|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
33-513 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 1023.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 33 NPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWRRMDASERGRLLNRLAD 112
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 113 LVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLV 192
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 193 MQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 273 QKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKI 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 81904561 513 K 513
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
39-512 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 887.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 39 NKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSpWRRMDASERGRLLNRLADLVERDR 118
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 119 VYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 279 SNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQR 438
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81904561 439 ANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
38-510 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 741.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 38 YNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADLVERD 117
Cdd:cd07142 3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 118 RVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWK 197
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 198 LAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAG 277
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 278 ESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELD 357
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 358 TQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81904561 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-518 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 731.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 22 STAAALPNPI-PNPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDA 100
Cdd:PLN02466 40 TAAAAVEEPItPPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 101 SERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGV 180
Cdd:PLN02466 119 YERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 181 CGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKV 260
Cdd:PLN02466 199 AGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 261 AFTGSTEVGHLIQKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLER 340
Cdd:PLN02466 279 AFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 341 TVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIF 420
Cdd:PLN02466 359 AKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIF 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 421 GPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDG 500
Cdd:PLN02466 439 GPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYS 518
|
490
....*....|....*...
gi 81904561 501 LRAYTEVKTVTikVPEKN 518
Cdd:PLN02466 519 LNNYLQVKAVV--TPLKN 534
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
40-512 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 693.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07144 87 LLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeS 279
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-Q 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQR-KVGNPFELDT 358
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE---RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
40-513 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 686.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:COG1012 84 ELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 279 sNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:COG1012 243 -NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL-GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIV-TCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
41-514 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 685.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRR-MDASERGRLLNRLADLVERDRV 119
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGES 279
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRA 439
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 440 NNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKV 514
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
47-510 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 673.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 47 WHDAVSKkTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLET 126
Cdd:pfam00171 1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 127 LDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGN 206
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 207 TVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 287 ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDK 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 367 EQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGL 446
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 447 AAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
34-515 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 653.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 34 PEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADL 113
Cdd:PLN02766 16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 114 VERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVM 193
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 274 KAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNP 353
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 354 FELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIE 433
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 434 EVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
..
gi 81904561 514 VP 515
Cdd:PLN02766 495 LY 496
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
42-512 |
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: 624.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:cd07119 80 ARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 202 LATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 282 KRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQG 361
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 362 PQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
79-512 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 616.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 79 DLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKW 158
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 159 HGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVV 237
Cdd:cd07078 77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 238 NIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNM 317
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 318 GQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL-GER 396
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 397 GFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYN 476
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 81904561 477 IVTC-HTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07078 396 VGAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-512 |
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: 613.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 54 KTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSpWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPF 133
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 134 QESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTLELGGKSP 293
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 294 SIVLADA-DMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERI 372
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 373 LGYIRLGQKEGAKLLCGGERLGE--RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAV 450
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81904561 451 FTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
58-512 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 611.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESy 137
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRET- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQT 216
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 217 PLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIV 296
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 297 LADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYI 376
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 377 RLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFT 452
Cdd:cd07114 318 ARAREEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 453 RDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
58-514 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 592.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGKSPSIVL 297
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 378 LGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDK 457
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 458 AIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKV 514
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
58-512 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 577.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVL 297
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 378 LGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTR 453
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 81904561 454 DLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
40-512 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 570.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEs 279
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 NLKRVTLELGGKSPSIVLADA-----DMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK 430
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 81904561 511 TI 512
Cdd:cd07559 477 LV 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
39-513 |
0e+00 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 567.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 39 NKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRMDASERGRLLNRLADLVERDR 118
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 119 VYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEH----FCFTRHEPVGVCGQIIPWNFPLVMQ 194
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARpnrnLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 195 GWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQK 274
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 275 AAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK--KI 432
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 81904561 513 K 513
Cdd:cd07140 485 E 485
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-512 |
0e+00 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 547.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 lDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPL 218
Cdd:cd07109 80 -DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 219 SALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLA 298
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 299 DADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGnPFELDTQQGPQVDKEQFERILGYIRL 378
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 379 GQKEGAKLLCGGERL---GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDL 455
Cdd:cd07109 317 ARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 81904561 456 DKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
58-510 |
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: 540.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07090 78 V-DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGKSPSIVL 297
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 378 LGQKEGAKLLCGGERLG-----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFT 452
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 81904561 453 RDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
40-512 |
0e+00 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 537.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEs 279
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
59-512 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 534.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyv 138
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 ldLDEVikVY-----RYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKV 212
Cdd:cd07103 77 --RGEV--DYaasflEWFAEEARRIYGRTIPsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 213 AEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQKAAgeSNLKRVTLELGGK 291
Cdd:cd07103 153 AEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGkLLMAQAA--DTVKRVSLELGGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 292 SPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFER 371
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 372 ILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07103 311 VEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81904561 452 TRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
40-510 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 532.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLV-ERDR 118
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 119 VyLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:PRK13252 85 E-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 279 SnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:PRK13252 243 S-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81904561 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
58-511 |
0e+00 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 528.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESy 137
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VLDLDEVIKVYRYFAGWA---DKWHGKTIPMDGEHF-CFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSP 293
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 374 GYIRLGQKEGAKLLCGGER--LGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 452 TRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-511 |
0e+00 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 527.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKP------FQ-ESYVLDLDEVIKVYRYFAgWADKWHGKTIpmdgehfcftRHEPVGVCGQIIPWNFPLVM 193
Cdd:cd07138 78 LAQAITLEMGAPitlaraAQvGLGIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 274 KAAGESnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNP 353
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 354 FELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGG----ERLgERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKF 429
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 430 KKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKT 509
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
..
gi 81904561 510 VT 511
Cdd:cd07138 464 IQ 465
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
42-508 |
0e+00 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 518.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 202 LATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 282 KRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 362 PQVDKEQFERILGYIRLGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81904561 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
61-512 |
3.92e-180 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 513.81 E-value: 3.92e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 61 PTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlD 140
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 141 LDEVIKVYRYFAGWADKWHGKTIPMDGEH-FCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLS 219
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDmLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 220 ALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLAD 299
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 300 ADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLG 379
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 380 QKEGAKLLCGGERLGER-GFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKA 458
Cdd:cd07118 321 RAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 81904561 459 IYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
41-512 |
5.91e-176 |
|
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: 503.65 E-value: 5.91e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADK--WHGKTIPMDGEHfCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpFEERRPGSGGGH-VLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 279 sNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:cd07139 238 -RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLG--ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVI 436
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81904561 437 QRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNiVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07139 397 RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
27-511 |
9.46e-174 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 499.26 E-value: 9.46e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 27 LPNPIPNpeicyNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFR--LGSPWRRMDASERG 104
Cdd:PLN02467 1 MAIPVPR-----RQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 105 RLLNRLADLVERDRVYLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGK-----TIPMDgEHFCFTRHEPVG 179
Cdd:PLN02467 76 KYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 180 VCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDK 259
Cdd:PLN02467 154 VVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 260 VAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLE 339
Cdd:PLN02467 234 IAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 340 RTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLG--ERGFFIKPTVFGDVQDGMRIAKE 417
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 418 EIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELG 497
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELG 472
|
490
....*....|....
gi 81904561 498 EDGLRAYTEVKTVT 511
Cdd:PLN02467 473 EWGLENYLSVKQVT 486
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
42-512 |
1.56e-171 |
|
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: 492.63 E-value: 1.56e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTG-EVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07131 79 LARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGES 279
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 NlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL----GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81904561 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI-VTCHTPFGGFKESGNG-RELGEDGLRAYTEVKTVTI 512
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
83-512 |
9.23e-171 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 486.35 E-value: 9.23e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 83 KAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKT 162
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 163 IP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIIT 241
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 242 GYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCC 321
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 322 CAGSRTFVEESIYREFLERTVekakqrkvgnpfeldtqqgpqvdkeqferilgyirlgqkegakllcggerlgergffik 401
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 402 pTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTC- 480
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGp 335
|
410 420 430
....*....|....*....|....*....|..
gi 81904561 481 HTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
42-510 |
2.25e-169 |
|
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: 487.14 E-value: 2.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSkkTFPTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESyvldLDEV---IKVYRYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGW 196
Cdd:cd07097 79 LARLLTREEGKTLPEA----RGEVtraGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 197 KLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:cd07097 155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 277 GeSNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:cd07097 235 A-ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 357 DTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL--GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81904561 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI-VTCHTPFGGFKESGNG-RELGEDGLRAYTEVKTV 510
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-512 |
4.05e-168 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 482.98 E-value: 4.05e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 LDLDEVIKVYRYFAGWADKWHGktiPMDGE----HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAE 214
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEG---PAAGEylpgHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 215 QTPLSALYLASLIKEaGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGKSPS 294
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 295 IVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILG 374
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 375 YIRlGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD 454
Cdd:cd07092 314 FVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 81904561 455 LDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-510 |
8.95e-168 |
|
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: 482.51 E-value: 8.95e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRrMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 LDLDEVIKVYRYFAGWADKWHGKTI-----PMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDlpvpaLRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSP 293
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 374 GYIRLGQKEGAKLLCGGERL--GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 81904561 452 TRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-512 |
9.27e-168 |
|
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: 481.64 E-value: 9.27e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYv 138
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAF---PGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 LDLDEVIKVYRYFAGWADKwhGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPL 218
Cdd:cd07106 78 FEVGGAVAWLRYTASLDLP--DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 219 SALYLASLIKEAgFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLA 298
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 299 DADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRL 378
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 379 GQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKA 458
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 81904561 459 IYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
41-504 |
1.02e-167 |
|
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: 483.05 E-value: 1.02e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKwhgktipMDGEhfcFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:cd07111 101 FAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTE---LAGWKPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 201 ALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKA-AGES 279
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 nlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07111 250 --KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRA 439
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 440 NNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAY 504
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
40-513 |
7.75e-160 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 462.84 E-value: 7.75e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWhDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTipmDGE----HFCFTRHEPVGVCGQIIPWNFPLVMQG 195
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA---AGEylegHTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQK 274
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGkHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 275 AAGesNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:PRK13473 236 AAD--SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 355 ELDTQQGPQVDKEQFERILGYIRLGQKEG-AKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIE 433
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 434 EVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
58-512 |
2.19e-159 |
|
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: 461.07 E-value: 2.19e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESy 137
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAM- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESnLKRVTLELGGKSPSIVL 297
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 298 ADADMEHAVDqcheALFFNM-----GQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERI 372
Cdd:cd07107 235 PDADPEAAAD----AAVAGMnftwcGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 373 LGYIRLGQKEGAKLLCGGER----LGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAA 448
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81904561 449 AVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
58-512 |
2.25e-158 |
|
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: 458.36 E-value: 2.25e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVL 297
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 298 ADADMEHAVDQCHEAL-FFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYI 376
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 377 RLGQKE-GAKLLCGG----ERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07108 316 DLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 452 TRDLDKAIYFTQALQAGTVWVNtynivTCHTP-----FGGFKESGNGRELGEDG-LRAYTEVKTVTI 512
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVN-----QGGGQqpgqsYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-513 |
8.63e-157 |
|
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: 454.98 E-value: 8.63e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKT----IP-MDGEHF-CFTRHEPVGVCGQIIPWNFPLVMQ 194
Cdd:cd07113 80 LAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPsMQGERYtAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 195 GWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQK 274
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 275 AAgESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:cd07113 239 QA-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPT--VFGDVQDgmRIAKEEIFGPVQPLFKFKKI 432
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADS--RLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
.
gi 81904561 513 K 513
Cdd:cd07113 476 R 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-512 |
3.04e-156 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 454.35 E-value: 3.04e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 39 NKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSpWRRMDASERGRLLNRLADLVERDR 118
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 119 VYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 279 SNLKRVTLELGGKSPSIVLADA-DMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELD 357
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 358 TQQGPQVDKEQFERILGYIRLGQKEGAKLLCGgeRLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
42-512 |
1.14e-154 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 449.41 E-value: 1.14e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMD--GEHFcFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07088 78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDrpNENI-FIFKVPIGVVAGILPWNFPFFLIARKLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEs 279
Cdd:cd07088 156 PALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07088 235 NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL-GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQR 438
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81904561 439 ANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
42-512 |
3.12e-153 |
|
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: 446.13 E-value: 3.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAK---EAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 202 LATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 282 KRVTLELGGKSPSIVLADADMEHA--VDQCHE--ALF-FNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:cd07116 239 IPVTLELGGKSPNIFFADVMDADDafFDKALEgfVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 357 DTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGER-----LGERGFFIKPTVFGDVQdgMRIAKEEIFGPVQPLFKFKK 431
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 432 IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
.
gi 81904561 512 I 512
Cdd:cd07116 477 V 477
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
42-512 |
3.11e-152 |
|
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: 443.54 E-value: 3.11e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAvSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 201 ALATGNTVVMKVAEQTPLSALYLASLIKEA----GFPPGVVNIITGYGPtAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 277 GESNlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 357 DTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL--GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQA--LQAGTVWVntyNIVT----CHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNV---NIPTsgaeIGGAFGGEKETGGGRESGSDAWKQYMRRS 471
|
....
gi 81904561 509 TVTI 512
Cdd:cd07086 472 TCTI 475
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
56-512 |
1.47e-150 |
|
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: 438.18 E-value: 1.47e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGspwRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 136 SYVlDLDEVIKVYRYFAGWADKWHGKTIPMD----GEH-FCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM 210
Cdd:cd07149 78 ARK-EVDRAIETLRLSAEEAKRLAGETIPFDaspgGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 211 KVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGesnLKRVTLELGG 290
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 291 KSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFE 370
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 371 RILGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAV 450
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 451 FTRDLDKAIYFTQALQAGTVWVN---TYNIVtcHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINdssTFRVD--HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
41-511 |
6.34e-150 |
|
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: 438.97 E-value: 6.34e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDavSKKTFPTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPM-DGEHfCFTRHEPVGVCGQIIPWNFPL-VMQGWK 197
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMvPGED-NRYVYRPLGVGAVISPWNFPLaILAGMT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 198 LApALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA- 276
Cdd:cd07124 188 TA-ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAa 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 277 ----GESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07124 267 kvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGaKLLCGGERLGE--RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK 430
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN---TYNIVTCHtPFGGFKESG-NGRELGEDGLRAYTE 506
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALVGRQ-PFGGFKMSGtGSKAGGPDYLLQFMQ 504
|
....*
gi 81904561 507 VKTVT 511
Cdd:cd07124 505 PKTVT 509
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
42-510 |
2.73e-148 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 434.12 E-value: 2.73e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESYvldlDEVikVY-----RYFAGWADKWHGKTIPM-DGEHFCFTRHEPVGVCGQIIPWNFPLVMQG 195
Cdd:PLN02278 105 AQLMTLEQGKPLKEAI----GEV--AYgasflEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKA 275
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 276 AGESnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFE 355
Cdd:PLN02278 259 AAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 356 LDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81904561 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:PLN02278 418 IAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
56-512 |
1.15e-145 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 425.99 E-value: 1.15e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAK---DVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 136 SyVLDLDEVIKVYRYFAGWADKWHGKTIPMDG-----EHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM 210
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 211 KVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGG 290
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 291 KSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFE 370
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 371 RILGYIRLGQKEGAKLLCGGERlgERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAV 450
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81904561 451 FTRDLDKAIYFTQALQAGTVWVN-TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
56-512 |
5.61e-144 |
|
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: 421.35 E-value: 5.61e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 136 SYVldldEVIKVYRYF---AGWADKWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMK 211
Cdd:cd07150 78 AWF----ETTFTPELLraaAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 212 VAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGK 291
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 292 SPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFER 371
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 372 ILGYIRLGQKEGAKLLCGGERLGErgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81904561 452 TRDLDKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
77-512 |
4.63e-140 |
|
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: 410.77 E-value: 4.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 77 DVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWAD 156
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 157 KWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLS-ALYLASLIKEAGFPP 234
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 235 GVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALF 314
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 315 FNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERlg 394
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 395 eRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN- 473
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINd 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 81904561 474 -TYNiVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07104 393 qTVN-DEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
58-511 |
2.95e-138 |
|
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: 407.11 E-value: 2.95e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRmDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07120 79 F-EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEA-GFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQkAAGESNLKRVTLELGGKSPSIV 296
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIM-AAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 297 LADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYI 376
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 377 RLGQKEGAKLLCGGERLGE---RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTR 453
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 81904561 454 DLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
78-512 |
7.13e-133 |
|
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: 392.21 E-value: 7.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 78 VDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyvldLDEVIK---VYRYFAGW 154
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA----RAEVEKcawICRYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 155 ADKW-HGKTIPMDGEHfCFTRHEPVGVCGQIIPWNFPL--VMQGwkLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG 231
Cdd:cd07100 74 AEAFlADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFwqVFRF--AAPNLMAGNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 232 FPPGV-VNIITGYGpTAGAAIAqHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCH 310
Cdd:cd07100 151 FPEGVfQNLLIDSD-QVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 311 EALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGG 390
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 391 ERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTV 470
Cdd:cd07100 308 KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 81904561 471 WVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07100 388 FINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
59-512 |
2.36e-131 |
|
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: 389.48 E-value: 2.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 lDLDEVIKVYRYFAGWADKWHGKTIPMD-----GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07094 81 -EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGesnLKRVTLELGGKSP 293
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 374 GYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTR 453
Cdd:cd07094 317 RWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 454 DLDKAIYFTQALQAGTVWVNTYNIV-TCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFrTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
40-511 |
2.69e-128 |
|
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: 382.25 E-value: 2.69e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGwadkwhgktIP--MDGEHF--------CFTRHEPVGVCGQIIPWNF 189
Cdd:cd07085 79 ELARLITLEHGKTLADARG-DVLRGLEVVEFACS---------IPhlLKGEYLenvargidTYSYRQPLGVVAGITPFNF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 190 PLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVG 269
Cdd:cd07085 149 PAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 270 HLIQKAAGeSNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRK 349
Cdd:cd07085 228 EYIYERAA-ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 350 VGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL----GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQP 425
Cdd:cd07085 307 VGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 426 LFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtyniV-----TCHTPFGGFKES--GNGRELGE 498
Cdd:cd07085 387 IVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VpipvpLAFFSFGGWKGSffGDLHFYGK 462
|
490
....*....|...
gi 81904561 499 DGLRAYTEVKTVT 511
Cdd:cd07085 463 DGVRFYTQTKTVT 475
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
59-512 |
6.55e-128 |
|
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: 380.41 E-value: 6.55e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyV 138
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 LDLDEVIKVYRYFAGWADK-------WHGKTIPmdgEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMK 211
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRvlaprkvPTGLLMP---NKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 212 VAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQhmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGK 291
Cdd:cd07099 154 PSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 292 SPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFER 371
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 372 ILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81904561 452 TRDLDKAIYFTQALQAGTVWVN--TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
41-511 |
7.76e-128 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 382.36 E-value: 7.76e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDavSKKTFPTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKW-HGKTI-PMDGEHfCFTRHEPVGVCGQIIPWNFPL-VMQGW 196
Cdd:PRK03137 114 EFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGKPVeSRPGEH-NRYFYIPLGVGVVISPWNFPFaIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 197 KLAPaLATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQKA 275
Cdd:PRK03137 192 TLAA-IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 276 A----GESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVG 351
Cdd:PRK03137 271 AkvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 352 NPfELDTQQGPQVDKEQFERILGYIRLGQKEGaKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKK 431
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 432 IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN---TYNIVTCHtPFGGFKESG-NGRELGEDGLRAYTEV 507
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVGYH-PFGGFNMSGtDSKAGGPDYLLLFLQA 507
|
....
gi 81904561 508 KTVT 511
Cdd:PRK03137 508 KTVS 511
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
45-513 |
1.21e-122 |
|
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: 367.40 E-value: 1.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 45 NEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAfrlGSPWRRMDASERGRLLNRLADLVERDRVYLASL 124
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 125 ETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPMD---GEHFCFtrHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:cd07151 78 LIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvpgKENRVY--REPLGVVGVISPWNFPLHLSMRSVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 202 LATGNTVVMKVAEQTPLSA-LYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsN 280
Cdd:cd07151 155 LALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-H 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 281 LKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQ 360
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 361 GPQVDKEQFERILGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRAN 440
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81904561 441 NTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIV-TCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
59-512 |
7.48e-122 |
|
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: 364.76 E-value: 7.48e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRadvdlavKAAREAFRLGSPWR-RMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07146 4 RNPYTGEVVGTVPAGTE-------EALREALALAASYRsTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VlDLDEVIKVYRYFAGWADKWHGKTIPMD-----GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKV 212
Cdd:cd07146 77 Y-EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 213 AEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGesnLKRVTLELGGKS 292
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 293 PSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERI 372
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 373 LGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFT 452
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81904561 453 RDLDKAIYFTQALQAGTVWVNT---YNivTCHTPFGGFKESGNG-RELGEDGLRAYTEVKTVTI 512
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEvpgFR--SELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
40-513 |
1.75e-119 |
|
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: 359.58 E-value: 1.75e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAvSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQES---------YVLDLDEVIKvyryfagwadKWHGKTIPMDGEHF-----CFTRHEPVGVCGQII 185
Cdd:cd07082 80 EVANLLMWEIGKTLKDAlkevdrtidYIRDTIEELK----------RLDGDSLPGDWFPGtkgkiAQVRREPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 186 PWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGS 265
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 266 TEVGHLIQKAAGesnLKRVTLELGGKSPSIVLADADMEHAVDQCHE-ALFFNmGQCCCAGSRTFVEESIYREFLERTVEK 344
Cdd:cd07082 230 TEVGNRLKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEIVKgALSYS-GQRCTAIKRVLVHESVADELVELLKEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 345 AKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERgfFIKPTVFGDVQDGMRIAKEEIFGPVQ 424
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 425 PLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYnivtC-----HTPFGGFKESGNGRELGED 499
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK----CqrgpdHFPFLGRKDSGIGTQGIGD 459
|
490
....*....|....
gi 81904561 500 GLRAYTEVKTVTIK 513
Cdd:cd07082 460 ALRSMTRRKGIVIN 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-511 |
2.21e-117 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 356.11 E-value: 2.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 49 DAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLD 128
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQR---AWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 129 NGK----PFQEsyVLDldeVIKVYRYFAGWA-----DKWHGKTIPMdgehfcFTR----HEPVGVCGQIIPWNFPLVMQG 195
Cdd:PRK09407 104 TGKarrhAFEE--VLD---VALTARYYARRApkllaPRRRAGALPV------LTKttelRQPKGVVGVISPWNYPLTLAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHmdVDKVAFTGSTEVGHLIQKA 275
Cdd:PRK09407 173 SDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 276 AGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFE 355
Cdd:PRK09407 251 AGR-RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 356 LDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERG-FFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN-----TYNIVTchTPFGGFKESGNGRELGEDGLRAYTEVKT 509
Cdd:PRK09407 410 AVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
..
gi 81904561 510 VT 511
Cdd:PRK09407 488 IA 489
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
61-511 |
7.18e-116 |
|
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: 349.69 E-value: 7.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 61 PTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGK----PFQEs 136
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQR---AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 137 yVLDldeVIKVYRYFAGWADKW-----HGKTIPMdgehfcFTR----HEPVGVCGQIIPWNFPLVMQGWKLAPALATGNT 207
Cdd:cd07101 79 -VLD---VAIVARYYARRAERLlkprrRRGAIPV------LTRttvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 208 VVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHmdVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLE 287
Cdd:cd07101 149 VVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 288 LGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKE 367
Cdd:cd07101 226 LGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 368 QFERILGYIRLGQKEGAKLLCGGERLGERG-FFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGL 446
Cdd:cd07101 306 QLDRVTAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 447 AAAVFTRDLDKAIYFTQALQAGTVWVN-----TYNIVTchTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
56-512 |
2.49e-113 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 343.07 E-value: 2.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 136 SYVlDLDEVIKVYRYFAGWADKWHGKTIPMDG-----EHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM 210
Cdd:cd07147 78 ARG-EVARAIDTFRIAAEEATRIYGEVLPLDIsargeGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 211 KVAEQTPLSALYLASLIKEAGFPPGVVNIITGygPTAGAAI-AQHMDVDKVAFTGSTEVGHLIQKAAGEsnlKRVTLELG 289
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 290 GKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQF 369
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 370 ERILGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAA 449
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 450 VFTRDLDKAIYFTQALQAGTVWVN---TYNIVtcHTPFGGFKESGNGRElgedGLR----AYTEVKTVTI 512
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdvpTFRVD--HMPYGGVKDSGIGRE----GVRyaieEMTEPRLLVI 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
77-512 |
2.00e-112 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 339.94 E-value: 2.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 77 DVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNG--KPFQEsyvLDLDEVIKVYRYFAGW 154
Cdd:cd07105 1 DADQAVEAAAAAF---PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGatAAWAG---FNVDLAAGMLREAASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 155 ADKWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFP 233
Cdd:cd07105 75 ITQIIGGSIPSDKPgTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 234 PGVVNIITGY---GPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCH 310
Cdd:cd07105 155 KGVLNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 311 EALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGnpfelDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGG 390
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 391 -ERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGT 469
Cdd:cd07105 309 lADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 81904561 470 VWVNTYNIVTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07105 389 VHINGMTVHDEPTlPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
64-497 |
1.20e-111 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 338.50 E-value: 1.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 64 GEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKpFQESYVLDLDE 143
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 144 VIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSA-LY 222
Cdd:cd07152 77 AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 223 LASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADM 302
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 303 EHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKE 382
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 383 GAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFT 462
Cdd:cd07152 315 GARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|....*..
gi 81904561 463 QALQAGTVWVN--TYNiVTCHTPFGGFKESGNGRELG 497
Cdd:cd07152 392 DRLRTGMLHINdqTVN-DEPHNPFGGMGASGNGSRFG 427
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
42-514 |
8.51e-111 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 337.65 E-value: 8.51e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQE-----SYVLDLDEvikvyrYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQG 195
Cdd:PRK11241 91 ARLMTLEQGKPLAEakgeiSYAASFIE------WFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQK 274
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGrQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 275 AAgeSNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:PRK11241 245 CA--KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKV 514
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
59-510 |
8.45e-109 |
|
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: 331.52 E-value: 8.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQEsYV 138
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQ-AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 LDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFC-FTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07102 77 GEIRGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVL 297
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 378 LGQKEGAKLLCGGERLGER---GFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD 454
Cdd:cd07102 315 DAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 81904561 455 LDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
150-513 |
3.76e-101 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 310.51 E-value: 3.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 150 YFAGWADKWHGKTIPMD--GEH-FCFTRhePVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASL 226
Cdd:PRK10090 43 YMAEWARRYEGEIIQSDrpGENiLLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 227 IKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAV 306
Cdd:PRK10090 121 VDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 307 DQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFE-LDTQQGPQVDKEQFERILGYIRLGQKEGAK 385
Cdd:PRK10090 200 KAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGAR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 386 LLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQAL 465
Cdd:PRK10090 280 VALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGL 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 81904561 466 QAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PRK10090 360 KFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQ 407
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
59-511 |
2.80e-100 |
|
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: 310.00 E-value: 2.80e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPfqesyV 138
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR---EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT-----M 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 LD--LDEVIKVyryfagwADK--W---HG----KTIPMDGEHFCFTR-----HEPVGVCGQIIPWNFPLVMQGWKLAPAL 202
Cdd:cd07098 73 VDasLGEILVT-------CEKirWtlkHGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 203 ATGNTVVMKVAEQTPLSALYLASLIKEA----GFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:cd07098 146 FAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 279 SnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:cd07098 225 S-LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGER----LGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:cd07098 304 DVGAMISPARFDRLEELVADAVEKGARLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEE 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81904561 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTY--NIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07098 384 AVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
58-512 |
2.37e-94 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 294.34 E-value: 2.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 vldlDEVIKVYRYFAGWADkwHGKTI----PMD----GEHFCFTRHEPVGVCGQIIPWNFPLvmqgWKL----APALATG 205
Cdd:PRK09406 82 ----AEALKCAKGFRYYAE--HAEALladePADaaavGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 206 NTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITgYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESnLKRVT 285
Cdd:PRK09406 152 NVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 286 LELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVD 365
Cdd:PRK09406 230 LELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 366 KEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYG 445
Cdd:PRK09406 310 EQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 446 LAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
44-512 |
1.30e-93 |
|
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: 292.96 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 44 NNEWhdAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLAS 123
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 124 LETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPmdGE---HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:cd07130 79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIP--SErpgHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 201 ALATGNTVVMKVAEQTPLSAL----YLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 277 GEsNLKRVTLELGGKSPSIVLADADMEHAVDqcheALFF----NMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07130 235 AA-RFGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPT-VFGDVQDGmrIAKEEIFGPVQPLFKFKK 431
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTiVEGLSDAP--IVKEETFAPILYVLKFDT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 432 IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTyNIVTCHT----PFGGFKESGNGRELGEDGLRAYTEV 507
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQYMRR 466
|
....*
gi 81904561 508 KTVTI 512
Cdd:cd07130 467 STCTI 471
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
41-511 |
3.94e-89 |
|
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: 282.16 E-value: 3.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHDAVSKKTfpTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTI------PMDGEHFcftrHEPVGVCGQIIPWNFPLVM 193
Cdd:cd07083 96 ELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESF----YVGLGAGVVISPWNFPVAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:cd07083 171 FTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 274 KAAGE-----SNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQR 348
Cdd:cd07083 251 EAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 349 KVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGaKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFK 428
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 429 FK--KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESG-NGRELGEDGLRA 503
Cdd:cd07083 410 YKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGtNAKTGGPHYLRR 489
|
....*...
gi 81904561 504 YTEVKTVT 511
Cdd:cd07083 490 FLEMKAVA 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-497 |
6.96e-86 |
|
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: 274.46 E-value: 6.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 21 YSTAAALPNPIPNPEICY----NKLFINNEWHDAVSKktfptvnPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWR 96
Cdd:cd07125 17 EALADALKAFDEKEWEAIpiinGEETETGEGAPVIDP-------ADHERTIGEVSLADAEDVDAALAIAAAAF---AGWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 97 RMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyvldLDEV---IKVYRYFAGWADK-WHGKTIPMDGEHFCF 172
Cdd:cd07125 87 ATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA----DAEVreaIDFCRYYAAQARElFSDPELPGPTGELNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 173 TRHEP--VGVCgqIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAA 250
Cdd:cd07125 163 LELHGrgVFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 251 IAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTF 328
Cdd:cd07125 241 LVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 329 VEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEgAKLLCGGERLGERGFFIKPTVFGDV 408
Cdd:cd07125 321 LQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 409 qdGMRIAKEEIFGPVQPL--FKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN---TYNIVTCHtP 483
Cdd:cd07125 400 --GIFDLTTEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrniTGAIVGRQ-P 476
|
490
....*....|....
gi 81904561 484 FGGFKESGNGRELG 497
Cdd:cd07125 477 FGGWGLSGTGPKAG 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
77-494 |
9.60e-81 |
|
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: 258.36 E-value: 9.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 77 DVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyvldLDEV----------IK 146
Cdd:cd07095 1 QVDAAVAAARAAFP---GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA----QTEVaamagkidisIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 147 VYRYFAGwadkwhGKTIPMdGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASL 226
Cdd:cd07095 74 AYHERTG------ERATPM-AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 227 IKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTLELGGKSPSIVLADADMEHAV 306
Cdd:cd07095 147 WEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 307 DQCHEALFFNMGQCCCAGSRTFVEESIY-REFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERilgYIRLGQK---E 382
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR---YLLAQQDllaL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 383 GAKLLCGGERLGERGFFIKPTVFgDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFT 462
Cdd:cd07095 303 GGEPLLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
410 420 430
....*....|....*....|....*....|...
gi 81904561 463 QALQAGTV-WVNTYNIVTCHTPFGGFKESGNGR 494
Cdd:cd07095 382 ARIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
59-493 |
2.31e-76 |
|
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: 247.72 E-value: 2.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWrrMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 139 lDLDEVIKVYRYFAGWADKWHGKTIPMD----GE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07148 82 -EVTRAIDGVELAADELGQLGGREIPMGltpaSAgRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITgygptAGAAIAQHMDVD-KVA---FTGSTEVG-HLIQKAAGESnlkRVTLEL 288
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-----CENAVAEKLVTDpRVAffsFIGSARVGwMLRSKLAPGT---RCALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 289 GGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQ 368
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 369 FERILGYIRLGQKEGAKLLCGGERLGERGFfiKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAA 448
Cdd:cd07148 313 VDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 81904561 449 AVFTRDLDKAIYFTQALQAGTVWVNTynivtcHT-------PFGGFKESGNG 493
Cdd:cd07148 391 AVFTKDLDVALKAVRRLDATAVMVND------HTafrvdwmPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
40-511 |
9.75e-76 |
|
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: 246.72 E-value: 9.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIP-----MDgehfCFTRHEPVGVCGQIIPWNFPLVMQ 194
Cdd:TIGR01722 79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTqvatrVD----VYSIRQPLGVCAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 195 GWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQK 274
Cdd:TIGR01722 154 LWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 275 aAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSrTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:TIGR01722 233 -TGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK 430
Cdd:TIGR01722 311 DPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtyniVTCHTP-----FGGFKES--GNGRELGEDGLRA 503
Cdd:TIGR01722 391 TLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN----VPIPVPlpyfsFTGWKDSffGDHHIYGKQGTHF 466
|
....*...
gi 81904561 504 YTEVKTVT 511
Cdd:TIGR01722 467 YTRGKTVT 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
58-510 |
2.89e-73 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 239.76 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 138 VldldEVIKVyryfAGWADkW---HG----KTIPMDGEHF-CFTRHEPVGVCGQIIPWNFPL--VMQGwkLAPALATGNT 207
Cdd:PRK13968 88 A----EVAKS----ANLCD-WyaeHGpamlKAEPTLVENQqAVIEYRPLGTILAIMPWNFPLwqVMRG--AVPILLAGNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 208 VVMKVAEQTPLSALYLASLIKEAGFPPGVVniitGYGPTAGAAIAQHMDVDKVA---FTGSTEVGHLIQKAAGESnLKRV 284
Cdd:PRK13968 157 YLLKHAPNVMGCAQLIAQVFKDAGIPQGVY----GWLNADNDGVSQMINDSRIAavtVTGSVRAGAAIGAQAGAA-LKKC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 285 TLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQV 364
Cdd:PRK13968 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 365 DKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRY 444
Cdd:PRK13968 312 RFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81904561 445 GLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
95-510 |
1.71e-72 |
|
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: 236.74 E-value: 1.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 95 WRRMDASERGRLLNRLADLVE--RDRVYLASLEtlDNGKPFQEsyvLDLDEVIKVY-------RYFAGW-ADKWHGKTIP 164
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILarREEIIAALAA--DFRKPAAE---VDLTEILPVLseinhaiKHLKKWmKPKRVRTPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 165 MDGEHfCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGyg 244
Cdd:cd07134 89 LFGTK-SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 245 ptaGAAIAQH---MDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCC 321
Cdd:cd07134 165 ---DAEVAQAlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 322 CAGSRTFVEESIYREFLERtVEKAKQRKVGNpfELDTQQGPQ----VDKEQFERILGYIRLGQKEGAKLLCGGE-RLGER 396
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQfDAAQR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 397 gfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDlDKAI-YFTQALQAGTVWVNT- 474
Cdd:cd07134 318 --YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVnKVLARTSSGGVVVNDv 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 81904561 475 -YNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07134 395 vLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
81-512 |
8.47e-72 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 234.73 E-value: 8.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 81 AVKAAREAFRLGS----PWRRmdaserGRLLNRLADLVERDRVYLASLETlDNGKPFQESYVLD---LDEVIKVY-RYFA 152
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRK------AQLKALKRMLTENEEEIAAALYA-DLGKPPAEAYLTEiavVLGEIDHAlKHLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 153 GWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgF 232
Cdd:cd07087 76 KWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-F 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 233 PPGVVNIITGYGPTAGAAIAQHMDvdKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEA 312
Cdd:cd07087 155 DPEAVAVVEGGVEVATALLAEPFD--HIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 313 LFFNMGQCCCAGSRTFVEESIYREFLERtVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgqkEGAKLLCGGER 392
Cdd:cd07087 232 KFLNAGQTCIAPDYVLVHESIKDELIEE-LKKAIKEFYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 393 -LGERgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVW 471
Cdd:cd07087 306 dKEER--YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVC 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 81904561 472 VNTYNI-VTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07087 384 VNDVLLhAAIPNlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
40-515 |
1.19e-69 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 231.18 E-value: 1.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRV 119
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 120 YLASLETLDNGKPFQESyvldLDEVIK---VYRYFA-------GWADKWHGKTIPMDGEH-FCFTRHEPVGVCGQIIPWN 188
Cdd:PLN00412 94 PIAECLVKEIAKPAKDA----VTEVVRsgdLISYTAeegvrilGEGKFLVSDSFPGNERNkYCLTSKIPLGVVLAIPPFN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 189 FPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGStEV 268
Cdd:PLN00412 170 YPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 269 GHLIQKAAGESNLKrvtLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQR 348
Cdd:PLN00412 249 GIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 349 KVGNPfELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGErgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFK 428
Cdd:PLN00412 326 TVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 429 FKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTC-HTPFGGFKESGNGRELGEDGLRAYTEV 507
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKV 481
|
....*...
gi 81904561 508 KTVTIKVP 515
Cdd:PLN00412 482 KSTVINLP 489
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
41-494 |
2.50e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 230.23 E-value: 2.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 41 LFINNEWHdAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESyvldLDEV----------IKVYRYFAGwadkwHGKTIPMDGEhfCFTRHEPVGVCGQIIPWNFP 190
Cdd:PRK09457 79 LAEVIARETGKPLWEA----ATEVtaminkiaisIQAYHERTG-----EKRSEMADGA--AVLRHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 191 LVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGH 270
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 271 LI-QKAAGESNlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIY-REFLERTVEKAKQR 348
Cdd:PRK09457 227 LLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 349 KVGNPFElDTQ--QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFgDVQDGMRIAKEEIFGPVQPL 426
Cdd:PRK09457 306 TVGRWDA-EPQpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81904561 427 FKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTV-WVNTYNIVTCHTPFGGFKESGNGR 494
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
40-512 |
4.58e-69 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 239.33 E-value: 4.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 40 KLFINNEWH----DAVSKKTFPTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLV 114
Cdd:PRK11904 544 AAFLEKQWQagpiINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLL 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 115 ERDRVYLASLETLDNGKPFQESyvldLDEV---IKVYRYFAGWADKWHGKTIPM---DGEHfCFTRHEPVGV--CgqIIP 186
Cdd:PRK11904 621 EANRAELIALCVREAGKTLQDA----IAEVreaVDFCRYYAAQARRLFGAPEKLpgpTGES-NELRLHGRGVfvC--ISP 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 187 WNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGST 266
Cdd:PRK11904 694 WNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGST 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 267 EVGHLIQKAAGESNLKRVTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEK 344
Cdd:PRK11904 774 ETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 345 AKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEgAKLLCGGE--RLGERGFFIKPTVFgDVqDGMRIAKEEIFGP 422
Cdd:PRK11904 854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPlpAGTENGHFVAPTAF-EI-DSISQLEREVFGP 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 423 VQPLFKFKK--IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESGNGRELGe 498
Cdd:PRK11904 931 ILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIgaVVGVQPFGGQGLSGTGPKAG- 1009
|
490
....*....|....*...
gi 81904561 499 dG----LRAYTEvKTVTI 512
Cdd:PRK11904 1010 -GphylLRFATE-KTVTV 1025
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
42-493 |
2.07e-67 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 235.53 E-value: 2.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWH-------DAVSKKTFPTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADL 113
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPaDHDDVVGTVTEASAEDVERALAAAQAAF---PEWSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 114 VERDRVYLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWhgktipmdgehFCFTRHEPVGVCGQIIPWNFPLVM 193
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANA-IAEVREAVDFLRYYAAQARRL-----------LNGPGHKPLGPVVCISPWNFPLAI 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:PRK11905 693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQ 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 274 KAAGESNLKRVTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVG 351
Cdd:PRK11905 773 RTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 352 NPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLlcggERLG-----ERGFFIKPTVFgDVqDGMRIAKEEIFGPVqpL 426
Cdd:PRK11905 853 DPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPlpaetEKGTFVAPTLI-EI-DSISDLEREVFGPV--L 924
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81904561 427 ----FKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTyNI---VTCHTPFGGFKESGNG 493
Cdd:PRK11905 925 hvvrFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NIigaVVGVQPFGGEGLSGTG 997
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
22-511 |
1.09e-66 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 226.17 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 22 STAAALPNPIPNpeicynklFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDAS 101
Cdd:PLN02419 105 STQPQMPPRVPN--------LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 102 ERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGV 180
Cdd:PLN02419 174 TRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 181 CGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGaAIAQHMDVDKV 260
Cdd:PLN02419 253 CAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 261 AFTGSTEVG-HLIQKAAGESnlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSR-TFVEESiyREFL 338
Cdd:PLN02419 332 SFVGSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 339 ERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL----GERGFFIKPTVFGDVQDGMRI 414
Cdd:PLN02419 408 DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMEC 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 415 AKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtyniVTCHTPFGGFKESGNGR 494
Cdd:PLN02419 488 YKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN----VPIPVPLPFFSFTGNKA 563
|
490 500
....*....|....*....|....
gi 81904561 495 EL-------GEDGLRAYTEVKTVT 511
Cdd:PLN02419 564 SFagdlnfyGKAGVDFFTQIKLVT 587
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
57-497 |
2.60e-66 |
|
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: 222.48 E-value: 2.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 57 PTVNPTT-GEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 136 SyVLDLDEVIKVYRYFAGWADKwhgkTIPMDGehfcftrHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQ 215
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 216 TPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTL--ELGGKSP 293
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 374 GYI---RLGQKEGAKLLCGGERLGERGFFIKPTVFGdvQDGMRIAKEEIFGPVQPLFKFK--KIEEVIQRANNTRYGLAA 448
Cdd:TIGR01238 359 AHIehmSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTM 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 81904561 449 AVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESGNGRELG 497
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQVgaVVGVQPFGGQGLSGTGPKAG 487
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
42-512 |
6.85e-65 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 218.94 E-value: 6.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHdaVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 122 ASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:PLN02315 99 GRLVSLEMGKILAEG-IGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 201 ALATGNTVVMKVAEQTPLSAL----YLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 277 gESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 357 DTQQGP---QVDKEQFERILGYIRlgqKEGAKLLCGGERLGERGFFIKPTVFgDVQDGMRIAKEEIFGPVQPLFKFKKIE 433
Cdd:PLN02315 336 GTLLGPlhtPESKKNFEKGIEIIK---SQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 434 EVIQRANNTRYGLAAAVFTRDLDkaIYFT----QALQAGTVWVNT-YNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPE--TIFKwigpLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRS 489
|
....
gi 81904561 509 TVTI 512
Cdd:PLN02315 490 TCTI 493
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
57-493 |
2.98e-64 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 226.36 E-value: 2.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 57 PTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDR---VYLASLE---TLDN 129
Cdd:COG4230 573 PVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRaelMALLVREagkTLPD 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 130 GkpfqesyvldLDEV---IKVYRYFAGWADKWHGKTipmdgehfcfTRHEPVGVCGQIIPWNFPL---VMQgwkLAPALA 203
Cdd:COG4230 650 A----------IAEVreaVDFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLaifTGQ---VAAALA 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 204 TGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKR 283
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 284 VTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQG 361
Cdd:COG4230 787 VPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVG 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 362 PQVDKEQFERILGYIRLGQKEGaKLL--CGGERLGERGFFIKPTVFgdvqdgmRIA-----KEEIFGPVqpL----FKFK 430
Cdd:COG4230 867 PVIDAEARANLEAHIERMRAEG-RLVhqLPLPEECANGTFVAPTLI-------EIDsisdlEREVFGPV--LhvvrYKAD 936
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81904561 431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTyNIVtc---htPFGGFKESGNG 493
Cdd:COG4230 937 ELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR-NIIgavvgvqPFGGEGLSGTG 1001
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
76-510 |
6.80e-64 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 214.39 E-value: 6.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 76 ADVDLAVKAAREAFRLGspwRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLD----LDEVIKVYRYF 151
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEvsgvKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 152 AGWA-DKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEA 230
Cdd:cd07135 82 KKWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 231 gFPPGVVNIITGYGPTAGAAIAQHMdvDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCH 310
Cdd:cd07135 162 -LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 311 EALFFNMGQCCCAGSRTFVEESIYREFLERtVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgQKEGAKLLCGG 390
Cdd:cd07135 238 WGKFGNAGQICVAPDYVLVDPSVYDEFVEE-LKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLL---DTTKGKVVIGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 391 ERlGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD---LDKAIYFTQAlqA 467
Cdd:cd07135 314 EM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkseIDHILTRTRS--G 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 81904561 468 GTVWVNTYNIVTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07135 391 GVVINDTLIHVGVDNaPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
127-510 |
4.43e-62 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 210.05 E-value: 4.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 127 LDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHG-KTIPMDGEHF---CFTRHEPVGVCGQIIPWNFP--LVMQgwKLAP 200
Cdd:cd07136 46 KDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKpKRVKTPLLNFpskSYIYYEPYGVVLIIAPWNYPfqLALA--PLIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 201 ALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDvdKVAFTGSTEVGHLIQKAAGEsN 280
Cdd:cd07136 124 AIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-H 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 281 LKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFElDTQQ 360
Cdd:cd07136 200 LTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 361 GPQVDKEQFERILGYIrlgqkEGAKLLCGGERlGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRAN 440
Cdd:cd07136 279 GRIINEKHFDRLAGLL-----DNGKIVFGGNT-DRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIK 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81904561 441 NTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN--TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07136 353 SRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
174-510 |
3.51e-60 |
|
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: 204.26 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 174 RHEPVGVCGQIIPWNFPLVMQgwkLAP---ALATGNTVVMKVAEQTP-LSALyLASLIKEAgFPPGVVNIITGyGPTAGA 249
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 250 AIAqHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFV 329
Cdd:cd07133 172 AFS-SLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 330 EESIYREFLERTVEKAKQR---KVGNPfeldtQQGPQVDKEQFERILGYIRLGQKEGAKLL-CG--GERLGERGfFIKPT 403
Cdd:cd07133 250 PEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeLNpaGEDFAATR-KLPPT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 404 VFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN-TYNIVTCHT 482
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdTLLHVAQDD 403
|
330 340
....*....|....*....|....*....
gi 81904561 483 -PFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07133 404 lPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
64-491 |
1.72e-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: 199.74 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 64 GEVIGHVAEGDRADVDLAVKAAREAfrlGSPWRRMDASERGRLLNRLADLVE---RDRVYLASLetLDNGK-PFQEsyvl 139
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKnVWQA---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 140 DLD---EVIKVYRYFAGWADKWHGKTiPMDGEHFCFTR--HEPV-GVCGQIIPWNFPLVMQGWKLAPALaTGNTVVMKVA 213
Cdd:cd07123 128 EIDaacELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRleYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGES-----NLKRVTLEL 288
Cdd:cd07123 206 DTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGET 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 289 GGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQ 368
Cdd:cd07123 286 GGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 369 FERILGYIRLGQKE-GAKLLCGGERLGERGFFIKPTVFgDVQDGM-RIAKEEIFGPVQPLFKF--KKIEEVIQRANNT-R 443
Cdd:cd07123 366 FDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI-ETTDPKhKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsP 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 81904561 444 YGLAAAVFTRDlDKAIY-FTQALQ--AGTVWVN---TYNIVTCHtPFGGFKESG 491
Cdd:cd07123 445 YALTGAIFAQD-RKAIReATDALRnaAGNFYINdkpTGAVVGQQ-PFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
76-513 |
3.59e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 187.16 E-value: 3.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 76 ADVDLAVKAAREAFRLGS----PWRRMdasergRLLNRLADLVERDRVYLASLEtLDNGKPFQESYVLDLDEVIKVYRYF 151
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKtrplEFRKQ------QLRNLLRMLEENKQEFSEAVH-KDLGRHPFETKMTEVLLTVAEIEHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 152 AGWADKWhGKTIPMDGE-HF----CFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASL 226
Cdd:PTZ00381 80 LKHLDEY-LKPEKVDTVgVFgpgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 227 IKEAgFPPGVVNIITGYGPTAGAAIAQHMDVdkVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAV 306
Cdd:PTZ00381 159 LTKY-LDPSYVRVIEGGVEVTTELLKEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 307 DQCHEALFFNMGQCCCAGSRTFVEESIYREFLErTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgQKEGAKL 386
Cdd:PTZ00381 235 RRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE-ALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 387 LCGGErLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQ 466
Cdd:PTZ00381 311 VYGGE-VDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 81904561 467 AGTVWVN--TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PTZ00381 390 SGAVVINdcVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
57-493 |
6.26e-52 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 190.57 E-value: 6.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 57 PTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAfrlGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:PRK11809 662 PVINPaDPRDIVGYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSN 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 136 SyVLDLDEVIKVYRYFAGWADkwhgktipmdgEHFCFTRHEPVG--VCgqIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:PRK11809 739 A-IAEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKA-AG--ESNLKRVTL--EL 288
Cdd:PRK11809 805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNlAGrlDPQGRPIPLiaET 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 289 GGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIyrefLERTVEKAK----QRKVGNPFELDTQQGPQV 364
Cdd:PRK11809 885 GGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV----ADRTLKMLRgamaECRMGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 365 DKEQFERILGYIRLGQKEGAK---LLCGGERLGERGFFIKPTV--FGDVQDgmriAKEEIFGPVQPLFKFKK--IEEVIQ 437
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIE 1036
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 438 RANNTRYGLAAAVFTRdLDKAI-YFTQALQAGTVWVNTyNIVTCHT---PFGGFKESGNG 493
Cdd:PRK11809 1037 QINASGYGLTLGVHTR-IDETIaQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
81-513 |
7.57e-48 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 171.64 E-value: 7.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 81 AVKAAREAFRLGspwRRMDASERGRLLNRLADLV-ERDRVYLASLEtLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWH 159
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYAISNLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 160 -----GKTIP--MDGehfCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLI----- 227
Cdd:cd07132 79 kpepvKKNLAtlLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyld 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 228 KEAgFPpgvvnIITGYGPTAGAAIAQHMDvdKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVD 307
Cdd:cd07132 156 KEC-YP-----VVLGGVEETTELLKQRFD--YIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 308 QCHEALFFNMGQCCCAGSRTFVEESIYREFLERtVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgqkEGAKLL 387
Cdd:cd07132 227 RIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEA-LKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 388 CGGE-RLGERgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQ 466
Cdd:cd07132 301 IGGQtDEKER--YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 81904561 467 AGTVWVN-TYNIVTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:cd07132 379 SGGVCVNdTIMHYTLDSlPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
82-510 |
6.07e-46 |
|
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: 166.43 E-value: 6.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 82 VKAAREAFRLGspwRRMDASERGRLLNRLADLV-ERDRVYLASLETlDNGKPFQESYVLDLDEVIKVYRYFAGWADKW-- 158
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSSCKLAIKELKKWma 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 159 --HGK----TIPMDGEHFCftrhEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgF 232
Cdd:cd07137 81 peKVKtpltTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 233 PPGVVNIITGyGPTAGAAIAQHmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEA 312
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 313 LF-FNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQgPQVDKEQFERILGYIRlGQKEGAKLLCGGE 391
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS-RIVNSHHFQRLSRLLD-DPSVADKIVHGGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 392 RlGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVW 471
Cdd:cd07137 311 R-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVT 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 81904561 472 VNTYNI-VTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07137 390 FNDTVVqYAIDTlPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
86-511 |
4.66e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 139.86 E-value: 4.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 86 REAFRLGS----PWRRmdaSERGRLLNRLADlvERDRVYLASLETLdnGKPFQESYVLDLDEVIKVYRYFAGWADKW--- 158
Cdd:PLN02203 16 RETYESGRtrslEWRK---SQLKGLLRLLKD--NEEAIFKALHQDL--GKHRVEAYRDEVGVLTKSANLALSNLKKWmap 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 159 -HGK----TIPMDGEHFcftrHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKeAGFP 233
Cdd:PLN02203 89 kKAKlplvAFPATAEVV----PEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 234 PGVVNIITGyGPTAGAAIAQHmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIV---LADADMEHAVDQCH 310
Cdd:PLN02203 164 SKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslSSSRDTKVAVNRIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 311 EALFFN-MGQCCCAGSRTFVEE---SIYREFLERTVekaKQRKVGNPFELDTqQGPQVDKEQFERILGYirLGQKEGAKL 386
Cdd:PLN02203 241 GGKWGScAGQACIAIDYVLVEErfaPILIELLKSTI---KKFFGENPRESKS-MARILNKKHFQRLSNL--LKDPRVAAS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 387 LCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD--LDKAIyfTQA 464
Cdd:PLN02203 315 IVHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNekLKRRI--LSE 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 81904561 465 LQAGTVWVNTYNI-VTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:PLN02203 393 TSSGSVTFNDAIIqYACDSlPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
81-503 |
8.79e-34 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 132.75 E-value: 8.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 81 AVKAAREAfrlGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHG 160
Cdd:cd07084 4 ALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 161 KTIPMDGEHFCFTRHE---PVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG-FPPGV 236
Cdd:cd07084 81 EPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 237 VNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGhliQKAAGESNLKRVTLELGGKSPSIVLADADMEHAV-DQCHEALFF 315
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA---EKLALDAKQARIYLELAGFNWKVLGPDAQAVDYVaWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 316 NMGQCCCAGSRTFVEESIY-REFLERTVEKAKQRKVGnpfelDTQQGPqvdkEQFERILGYI-RLGQKEGAKLLCGGERL 393
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGP----VQTFTTLAMIaHMENLLGSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 394 GER------GFFIKPTVFGDVQDGMRIAK---EEIFGPVQPLFKFKKIEE--VIQRANNTRYGLAAAVFTRDLDkaiyFT 462
Cdd:cd07084 308 KNHsipsiyGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPI----FL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 81904561 463 QALqAGTVWVN--TYNIVTCHTPF-------GGFKESGNGRELGedGLRA 503
Cdd:cd07084 384 QEL-IGNLWVAgrTYAILRGRTGVapnqnhgGGPAADPRGAGIG--GPEA 430
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
42-503 |
4.32e-31 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 126.36 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAVSKKTfPTVNPTTGEVIGHV-AEGdrADVDLAVKAAREafRLGSPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:PRK11903 8 YVAGRWQAGSGAGT-PLFDPVTGEELVRVsATG--LDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 121 LASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWH-------------GKTIPMDGEHFCFTRHepvGVCGQIIPW 187
Cdd:PRK11903 83 YYDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGdarllrdgeavqlGKDPAFQGQHVLVPTR---GVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 188 NFPlvmqGW----KLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG-FPPGVVNIITGygpTAGAAIAQHMDVDKVAF 262
Cdd:PRK11903 159 NFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAGLLDHLQPFDVVSF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 263 TGSTEVGHLIQK-AAGESNLKRVTLELGGKSPSIVLADAD-----MEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYRE 336
Cdd:PRK11903 232 TGSAETAAVLRShPAVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 337 FLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL-GYIRLgqKEGAKLLCGGERLG------ERGFFIKPTVFG--D 407
Cdd:PRK11903 312 VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRaGLAAL--RAQAEVLFDGGGFAlvdadpAVAACVGPTLLGasD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 408 VQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQA--GTVWVNTYNIVTCHT--- 482
Cdd:PRK11903 390 PDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVISPDVAALHTghg 469
|
490 500
....*....|....*....|....*..
gi 81904561 483 ---P---FGGFKESGNGRELGedGLRA 503
Cdd:PRK11903 470 nvmPqslHGGPGRAGGGEELG--GLRA 494
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
176-510 |
1.69e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 124.00 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 176 EPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIkEAGFPPGVVNIITGYGPTAGAAIAQHM 255
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 256 dvDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALF-FNMGQCCCAGSRTFVEESIY 334
Cdd:PLN02174 190 --DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 335 REFLERTVEKAKQRKVGNPFElDTQQGPQVDKEQFERILGYirLGQKEGA-KLLCGGERLGErGFFIKPTVFGDVQDGMR 413
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKL--LDEKEVSdKIVYGGEKDRE-NLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 414 IAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI-VTCHT-PFGGFKESG 491
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVhLALHTlPFGGVGESG 422
|
330
....*....|....*....
gi 81904561 492 NGRELGEDGLRAYTEVKTV 510
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
42-503 |
3.15e-29 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 120.84 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHdAVSKKTFPTVNPTTGEVIGHVAeGDRADVDLAVKAAREAfrlGSP-WRRMDASERGRLLNRLADLV--ERDR 118
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREK---GGPaLRALTFHERAAMLKALAKYLmeRKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 119 VYLASLETldnGKPFQESYVlDLDEVIKVYRYFAGWA------DKWH--GKTIPMD------GEHFCFTRHepvGVCGQI 184
Cdd:cd07128 79 LYALSAAT---GATRRDSWI-DIDGGIGTLFAYASLGrrelpnAHFLveGDVEPLSkdgtfvGQHILTPRR---GVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 185 IPWNFPLvmqgW----KLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG-FPPGVVNIITGygpTAGAAIAQHMDVDK 259
Cdd:cd07128 152 NAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQDV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 260 VAFTGSTEVG-------HLIQKAAgesnlkRVTLELGGKSPSIVLADA--DMEhAVDQCHEALFFNM----GQCCCAGSR 326
Cdd:cd07128 225 VAFTGSAATAaklrahpNIVARSI------RFNAEADSLNAAILGPDAtpGTP-EFDLFVKEVAREMtvkaGQKCTAIRR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 327 TFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL------GERGFFI 400
Cdd:cd07128 298 AFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFevvgadAEKGAFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 401 KPTVF-GDVQDGMRIAKE-EIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQA--GTVWVNTYN 476
Cdd:cd07128 378 PPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLNRD 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 81904561 477 IV---TCH-TPF-----GGFKESGNGRELGedGLRA 503
Cdd:cd07128 458 SAkesTGHgSPLpqlvhGGPGRAGGGEELG--GLRG 491
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
42-475 |
4.39e-19 |
|
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: 89.86 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 42 FINNEWHDAvsKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLG--SPWRrmdASER----GRLLNRLADLVE 115
Cdd:cd07126 2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhNPLK---NPERyllyGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 116 RDRV--YLASLetLDNGKPfqESYVLDLDEVIKVYRY---FAGWADKWHGKTIPMDGEHFCFTRHE---PVGVCGQIIPW 187
Cdd:cd07126 77 KPEVedFFARL--IQRVAP--KSDAQALGEVVVTRKFlenFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 188 NFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQhMDVDKVAFTGSTE 267
Cdd:cd07126 153 NFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 268 VGHliqKAAGESNlKRVTLELGGKSPSIVLAD-ADMEHAVDQCHEALFFNMGQCCCAGSRTFVEES-IYREFLERTVEKA 345
Cdd:cd07126 232 VAE---RLALELH-GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 346 KQRKVGnpfelDTQQGPqVDKEQFERILGYI-RLGQKEGAKLLCGGERLGERGffiKPTVFGDVQ--------------D 410
Cdd:cd07126 308 EQRKLE-----DLTIGP-VLTWTTERILDHVdKLLAIPGAKVLFGGKPLTNHS---IPSIYGAYEptavfvpleeiaieE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81904561 411 GMRIAKEEIFGPVQPLFKFKKIEE--VIQRANNTRYGLAAAVFTRDldkaIYFTQALQAGTVWVNTY 475
Cdd:cd07126 379 NFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSND----IRFLQEVLANTVNGTTY 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
78-321 |
2.75e-16 |
|
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: 81.05 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 78 VDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDR---VYLASLET-LDNGKPFQEsyvldLDEVIKVYRYFAG 153
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGdelVARAHAETgLPEARLQGE-----LGRTTGQLRLFAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 154 WADK--WHGKTI-PMDGEHFCFTRHE---------PVGVCGqiiPWNFPL---VMQGwKLAPALATGNTVVMKVAEQTP- 217
Cdd:cd07129 73 LVREgsWLDARIdPADPDRQPLPRPDlrrmlvplgPVAVFG---ASNFPLafsVAGG-DTASALAAGCPVVVKAHPAHPg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 218 LSALyLASLI----KEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAgesnLKR-----VTLEL 288
Cdd:cd07129 149 TSEL-VARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA----AARpepipFYAEL 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 81904561 289 GGKSPSIVLADADMEHA---VDQCHEALFFNMGQCC 321
Cdd:cd07129 224 GSVNPVFILPGALAERGeaiAQGFVGSLTLGAGQFC 259
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
78-474 |
2.87e-14 |
|
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: 74.57 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 78 VDLAVKAAREA-FRLGSPWRRMDASERGRLLNRLAdlverdrvylasletldngKPFQESYVLDLDEVIKVY---RYFAG 153
Cdd:cd07077 18 RDLIINAIANAlYDTRQRLASEAVSERGAYIRSLI-------------------ANWIAMMGCSESKLYKNIdteRGITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 154 WADKWHGKTIPMDGEhfCFTRHEPVGVCGQIIPWNFPL-VMQgwKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgF 232
Cdd:cd07077 79 SVGHIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLsGIT--SALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 233 PPGVVNIITGYGPTAGAAIAQ----HMDVDKVAFTGSTEVGHLIQKAageSNLKRVTLELGGKSPSIVLADADMEHAVDQ 308
Cdd:cd07077 154 AAHGPKILVLYVPHPSDELAEellsHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 309 CHEALFFNMGQCccagsrtFVEESIYrefLERTVEKAKqrkvgnpfeldtqqgpqvdKEQFERILGYIRLGQKEGAKLLc 388
Cdd:cd07077 231 VHDSKFFDQNAC-------ASEQNLY---VVDDVLDPL-------------------YEEFKLKLVVEGLKVPQETKPL- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 389 ggerlgergffikptvFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRY----GLAAAVFTRDLDKAIYFTQA 464
Cdd:cd07077 281 ----------------SKETTPSFDDEALESMTPLECQFRVLDVISAVENAWMIIEsgggPHTRCVYTHKINKVDDFVQY 344
|
410
....*....|
gi 81904561 465 LQAGTVWVNT 474
Cdd:cd07077 345 IDTASFYPNE 354
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
78-474 |
1.82e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 47.26 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 78 VDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQEsyvldlDEVIKvyRYFAG---- 153
Cdd:cd07081 1 LDDAVAAAKVAQQ---GLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVE------DKVIK--NHFAAeyiy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 154 --WADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM----KVAEQTPLSALYLASLI 227
Cdd:cd07081 70 nvYKDEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 228 KEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGstevGHLIQKAAGESNlKRVTLELGGKSPSIVLADADMEHAVD 307
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 308 QCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVE------KAKQRKVGNPFEL-DTQQGPQVDKEQFERILGYIRLGQ 380
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGqgayklTAEELQQVQPVILkNGDVNRDIVGQDAYKIAAAAGLKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 381 KEGAKLLCGG-ERLGERGFFIkptvfgdvqdgmriakEEIFGPVQPLFKFKKIEEVIQRA----NNTRYGLAAAVFTRDL 455
Cdd:cd07081 305 PQETRILIGEvTSLAEHEPFA----------------HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNI 368
|
410 420
....*....|....*....|..
gi 81904561 456 ---DKAIYFTQALQAGTVWVNT 474
Cdd:cd07081 369 kaiENMNQFANAMKTSRFVKNG 390
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
181-329 |
9.02e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 45.16 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 181 CGQIIPWNfplvmqGWK-LAPALATGNTVVMKvaeQTPLSALYLASLIK-------EAGFPPGVVNIITgygPTAGAAIA 252
Cdd:cd07127 202 CSTFPTWN------GYPgLFASLATGNPVIVK---PHPAAILPLAITVQvarevlaEAGFDPNLVTLAA---DTPEEPIA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81904561 253 QHM----DVDKVAFTGSTEVG-HLIQKAAGesnlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRT 327
Cdd:cd07127 270 QTLatrpEVRIIDFTGSNAFGdWLEANARQ----AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNI 345
|
..
gi 81904561 328 FV 329
Cdd:cd07127 346 YV 347
|
|
| |
