYIKSGqqegaKLLCG 389
Cdd:cd07087 229 AWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDG-----KVVIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 390 GGA-AADRgyFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAG 468
Cdd:cd07087 303 GQVdKEER--YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSG 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 13529509 469 TVWINcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07087 381 GVCVN--DVllhAAIPNlPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
57-512 |
2.27e-70 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 243.18 E-value: 2.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 57 PTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGK--PY 133
Cdd:PRK11904 565 PVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAGKtlQD 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 134 VISYL---VDLdmvlkcLRYYAGWADKYHGKTIPIDGdffsytrhePVG-------------VCgqIIPWNFPLlmqAWK 197
Cdd:PRK11904 642 AIAEVreaVDF------CRYYAAQARRLFGAPEKLPG---------PTGesnelrlhgrgvfVC--ISPWNFPL---AIF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 198 LGP---ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQV 274
Cdd:PRK11904 702 LGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 275 AAGSSNLKRVTL--ELGGKSPNIIMSDA-------DmdwAVEQAhfalFFNQGQCCCAGSRTFVQENVYDEFVERSVARA 345
Cdd:PRK11904 782 TLAARDGPIVPLiaETGGQNAMIVDSTAlpeqvvdD---VVTSA----FRSAGQRCSALRVLFVQEDIADRVIEMLKGAM 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 346 KSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEgAKLLCGG--GAAADRGYFIQPTVF--GDVKDgmtiAKEEIFG 421
Cdd:PRK11904 855 AELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLplPAGTENGHFVAPTAFeiDSISQ----LEREVFG 929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 422 PVMQILKFKT--IEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcYDVFGA----QsPFGGYKMSGSGRE 495
Cdd:PRK11904 930 PILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ-PFGGQGLSGTGPK 1007
|
490
....*....|....*....
gi 13529509 496 LG--EYgLQAYTEVKTVTV 512
Cdd:PRK11904 1008 AGgpHY-LLRFATEKTVTV 1025
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
59-493 |
4.73e-68 |
|
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: 225.76 E-value: 4.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWrrMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISyL 138
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 139 VDLDMVLKCLRYYAGWADKYHGKTIPID-----GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 213
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 214 EQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEgVDKVAFTGSTEVGHLI--QVAAGSsnlkRVTLELGGK 291
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLrsKLAPGT----RCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 292 SPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKK 371
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 372 ILGYIKSGQQEGAKLLCGGGAAADRGYfiQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVF 451
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 13529509 452 TKDLDKANYLSQALQAGTVWINCYDVFGAQ-SPFGGYKMSGSG 493
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
49-493 |
8.44e-67 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 233.68 E-value: 8.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 49 DAVSRKTFPTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAAL--- 124
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALlvr 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 125 E---TLDNGkpyvISYL---VDLdmvlkcLRYYAGWADKyhgktipidgDFFSYTRHEPVGVCGQIIPWNFPLlmqAWKL 198
Cdd:COG4230 642 EagkTLPDA----IAEVreaVDF------CRYYAAQARR----------LFAAPTVLRGRGVFVCISPWNFPL---AIFT 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 199 GP---ALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLI--Q 273
Cdd:COG4230 699 GQvaaALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrT 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 274 VAAGSSNLkrVTL--ELGGKSPNIIMSDA-------DmdwAVEQAhfalFFNQGQCCCAGSRTFVQENVYDEFVERSVAR 344
Cdd:COG4230 779 LAARDGPI--VPLiaETGGQNAMIVDSSAlpeqvvdD---VLASA----FDSAGQRCSALRVLCVQEDIADRVLEMLKGA 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 345 AKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGaKLL--CGGGAAADRGYFIQPTVF--GDVKDgmtiAKEEIF 420
Cdd:COG4230 850 MAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVhqLPLPEECANGTFVAPTLIeiDSISD----LEREVF 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 421 GPVMQILKFK--TIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGtvwiNCY-------DVFGAQsPFGGYKMSG 491
Cdd:COG4230 925 GPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYvnrniigAVVGVQ-PFGGEGLSG 999
|
..
gi 13529509 492 SG 493
Cdd:COG4230 1000 TG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
57-508 |
3.07e-65 |
|
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: 219.78 E-value: 3.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 57 PTVNPSTGEVIC-QVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVI 135
Cdd:TIGR01238 54 PVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 136 SyLVDLDMVLKCLRYYAGWADkyhgktipidgDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQ 215
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 216 TPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTL--ELGGKSP 293
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 294 NIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKIL 373
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 374 GYIKSGQQEG---AKLLCGGGAAADRGYFIQPTVFGdvKDGMTIAKEEIFGPVMQILKFKT--IEEVVGRANDSKYGLAA 448
Cdd:TIGR01238 359 AHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTM 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13529509 449 AVFTKDLDKANYLSQALQAGTVWINcYDVFGA---QSPFGGYKMSGSG-RELGEYGLQAYTEVK 508
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVN-RNQVGAvvgVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
42-494 |
1.45e-64 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 217.52 E-value: 1.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHdAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFqlgSPWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKPY------VISYLVDLDMVLKClryyagwadkYHGKTIPIDGDFFSYT---RHEPVGVCGQIIPWNFPLL 192
Cdd:PRK09457 80 AEVIARETGKPLweaateVTAMINKIAISIQA----------YHERTGEKRSEMADGAavlRHRPHGVVAVFGPYNFPGH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 193 MQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLI 272
Cdd:PRK09457 150 LPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 273 -QVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVY-DEFVERSVARAKSRVV 350
Cdd:PRK09457 229 hRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 351 GNPF-DSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFgDVKDGMTIAKEEIFGPVMQILKF 429
Cdd:PRK09457 308 GRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRY 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13529509 430 KTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTV-W---INcydvfGAQS--PFGGYKMSGSGR 494
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWnkpLT-----GASSaaPFGGVGASGNHR 452
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
76-510 |
8.21e-64 |
|
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: 214.01 E-value: 8.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 76 EDVDKAVKAARAAFQLGS----PWRRmdasdrgRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL-KCLRY 150
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKtkdlEYRL-------WQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKnDILHM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 151 YAG---WA-DKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYV 223
Cdd:cd07135 78 LKNlkkWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 224 ANLIKEAgFPPGVVNIVPGFGPTAGAAIAshEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMD 303
Cdd:cd07135 155 AELVPKY-LDPDAFQVVQGGVPETTALLE--QKFDKIFYTGSGRVGRIIAEAA-AKHLTPVTLELGGKSPVIVTKNADLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 304 WAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSvARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIksgQQEG 383
Cdd:cd07135 231 LAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLL---DTTK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 384 AKLLCGGGA-AADRgyFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLS 462
Cdd:cd07135 307 GKVVIGGEMdEATR--FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHIL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 13529509 463 QALQAGTVWINcyDVFGA----QSPFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07135 385 TRTRSGGVVIN--DTLIHvgvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
42-493 |
1.18e-63 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 224.74 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWH-------DAVSRKTFPTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADL 113
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 114 IERDRTYLAALETLDNGK--PYVISYL---VDLdmvlkcLRYYAGWADkyhgktipidgDFFSYTRHEPVGVCGQIIPWN 188
Cdd:PRK11905 625 MEAHMPELFALAVREAGKtlANAIAEVreaVDF------LRYYAAQAR-----------RLLNGPGHKPLGPVVCISPWN 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 189 FPLlmqAWKLG---PALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGS 265
Cdd:PRK11905 688 FPL---AIFTGqiaAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGS 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 266 TEVGHLIQvAAGSSNLKR-VTL--ELGGKSPNIIMSDAdmdwAVEQAHFAL----FFNQGQCCCAGSRTFVQENVYDEFV 338
Cdd:PRK11905 765 TEVARLIQ-RTLAKRSGPpVPLiaETGGQNAMIVDSSA----LPEQVVADViasaFDSAGQRCSALRVLCLQEDVADRVL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 339 ERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLL-CGGGAAADRGYFIQPTVFgDVkDGMTIAKE 417
Cdd:PRK11905 840 TMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVAPTLI-EI-DSISDLER 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 418 EIFGPVMQILKFKT--IEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWIN---CYDVFGAQsPFGGYKMSGS 492
Cdd:PRK11905 918 EVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniIGAVVGVQ-PFGGEGLSGT 996
|
.
gi 13529509 493 G 493
Cdd:PRK11905 997 G 997
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-515 |
8.03e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 213.08 E-value: 8.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 22 AATSAVPAPNHQPEVFcnQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDAS 101
Cdd:PLN00412 1 MAGTGFFAEILDGDVY--KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 102 DRGRLLYRLADLIERDRTYLAALETLDNGKPYVisylvdlDMVLKCLR------YYAGWADKYHGKTIPIDGDFFS---- 171
Cdd:PLN00412 76 KRAELLHKAAAILKEHKAPIAECLVKEIAKPAK-------DAVTEVVRsgdlisYTAEEGVRILGEGKFLVSDSFPgner 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 172 ----YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTA 247
Cdd:PLN00412 149 nkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 248 GAAIASHEGVDKVAFTGStEVGHLIQVAAGSSNLKrvtLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRT 327
Cdd:PLN00412 229 GDFLTMHPGVNCISFTGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 328 FVQENVYDEFVERSVARAKSRVVGNPFDSrTEQGPQVDETQFKKILGYIKSGQQEGAKLLcggGAAADRGYFIQPTVFGD 407
Cdd:PLN00412 305 LVMESVADALVEKVNAKVAKLTVGPPEDD-CDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 408 VKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQS-PFGG 486
Cdd:PLN00412 381 VRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQG 460
|
490 500
....*....|....*....|....*....
gi 13529509 487 YKMSGSGRELGEYGLQAYTEVKTVTVKVP 515
Cdd:PLN00412 461 LKDSGIGSQGITNSINMMTKVKSTVINLP 489
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
171-510 |
6.69e-62 |
|
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: 208.88 E-value: 6.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 171 SYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGfGPTA 247
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 248 GAAIaSHEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRT 327
Cdd:cd07133 170 AAAF-SSLPFDHLLFTGSTAVGRHVMRAA-AENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 328 FVQENVYDEFVERSVARAKSR---VVGNPFDSRTeqgpqVDETQFKKILGYIKSGQQEGAKL--LCGGGAAADRGYFIQP 402
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAKMyptLADNPDYTSI-----INERHYARLQGLLEDARAKGARVieLNPAGEDFAATRKLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 403 TVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINcyDVF--GA 480
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--DTLlhVA 400
|
330 340 350
....*....|....*....|....*....|..
gi 13529509 481 QS--PFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07133 401 QDdlPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
103-510 |
1.15e-60 |
|
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: 206.20 E-value: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 103 RGRLLYRLADLI-ERDRTYLAALEtLDNGKPYVISYLVDLDMVLKCLRYY----AGWAdkyhgKTIPIDGDFF-----SY 172
Cdd:cd07136 22 RIEQLKKLKQAIkKYENEILEALK-KDLGKSEFEAYMTEIGFVLSEINYAikhlKKWM-----KPKRVKTPLLnfpskSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 173 TRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLTALYVANLIKEAgFPPGVVNIVPGfgptaGA 249
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-----GV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 250 AIAS---HEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSR 326
Cdd:cd07136 167 EENQellDQKFDYIFFTGSVRVGKIVMEAA-AKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 327 TFVQENVYDEFVERSVARAKSRVVGNPFDSRtEQGPQVDETQFKKILGYIKSGqqegaKLLCGGGAAADRGYfIQPTVFG 406
Cdd:cd07136 246 VLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGNTDRETLY-IEPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 407 DVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQS--PF 484
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPylPF 398
|
410 420
....*....|....*....|....*.
gi 13529509 485 GGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07136 399 GGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
19-511 |
1.45e-60 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 209.99 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 19 LSAAATSAVPAPNHQPEVFCN-QIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRR 97
Cdd:PLN02419 93 LRSSWLSTSPEQSTQPQMPPRvPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 98 MDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYlVDLDMVLKCLRYYAGWADKYHGKTIP-IDGDFFSYTRHE 176
Cdd:PLN02419 170 TPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIRE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 177 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGaAIASHEG 256
Cdd:PLN02419 249 PLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 257 VDKVAFTGSTEVGHLIQVAAGSSNlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSrTFVQENVYDE 336
Cdd:PLN02419 328 IRAVSFVGSNTAGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALS-TVVFVGDAKS 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 337 FVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGG----AAADRGYFIQPTVFGDVKDGM 412
Cdd:PLN02419 406 WEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvPGYEKGNFIGPTILSGVTPDM 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 413 TIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINC-YDVFGAQSPFGGYKMSG 491
Cdd:PLN02419 486 ECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVpIPVPLPFFSFTGNKASF 565
|
490 500
....*....|....*....|..
gi 13529509 492 SG--RELGEYGLQAYTEVKTVT 511
Cdd:PLN02419 566 AGdlNFYGKAGVDFFTQIKLVT 587
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
59-492 |
2.60e-59 |
|
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: 204.36 E-value: 2.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 59 VNPST-GEVICQVAEGNKEDVDKAVKAARAAfqlGSPWRRMDASDRGRLLYRLADLIE-RDRTYLAALETLDNGK-PY-- 133
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKnVWqa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 134 ---VISYLVDLdmvlkcLRYYAGWADK-YHGKTIPIDGDFFSYTRHEPV-GVCGQIIPWNFPLLMQAWKLGPALaTGNVV 208
Cdd:cd07123 128 eidAACELIDF------LRFNVKYAEElYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 209 VMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLI--QVAAGSSNLK---R 283
Cdd:cd07123 201 LWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLwkQIGENLDRYRtypR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 284 VTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQ 363
Cdd:cd07123 281 IVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 364 VDETQFKKILGYIKSGQQE-GAKLLCGGGAAADRGYFIQPTVFgDVKDGM-TIAKEEIFGPVMQIL-----KFKTIEEVV 436
Cdd:cd07123 361 IDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI-ETTDPKhKLMTEEIFGPVLTVYvypdsDFEETLELV 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13529509 437 GraNDSKYGLAAAVFTKDLDKANYLSQALQ--AGTVWINCY---DVFGAQsPFGGYKMSGS 492
Cdd:cd07123 440 D--TTSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKptgAVVGQQ-PFGGARASGT 497
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
52-492 |
8.95e-59 |
|
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: 203.48 E-value: 8.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 52 SRKTFPTVNPST-GEVICQVAEGNKEDVDKAVKAARAAfqlGSPWRRMDASDRGRLLYRLADLIERDRTY-LAALETLDN 129
Cdd:TIGR01236 44 SNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDA---KKDWSNLPFYDRAAIFLKAADLLSGPYRYeILAATMLGQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 130 GK-PY-----VISYLVDLdmvlkcLRYYAGWADKYHGKTiPIDGD-FFSYTRHEPV-GVCGQIIPWNFPLLMQAWKLGPA 201
Cdd:TIGR01236 121 SKtVYqaeidAVAELIDF------FRFNVKYARELYAQQ-PISAPgEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 202 LaTGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEV-GHLIQVAAGS-- 278
Cdd:TIGR01236 194 L-MGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTfKHLWKKVAQNld 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 279 --SNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDS 356
Cdd:TIGR01236 273 ryHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 357 RTEQGPQVDETQFKKILGYIKSGQQEGAKL--LCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQIL-----KF 429
Cdd:TIGR01236 353 RGFMGAVIDEQSFDKIVKYIEDAKKDPEALtiLYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYvypddKY 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 430 KTIEEVVGRAndSKYGLAAAVFTKDLDKANYLSQALQ--AGTVWIN--CYDVFGAQSPFGGYKMSGS 492
Cdd:TIGR01236 433 KEILDLVDST--SQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSGT 497
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
42-512 |
3.93e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 193.13 E-value: 3.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHdaVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLgspWRRMDASDRGRLLYRLADLIERDRTYL 121
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 122 AALETLDNGKpYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPID-GDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 200
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 201 ALATGNVVVMKVAEQTPLTAL----YVANLIKEAGFPPGVVNIVPGfGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAA 276
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 277 gSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDS 356
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 357 RTEQGP---QVDETQFKKILGYIKSgqqEGAKLLCGGGAAADRGYFIQPTVFgDVKDGMTIAKEEIFGPVMQILKFKTIE 433
Cdd:PLN02315 336 GTLLGPlhtPESKKNFEKGIEIIKS---QGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 434 EVVGRANDSKYGLAAAVFTKDLDKA-NYLS-QALQAGTVWINC----YDVFGAqspFGGYKMSGSGRELGEYGLQAYTEV 507
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPETIfKWIGpLGSDCGIVNVNIptngAEIGGA---FGGEKATGGGREAGSDSWKQYMRR 488
|
....*
gi 13529509 508 KTVTV 512
Cdd:PLN02315 489 STCTI 493
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
74-513 |
2.63e-52 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 184.85 E-value: 2.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 74 NKEDVDKAVKAARAAFQLGS----PWRRMDAsdrgRLLYRLadLIERDRTYLAALEtLDNGKPYVISYLVDLDMVLKCLR 149
Cdd:PTZ00381 5 NPEIIPPIVKKLKESFLTGKtrplEFRKQQL----RNLLRM--LEENKQEFSEAVH-KDLGRHPFETKMTEVLLTVAEIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 150 YYAGWADKYhGKTIPIDGDFF-----SYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVA 224
Cdd:PTZ00381 78 HLLKHLDEY-LKPEKVDTVGVfgpgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 225 NLIKEAgFPPGVVNIVPGfGPTAGAAIASHEgVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMDW 304
Cdd:PTZ00381 157 KLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAA-AENLTPCTLELGGKSPVIVDKSCNLKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 305 AVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVErSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKsgqQEGA 384
Cdd:PTZ00381 233 AARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE-ALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 385 KLLCGGGA-AADRgyFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQ 463
Cdd:PTZ00381 309 KVVYGGEVdIENK--YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 13529509 464 ALQAGTVWIN-CYDVFGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:PTZ00381 387 NTSSGAVVINdCVFHLLNPNlPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
14-493 |
5.36e-50 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 184.79 E-value: 5.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 14 RLSRLLSAAATSAVPAPNHQPevfcnqiFINNEWHDAVSRktfPTVNPS-TGEVICQVAEGNKEDVDKAVKAARAAFQLg 92
Cdd:PRK11809 629 RLASLSSALLASAHQKWQAAP-------MLEDPVAAGEMS---PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI- 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 93 spWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGK--PYVISYL---VDLdmvlkcLRYYAGWADkyhgktipidg 167
Cdd:PRK11809 698 --WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKtfSNAIAEVreaVDF------LRYYAGQVR----------- 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 168 DFFSYTRHEPVG--VCgqIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGP 245
Cdd:PRK11809 759 DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGE 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 246 TAGAAIASHEGVDKVAFTGSTEVGHLIQ--VAAGSSNLKRVT---LELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQC 320
Cdd:PRK11809 837 TVGAALVADARVRGVMFTGSTEVARLLQrnLAGRLDPQGRPIpliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 321 CCAGSRTFVQENVYDEFVE--RSvARAKSRvVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAK---LLCGGGAAAD 395
Cdd:PRK11809 917 CSALRVLCLQDDVADRTLKmlRG-AMAECR-MGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQ 994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 396 RGYFIQPTV-----FGDVkdgmtiaKEEIFGPVMQILKFK--TIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAG 468
Cdd:PRK11809 995 SGTFVPPTLieldsFDEL-------KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVG 1067
|
490 500
....*....|....*....|....*...
gi 13529509 469 TVWIN---CYDVFGAQsPFGGYKMSGSG 493
Cdd:PRK11809 1068 NLYVNrnmVGAVVGVQ-PFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
80-513 |
6.97e-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: 171.64 E-value: 6.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 80 KAVKAARAAFQLGspwRRMDASDRGRLLYRLADLIERDRT-YLAALEtLDNGKPYVISYLVDLDMVLKCLRY----YAGW 154
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEENEDeIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 155 A-DKYHGKTIP--IDGdffSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLI---- 227
Cdd:cd07132 78 MkPEPVKKNLAtlLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 228 -KEAgFPpgVVnivpgfgpTAGAAIAS---HEGVDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNIIMSDADMD 303
Cdd:cd07132 155 dKEC-YP--VV--------LGGVEETTellKQRFDYIFYTGSTSVGKIVMQAA-AKHLTPVTLELGGKSPCYVDKSCDID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 304 WAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRtEQGPQVDETQFKKILGYIKSGqqeg 383
Cdd:cd07132 223 VAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLLSGG---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 384 aKLLCGG-GAAADRgyFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLS 462
Cdd:cd07132 298 -KVAIGGqTDEKER--YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKIL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 13529509 463 QALQAGTVWINcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVTVK 513
Cdd:cd07132 375 SNTSSGGVCVN--DTimhYTLDSlPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
82-510 |
4.03e-44 |
|
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: 161.42 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 82 VKAARAAFQLG----SPWRRmdasDRGRLLYRLADliERDRTYLAALETlDNGKPYVISYLVDLDMV-------LKCLRy 150
Cdd:cd07137 5 VRELRETFRSGrtrsAEWRK----SQLKGLLRLVD--ENEDDIFAALRQ-DLGKPSAESFRDEVSVLvsscklaIKELK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 151 yaGWADKYHGK----TIPIDGDFFSytrhEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL 226
Cdd:cd07137 77 --KWMAPEKVKtpltTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 227 IKEAgFPPGVVNIVPGfGPTAGAAIASHEGvDKVAFTGSTEVGHLIqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAV 306
Cdd:cd07137 151 IPEY-LDTKAIKVIEG-GVPETTALLEQKW-DKIFFTGSPRVGRII-MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 307 EQAHFALF-FNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQgpQVDETQFKKILGYIKSGQQEGAK 385
Cdd:cd07137 227 RRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS--RIVNSHHFQRLSRLLDDPSVADK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 386 LLCGGGAAADRGYfIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQAL 465
Cdd:cd07137 305 IVHGGERDEKNLY-IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAET 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 13529509 466 QAGTVWINcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTV 510
Cdd:cd07137 384 SSGGVTFN--DTvvqYAIDTlPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
71-511 |
6.61e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 136.78 E-value: 6.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 71 AEGNKEDVDKAVKAARAAFQLGS----PWRRmdASDRGrlLYRLadLIERDRTYLAALETlDNGKPYVISYLVDLDMVLK 146
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESGRtrslEWRK--SQLKG--LLRL--LKDNEEAIFKALHQ-DLGKHRVEAYRDEVGVLTK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 147 CLRY----YAGWADKYHGK----TIPIDGDFFSytrhEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 218
Cdd:PLN02203 74 SANLalsnLKKWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 219 TALYVANLIKeAGFPPGVVNIVPGfGPTAGAAIASHEGvDKVAFTGSTEVGHLIQVAAgSSNLKRVTLELGGKSPNI--- 295
Cdd:PLN02203 150 TSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAA-AKHLTPVALELGGKCPCIvds 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 296 IMSDADMDWAVEQAHFALFFN-QGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTeQGPQVDETQFKKILG 374
Cdd:PLN02203 226 LSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 375 YIKSGQQEgAKLLCGGGAAADRgYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKD 454
Cdd:PLN02203 305 LLKDPRVA-ASIVHGGSIDEKK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13529509 455 LD-KANYLSQAlQAGTVWINcyDV---FGAQS-PFGGYKMSGSGRELGEYGLQAYTEVKTVT 511
Cdd:PLN02203 383 EKlKRRILSET-SSGSVTFN--DAiiqYACDSlPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
78-497 |
6.24e-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: 124.66 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 78 VDKAVKAARAAfqlGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADK 157
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 158 YH---GKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAG-FP 233
Cdd:cd07084 78 IPhepGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 234 PGVVNIVPGFGPTaGAAIASHEGVDKVAFTGSTEVGhliqvAAGSSNLK--RVTLELGGKSPNIIMSDAD-MDWAVEQAH 310
Cdd:cd07084 158 PEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 311 FALFFNQGQCCCAGSRTFVQENVYDE-FVERSVARAKSRVVGNpfdsrTEQGPQVDETQFKKIlgyIKSGQQEGAKLLCG 389
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQTFTTLAMI---AHMENLLGSVLLFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 390 G------GAAADRGYFIQPTVF--GDVKDGMTIA-KEEIFGPVMQILKFKTIEE--VVGRANDSKYGLAAAVFTKDLDKA 458
Cdd:cd07084 304 GkelknhSIPSIYGACVASALFvpIDEILKTYELvTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 13529509 459 NYLSQALQ-AGTVWINCYD---VFGAQSPFGGYKMSGSGRELG 497
Cdd:cd07084 384 QELIGNLWvAGRTYAILRGrtgVAPNQNHGGGPAADPRGAGIG 426
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
42-503 |
3.62e-30 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 123.66 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAVSRKTfPTVNPSTGEVICQV-AEGnkEDVDKAVKAARAafQLGSPWRRMDASDRGRLLYRLADLIERDRTY 120
Cdd:PRK11903 8 YVAGRWQAGSGAGT-PLFDPVTGEELVRVsATG--LDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 121 LAALETLDNGKPYVISyLVDLDMVLKCLRYYAGWADKYHGKTIPIDGD---------FFSytRHEPV---GVCGQIIPWN 188
Cdd:PRK11903 83 YYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpaFQG--QHVLVptrGVALFINAFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 189 FPllmqAW----KLGPALATGNVVVMKVAEQTP-LTALYVANLIKEAGFPPGVVNIVPGfgpTAGAAIASHEGVDKVAFT 263
Cdd:PRK11903 160 FP----AWglweKAAPALLAGVPVIVKPATATAwLTQRMVKDVVAAGILPAGALSVVCG---SSAGLLDHLQPFDVVSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 264 GSTEVGHLIQ----VAAGSSnlkRVTLELGGKSPNIIMSDADMDwaveQAHFALFFNQ---------GQCCCAGSRTFVQ 330
Cdd:PRK11903 233 GSAETAAVLRshpaVVQRSV---RVNVEADSLNSALLGPDAAPG----SEAFDLFVKEvvremtvksGQKCTAIRRIFVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 331 ENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIkSGQQEGAKLLCGGG------AAADRGYFIQPTV 404
Cdd:PRK11903 306 EALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGgfalvdADPAVAACVGPTL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 405 FG--DVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDldkANYLSQALQA-----GTVWINCYDV 477
Cdd:PRK11903 385 LGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD---AAFLAAAALEladshGRVHVISPDV 461
|
490 500 510
....*....|....*....|....*....|....*
gi 13529509 478 FGA---------QSPFGGYKMSGSGRELGeyGLQA 503
Cdd:PRK11903 462 AALhtghgnvmpQSLHGGPGRAGGGEELG--GLRA 494
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
119-510 |
2.30e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 117.84 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 119 TYLAALETlDNGKPYVISYLVDLDMVLK----CLRYYAGWADKYHGKT----IPIDGDFFSytrhEPVGVCGQIIPWNFP 190
Cdd:PLN02174 51 EIVAALRD-DLGKPELESSVYEVSLLRNsiklALKQLKNWMAPEKAKTslttFPASAEIVS----EPLGVVLVISAWNYP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 191 LLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIkEAGFPPGVVNIVPGFGPTAGAAIasHEGVDKVAFTGSTEVGH 270
Cdd:PLN02174 126 FLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 271 LIqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALF-FNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRV 349
Cdd:PLN02174 203 VI-MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 350 VGNPFDSRtEQGPQVDETQFKKILGYIKsgQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKF 429
Cdd:PLN02174 282 GKNPMESK-DMSRIVNSTHFDRLSKLLD--EKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 430 KTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQS--PFGGYKMSGSGRELGEYGLQAYTEV 507
Cdd:PLN02174 359 NNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtlPFGGVGESGMGAYHGKFSFDAFSHK 438
|
...
gi 13529509 508 KTV 510
Cdd:PLN02174 439 KAV 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
40-503 |
5.80e-28 |
|
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: 116.99 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 40 QIFINNEWHdAVSRKTFPTVNPSTGEVICQV-AEGnkEDVDKAVKAARAAfqlGSP-WRRMDASDRGRLLYRLAD-LIER 116
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVsSEG--LDFAAAVAYAREK---GGPaLRALTFHERAAMLKALAKyLMER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 117 DRTYlaaletldngkpYVISYL---------VDLDMVLKCLRYYAGWA------DKYH--GKTIPI--DGDFFSytRHEP 177
Cdd:cd07128 76 KEDL------------YALSAAtgatrrdswIDIDGGIGTLFAYASLGrrelpnAHFLveGDVEPLskDGTFVG--QHIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 178 V---GVCGQIIPWNFPllmqAW----KLGPALATGNVVVMKVAEQTPLTALYVANLIKEAG-FPPGVVNIVPGfgpTAGA 249
Cdd:cd07128 142 TprrGVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 250 AIASHEGVDKVAFTGSTEVGHLIQVAAG-SSNLKRVTLELGGKSPNIIMSDADMDwaveQAHFALFFNQ---------GQ 319
Cdd:cd07128 215 LLDHLGEQDVVAFTGSAATAAKLRAHPNiVARSIRFNAEADSLNAAILGPDATPG----TPEFDLFVKEvaremtvkaGQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 320 CCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEgAKLLCGG-------GA 392
Cdd:cd07128 291 KCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfevvGA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 393 AADRGYFIQPTVF-GDVKDGMTIAKE-EIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQA--G 468
Cdd:cd07128 370 DAEKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 13529509 469 TVWINCYDVFGAQ----SPF-----GGYKMSGSGRELGeyGLQA 503
Cdd:cd07128 450 RLLVLNRDSAKEStghgSPLpqlvhGGPGRAGGGEELG--GLRG 491
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
78-423 |
6.70e-15 |
|
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: 76.81 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 78 VDKAVKAARAAFQlgsPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPyVISYLVDLDMVLKCLRYYAGWADK 157
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP-EARLQGELGRTTGQLRLFADLVRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 158 --YHGKTI-PIDGDFFSYTRHE---------PVGVCGqiiPWNFPLlmqAWKLG-----PALATGNVVVMKVAEQTPLTA 220
Cdd:cd07129 77 gsWLDARIdPADPDRQPLPRPDlrrmlvplgPVAVFG---ASNFPL---AFSVAggdtaSALAAGCPVVVKAHPAHPGTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 221 LYVANLI----KEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGH-LIQVAAGSSNLKRVTLELGGKSPNI 295
Cdd:cd07129 151 ELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 296 IMSDADMDWAVEQAH-FA--LFFNQGQCCCAGSRTFVQENV-YDEFVE---RSVARAKSRVVGNP-----FDSRTEQgpq 363
Cdd:cd07129 231 ILPGALAERGEAIAQgFVgsLTLGAGQFCTNPGLVLVPAGPaGDAFIAalaEALAAAPAQTMLTPgiaeaYRQGVEA--- 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13529509 364 vdetqfkkilgyIKSgqQEGAKLLcGGGAAADRGYFIQPTVFgdVKDGMTIAK-----EEIFGPV 423
Cdd:cd07129 308 ------------LAA--APGVRVL-AGGAAAEGGNQAAPTLF--KVDAAAFLAdpalqEEVFGPA 355
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
42-427 |
1.09e-12 |
|
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: 70.22 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 42 FINNEWHDAvsRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLG--SPWRrmdASDR----GRLLYRLADLIE 115
Cdd:cd07126 2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhNPLK---NPERyllyGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 116 RDR--TYLAALETLDNGKPYvISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHE---PVGVCGQIIPWNFP 190
Cdd:cd07126 77 KPEveDFFARLIQRVAPKSD-AQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 191 LLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEgVDKVAFTGSTEVGH 270
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN-PRMTLFTGSSKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 271 liqvaagssnlkRVTLELGGKspnIIMSDADMDWAV------EQAHFALFFNQ------GQCCCAGSRTFVQEN-VYDEF 337
Cdd:cd07126 235 ------------RLALELHGK---VKLEDAGFDWKIlgpdvsDVDYVAWQCDQdayacsGQKCSAQSILFAHENwVQAGI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 338 VERSVARAKSRVVGNpfdsrTEQGPQVDETQfKKILGYIKS-GQQEGAKLLCGG------------GAAADRGYFIqPTV 404
Cdd:cd07126 300 LDKLKALAEQRKLED-----LTIGPVLTWTT-ERILDHVDKlLAIPGAKVLFGGkpltnhsipsiyGAYEPTAVFV-PLE 372
|
410 420
....*....|....*....|...
gi 13529509 405 FGDVKDGMTIAKEEIFGPvMQIL 427
Cdd:cd07126 373 EIAIEENFELVTTEVFGP-FQVV 394
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
76-486 |
5.41e-11 |
|
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: 64.55 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 76 EDVDKAVKAAR-AAFQLGSPWRRMDASDRGRLLYRLAdlierdrtylaaletldngKPYVISYLVDLDMVLK---CLRYY 151
Cdd:cd07077 16 EQRDLIINAIAnALYDTRQRLASEAVSERGAYIRSLI-------------------ANWIAMMGCSESKLYKnidTERGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 152 AGWADKYHGKTIPIDGDffSYTRHEPVGVCGQIIPWNFPLLMqAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEA- 230
Cdd:cd07077 77 TASVGHIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 231 --GFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVghlIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQ 308
Cdd:cd07077 154 aaHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 309 AHFALFFNQGQCccagsrtFVQENVYdefVERSVARAKSRvvgnpfdsrteqgpqvdetQFKKILGYIKSGQQEGAKLLc 388
Cdd:cd07077 231 VHDSKFFDQNAC-------ASEQNLY---VVDDVLDPLYE-------------------EFKLKLVVEGLKVPQETKPL- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 389 gggaaadrgyfiqptvFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRAND--SKYG--LAAAVFTKDLDKANYLSQA 464
Cdd:cd07077 281 ----------------SKETTPSFDDEALESMTPLECQFRVLDVISAVENAWMiiESGGgpHTRCVYTHKINKVDDFVQY 344
|
410 420
....*....|....*....|..
gi 13529509 465 LQAGTVWINCYDVFGAQSPFGG 486
Cdd:cd07077 345 IDTASFYPNESSKKGRGAFAGK 366
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
181-353 |
1.23e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 47.86 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 181 CGQIIPWN-FPLLMQAwklgpaLATGNVVVMKvaeQTPLTALYVANLIK-------EAGFPPGVVNIVpGFGPTAGAA-- 250
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVK---PHPAAILPLAITVQvarevlaEAGFDPNLVTLA-ADTPEEPIAqt 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 251 IASHEGVDKVAFTGSTEVG-HLIQVAAGssnlKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCA------ 323
Cdd:cd07127 272 LATRPEVRIIDFTGSNAFGdWLEANARQ----AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTpqniyv 347
|
170 180 190
....*....|....*....|....*....|...
gi 13529509 324 ---GSRTFVQENVYDEfVERSVARAKSRVVGNP 353
Cdd:cd07127 348 prdGIQTDDGRKSFDE-VAADLAAAIDGLLADP 379
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
166-473 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 166 DGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM----KVAEQTPLTALYVANLIKEAGFPPGVVNIVP 241
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 242 GFGPTAGAAIASHEGVDKVAFTGSTEVghliqVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCC 321
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATGGPAV-----VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 322 CAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDsrteqgpQVDETQFKKILGYIKSGQQEGAKLLCGGGAAA---DRGY 398
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQ-------QVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVpqeTRIL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 399 FIQPTVFGDVKDGMTiakeEIFGPVMQILKFKTIEEVVGRA----NDSKYGLAAAVFT---KDLDKANYLSQALQAGTVW 471
Cdd:cd07081 312 IGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSdniKAIENMNQFANAMKTSRFV 387
|
..
gi 13529509 472 IN 473
Cdd:cd07081 388 KN 389
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
106-229 |
9.36e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 38.41 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13529509 106 LLYRLADLIERDRtYLAALETLDNgKPYVISYlvDLDMVLKCLRYYAGWADKYHGKTI-------------PIDGDFFSY 172
Cdd:cd07080 32 FLDRAGKRLLDPD-YPLRQQAERL-LPTVTGY--SEEMLREGLKRLMALFRRENLERIlerelgspgildeWVPPGRGGY 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 13529509 173 TRHEPVGVCGQIIPWNFPLLmQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKE 229
Cdd:cd07080 108 IRAQPRGLVVHIIAGNVPLL-PVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLAD 163
|
|
| |
