|
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 ... |
35-514 |
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: 988.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 35 PDIAYNKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGSPWRRMDASHRGKLLNRLADL 114
Cdd:cd07141 2 PEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 115 IERDRAYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLM 194
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 195 QAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQ 274
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 275 KAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNP 354
Cdd:cd07141 242 QAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 355 FDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIE 434
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 435 EVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIK 514
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
40-513 |
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: 888.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 40 NKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGSpWRRMDASHRGKLLNRLADLIERDR 119
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 120 AYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAE 279
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 280 SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKT 359
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 360 EQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIER 439
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2517771359 440 ANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
37-511 |
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: 741.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 37 IAYNKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGsPWRRMDASHRGKLLNRLADLIE 116
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 117 RDRAYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQA 196
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 197 WKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKA 276
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 277 AAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFD 356
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 357 FKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
36-519 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 717.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 36 DIAYNKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGsPWRRMDASHRGKLLNRLADLI 115
Cdd:PLN02466 54 QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSRILLRFADLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 116 ERDRAYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQ 195
Cdd:PLN02466 133 EKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 196 AWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQK 275
Cdd:PLN02466 213 AWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 276 AAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPF 355
Cdd:PLN02466 293 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 356 DFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEE 435
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 436 VIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTikI 515
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV--T 530
|
....
gi 2517771359 516 PQKN 519
Cdd:PLN02466 531 PLKN 534
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
42-515 |
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: 677.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 42 IFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgSPWRR-MDASHRGKLLNRLADLIERDRA 120
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAES 280
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 NLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTE 360
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 361 QGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERA 440
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 441 NDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIKI 515
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
41-513 |
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: 665.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgSPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07144 87 LLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeS 280
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-Q 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 NLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKAR-VVGNPFDFKT 359
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 360 EQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAAD---RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
35-516 |
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 2517771359 35 PDIAYNKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGsPWRRMDASHRGKLLNRLADL 114
Cdd:PLN02766 16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 115 IERDRAYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLM 194
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 195 QAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQ 274
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 275 KAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNP 354
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 355 FDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIE 434
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 435 EVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIK 514
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
..
gi 2517771359 515 IP 516
Cdd:PLN02766 495 LY 496
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
41-514 |
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: 647.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:COG1012 84 ELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAE 279
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 280 sNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKT 359
Cdd:COG1012 243 -NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 360 EQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAAD-RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIE 438
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 439 RANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFG-AQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIK 514
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-511 |
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: 633.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 48 WHDAVSKkTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALET 127
Cdd:pfam00171 1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 128 LDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGN 207
Cdd:pfam00171 77 LENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 208 VVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTL 287
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 288 ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDE 367
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 368 DQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGL 447
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 448 AAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGA-QAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-513 |
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: 625.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlGSPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 202
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 203 LATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNL 282
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 283 KRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQG 362
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 363 PQVDEDQFKKILGYISTGQREGAKLLCGGSAAAD----RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIE 438
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 439 RANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
96-513 |
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: 613.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAiSYLVDLDMVVKCLRYFAGWSDKFHGKTIPL-DGDFFCYT 174
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSpDPGELAIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 175 RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISS 254
Cdd:cd07078 93 RREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 255 HMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 334
Cdd:cd07078 173 HPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 335 YNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSA-AADRGYFIQPTVFGDVQDNM 413
Cdd:cd07078 252 YDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGKGYFVPPTVLTDVDPDM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 414 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFG-AQAPFGGYKASG 492
Cdd:cd07078 332 PIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAePSAPFGGVKQSG 411
|
410 420
....*....|....*....|.
gi 2517771359 493 NGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07078 412 IGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
55-513 |
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: 596.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 55 KTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGSpWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPY 134
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 135 AISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 214
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 215 EQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSP 294
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 295 NIIMSDA-DMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKI 373
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 374 LGYISTGQREGAKLLCGGSA--AADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAV 451
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2517771359 452 FTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
59-515 |
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: 578.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISY 138
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 LVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIM 298
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 299 SDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYIS 378
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 379 TGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDK 458
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 459 ANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIKI 515
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
59-513 |
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: 576.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlGSPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYA--- 135
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRetr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 136 --ISYLVDldmvvkCLRYFAGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMK 212
Cdd:cd07114 80 aqVRYLAE------WYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 213 VAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGK 292
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 293 SPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKK 372
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 373 ILGYISTGQREGAKLLCGGSAAA----DRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLA 448
Cdd:cd07114 313 VERYVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 449 AAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-513 |
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: 550.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEs 280
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 NLKRVTLELGGKSPNIIMSDA-----DMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPF 355
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 356 DFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGG----SAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFK 431
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 432 TIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 2517771359 512 TI 513
Cdd:cd07559 477 LV 478
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
59-513 |
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: 547.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISY 138
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 LVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIM 298
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 299 SDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYIS 378
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 379 TGQREGAKLLCGG----SAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTK 454
Cdd:cd07093 317 LARAEGATILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2517771359 455 DLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
40-514 |
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: 533.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 40 NKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlGSPWRRMDASHRGKLLNRLADLIERDR 119
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 120 AYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLD----GDFFCYTRHEPVGVCGQIIPWNFPLLMQ 195
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 196 AWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQK 275
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 276 AAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPF 355
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 356 DFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKT--I 433
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 434 EEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 2517771359 514 K 514
Cdd:cd07140 485 E 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-511 |
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: 519.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISy 138
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 LVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAGFPPGVVNIIPGYGPTaGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIM 298
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 299 SDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYIS 378
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 379 TGQREGAKLLCGGSAAA-----DRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFT 453
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 454 KDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
43-509 |
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: 518.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ---GEWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 202
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 203 LATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNL 282
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 283 KRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQG 362
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 363 PQVDEDQFKKILGYISTGQREGAKLLCGGS----AAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIE 438
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGrpenVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2517771359 439 RANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVK 509
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-513 |
5.49e-180 |
|
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: 514.31 E-value: 5.49e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEs 280
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 NLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTE 360
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 361 QGPQVDEDQFKKILGYISTGQREGAKLLCGG----SAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-512 |
6.58e-180 |
|
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: 513.59 E-value: 6.58e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 42 IFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRAY 121
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 122 LAALETLDNGKPYAISYLVDLDMVVKCLRYFAG------WSDKFHGKTIpldgdffcytRHEPVGVCGQIIPWNFPLLMQ 195
Cdd:cd07138 78 LAQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VREPIGVCGLITPWNWPLNQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 196 AWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQK 275
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 276 AAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPF 355
Cdd:cd07138 228 AAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 356 DFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAA---ADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKT 432
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRpegLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 433 IEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
43-511 |
1.76e-179 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 513.27 E-value: 1.76e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLI-ERDRAy 121
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 122 LAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 201
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 202 ALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTaGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESn 281
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 282 LKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQ 361
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 362 GPQVDEDQFKKILGYISTGQREGAKLLCGGSA----AADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVI 437
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2517771359 438 ERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-512 |
1.35e-176 |
|
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: 504.96 E-value: 1.35e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISy 138
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 LVDLDMVVKCLRYFAGWS---DKFHGKTIPL-DGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 214
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 215 EQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSP 294
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 295 NIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKIL 374
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 375 GYISTGQREGAKLLCGGSAAA--DRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVF 452
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 453 TKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
60-513 |
1.91e-175 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 501.76 E-value: 1.91e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgSPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYl 139
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 VDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 219
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 220 SALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMS 299
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 300 DADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDfKTEQGPQVDEDQFKKILGYIST 379
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 380 GQREGAKLLCGGSAAADR---GYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDL 456
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 457 DKANFVSQSLRAGTVWINCY-DVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
96-513 |
4.92e-174 |
|
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: 494.83 E-value: 4.92e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPL-DGDFFCYT 174
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPSpDPGGEAYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 175 RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISS 254
Cdd:cd06534 89 RREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 255 HMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 334
Cdd:cd06534 169 HPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 335 YNEFVERSVekakarvvgnpfdfkteqgpqvdedqfkkilgyistgqregakllcggsaaadrgyfiqpTVFGDVQDNMT 414
Cdd:cd06534 248 YDEFVEKLV------------------------------------------------------------TVLVDVDPDMP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 415 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVF-GAQAPFGGYKASGN 493
Cdd:cd06534 268 IAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGPEAPFGGVKNSGI 347
|
410 420
....*....|....*....|
gi 2517771359 494 GRELGEYGLEAYVEVKNVTI 513
Cdd:cd06534 348 GREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
60-513 |
1.15e-170 |
|
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: 489.25 E-value: 1.15e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyL 139
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 VDLDMVVKCLRYFAGWSDKFHGKTIPL-DGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVG-HLIQKAAaeSNLKRVTLELGGKSPNII 297
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGkLLMAQAA--DTVKRVSLELGGNAPFIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 298 MSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI 377
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 378 STGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLD 457
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2517771359 458 KANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-513 |
1.39e-170 |
|
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: 489.54 E-value: 1.39e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyL 139
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 VDLDMVVKCLRYFAGWSDKFHGKTI-PLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07118 80 GEIEGAADLWRYAASLARTLHGDSYnNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIM 298
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 299 SDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYIS 378
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 379 TGQREGAKLLCGGSAAADR-GYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLD 457
Cdd:cd07118 319 AGRAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2517771359 458 KANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
41-512 |
2.10e-167 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 483.08 E-value: 2.10e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAF--QLGSPWRRMDASHRGKLLNRLADLIERD 118
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 119 RAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGK-----TIPLDgDFFCYTRHEPVGVCGQIIPWNFPLL 193
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 194 MQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLI 273
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 274 QKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGN 353
Cdd:PLN02467 247 MTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 354 PFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAAD--RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFK 431
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 432 TIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
.
gi 2517771359 512 T 512
Cdd:PLN02467 486 T 486
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
60-513 |
7.23e-161 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 464.49 E-value: 7.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYL 139
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 VDLDMVVKCLRYFAGWSDKFHGktiPLDGDFF----CYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 215
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 216 QTPLSALYVASLIKEaGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPN 295
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 296 IIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILG 375
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 376 YIsTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 455
Cdd:cd07092 314 FV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 456 LDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
42-513 |
4.01e-160 |
|
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: 463.20 E-value: 4.01e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 42 IFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGsPWRRMDASHRGKLLNRLADLIERDRAY 121
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 122 LAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTI---PLDGDffCYTRHEPVGVCGQIIPWNFPLLMQAWK 198
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERrpgSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 199 LGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAA 278
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 279 EsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFK 358
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 359 TEQGPQVDEDQFKKILGYISTGQREGAKLLCGGS--AAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVfGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
60-511 |
5.00e-160 |
|
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: 462.87 E-value: 5.00e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQlGSPWRrMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYL 139
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 VDLDMVVKCLRYFAGWSDKFHGK-TIPLDGDFFCYT----RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVA 214
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 215 EQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSP 294
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 295 NIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKIL 374
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 375 GYISTGQREGAKLLCGGSAAA--DRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVF 452
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2517771359 453 TKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
43-507 |
2.66e-159 |
|
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: 461.87 E-value: 2.66e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKfhgktipLDGDFfcyTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 202
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTEL---AGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 203 LATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTaGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNl 282
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 283 KRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQG 362
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 363 PQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERAND 442
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 443 SKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVE 507
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
41-515 |
5.52e-155 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 450.52 E-value: 5.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWhDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGK-TIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKaAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAe 279
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 280 SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKT 359
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 360 EQGPQVDEDQFKKILGYISTGQREG-AKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIE 438
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 439 RANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIKI 515
Cdd:PRK13473 398 WANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
43-513 |
1.59e-153 |
|
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: 446.79 E-value: 1.59e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTG-EVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRAY 121
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 122 LAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAES 280
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 NlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTE 360
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 361 QGPQVDEDQFKKILGYISTGQREGAKLLCGGSAA----ADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVfGAQA--PFGGYKASGNG-RELGEYGLEAYVEVKNVTI 513
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTI-GAEVhlPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
60-513 |
4.86e-153 |
|
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: 444.28 E-value: 4.86e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYL 139
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 vDLDMVVKCLRYFAGWSDKfhGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPL 219
Cdd:cd07106 79 -EVGGAVAWLRYTASLDLP--DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 220 SALYVASLIKEAgFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMS 299
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 300 DADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYIST 379
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 380 GQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKA 459
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2517771359 460 NFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
43-513 |
4.02e-152 |
|
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: 443.43 E-value: 4.02e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 202
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 203 LATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNL 282
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 283 KRVTLELGGKSPNIIMSD--ADMDWAVDQA--HFALF-FNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDF 357
Cdd:cd07116 239 IPVTLELGGKSPNIFFADvmDADDAFFDKAleGFVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 358 KTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAA-----ADRGYFIQPTVFGdvQDNMTIAREEIFGPVMQILKFKT 432
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelgglLGGGYYVPTTFKG--GNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 433 IEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
.
gi 2517771359 513 I 513
Cdd:cd07116 477 V 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-515 |
1.37e-151 |
|
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: 441.04 E-value: 1.37e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAiSY 138
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 LVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAgFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIM 298
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 299 SDADMDWAVDQAHFALFFN-QGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI 377
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 378 STGQREGAKLLCGGSAAAD----RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFT 453
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2517771359 454 KDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIKI 515
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-513 |
1.33e-150 |
|
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: 438.72 E-value: 1.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISY 138
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 LVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEAgFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIM 298
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 299 SDADMDWAVDQAHFAL-FFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI 377
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 378 STGQRE-GAKLLCGGSAAAD----RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVF 452
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 453 TKDLDKANFVSQSLRAGTVWINcydVFGAQAP---FGGYKASGNGRELG-EYGLEAYVEVKNVTI 513
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVN---QGGGQQPgqsYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
43-511 |
1.43e-150 |
|
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: 438.99 E-value: 1.43e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSkkTFPTINPS-TGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAY 121
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 122 LAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIP-LDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeS 280
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 NLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTE 360
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 361 QGPQVDEDQFKKILGYISTGQREGAKLLCGGSA--AADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIE 438
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 439 RANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINC----YDVfgaQAPFGGYKASGNG-RELGEYGLEAYVEVKNV 511
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptagVDY---HVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-513 |
1.87e-150 |
|
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: 438.62 E-value: 1.87e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 201
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 202 ALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsN 281
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 282 LKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQ 361
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 362 GPQVDEDQFKKILGYISTGQREGAKLLCGGSAAA-DRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERA 440
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2517771359 441 NDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
40-515 |
8.63e-150 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 438.18 E-value: 8.63e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 40 NKIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGSpWRRMDASHRGKLLNRLADLIERDR 119
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 120 AYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAE 279
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 280 SNLKRVTLELGGKSPNIIMSDA-DMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFK 358
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 359 TEQGPQVDEDQFKKILGYISTGQREGaKLLCGGSAAADRGYfIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIE 438
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 439 RANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIKI 515
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
43-514 |
1.18e-143 |
|
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: 421.85 E-value: 1.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgSPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKT----IPLDGD--FFCYTRHEPVGVCGQIIPWNFPLLMQA 196
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSMQGerYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 197 WKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTaGAAISSHMDIDKVAFTGSTEVGHLIQKA 276
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 277 AAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFD 356
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 357 FKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIK 514
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-511 |
7.49e-141 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 415.24 E-value: 7.49e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGKTIPL-DGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 201
Cdd:PLN02278 105 AQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 202 ALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESn 281
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 282 LKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQ 361
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 362 GPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERAN 441
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 442 DSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
57-513 |
2.37e-138 |
|
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: 407.10 E-value: 2.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 57 FPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAI 136
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 137 SYLvDLDMVVKCLRYFAGWSDKFHGKTIPLDG-DFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 215
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 216 QTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVG-HLIQKAAAesNLKRVTLELGGKSP 294
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGrEIAEKAGR--HLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 295 NIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKIL 374
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 375 GYISTGQREGAKLLCGGSAAadrGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTK 454
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 455 DLDKANFVSQSLRAGTVWINCYDVFG-AQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
96-513 |
2.75e-137 |
|
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: 403.83 E-value: 2.75e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGKTIPLDGD-FFCYT 174
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAAIAILREAAGLPRRPEGEILPSDVPgKESMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 175 RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLS-ALYVASLIKEAGFPPGVVNIIPGYGPTAGAAIS 253
Cdd:cd07104 95 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 254 SHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 333
Cdd:cd07104 175 EHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHES 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 334 IYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAadrGYFIQPTVFGDVQDNM 413
Cdd:cd07104 254 VYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLFYQPTVLSDVTPDM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 414 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVF-GAQAPFGGYKASG 492
Cdd:cd07104 331 PIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNdEPHVPFGGVKASG 410
|
410 420
....*....|....*....|.
gi 2517771359 493 NGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07104 411 GGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
42-515 |
5.97e-132 |
|
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: 393.13 E-value: 5.97e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 42 IFINNEWHDavSKKTFPTINPS-TGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLG 200
Cdd:cd07124 110 ELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 201 PALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAA-- 278
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 279 ---ESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPF 355
Cdd:cd07124 269 qpgQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 356 DFKTEQGPQVDEDQFKKILGYISTGQREGaKLLCGGSAAAD--RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTI 433
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 434 EEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN--CYD-VFGAQaPFGGYKASG-NGRELGEYGLEAYVEVK 509
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGaLVGRQ-PFGGFKMSGtGSKAGGPDYLLQFMQPK 506
|
....*.
gi 2517771359 510 NVTIKI 515
Cdd:cd07124 507 TVTENF 512
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-513 |
3.90e-131 |
|
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: 388.88 E-value: 3.90e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 57 FPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLGspwRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAI 136
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 137 SyLVDLDMVVKCLRYFAGWSDKFHGKTIPLDG-----DFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 211
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 212 KVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAesnLKRVTLELGG 291
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 292 KSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFK 371
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 372 KILGYISTGQREGAKLLCGGSAaadRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAV 451
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2517771359 452 FTKDLDKANFVSQSLRAGTVWINCYDVFGAQA-PFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
43-513 |
1.29e-130 |
|
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: 388.46 E-value: 1.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAvSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 201
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 202 ALATGNVVVMKVAEQTPLSALYVASLIKEA----GFPPGVVNIIPGYGPtAGAAISSHMDIDKVAFTGSTEVGHLIQKAA 277
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 278 AESNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDF 357
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 358 KTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAA--ADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEE 435
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 436 VIERANDSKYGLAAAVFTKDLDKA-NFVSQS-LRAGTVWINCyDVFGA--QAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAfRWLGPKgSDCGIVNVNI-PTSGAeiGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
..
gi 2517771359 512 TI 513
Cdd:cd07086 474 TI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-513 |
1.45e-128 |
|
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: 382.47 E-value: 1.45e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 57 FPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAI 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 137 SyLVDLDMVVKCLRYFAGWSDKFHGKTIPLDG-----DFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 211
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 212 KVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGG 291
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 292 KSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFK 371
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 372 KILGYISTGQREGAKLLCGGSaaADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAV 451
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2517771359 452 FTKDLDKANFVSQSLRAGTVWINCYDVFGAQA-PFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
59-512 |
2.37e-122 |
|
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: 366.28 E-value: 2.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlGSPWRRmDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISY 138
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 lVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTP 218
Cdd:cd07120 79 -FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 219 LSALYVASLIKEA-GFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNII 297
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 298 MSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI 377
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 378 STGQREGAKLLCGGSAAAD---RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTK 454
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 455 DLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
96-513 |
1.94e-120 |
|
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: 360.62 E-value: 1.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKF-HGKTIPLDGDFfCYT 174
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAEAFlADEPIETDAGK-AYV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 175 RHEPVGVCGQIIPWNFPLlmqaWK----LGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGA 250
Cdd:cd07100 93 RYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 251 AISSHMdIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYV 330
Cdd:cd07100 169 IIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 331 QEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQ 410
Cdd:cd07100 247 HEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 411 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKA 490
Cdd:cd07100 327 PGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKR 406
|
410 420
....*....|....*....|...
gi 2517771359 491 SGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07100 407 SGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-513 |
2.54e-118 |
|
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: 356.15 E-value: 2.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYL 139
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 vDLDMVVKCLRYFAGWSDKFHGKT-IPLDGDFF---CYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 215
Cdd:cd07099 78 -EVLLALEAIDWAARNAPRVLAPRkVPTGLLMPnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 216 QTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISShmDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPN 295
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 296 IIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILG 375
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 376 YISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 455
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 456 LDKANFVSQSLRAGTVWINCYDVFGA--QAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-514 |
6.44e-115 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 347.75 E-value: 6.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 46 NEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKaafQLGSPWRRMDASHRGKLLNRLADLIERDRAYLAAL 125
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAA---AAQKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 126 ETLDNGKPYaISYLVDLDMVVKCLRYFAGWSDKFHGKTIP--LDGDFFCYTRhEPVGVCGQIIPWNFPLLMQAWKLGPAL 203
Cdd:cd07151 78 LIRESGSTR-IKANIEWGAAMAITREAATFPLRMEGRILPsdVPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 204 ATGNVVVMKVAEQTPLSA-LYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAEsNL 282
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 283 KRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQG 362
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 363 PQVDEDQFKKILGYISTGQREGAKLLCGGSAAadrGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERAND 442
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2517771359 443 SKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFG-AQAPFGGYKASGNGRELGEYGLEAYVEVKNVTIK 514
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
96-513 |
5.51e-113 |
|
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: 342.49 E-value: 5.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLD-----GDF 170
Cdd:cd07094 37 RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 FCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGA 250
Cdd:cd07094 116 LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 251 AISSHMDIDKVAFTGSTEVGHLIQKAAAesnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYV 330
Cdd:cd07094 196 AFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 331 QEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAaadRGYFIQPTVFGDVQ 410
Cdd:cd07094 273 HEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 411 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQA-PFGGYK 489
Cdd:cd07094 350 RDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVK 429
|
410 420
....*....|....*....|....
gi 2517771359 490 ASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07094 430 ESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
96-512 |
2.19e-112 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 340.83 E-value: 2.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYLVDLDMVVKClRYFAGWSDKF-----HGKTIPLdgdf 170
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA-RYYARRAERLlkprrRRGAIPV---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 fcYTR----HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGP 246
Cdd:cd07101 109 --LTRttvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 247 TAGAAISSHMDIdkVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGS 326
Cdd:cd07101 187 EVGGAIVDNADY--VMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 327 RTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRG-YFIQPTV 405
Cdd:cd07101 264 RIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpYFYEPTV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 406 FGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDVFGA---- 481
Cdd:cd07101 344 LTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVN--EGYAAawas 421
|
410 420 430
....*....|....*....|....*....|..
gi 2517771359 482 -QAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:cd07101 422 iDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
96-512 |
1.66e-110 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 338.39 E-value: 1.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYLVDLDmVVKCLRYFAGWSDKF-----HGKTIPLdgdf 170
Cdd:PRK09407 70 WAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLD-VALTARYYARRAPKLlaprrRAGALPV---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 fcYTR----HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGP 246
Cdd:PRK09407 145 --LTKttelRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 247 TAGAAISSHmdIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGS 326
Cdd:PRK09407 223 VVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 327 RTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRG-YFIQPTV 405
Cdd:PRK09407 300 RIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 406 FGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDVFGA---- 481
Cdd:PRK09407 380 LTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN--EGYAAawgs 457
|
410 420 430
....*....|....*....|....*....|..
gi 2517771359 482 -QAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:PRK09407 458 vDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
41-512 |
1.05e-107 |
|
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: 329.48 E-value: 1.05e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGKTIP-LDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:cd07085 79 ELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAe 279
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 280 SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKT 359
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 360 EQGPQVDEDQFKKILGYISTGQREGAKLLCGG----SAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEE 435
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 436 VIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcydvFGAQAP-----FGGYKASGNGrELGEYGLEA---YVE 507
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLHFYGKDGvrfYTQ 470
|
....*
gi 2517771359 508 VKNVT 512
Cdd:cd07085 471 TKTVT 475
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
44-492 |
2.90e-107 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 329.59 E-value: 2.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 44 INNEWHDavSKKTFPTINPS-TGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:PRK03137 41 IGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYA-----ISYLVDLdmvvkcLRYFA----GWSDkfhGKTI-PLDGDFFCYtRHEPVGVCGQIIPWNFPL 192
Cdd:PRK03137 116 SAWLVKEAGKPWAeadadTAEAIDF------LEYYArqmlKLAD---GKPVeSRPGEHNRY-FYIPLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 193 LMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHL 272
Cdd:PRK03137 186 AIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 273 IQKAAAESN-----LKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAK 347
Cdd:PRK03137 266 IYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 348 ARVVGNPFDFkTEQGPQVDEDQFKKILGYISTGQREGaKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQI 427
Cdd:PRK03137 346 ELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517771359 428 LKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN--CYD-VFGAQaPFGGYKASG 492
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGaIVGYH-PFGGFNMSG 490
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-515 |
3.47e-107 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 328.40 E-value: 3.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYA-----ISYLVDLdmvvkcLRYFAGWSDKFHGKTIP-LDGDFFCYTRHEPVGVCGQIIPWNFPLLMQA 196
Cdd:PRK11241 91 ARLMTLEQGKPLAeakgeISYAASF------IEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 197 WKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKA 276
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 277 AAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVER---SVEKAKarvVGN 353
Cdd:PRK11241 245 CAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKlqqAVSKLH---IGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 354 PFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTI 433
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 434 EEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
..
gi 2517771359 514 KI 515
Cdd:PRK11241 481 GL 482
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
96-498 |
3.89e-107 |
|
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: 326.94 E-value: 3.89e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNG--KPYAisyLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGDFFCY 173
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsiRPKA---GFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 174 TRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYV-ASLIKEAGFPPGVVNIIPGyGPTAGAAI 252
Cdd:cd07152 106 ARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViARLFEEAGLPAGVLHVLPG-GADAGEAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 253 SSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 332
Cdd:cd07152 185 VEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 333 DIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAaadRGYFIQPTVFGDVQDN 412
Cdd:cd07152 264 SVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---DGLFYRPTVLSGVKPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 413 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVF-GAQAPFGGYKAS 491
Cdd:cd07152 341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNdEPHNPFGGMGAS 420
|
....*..
gi 2517771359 492 GNGRELG 498
Cdd:cd07152 421 GNGSRFG 427
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
108-514 |
1.14e-106 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 324.38 E-value: 1.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 108 LNRLADLIERDRAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLD---GDFFCYTRhePVGVCGQ 184
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 185 IIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFT 264
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 265 GSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVE 344
Cdd:PRK10090 158 GSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 345 KAKARVVGNPFD-FKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGP 423
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 424 VMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLE 503
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
410
....*....|.
gi 2517771359 504 AYVEVKNVTIK 514
Cdd:PRK10090 397 EYLQTQVVYLQ 407
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
96-513 |
3.15e-106 |
|
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: 324.15 E-value: 3.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPyAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLD-GDFFCYT 174
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQIIGGSIPSDkPGTLAMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 175 RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNII---PGYGPTAGAA 251
Cdd:cd07105 95 VKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 252 ISSHMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQ 331
Cdd:cd07105 175 LIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 332 EDIYNEFVERSVEKAKARVVGnpfdfKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGG-SAAADRGYFIQPTVFGDVQ 410
Cdd:cd07105 254 ESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPSGTSMPPTILDNVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 411 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN---CYDvfGAQAPFGG 487
Cdd:cd07105 329 PDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINgmtVHD--EPTLPHGG 406
|
410 420
....*....|....*....|....*.
gi 2517771359 488 YKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07105 407 VKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
60-509 |
1.65e-105 |
|
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: 323.04 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 60 INPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPyaISYL 139
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP--IAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 140 V-DLDMVVKCLRYFAGWSDK-FHGKTIPLDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQT 217
Cdd:cd07102 76 GgEIRGMLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 218 PLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHmDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNII 297
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 298 MSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI 377
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 378 STGQREGAKLLCGG---SAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTK 454
Cdd:cd07102 314 ADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2517771359 455 DLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVK 509
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-513 |
1.10e-102 |
|
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: 315.72 E-value: 1.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 57 FPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAI 136
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 137 SYlVDLDMVVKCLRYFAGWSDKFHGKTIPLDGD-----FFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM 211
Cdd:cd07147 78 AR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 212 KVAEQTPLSALYVASLIKEAGFPPGVVNIIPGygPTAGAAI-SSHMDIDKVAFTGSTEVGHLIQKAAAEsnlKRVTLELG 290
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 291 GKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQF 370
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 371 KKILGYISTGQREGAKLLCGGSAaadRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAA 450
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517771359 451 VFTKDLDKANFVSQSLRAGTVWINcyDV--FGA-QAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVIN--DVptFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-514 |
1.63e-102 |
|
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: 316.05 E-value: 1.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAvSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgSPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPY---------AISYLVDLDMVVKclryfagwsdKFHGKTIPLDGDFF-----CYTRHEPVGVCGQII 186
Cdd:cd07082 80 EVANLLMWEIGKTLkdalkevdrTIDYIRDTIEELK----------RLDGDSLPGDWFPGtkgkiAQVRREPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 187 PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGS 266
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 267 TEVGHLIQKAAAesnLKRVTLELGGKSPNIIMSDADMDWAVDQ-AHFALFFNqGQCCCAGSRTYVQEDIYNEFVERSVEK 345
Cdd:cd07082 230 TEVGNRLKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEiVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 346 AKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGsaAADRGYFIQPTVFGDVQDNMTIAREEIFGPVM 425
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG--GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 426 QILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCY-----DVFgaqaPFGGYKASGNGRELGEY 500
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQGIGD 459
|
490
....*....|....
gi 2517771359 501 GLEAYVEVKNVTIK 514
Cdd:cd07082 460 ALRSMTRRKGIVIN 473
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
61-513 |
2.66e-102 |
|
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: 314.68 E-value: 2.66e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 61 NPSTGEVICQVAEGDKADVDKAVKAAkaafqlGSPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyLV 140
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT-RY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 141 DLDMVVKCLRYFAGWSDKFHGKTIPLD-----GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAE 215
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 216 QTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIqkaAAESNLKRVTLELGGKSPN 295
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 296 IIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILG 375
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 376 YISTGQREGAKLLCGGSAaadRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 455
Cdd:cd07146 315 RVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2517771359 456 LDKANFVSQSLRAGTVwiNCYDVFGAQ---APFGGYKASGNG-RELGEYGLEAYVEVKNVTI 513
Cdd:cd07146 392 LDTIKRLVERLDVGTV--NVNEVPGFRselSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
42-512 |
6.62e-97 |
|
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: 302.94 E-value: 6.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 42 IFINNEWHDAVSKktFPTINPS-TGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:TIGR01237 35 LVINGERVETENK--IVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFE---AWKKTDPEERAAILFKAAAIVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGK----TIPLDGDFFCYTrhePVGVCGQIIPWNFPLLMQA 196
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 197 WKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKA 276
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 277 AA-----ESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVV 351
Cdd:TIGR01237 266 AAkvqpgQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 352 GNPFDFKTEQGPQVDEDQFKKILGYISTGQREGaKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFK 431
Cdd:TIGR01237 346 GPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 432 TIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN--CYDVFGAQAPFGGYKASGNGRELG--EYgLEAYVE 507
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQ 503
|
....*
gi 2517771359 508 VKNVT 512
Cdd:TIGR01237 504 AKTVT 508
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
96-512 |
1.69e-92 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 289.97 E-value: 1.69e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPyaisyLVDLDM---VVKC--LRYFAGWSDKfHGKTIPLDGDF 170
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT-----MVDASLgeiLVTCekIRWTLKHGEK-ALRPESRPGGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 FCYTR-----HEPVGVCGQIIPWNFPL--LmqawkLGPALA---TGNVVVMKVAEQTPLSALYVASLIKEA----GFPPG 236
Cdd:cd07098 108 LMFYKrarveYEPLGVVGAIVSWNYPFhnL-----LGPIIAalfAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 237 VVNIIPGYGPTaGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFF 316
Cdd:cd07098 183 LVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 317 NQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAAD 396
Cdd:cd07098 261 SSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 397 ----RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVW 472
Cdd:cd07098 341 peypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2517771359 473 INCYDVF--GAQAPFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:cd07098 421 INDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
59-513 |
3.60e-85 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 270.84 E-value: 3.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISY 138
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 139 lvdlDMVVKC---LRYFAGWSDKFHGKTiPLD----GDFFCYTRHEPVGVCGQIIPWNFPLlmqaWKL----GPALATGN 207
Cdd:PRK09406 82 ----AEALKCakgFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 208 VVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPgYGPTAGAAISSHMDIDKVAFTGSTEVGHLIqKAAAESNLKRVTL 287
Cdd:PRK09406 153 VGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 288 ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDE 367
Cdd:PRK09406 231 ELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 368 DQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGL 447
Cdd:PRK09406 311 QGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517771359 448 AAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
45-513 |
1.11e-79 |
|
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: 256.75 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 45 NNEWhdAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYLAA 124
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 125 LETLDNGKPYA-----ISYLVDL-DMVVkclryfaGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAW 197
Cdd:cd07130 79 LVSLEMGKILPeglgeVQEMIDIcDFAV-------GLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 198 KLGPALATGNVVVMKVAEQTPLSALYVASLIKEA----GFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLI 273
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 274 QKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERsVEKAKARV-VG 352
Cdd:cd07130 231 GQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLER-LKKAYKQVrIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 353 NPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFgDVQDNMTIAREEIFGPVMQILKFKT 432
Cdd:cd07130 309 DPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 433 IEEVIERANDSKYGLAAAVFTKDLDKA-NFVSQSLR-AGTVWINC----YDVFGAqapFGGYKASGNGRELGEYGLEAYV 506
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNAfRWLGPKGSdCGIVNVNIgtsgAEIGGA---FGGEKETGGGRESGSDAWKQYM 464
|
....*..
gi 2517771359 507 EVKNVTI 513
Cdd:cd07130 465 RRSTCTI 471
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
42-498 |
1.81e-79 |
|
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: 257.12 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 42 IFINNEWHDAVSKKTfpTINPS-TGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYaISYLVDLDMVVKCLRYFAGWSDKFHGKTI------PLDGDFFcytrHEPVGVCGQIIPWNFPLLM 194
Cdd:cd07083 96 ELIATLTYEVGKNW-VEAIDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESF----YVGLGAGVVISPWNFPVAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 195 QAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQ 274
Cdd:cd07083 171 FTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 275 KAAAE-----SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKAR 349
Cdd:cd07083 251 EAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 350 VVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGaKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILK 429
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2517771359 430 FKTIE--EVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcYDVFGA---QAPFGGYKASGNGRELG 498
Cdd:cd07083 410 YKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN-RKITGAlvgVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
94-518 |
2.89e-78 |
|
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: 254.43 E-value: 2.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 94 SPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYA-----ISYLVDLdmvvkcLRYFA------GWSDKFHGK 162
Cdd:cd07125 83 AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLAdadaeVREAIDF------CRYYAaqarelFSDPELPGP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 163 TIPLDGDFFcytrhEP--VGVCgqIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNI 240
Cdd:cd07125 157 TGELNGLEL-----HGrgVFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 241 IPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQ 318
Cdd:cd07125 230 VPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 319 GQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREgAKLLCGGSAAADRG 398
Cdd:cd07125 310 GQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNG 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 399 YFIQPTVFGDVqdNMTIAREEIFGPVMQILKFK--TIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcY 476
Cdd:cd07125 389 YFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-R 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2517771359 477 DVFGA----QaPFGGYKASGNGRELG--EYgLEAYVEVKNVTIKIPQK 518
Cdd:cd07125 466 NITGAivgrQ-PFGGWGLSGTGPKAGgpNY-LLRFGNEKTVSLNTTAA 511
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
96-505 |
6.78e-74 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 240.59 E-value: 6.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYLVDLDMVVKCLRY----FAGW-SDKFHGKTIPLDGDF 170
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHaikhLKKWmKPKRVRTPLLLFGTK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 fCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGygptaGA 250
Cdd:cd07134 94 -SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 251 AISSH---MDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSR 327
Cdd:cd07134 167 EVAQAlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 328 TYVQEDIYNEFVERsVEKAKARVVGNpfDFKTEQGPQ----VDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYfIQP 403
Cdd:cd07134 246 VFVHESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRY-IAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 404 TVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDVFG--- 480
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN--DVVLhfl 399
|
410 420
....*....|....*....|....*.
gi 2517771359 481 -AQAPFGGYKASGNGRELGEYGLEAY 505
Cdd:cd07134 400 nPNLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
100-513 |
2.49e-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: 230.88 E-value: 2.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 100 DASHRGKLLNRLADLI-ERDRAYLAALETlDNGKPYAISYLVDLDMVVKCLRY----FAGWSDKFHGKTIPLDGDFFCYT 174
Cdd:cd07087 18 SLEWRKAQLKALKRMLtENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHalkhLKKWMKPRRVSVPLLLQPAKAYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 175 RHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGyGPTAGAA 251
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 252 ISSHmDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQ 331
Cdd:cd07087 172 LLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 332 EDIYNEFVErsveKAKARVVgnpfDFKTEQgPQ--------VDEDQFKKILGYIstgqrEGAKLLCGGSA-AADRgyFIQ 402
Cdd:cd07087 250 ESIKDELIE----ELKKAIK----EFYGED-PKespdygriINERHFDRLASLL-----DDGKVVIGGQVdKEER--YIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 403 PTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDVFgAQ 482
Cdd:cd07087 314 PTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN--DVL-LH 390
|
410 420 430
....*....|....*....|....*....|....*.
gi 2517771359 483 A-----PFGGYKASGNGRELGEYGLEAYVEVKNVTI 513
Cdd:cd07087 391 AaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
100-501 |
2.94e-67 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 223.13 E-value: 2.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 100 DASHRGKLLNRLADLIERDRAYLA-ALETLDNGKPYAISYLVDLDMVVKCLRY----FAGWSDKFHGKTIPLdgdFF--- 171
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAeAISADFGHRSRHETLLAEILPSIAGIKHarkhLKKWMKPSRRHVGLL---FLpak 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 172 CYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTP-LSALyVASLIKEAgFPPGVVNIIPGyGPT 247
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVTG-GAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 248 AGAAISShMDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSR 327
Cdd:cd07133 169 VAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 328 TYVQEDIYNEFVERSVEKAKAR---VVGNPfDFkteqGPQVDEDQFKKILGYISTGQREGAKL--LCGGSAAADRGYFIQ 402
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKMyptLADNP-DY----TSIINERHYARLQGLLEDARAKGARVieLNPAGEDFAATRKLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 403 PTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDVF--G 480
Cdd:cd07133 322 PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--DTLlhV 399
|
410 420
....*....|....*....|...
gi 2517771359 481 AQ--APFGGYKASGNGRELGEYG 501
Cdd:cd07133 400 AQddLPFGGVGASGMGAYHGKEG 422
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
59-511 |
4.41e-67 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 223.58 E-value: 4.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 59 TINPSTGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADLIeRDRA-YLAALETLDNGKPYAIS 137
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKAL-RARSeEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 138 YlvdlDMVVKClryfAGWSDKF--HG----KTIP-LDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVV 210
Cdd:PRK13968 87 R----AEVAKS----ANLCDWYaeHGpamlKAEPtLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 211 MKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMdIDKVAFTGSTEVGHLIqKAAAESNLKRVTLELG 290
Cdd:PRK13968 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAI-GAQAGAALKKCVLELG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 291 GKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQF 370
Cdd:PRK13968 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 371 KKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAA 450
Cdd:PRK13968 317 DELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2517771359 451 VFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAPFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
97-494 |
5.02e-67 |
|
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: 223.06 E-value: 5.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 97 RRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIPLD-----GDFF 171
Cdd:cd07148 39 NWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDA-KVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 172 CYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAA 251
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 252 ISSHmdidKVA---FTGSTEVG-HLIQKAAAESnlkRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSR 327
Cdd:cd07148 198 VTDP----RVAffsFIGSARVGwMLRSKLAPGT---RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 328 TYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYfiQPTVFG 407
Cdd:cd07148 271 VFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 408 DVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQ-APFG 486
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFA 428
|
....*...
gi 2517771359 487 GYKASGNG 494
Cdd:cd07148 429 GRRQSGYG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
94-495 |
1.70e-66 |
|
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: 220.99 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 94 SPWRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPY------AISYLVDLDMVVKCLRYFAGwsdkfhGKTIPlD 167
Cdd:cd07095 14 PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHERTG------ERATP-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 168 GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGyGPT 247
Cdd:cd07095 87 AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 248 AGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSR 327
Cdd:cd07095 166 TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 328 TYVQEDIY-NEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVF 406
Cdd:cd07095 246 LIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGII 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 407 gDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGA-QAPF 485
Cdd:cd07095 326 -DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASsTAPF 404
|
410
....*....|
gi 2517771359 486 GGYKASGNGR 495
Cdd:cd07095 405 GGVGLSGNHR 414
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
96-494 |
1.29e-65 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 229.70 E-value: 1.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGK--PYAISYL---VDLdmvvkcLRYFAGWSDKFHGKTIPLDGdf 170
Cdd:PRK11904 601 WSRTPVEERAAILERAADLLEANRAELIALCVREAGKtlQDAIAEVreaVDF------CRYYAAQARRLFGAPEKLPG-- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 fcytrhePVG-------------VCgqIIPWNFPLlmqAWKLGP---ALATGNVVVMKVAEQTPLSALYVASLIKEAGFP 234
Cdd:PRK11904 673 -------PTGesnelrlhgrgvfVC--ISPWNFPL---AIFLGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIP 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 235 PGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHF 312
Cdd:PRK11904 741 KDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVT 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 313 ALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREgAKLLCGG- 391
Cdd:PRK11904 821 SAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLp 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 392 -SAAADRGYFIQPTVFgDVqDNMTIAREEIFGPVMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRA 468
Cdd:PRK11904 900 lPAGTENGHFVAPTAF-EI-DSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRV 977
|
410 420 430
....*....|....*....|....*....|
gi 2517771359 469 GTVWINcYDVFGA----QaPFGGYKASGNG 494
Cdd:PRK11904 978 GNVYVN-RNQIGAvvgvQ-PFGGQGLSGTG 1005
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
41-512 |
5.39e-65 |
|
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: 218.60 E-value: 5.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFqlgSPWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDKFHGKTIP-LDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:TIGR01722 79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAE 279
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 280 SNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSrTYVQEDIYNEFVERSVEKAKARVVGNPFDFKT 359
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 360 EQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGY----FIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEE 435
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 436 VIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINC-YDVFGAQAPFGGYKAS--GNGRELGEYGLEAYVEVKNVT 512
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVpIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
173-506 |
3.00e-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: 215.16 E-value: 3.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 173 YTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGYGPTAG 249
Cdd:cd07135 103 RIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 250 AAISSHMDidKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTY 329
Cdd:cd07135 179 ALLEQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 330 VQEDIYNEFVERSvEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTgqrEGAKLLCGGSA-AADRgyFIQPTVFGD 408
Cdd:cd07135 256 VDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEMdEATR--FIPPTIVSD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 409 VQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDVFGA----QAP 484
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN--DTLIHvgvdNAP 407
|
330 340
....*....|....*....|..
gi 2517771359 485 FGGYKASGNGRELGEYGLEAYV 506
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFT 429
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
96-498 |
3.48e-63 |
|
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: 214.39 E-value: 3.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISyLVDLDMVVKCLRYFAGWSDkfhgktipldgDFFCYTR 175
Cdd:TIGR01238 90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVR-----------DVLGEFS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 176 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSH 255
Cdd:TIGR01238 158 VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 256 MDIDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 333
Cdd:TIGR01238 238 PRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 334 IYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI---STGQREGAKLLCGGSAAADRGYFIQPTVFGdvQ 410
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIehmSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--L 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 411 DNMTIAREEIFGPVMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcYDVFGAQA---PF 485
Cdd:TIGR01238 396 DDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN-RNQVGAVVgvqPF 474
|
410
....*....|...
gi 2517771359 486 GGYKASGNGRELG 498
Cdd:TIGR01238 475 GGQGLSGTGPKAG 487
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
100-503 |
1.81e-61 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 208.13 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 100 DASHRGKLLNRLADLI-ERDRAYLAALEtLDNGKPYAISYLVDLDMVVKCLRYF----AGWSDK---------FHGKtip 165
Cdd:cd07136 18 DVEFRIEQLKKLKQAIkKYENEILEALK-KDLGKSEFEAYMTEIGFVLSEINYAikhlKKWMKPkrvktpllnFPSK--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 166 ldgdffCYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIP 242
Cdd:cd07136 94 ------SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 243 GYGPTAGAAISSHMDidKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCC 322
Cdd:cd07136 164 GGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 323 CAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKtEQGPQVDEDQFKKILGYIstgqrEGAKLLCGGSAAADRGYfIQ 402
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETLY-IE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 403 PTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyD----V 478
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DtimhL 391
|
410 420
....*....|....*....|....*
gi 2517771359 479 FGAQAPFGGYKASGNGRELGEYGLE 503
Cdd:cd07136 392 ANPYLPFGGVGNSGMGSYHGKYSFD 416
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
96-494 |
2.48e-60 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 215.19 E-value: 2.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGK--PYAISYL---VDLdmvvkcLRYFAGWSDKfhgktipldgDF 170
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALLVREAGKtlPDAIAEVreaVDF------CRYYAAQARR----------LF 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 171 FCYTRHEPVGVCGQIIPWNFPLlmqAWKLGP---ALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPT 247
Cdd:COG4230 673 AAPTVLRGRGVFVCISPWNFPL---AIFTGQvaaALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGET 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 248 AGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAG 325
Cdd:COG4230 750 VGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSAL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 326 SRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGaKLL--CGGSAAADRGYFIQP 403
Cdd:COG4230 830 RVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVhqLPLPEECANGTFVAP 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 404 TVF--GDVQDnmtiAREEIFGPVMQILKFK--TIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGtvwiNCY--- 476
Cdd:COG4230 909 TLIeiDSISD----LEREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYvnr 980
|
410 420
....*....|....*....|..
gi 2517771359 477 ----DVFGAQaPFGGYKASGNG 494
Cdd:COG4230 981 niigAVVGVQ-PFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
43-494 |
3.60e-59 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 212.03 E-value: 3.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWH-------DAVSKKTFPTINPS-TGEVICQVAEGDKADVDKAVKAAKAAFQlgsPWRRMDASHRGKLLNRLADL 114
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 115 IERDRAYLAALETLDNGK--PYAISYL---VDLdmvvkcLRYFAGwsdkfHGKTIPLDgdffcyTRHEPVGVCGQIIPWN 189
Cdd:PRK11905 625 MEAHMPELFALAVREAGKtlANAIAEVreaVDF------LRYYAA-----QARRLLNG------PGHKPLGPVVCISPWN 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 190 FPLlmqAWKLG---PALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGS 266
Cdd:PRK11905 688 FPL---AIFTGqiaAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGS 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 267 TEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVE 344
Cdd:PRK11905 765 TEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKG 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 345 KAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAKLL-CGGSAAADRGYFIQPTVFgDVqDNMTIAREEIFGP 423
Cdd:PRK11905 845 AMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVAPTLI-EI-DSISDLEREVFGP 922
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517771359 424 VMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN---CYDVFGAQaPFGGYKASGNG 494
Cdd:PRK11905 923 VLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniIGAVVGVQ-PFGGEGLSGTG 997
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
96-492 |
9.84e-57 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 197.42 E-value: 9.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIE-RDRAYLAALETLDNGK-PY-----AISYLVDLdmvvkcLR---YFAgwSDKFHGKtiP 165
Cdd:cd07123 85 WARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKnVWqaeidAACELIDF------LRfnvKYA--EELYAQQ--P 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 166 LDGDFFCYTR--HEPV-GVCGQIIPWNFPLLMQAWKLGPALaTGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIP 242
Cdd:cd07123 155 LSSPAGVWNRleYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 243 GYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAES-----NLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFN 317
Cdd:cd07123 234 GDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 318 QGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTGQRE-GAKLLCGGSAAAD 396
Cdd:cd07123 314 QGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 397 RGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKF--KTIEEVIERAND-SKYGLAAAVFTKDLDKANFVSQSLR--AGTV 471
Cdd:cd07123 394 VGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYpdSDFEETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNF 473
|
410 420
....*....|....*....|....
gi 2517771359 472 WINCYD---VFGAQaPFGGYKASG 492
Cdd:cd07123 474 YINDKPtgaVVGQQ-PFGGARASG 496
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
43-495 |
1.46e-56 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 196.33 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHdAVSKKTFPTINPSTGEVICQvaeGDKADVDKAVKAAKAAFQLGSPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQ---GNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLdGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPA 202
Cdd:PRK09457 80 AEVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEM-ADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 203 LATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAESNL 282
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 283 KRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY-NEFVERSVEKAKARVVGNPFD----F 357
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAepqpF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 358 kteQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFgDVQDNMTIAREEIFGPVMQILKFKTIEEVI 437
Cdd:PRK09457 318 ---MGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2517771359 438 ERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTV-W---INcydvfGAQ--APFGGYKASGNGR 495
Cdd:PRK09457 394 RLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWnkpLT-----GASsaAPFGGVGASGNHR 452
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
41-516 |
4.34e-56 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 195.36 E-value: 4.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 41 KIFINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRA 120
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 121 YLAALETLDNGKPY--AISYLV-DLDMVVKC----LRYFAGW----SDKFHGKtiplDGDFFCYTRHEPVGVCGQIIPWN 189
Cdd:PLN00412 94 PIAECLVKEIAKPAkdAVTEVVrSGDLISYTaeegVRILGEGkflvSDSFPGN----ERNKYCLTSKIPLGVVLAIPPFN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 190 FPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGStEV 269
Cdd:PLN00412 170 YPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 270 GHLIQKAAAESNLKrvtLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKAR 349
Cdd:PLN00412 249 GIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 350 VVGNPFDfKTEQGPQVDEDQFKKILGYISTGQREGAKLLcggSAAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILK 429
Cdd:PLN00412 326 TVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 430 FKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGA-QAPFGGYKASGNGRELGEYGLEAYVEV 508
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKV 481
|
....*...
gi 2517771359 509 KNVTIKIP 516
Cdd:PLN00412 482 KSTVINLP 489
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
43-513 |
3.67e-54 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 190.43 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHdaVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAkaaFQLGSPWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRAC---EEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGK--PYAISylvDLDMVVKCLRYFAGWSDKFHGKTIPLD-GDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKL 199
Cdd:PLN02315 99 GRLVSLEMGKilAEGIG---EVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 200 GPALATGNVVVMKVAEQTPLSAL----YVASLIKEAGFPPGVVNIIPGyGPTAGAAISSHMDIDKVAFTGSTEVGHLIQK 275
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 276 AAaESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPF 355
Cdd:PLN02315 255 TV-NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 356 DFKTEQGPQVDEDQFKKILGYISTGQREGAKLLCGGSAAADRGYFIQPTVFgDVQDNMTIAREEIFGPVMQILKFKTIEE 435
Cdd:PLN02315 334 EKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 436 VIERANDSKYGLAAAVFTKDLDKAN--FVSQSLRAGTVWINCyDVFGAQ--APFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:PLN02315 413 AIEINNSVPQGLSSSIFTRNPETIFkwIGPLGSDCGIVNVNI-PTNGAEigGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
..
gi 2517771359 512 TI 513
Cdd:PLN02315 492 TI 493
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
43-512 |
4.34e-54 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 192.27 E-value: 4.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHDAVSKKTFPTINPSTGEVICQVAEGDKADVDKAVKAAKAAFQLgspWRRMDASHRGKLLNRLADLIERDRAYL 122
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 123 AALETLDNGKPYAISYlVDLDMVVKCLRYFAGWSDKFHGKTIP-LDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGP 201
Cdd:PLN02419 194 AMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 202 ALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGaAISSHMDIDKVAFTGSTEVG-HLIQKAAAES 280
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGmHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 281 nlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIyNEFVERSVEKAKARVVGNPFDFKTE 360
Cdd:PLN02419 352 --KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLVERAKALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 361 QGPQVDEDQFKKILGYISTGQREGAKLLCGGS----AAADRGYFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEV 436
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2517771359 437 IERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINC-YDVFGAQAPFGGYKAS--GNGRELGEYGLEAYVEVKNVT 512
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVpIPVPLPFFSFTGNKASfaGDLNFYGKAGVDFFTQIKLVT 587
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
107-514 |
2.83e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 187.54 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 107 LLNRLADLIERDRAYLAALEtLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFhGKTIPLDGDFF-----CYTRHEPVGV 181
Cdd:PTZ00381 35 LRNLLRMLEENKQEFSEAVH-KDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY-LKPEKVDTVGVfgpgkSYIIPEPLGV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 182 CGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGyGPTAGAAISSHmDIDKV 261
Cdd:PTZ00381 113 VLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKE-PFDHI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 262 AFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYNEFVEr 341
Cdd:PTZ00381 190 FFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 342 SVEKAKARVVGNpfDFKTEQ--GPQVDEDQFKKILGYISTgqrEGAKLLCGGSA-AADRgyFIQPTVFGDVQDNMTIARE 418
Cdd:PTZ00381 268 ALKEAIKEFFGE--DPKKSEdySRIVNEFHTKRLAELIKD---HGGKVVYGGEVdIENK--YVAPTIIVNPDLDSPLMQE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 419 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN-CYDVFGAQA-PFGGYKASGNGRE 496
Cdd:PTZ00381 341 EIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLLNPNlPFGGVGNSGMGAY 420
|
410
....*....|....*...
gi 2517771359 497 LGEYGLEAYVEVKNVTIK 514
Cdd:PTZ00381 421 HGKYGFDTFSHPKPVLNK 438
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
96-492 |
2.32e-51 |
|
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: 183.45 E-value: 2.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIE-RDRAYLAALETLDNGK-PY-----AISYLVDLdmvvkcLRYFAGWSDKFHGKTiPLDG 168
Cdd:TIGR01236 85 WSNLPFYDRAAIFLKAADLLSgPYRYEILAATMLGQSKtVYqaeidAVAELIDF------FRFNVKYARELYAQQ-PISA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 169 D-FFCYTRHEPV-GVCGQIIPWNFPLLMQAWKLGPALaTGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGP 246
Cdd:TIGR01236 158 PgEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPAL-MGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 247 TAGAAISSHMDIDKVAFTGSTEV-GHLIQKAAAE----SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQC 321
Cdd:TIGR01236 237 QVSDQVLADPDLAGIHFTGSTNTfKHLWKKVAQNldryHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQK 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 322 CCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYI--STGQREGAKLLCGGSAAADRGY 399
Cdd:TIGR01236 317 CSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIedAKKDPEALTILYGGKYDDSQGY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 400 FIQPTVFGDVQDNMTIAREEIFGPVMQIL-----KFKTIEEVIERAndSKYGLAAAVFTKDLDKANFVSQSLR--AGTVW 472
Cdd:TIGR01236 397 FVEPTVVESKDPDHPLMSEEIFGPVLTVYvypddKYKEILDLVDST--SQYGLTGAVFAKDRKAILEADKKLRfaAGNFY 474
|
410 420
....*....|....*....|..
gi 2517771359 473 IN--CYDVFGAQAPFGGYKASG 492
Cdd:TIGR01236 475 INdkCTGAVVGQQPFGGARMSG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
104-514 |
1.35e-47 |
|
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: 170.87 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 104 RGKLLNRLADLI-ERDRAYLAALEtLDNGKPYAISYLVDLDMVVKCLRY----FAGWS-DKFHGKTIP--LDGdffCYTR 175
Cdd:cd07132 22 RIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEWMkPEPVKKNLAtlLDD---VYIY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 176 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLI-----KEAgFPpgVVniipgygpTAGA 250
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC-YP--VV--------LGGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 251 AISSHM---DIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSr 327
Cdd:cd07132 167 EETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 328 tYV--QEDIYNEFversVEKAKARVVgnpfDFKTEQ-------GPQVDEDQFKKILGYIstgqrEGAKLLCGGS-AAADR 397
Cdd:cd07132 245 -YVlcTPEVQEKF----VEALKKTLK----EFYGEDpkespdyGRIINDRHFQRLKKLL-----SGGKVAIGGQtDEKER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 398 gyFIQPTVFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyD 477
Cdd:cd07132 311 --YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN--D 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2517771359 478 VFGAQA----PFGGYKASGNGRELGEYGLEAYVEVKNVTIK 514
Cdd:cd07132 387 TIMHYTldslPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-494 |
4.67e-47 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 176.32 E-value: 4.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 104 RGKLLNRLADLIERDRAYLAALETLDNGK--PYAISYL---VDLdmvvkcLRYFAGW-SDKFHGKTipldgdffcytrHE 177
Cdd:PRK11809 706 RAAILERAADLMEAQMQTLMGLLVREAGKtfSNAIAEVreaVDF------LRYYAGQvRDDFDNDT------------HR 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 178 PVG--VCgqIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAGFPPGVVNIIPGYGPTAGAAISSH 255
Cdd:PRK11809 768 PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVAD 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 256 MDIDKVAFTGSTEVGHLIQKAAA---ESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYV 330
Cdd:PRK11809 846 ARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 331 QEDIynefVERSVEKAKAR----VVGNPFDFKTEQGPQVDEDQFKKILGYISTGQREGAK---LLCGGSAAADRGYFIQP 403
Cdd:PRK11809 926 QDDV----ADRTLKMLRGAmaecRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPP 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 404 TV-----FGDVQdnmtiarEEIFGPVMQILKFK--TIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWIN-- 474
Cdd:PRK11809 1002 TLieldsFDELK-------REVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrn 1074
|
410 420
....*....|....*....|.
gi 2517771359 475 -CYDVFGAQaPFGGYKASGNG 494
Cdd:PRK11809 1075 mVGAVVGVQ-PFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
97-511 |
1.25e-43 |
|
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: 159.88 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 97 RRMDASHRGKLLNRLADLI-ERDRAYLAALETlDNGKPYAISYLVDLDMVVK----CLRYFAGWSDKFHGK----TIPLD 167
Cdd:cd07137 16 RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSscklAIKELKKWMAPEKVKtpltTFPAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 168 GDFFCytrhEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAgFPPGVVNIIPGyGPT 247
Cdd:cd07137 95 AEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 248 AGAAISSHmDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALF-FNQGQCCCAGS 326
Cdd:cd07137 169 ETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 327 RTYVQEDIYNEFVERSVEKAKARVVGNPFDFKtEQGPQVDEDQFKKILGYISTgQREGAKLLCGGSAAADRGYfIQPTVF 406
Cdd:cd07137 247 YVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERDEKNLY-IEPTIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 407 GDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINcyDV---FGAQA 483
Cdd:cd07137 324 LDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN--DTvvqYAIDT 401
|
410 420
....*....|....*....|....*....
gi 2517771359 484 -PFGGYKASGNGRELGEYGLEAYVEVKNV 511
Cdd:cd07137 402 lPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
96-504 |
1.08e-34 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 135.44 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYAISYLVDLDMVVKCLRYFAGWSDKFH---GKTIPLDGDFFC 172
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPhepGNHLGQGLKQQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 173 YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKEAG-FPPGVVNIIPGYGPTaGAA 251
Cdd:cd07084 95 HGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-MQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 252 ISSHMDIDKVAFTGSTEVGhliQKAAAESNLKRVTLELGGKSPNIIMSDAD-MDWAVDQAHFALFFNQGQCCCAGSRTYV 330
Cdd:cd07084 174 LLLHPNPKMVLFTGSSRVA---EKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 331 QEDIYNE-FVERSVEKAKARVVGNpfdfkTEQGPQVDEDQFKKIlgyISTGQREGAKLLCGG------SAAADRGYFIQP 403
Cdd:cd07084 251 PENWSKTpLVEKLKALLARRKLED-----LLLGPVQTFTTLAMI---AHMENLLGSVLLFSGkelknhSIPSIYGACVAS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 404 TVF--GDVQDNMTIA-REEIFGPVMQILKFK-----TIEEVIERANDSkygLAAAVFTKDldkANFVSQ----SLRAGTV 471
Cdd:cd07084 323 ALFvpIDEILKTYELvTEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSND---PIFLQElignLWVAGRT 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 2517771359 472 WINCYD---VFGAQAPFGGYKASGNGRELGeyGLEA 504
Cdd:cd07084 397 YAILRGrtgVAPNQNHGGGPAADPRGAGIG--GPEA 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
96-512 |
1.61e-33 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 132.93 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRmdaSHRGKLLNRLADlieRDRAYLAALETlDNGKPYAISYLVDLDMVVKCLRY----FAGWSDKFHGKTiPLDgdFF 171
Cdd:PLN02203 29 WRK---SQLKGLLRLLKD---NEEAIFKALHQ-DLGKHRVEAYRDEVGVLTKSANLalsnLKKWMAPKKAKL-PLV--AF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 172 CYTRH---EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIKeAGFPPGVVNIIPGyGPTA 248
Cdd:PLN02203 99 PATAEvvpEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 249 GAAISSHmDIDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNI---IMSDADMDWAVDQAHFALFFN-QGQCCCA 324
Cdd:PLN02203 177 GEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 325 GSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTeQGPQVDEDQFKKILGYISTgQREGAKLLCGGSAAADRgYFIQPT 404
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDEKK-LFIEPT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 405 VFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLD-KANFVSQSlRAGTVWINcyDV---FG 480
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKlKRRILSET-SSGSVTFN--DAiiqYA 408
|
410 420 430
....*....|....*....|....*....|...
gi 2517771359 481 AQA-PFGGYKASGNGRELGEYGLEAYVEVKNVT 512
Cdd:PLN02203 409 CDSlPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
177-511 |
1.40e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 115.53 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 177 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVASLIkEAGFPPGVVNIIPGYGPTAGAAISSHM 256
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 257 diDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALF-FNQGQCCCAGSRTYVQEDIY 335
Cdd:PLN02174 190 --DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 336 NEFVERSVEKAKARVVGNPFDFKtEQGPQVDEDQFKKiLGYISTGQREGAKLLCGGSaaADRGYF-IQPTVFGDVQDNMT 414
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGE--KDRENLkIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 415 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGA--QAPFGGYKASG 492
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESG 422
|
330
....*....|....*....
gi 2517771359 493 NGRELGEYGLEAYVEVKNV 511
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
93-455 |
4.69e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 111.33 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 93 GSPWRRMDASHRGKLLNRLADLI--ERDRAYLAALEtldNGKPYAISYLVDLDMVVKCLRYFAGWSDKFHGKTIPLDGD- 169
Cdd:PRK11903 54 GAALRALTYAQRAALLAAIVKVLqaNRDAYYDIATA---NSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEa 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 170 --------FFcyTRHEPV---GVCGQIIPWNFPllmqAW----KLGPALATGNVVVMKVAEQTPLSALYVASLIKEAG-F 233
Cdd:PRK11903 131 vqlgkdpaFQ--GQHVLVptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 234 PPGVVNIIPGygptAGAAISSHMD-IDKVAFTGSTEVGHLIQK-AAAESNLKRVTLELGGKSPNIIMSDAdmdwAVDQAH 311
Cdd:PRK11903 205 PAGALSVVCG----SSAGLLDHLQpFDVVSFTGSAETAAVLRShPAVVQRSVRVNVEADSLNSALLGPDA----APGSEA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 312 FALFFNQ---------GQCCCAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDFKTEQGPQVDEDQFKKILGYISTgQR 382
Cdd:PRK11903 277 FDLFVKEvvremtvksGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 383 EGAKLLCGGS------AAADRGYFIQPTVFG-DVQDNMTIARE-EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTK 454
Cdd:PRK11903 356 AQAEVLFDGGgfalvdADPAVAACVGPTLLGaSDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSD 435
|
.
gi 2517771359 455 D 455
Cdd:PRK11903 436 D 436
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
43-462 |
1.36e-25 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 110.05 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 43 FINNEWHdAVSKKTFPTINPSTGEVICQV-AEGDKADVDKAVKAakaafQLGSP-WRRMDASHRGKLLNRLAD-LIERDR 119
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVsSEGLDFAAAVAYAR-----EKGGPaLRALTFHERAAMLKALAKyLMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 120 AYlaaletldngkpYAISYL---------VDLDMVVKCLRYFAGW------SDKFH--GKTIPL--DGDFF----CYTRH 176
Cdd:cd07128 78 DL------------YALSAAtgatrrdswIDIDGGIGTLFAYASLgrrelpNAHFLveGDVEPLskDGTFVgqhiLTPRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 177 epvGVCGQIIPWNFPllmqAW----KLGPALATGNVVVMKVAEQTPLSALYVASLIKEAG-FPPGVVNIIPGygptAGAA 251
Cdd:cd07128 146 ---GVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 252 ISSHMDI-DKVAFTGSTEVG-------HLIQKAAaesnlkRVTLELGGKSPNIIMSDAdmdwAVDQAHFALFFNQ----- 318
Cdd:cd07128 215 LLDHLGEqDVVAFTGSAATAaklrahpNIVARSI------RFNAEADSLNAAILGPDA----TPGTPEFDLFVKEvarem 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 319 ----GQCCCAGSRTYVQEDIynefVERSVEKAKAR----VVGNPFDFKTEQGPQVDEDQFKKILGYISTgQREGAKLLCG 390
Cdd:cd07128 285 tvkaGQKCTAIRRAFVPEAR----VDAVIEALKARlakvVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 391 G-------SAAADRGYFIQPTVF-GDVQDNMTIARE-EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANF 461
Cdd:cd07128 360 GpdrfevvGADAEKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
.
gi 2517771359 462 V 462
Cdd:cd07128 440 L 440
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
147-472 |
5.64e-13 |
|
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: 70.99 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 147 KCLRYFAGWSDKFHGKTIPLDGDFFCYTRHE---PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALY 223
Cdd:cd07126 108 KFLENFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 224 VASLIKEAGFPPGVVNIIPGYGPTAGAAISShMDIDKVAFTGSTEVGHliqkaaaesnlkRVTLELGGKspnIIMSDADM 303
Cdd:cd07126 188 FLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSKVAE------------RLALELHGK---VKLEDAGF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 304 DWAV---------------DQAHFALffnQGQCCCAGSRTYVQEDIYNE-FVERSVEKAKAR-----VVGNPFDFKTEQg 362
Cdd:cd07126 252 DWKIlgpdvsdvdyvawqcDQDAYAC---SGQKCSAQSILFAHENWVQAgILDKLKALAEQRkledlTIGPVLTWTTER- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 363 pqvDEDQFKKILgyistgQREGAKLLCGGSAAADRGYfiqPTVFGDVQ--------------DNMTIAREEIFGPvMQIL 428
Cdd:cd07126 328 ---ILDHVDKLL------AIPGAKVLFGGKPLTNHSI---PSIYGAYEptavfvpleeiaieENFELVTTEVFGP-FQVV 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2517771359 429 ---KFKTIEEVIERANDSKYGLAAAVFTKDLDKANFVSQSLRAGTVW 472
Cdd:cd07126 395 teyKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
104-487 |
1.91e-12 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 68.79 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 104 RGKLLNRLADLIERDRAYLAALETLDNGKpYAISYLVDLDMVVKC-----------LRYFAGWSDKFHGKTIPLDGDffC 172
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGA-YIRSLIANWIAMMGCsesklyknidtERGITASVGHIQDVLLPDNGE--T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 173 YTRHEPVGVCGQIIPWNFPLLMqAWKLGPALATGNVVVMKVAEQTPLSAlYVASLIKEAGFPPGVVNIIPGYGPTAGAAI 252
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHGPKILVLYVPHPSDEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 253 S----SHMDIDKVAFTGSTEVGHLIQKAaaeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQgQCCCAGSRT 328
Cdd:cd07077 173 AeellSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQ-NACASEQNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 329 YVQEDIYNEFVERSveKAKARVVGnpfdFKTEQGPqvdedqfkKILGYISTGQREGAkllcggsaaadrgyfiqptvfgd 408
Cdd:cd07077 249 YVVDDVLDPLYEEF--KLKLVVEG----LKVPQET--------KPLSKETTPSFDDE----------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 409 vqdnmtiAREEiFGPVMQILKFKTIEEVIERAND--SKYG--LAAAVFTKDLDKANFVSQSLRAGTVWINCYDVFGAQAP 484
Cdd:cd07077 292 -------ALES-MTPLECQFRVLDVISAVENAWMiiESGGgpHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAF 363
|
...
gi 2517771359 485 FGG 487
Cdd:cd07077 364 AGK 366
|
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| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
96-301 |
1.57e-11 |
|
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: 66.41 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 96 WRRMDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYA-ISylVDLDMVVKCLRYFA-----GWsdkFHGKTI-PLDG 168
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEArLQ--GELGRTTGQLRLFAdlvreGS---WLDARIdPADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 169 DFFCYTRHE---------PVGVCGqiiPWNFPLlmqAWKLG-----PALATGNVVVMKVAEQTP-LSALyVASLI----K 229
Cdd:cd07129 90 DRQPLPRPDlrrmlvplgPVAVFG---ASNFPL---AFSVAggdtaSALAAGCPVVVKAHPAHPgTSEL-VARAIraalR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517771359 230 EAGFPPGVVNIIPGYGPTAGAAISSHMDIDKVAFTGSTEVGHLIQKAAAesnlKR-----VTLELGGKSPNIIMSDA 301
Cdd:cd07129 163 ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAA----ARpepipFYAELGSVNPVFILPGA 235
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| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
182-492 |
2.62e-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: 46.70 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 182 CGQIIPWN-FPLLMQAwklgpaLATGNVVVMKVAEQTPLS-ALYVA---SLIKEAGFPPGVVNII--PGYGPTAGaAISS 254
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVKPHPAAILPlAITVQvarEVLAEAGFDPNLVTLAadTPEEPIAQ-TLAT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 255 HMDIDKVAFTGSTEVG-HLIQKAAAesnlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 333
Cdd:cd07127 275 RPEVRIIDFTGSNAFGdWLEANARQ----AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 334 -IYNEFVERSVEKAKARVVgnpfdfKTEQGPQVDEDQFKKILGYI---STGQREGAKLLCGGSAAADRGY----FIQPTV 405
Cdd:cd07127 351 gIQTDDGRKSFDEVAADLA------AAIDGLLADPARAAALLGAIqspDTLARIAEARQLGEVLLASEAVahpeFPDARV 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 406 F------GDVQDNMTIArEEIFGPVMQILKFKTIEEVIERANDS---KYGLAAAVFTKDldkANFVSQSLRA-------- 468
Cdd:cd07127 425 RtplllkLDASDEAAYA-EERFGPIAFVVATDSTDHSIELARESvreHGAMTVGVYSTD---PEVVERVQEAaldagval 500
|
330 340
....*....|....*....|....*....
gi 2517771359 469 -----GTVWINcydvfgAQAPFGGYKASG 492
Cdd:cd07127 501 sinltGGVFVN------QSAAFSDFHGTG 523
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
167-474 |
9.66e-04 |
|
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: 41.48 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 167 DGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVM----KVAEQTPLSALYVASLIKEAGFPPGVVNIIP 242
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 243 GYGPTAGAAISSHMDIDKVAFTGstevGHLIQKAAAESNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCC 322
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 323 CAGSRTYVQEDIYNEFVERSVEKAKARVVGNPFDfkteqgpQVDEDQFKKI-LGYISTGQRegakllcGGSAAADRGYFI 401
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQ-------QVQPVILKNGdVNRDIVGQD-------AYKIAAAAGLKV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517771359 402 QPT---VFGDVQ--DNMTIAREEIFGPVMQILKFKTIEEVIERA----NDSKYGLAAAVFT---KDLDKANFVSQSLRAG 469
Cdd:cd07081 305 PQEtriLIGEVTslAEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSdniKAIENMNQFANAMKTS 384
|
....*
gi 2517771359 470 TVWIN 474
Cdd:cd07081 385 RFVKN 389
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