|
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 ... |
26-506 |
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: 951.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 26 NLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLAD 105
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 106 LVERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 186 MLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV 265
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 266 KEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGD 345
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 346 PFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSI 425
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 426 EEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 52788258 506 K 506
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
32-505 |
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: 844.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSpWRRLDALSRGRLLHQLADLVERDR 111
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 112 ATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 192 APALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR 271
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKT 351
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 352 EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKR 431
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52788258 432 ANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
29-503 |
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: 710.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 29 VKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVE 108
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 109 RDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 189 WKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEA 268
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 269 ASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 348
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 349 VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 428
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 429 IKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
32-507 |
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: 684.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDR 111
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 112 ATLAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:COG1012 83 EELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 191 LAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 270
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 350
Cdd:COG1012 242 E-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED-KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVI 429
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52788258 430 KRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALY-AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
32-507 |
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: 680.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgSPWRR-LDALSRGRLLHQLADLVERD 110
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 111 RATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 191 LAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 270
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 271 RSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 350
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 430
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 431 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-512 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 678.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 19 ALPRPIR-NLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRG 97
Cdd:PLN02466 44 AVEEPITpPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 98 RLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAI 177
Cdd:PLN02466 123 RILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 178 TPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTG 257
Cdd:PLN02466 203 IPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 258 STEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEY 337
Cdd:PLN02466 283 STDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 338 AKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQ 417
Cdd:PLN02466 363 ALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 418 PILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEY 497
Cdd:PLN02466 443 SILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNY 522
|
490
....*....|....*
gi 52788258 498 TEVKTVTIKLgdKNP 512
Cdd:PLN02466 523 LQVKAVVTPL--KNP 535
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
40-503 |
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: 677.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 40 WHESkSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALET 119
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 120 MDTGKPFLHAFFiDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGN 199
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 200 TMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTL 279
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 280 ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQ 359
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 360 KQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGL 439
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 440 TAAVFTKNLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
32-507 |
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: 664.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgSPWRRLDALSRGRLLHQLADLVERDR 111
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 112 ATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 192 APALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASr 271
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKR-PVGDPFDVK 350
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED---KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 427
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 428 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
72-505 |
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: 623.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 72 DKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAFFIDLEGCIRTLRYFAGWADKI 151
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 152 QGKTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVV 230
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 231 NIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQ 310
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 311 GQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME-DK 389
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEgGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 390 GLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYN 469
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 52788258 470 A-LYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
28-509 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 620.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 28 EVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLV 107
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 108 ERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 188 VWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 267
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 268 AASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 427
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 428 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
..
gi 52788258 508 GD 509
Cdd:PLN02766 496 YN 497
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
35-507 |
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: 610.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 195 LCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNL 274
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 354
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 355 PQIDQKQFDKILELIESGKKEGAKLECGGSAMED----KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 430
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 431 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
46-505 |
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: 601.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 46 GKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSpWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKP 125
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 126 FLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKP 205
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 206 AEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKN 285
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 286 PCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDK 364
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 365 ILELIESGKKEGAKLECGGSA--MEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAA 442
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52788258 443 VFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
53-505 |
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: 588.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFqRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAFFI 132
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPL 211
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 212 TALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCA 291
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIES 371
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 372 GKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07114 320 AREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52788258 448 LDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-507 |
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: 580.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 51 TCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAF 130
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 131 FIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTP 210
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 211 LTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 371 SGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDK 450
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 451 ALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
51-505 |
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: 575.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 51 TCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAF 130
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 131 FIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTP 210
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 211 LTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVC 290
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 371 SGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 52788258 447 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
28-506 |
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 52788258 28 EVKF-TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADL 106
Cdd:cd07140 1 TLKMpHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 107 VERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTD----DNVVCFTRHEPIGVCGAITPWNF 182
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 183 PLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVG 262
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 263 KLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRP 342
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 343 VGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKF 422
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 423 KS--IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEV 500
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 52788258 501 KTVTIK 506
Cdd:cd07140 480 KTVTIE 485
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
53-505 |
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: 538.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfI 132
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPL 211
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 212 TALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCA 291
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIES 371
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 372 GKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKA 451
Cdd:cd07103 318 AVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 52788258 452 LKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07103 398 WRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
35-509 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 526.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLV-ERDRAt 113
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 114 LAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 194 ALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSn 273
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQ 353
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 354 GPQIDQKQFDKILELIESGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVI 429
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 430 KRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLGD 509
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
34-504 |
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: 525.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 34 IFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAF---QRGSPWRRLDALSRgrllhqLADLVERD 110
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFpawSATSVEERAALLER------IAEAYEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 111 RATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAG------WADKIQGKTIptddnvvcftRHEPIGVCGAITPWNFPL 184
Cdd:cd07138 75 ADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VREPIGVCGLITPWNWPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 185 LMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKL 264
Cdd:cd07138 145 NQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 265 VKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVG 344
Cdd:cd07138 225 VAEAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 345 DPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGS---AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILK 421
Cdd:cd07138 304 DPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 422 FKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:cd07138 384 YDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
...
gi 52788258 502 TVT 504
Cdd:cd07138 463 SIQ 465
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
33-507 |
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: 523.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 193 PALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 273 NLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFK 423
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 424 SIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
....
gi 52788258 504 TIKL 507
Cdd:cd07559 477 LVSY 480
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
53-508 |
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: 517.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfI 132
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLT 212
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 213 ALYLGSLIKEAGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCAD 292
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 293 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESG 372
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 373 KKEGAKLECGGS--AMEDK---GLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07090 317 KQEGAKVLCGGErvVPEDGlenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 448 LDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLG 508
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
53-505 |
1.09e-179 |
|
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: 512.07 E-value: 1.09e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFi 132
Cdd:cd07106 3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWAdkIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLT 212
Cdd:cd07106 79 EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 213 ALYLGSLIKEAgFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCAD 292
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 293 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESG 372
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 373 KKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKAL 452
Cdd:cd07106 314 KAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 52788258 453 KLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07106 394 AVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
65-505 |
3.53e-178 |
|
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: 508.42 E-value: 3.53e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 65 EGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFiDLEGCIRTLRYF 144
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EIEGAADLWRYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 145 AGWADKIQGKTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEA 223
Cdd:cd07118 93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 224 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAH 303
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 304 QGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG 383
Cdd:cd07118 252 FGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 384 SAMED-KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGT 462
Cdd:cd07118 332 ERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGT 411
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 52788258 463 VWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07118 412 VWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
35-501 |
7.03e-178 |
|
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: 508.20 E-value: 7.03e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 195 LCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNL 274
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 354
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 355 PQIDQKQFDKILELIESGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 430
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 431 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
53-504 |
8.75e-176 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 502.27 E-value: 8.75e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAFFI 132
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKI---QGKTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQ 208
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 209 TPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCI 288
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILEL 368
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 369 IESGKKEGAKLECGGSAME--DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07110 318 IARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52788258 447 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
53-505 |
8.01e-175 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 499.84 E-value: 8.01e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfI 132
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLT 212
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 213 ALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCAD 292
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 293 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVG----DPfDVkteqGPQIDQKQFDKILEL 368
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpgleDP-DL----GPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 369 IESGKKEGAKLECGGSAMED---KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07109 314 VARARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 446 KNLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
76-505 |
1.70e-174 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 495.60 E-value: 1.70e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 76 EAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAFFIDLEGCIRTLRYFAGWADKIQGKT 155
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 156 IP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVP 234
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 235 GFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCC 314
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 315 TAASRVFVEEQVYSEFVRRSVeyakkrpvgdpfdvkteqgpqidqkqfdkileliesgkkegaklecggsamedkglfik 394
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 395 pTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALY-A 473
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 52788258 474 QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
35-503 |
3.45e-173 |
|
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: 496.39 E-value: 3.45e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKkfATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 114 LAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWADKIQGKTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 193 PALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrS 272
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTE 352
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 353 QGPQIDQKQFDKILELIESGKKEGAKLECGGSA--MEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 430
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 431 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNA-LYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTV 503
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
33-507 |
1.28e-172 |
|
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: 495.05 E-value: 1.28e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 193 PALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTE 352
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 353 QGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 428
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52788258 429 IKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
35-505 |
2.32e-171 |
|
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: 491.39 E-value: 2.32e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 194 ALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsN 273
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQ 353
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 354 GPQIDQKQFDKILELIESGKKEGAKLECGGSAME-DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRA 432
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52788258 433 NSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
53-505 |
1.80e-170 |
|
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: 488.76 E-value: 1.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFI 132
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKT----IPtddNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQ 208
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 209 TPLTALYLGSLIKEaGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCI 288
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILEL 368
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 369 IEsGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 448
Cdd:cd07092 315 VE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 449 DKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
35-505 |
4.72e-168 |
|
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: 483.39 E-value: 4.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 114 LAALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07131 79 LARLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 193 PALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRS 272
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 273 NlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTE 352
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 353 QGPQIDQKQFDKILELIESGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 428
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 429 IKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAlYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
31-508 |
1.65e-167 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 482.10 E-value: 1.65e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 31 FTKIFINNEWhESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERD 110
Cdd:PRK13473 2 QTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 111 RATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTipTDDNVVCFT---RHEPIGVCGAITPWNFPLLML 187
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 188 VWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 267
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 268 AASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEG-AKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIE 426
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 427 EVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
..
gi 52788258 507 LG 508
Cdd:PRK13473 474 HT 475
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
53-503 |
7.75e-167 |
|
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: 479.82 E-value: 7.75e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRlDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFI 132
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDDNVVC-----FTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAE 207
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 208 QTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILE 367
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 368 LIESGKKEGAKLECGGSAME--DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52788258 446 KNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
70-505 |
2.63e-165 |
|
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: 474.71 E-value: 2.63e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 70 DVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWAD 149
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 150 KIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLT-ALYLGSLIKEAGFPP 227
Cdd:cd07104 77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 228 GVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVF 307
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 308 FNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAme 387
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 388 dKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINC 467
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 52788258 468 YNAL-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-504 |
3.87e-164 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 474.61 E-value: 3.87e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 19 ALPRPIRNLevkftkiFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQR--GSPWRRLDALSR 96
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 97 GRLLHQLADLVERDRATLAALETMDTGKPFLHAFF--IDLEGCirtLRYFAGWADKIQGK-----TIPtDDNVVCFTRHE 169
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWdmDDVAGC---FEYYADLAEALDAKqkapvSLP-METFKGYVLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQ 249
Cdd:PLN02467 151 PLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 250 INKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSE 329
Cdd:PLN02467 231 VDKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 330 FVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED--KGLFIKPTVFSEVTDNMRI 407
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 408 AKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGR 487
Cdd:PLN02467 390 WREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGR 469
|
490
....*....|....*..
gi 52788258 488 ELGEYALAEYTEVKTVT 504
Cdd:PLN02467 470 ELGEWGLENYLSVKQVT 486
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
51-507 |
3.12e-163 |
|
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: 470.32 E-value: 3.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 51 TCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAF 130
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 131 FIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTP 210
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 211 LTALYLGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVC 290
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 291 ADADLDLAVECAHQGVFFN-QGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 369
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 370 ESGKKEGAKLECGGSAMED----KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52788258 446 KNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
53-505 |
1.01e-159 |
|
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: 461.44 E-value: 1.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFI 132
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLT 212
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 213 ALYLGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASRsnLKRVTLELGGKNPCIVCA 291
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 292 DADLDLAVECAHQGV-FFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 371 SGKKE-GAKLECGGSAMED----KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07108 317 LGLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 446 KNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELG-EYALAEYTEVKTVTI 505
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
34-505 |
1.82e-159 |
|
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: 461.27 E-value: 1.82e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 34 IFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 114 LAALETMDTGKPFLHAFFIDLEGCIRTLRYFAG------WADKIQGKTipTDDNVVcftRHEPIGVCGAITPWNFPLLML 187
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAAlardfpFEERRPGSG--GGHVLV---RREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 188 VWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 267
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 268 AASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07139 234 VCGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGS--AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSI 425
Cdd:cd07139 313 DPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 426 EEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYnALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
53-505 |
4.74e-159 |
|
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: 459.49 E-value: 4.74e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFi 132
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPL 211
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 212 TALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCA 291
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIES 371
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 372 GKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKA 451
Cdd:cd07150 320 AVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 452 LKLASALESGTVWINCYNAL-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07150 397 FKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-497 |
6.65e-159 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 460.32 E-value: 6.65e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKtiptddnvvcFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTE----------LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 195 LCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNl 274
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 354
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 355 PQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANS 434
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52788258 435 TDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
15-503 |
1.39e-156 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 454.92 E-value: 1.39e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 15 RKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDAL 94
Cdd:PLN02278 8 MDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 95 SRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTDD-NVVCFTRHEPIGV 173
Cdd:PLN02278 85 ERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 174 CGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKI 253
Cdd:PLN02278 164 VGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 254 AFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRR 333
Cdd:PLN02278 244 TFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 334 SVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIF 413
Cdd:PLN02278 323 FSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 414 GPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYA 493
Cdd:PLN02278 403 GPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYG 482
|
490
....*....|
gi 52788258 494 LAEYTEVKTV 503
Cdd:PLN02278 483 IDEYLEIKYV 492
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-507 |
1.57e-154 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 449.73 E-value: 1.57e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSpWRRLDALSRGRLLHQLADLVERDR 111
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 112 ATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 192 APALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR 271
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 272 SNLKRVTLELGGKNPCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 350
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEdkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 430
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGL--AAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 431 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
53-505 |
2.33e-153 |
|
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: 445.25 E-value: 2.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfI 132
Cdd:cd07145 5 NPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDD-----NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAE 207
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 208 QTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASRsnLKRVTLELGGKNP 286
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIaSKAGGT--GKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKIL 366
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 367 ELIESGKKEGAKLECGGSAMEdkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 447 NLDKALKLASALESGTVWINCYNAL-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
52-505 |
5.54e-153 |
|
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: 444.35 E-value: 5.54e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 52 CNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGspwRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAFF 131
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 132 IDLEGCIRTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPA 206
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 207 EQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNP 286
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKIL 366
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 367 ELIESGKKEGAKLECGGSAMedkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 447 NLDKALKLASALESGTVWIN-CYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07149 394 DLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
35-506 |
2.12e-152 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 443.81 E-value: 2.12e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgSPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTI------PTDDNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 189 WKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGSTEVGKLVKEA 268
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 269 ASrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 348
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 349 VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 428
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52788258 429 IKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
35-505 |
8.46e-148 |
|
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: 431.99 E-value: 8.46e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESkSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAF-----FIDLegCIrtlrYFAGWADKIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07086 78 GRLVSLEMGKILPEGLgevqeMIDI--CD----YAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 189 WKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEA----GFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEVGKL 264
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 265 VKEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVG 344
Cdd:cd07086 231 VGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 345 DPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME--DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKF 422
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 423 KSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALES--GTVWIN--CYNAlYAQAPFGGFKMSGNGRELGEYALAEYT 498
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYM 468
|
....*..
gi 52788258 499 EVKTVTI 505
Cdd:cd07086 469 RRSTCTI 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-504 |
1.29e-145 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 427.41 E-value: 1.29e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 34 IFINNEwhESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07124 110 ELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 193 PALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR- 271
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 272 ----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMED--KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSI 425
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 426 EEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGFKMSG-NGRELGEYALAEYTEVKT 502
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
..
gi 52788258 503 VT 504
Cdd:cd07124 508 VT 509
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
35-505 |
1.70e-140 |
|
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: 413.39 E-value: 1.70e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 195 LCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNL 274
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 275 KRVTLELGGKNPCIVCA------DADLDLAVECAhqGVF-FNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGL----FIKPTVFSEvTDNMRIAKEEIFGPVQPILKFK 423
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 424 SIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
..
gi 52788258 504 TI 505
Cdd:cd07116 476 LV 477
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
35-507 |
1.88e-139 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 410.65 E-value: 1.88e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESksGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGsPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA-LKG-PWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFFIDLEGCIRTLRYFAgwaDKIqgKTIPTD---------DNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFA---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 186 MLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGP-TVGAAISSHPQINKIAFTGSTEVGKL 264
Cdd:TIGR03216 155 LMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 265 VKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVG 344
Cdd:TIGR03216 235 IMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 345 DPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG-----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPI 419
Cdd:TIGR03216 314 VPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 420 LKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTE 499
Cdd:TIGR03216 394 APFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTE 473
|
....*...
gi 52788258 500 VKTVTIKL 507
Cdd:TIGR03216 474 LTNVCIKL 481
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
38-506 |
4.56e-138 |
|
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: 406.69 E-value: 4.56e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 38 NEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRgsPWRRLDALSRGRLLHQLADLVERDRATLAAL 117
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 118 ETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTD----DNVVcftRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:cd07151 78 LIRESGSTRIKAN-IEWGAAMAITREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 194 ALCCGNTMVLKPAEQTPLTA-LYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTE 352
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 353 QGPQIDQKQFDKILELIESGKKEGAKLECGGSAmedKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRA 432
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788258 433 NSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALyAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDE-PHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
71-505 |
1.91e-137 |
|
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: 403.76 E-value: 1.91e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 71 VDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFF-IDLegCIRTLRYFAGWAD 149
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 150 K-IQGKTIPTDDNVvCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPG 228
Cdd:cd07100 76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 229 VVNIVPGFGPTVGAAISsHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFF 308
Cdd:cd07100 155 VFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 309 NQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED 388
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 389 KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCY 468
Cdd:cd07100 313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420 430
....*....|....*....|....*....|....*..
gi 52788258 469 NALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07100 393 VKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
52-501 |
3.25e-134 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 396.03 E-value: 3.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 52 CNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAff 131
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT---WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 132 idlEGCIRT----LRYFAGWADKIQGKTIPT--DDNVVCFTRhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKP 205
Cdd:TIGR01780 77 ---KGEILYaasfLEWFAEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 206 AEQTPLTALYLGSLIKEAGFPPGVVNIVPG-FGPTVGAAISSHPQINKIAFTGSTEVGK-LVKEAAsrSNLKRVTLELGG 283
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKiLMKQSA--STVKKVSMELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFD 363
Cdd:TIGR01780 231 NAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 364 KILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAV 443
Cdd:TIGR01780 311 KVEKHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52788258 444 FTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01780 391 FSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
53-504 |
1.46e-133 |
|
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: 394.79 E-value: 1.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFqRGSPWRRlDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFi 132
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTI-PTDDNVVCFTRhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPL 211
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 212 TALYLGSLIKEA-GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 371 SGKKEGAK-LECGGSAMED--KGLFIKPTVFsEVTDN-MRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07120 318 RAIAAGAEvVLRGGPVTEGlaKGAFLRPTLL-EVDDPdADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52788258 447 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
53-505 |
1.82e-133 |
|
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: 394.49 E-value: 1.82e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfI 132
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAE 207
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 208 QTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPC 287
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILE 367
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 368 LIESGKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07094 318 WVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 52788258 448 LDKALKLASALESGTVWINCYNALYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
58-505 |
4.52e-133 |
|
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: 393.20 E-value: 4.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 58 EQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFiDLEGC 137
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA-QRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 138 IRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTA-LYL 216
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 217 GSLIKEAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLD 296
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 297 LAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEG 376
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 377 AKLECGGSAmedKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLAS 456
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 52788258 457 ALESGTVWINCYNALY-AQAPFGGFKMSGNGRELGEYA-LAEYTEVKTVTI 505
Cdd:cd07152 393 RLRTGMLHINDQTVNDePHNPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
70-505 |
1.37e-132 |
|
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: 391.56 E-value: 1.37e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 70 DVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWAD 149
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 150 KIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPG 228
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 229 VVNIV---PGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQG 305
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 306 VFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDpfdvkTEQGPQIDQKQFDKILELIESGKKEGAKLECGG-S 384
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 385 AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVW 464
Cdd:cd07105 311 DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 52788258 465 INCYNaLY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07105 391 INGMT-VHdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
33-506 |
1.75e-130 |
|
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: 387.70 E-value: 1.75e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 33 KIFINNEWHESkSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGSpWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDA-GRGW-WPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:cd07082 80 EVANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 188 VWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 267
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 268 AASRsnlKRVTLELGGKNPCIVCADADLDLAV-ECAHQGVFFNqGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDP 346
Cdd:cd07082 239 QHPM---KRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 347 FDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEdkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIE 426
Cdd:cd07082 315 WDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 427 EVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNA----LYaqaPFGGFKMSGNGRELGEYALAEYTEVKT 502
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgpdHF---PFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
....
gi 52788258 503 VTIK 506
Cdd:cd07082 470 IVIN 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
36-507 |
1.46e-129 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 386.60 E-value: 1.46e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 36 INNEWHESKsgKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:PRK03137 41 IGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET---WKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAFfIDLEGCIRTLRYFA----GWADKIQGKTIPTDDNvvcFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:PRK03137 116 SAWLVKEAGKPWAEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 191 LAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 270
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 271 RSN-----LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGD 345
Cdd:PRK03137 272 KVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 346 PFDvKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSI 425
Cdd:PRK03137 352 PED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 426 EEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGFKMSGNGRELG--EYaLAEYTEVK 501
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLFLQAK 508
|
....*.
gi 52788258 502 TVTIKL 507
Cdd:PRK03137 509 TVSEMF 514
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
53-505 |
8.89e-129 |
|
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: 382.34 E-value: 8.89e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHAFFI 132
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAA-QRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKT-IPTDD---NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQ 208
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAPRkVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 209 TPLTALYLGSLIKEAGFPPGVVNIVPGFGPTvGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCI 288
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILEL 368
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 369 IESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 448
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 52788258 449 DKALKLASALESGTVWINC--YNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
42-504 |
2.74e-124 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 373.44 E-value: 2.74e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 42 ESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATLAALETMD 121
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 122 TGKPFLHAF--FIDLEGCIRtlrYFAGWADKI------QGkTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PRK09407 104 TGKARRHAFeeVLDVALTAR---YYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 194 ALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVKEAASRsN 273
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-R 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQ 353
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 354 GPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKG-LFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRA 432
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 433 NSTDYGLTAAVFTKNLDKALKLASALESGTVWIN-CYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
53-505 |
3.22e-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: 365.53 E-value: 3.22e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAqvafqrGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFi 132
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 DLEGCIRTLRYFAGWADKIQGKTIPTDDNV-----VCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAE 207
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 208 QTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPC 287
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILE 367
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 368 LIESGKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 448 LDKALKLASALESGTVWINCYNALYAQ-APFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
54-504 |
6.17e-121 |
|
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: 362.40 E-value: 6.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 54 PSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFfID 133
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 134 LEGCIRTLRYFAGWADKI-----QGKTIPT-DDNVVCftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAE 207
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 208 QTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILE 367
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 368 LIESGKKEGAKLECGGSAMEDKG-LFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 447 NLDKALKLASALESGTVWIN-CYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNeGYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
32-504 |
1.73e-118 |
|
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: 356.83 E-value: 1.73e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDR 111
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 112 ATLAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWADKIQGKTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07085 78 DELARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 191 LAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEVGKLVKEAAS 270
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 271 RSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 350
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIE 426
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 427 EVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNAL-YAQAPFGGFKMS--GNGRELGEYALAEYTEVKTV 503
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVpLAFFSFGGWKGSffGDLHFYGKDGVRFYTQTKTV 474
|
.
gi 52788258 504 T 504
Cdd:cd07085 475 T 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
52-505 |
7.31e-117 |
|
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: 351.93 E-value: 7.31e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 52 CNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFF 131
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 132 iDLEGCIRTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPA 206
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 207 EQTPLTALYLGSLIKEAGFPPGVVNIVPGfgPTVGAAI-SSHPQINKIAFTGSTEVGKLVKEAASRsnlKRVTLELGGKN 285
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKI 365
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 366 LELIESGKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 446 KNLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
35-507 |
9.26e-117 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 352.67 E-value: 9.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAffidlEGCIRT----LRYFAGWADKIQGKTIP---TDDNVVCFTrhEPIGVCGAITPWNFPLLML 187
Cdd:PRK11241 91 ARLMTLEQGKPLAEA-----KGEISYaasfIEWFAEEGKRIYGDTIPghqADKRLIVIK--QPIGVTAAITPWNFPAAMI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 188 VWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 267
Cdd:PRK11241 164 TRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 268 AASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 347
Cdd:PRK11241 244 QCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 348 DVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 427
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 428 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-504 |
5.31e-116 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 351.86 E-value: 5.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 34 IFINNEWHESKSgkKFATCNPSTREQ-ICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:TIGR01237 35 LVINGERVETEN--KIVSINPCDKSEvVGTVSKASQEHAEHALQAAAKAFEA---WKKTDPEERAAILFKAAAIVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGK----TIPTDDNVVCFTrhePIGVCGAITPWNFPLLMLV 188
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 189 WKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEA 268
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 269 ASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPV 343
Cdd:TIGR01237 266 AAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 344 GDPFDVKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFK 423
Cdd:TIGR01237 346 GPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 424 SIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGFKMSGNGRELG--EYaLAEYTE 499
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQ 503
|
....*
gi 52788258 500 VKTVT 504
Cdd:TIGR01237 504 AKTVT 508
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
100-506 |
1.43e-112 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 339.40 E-value: 1.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 100 LHQLADLVERDRATLAALETMDTGKPFLHA-----FFIDLegcirtLRYFAGWADKIQGKTIPTD---DNVVCFTRhePI 171
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAevevaFTADY------IDYMAEWARRYEGEIIQSDrpgENILLFKR--AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 172 GVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQIN 251
Cdd:PRK10090 73 GVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 252 KIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFV 331
Cdd:PRK10090 153 MVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 332 RRSVEYAKKRPVGDPFD-VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKE 410
Cdd:PRK10090 232 NRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 411 EIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELG 490
Cdd:PRK10090 312 ETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADG 391
|
410
....*....|....*.
gi 52788258 491 EYALAEYTEVKTVTIK 506
Cdd:PRK10090 392 KHGLHEYLQTQVVYLQ 407
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
53-503 |
3.82e-111 |
|
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: 337.30 E-value: 3.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAffi 132
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAA-QKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 dlEGCIRTL----RYFAGWADK-IQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAE 207
Cdd:cd07102 76 --GGEIRGMleraRYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 208 QTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07102 154 QTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILE 367
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 368 LIESGKKEGAKLECGG---SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVF 444
Cdd:cd07102 312 QIADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 52788258 445 TKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
45-503 |
6.13e-109 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 332.50 E-value: 6.13e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 45 SGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgSPWRRLDALsRGRLLHQLADLVERDRATLAALETMDTGK 124
Cdd:TIGR04284 13 SAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 125 PFLHAFFIDLEGCIRTLRYFAGWADKIQGKT---------IPTDDNVvcftRHEPIGVCGAITPWNFPLLMLVWKLAPAL 195
Cdd:TIGR04284 91 PRMLTAGAQLEGPVDDLGFAADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 196 CCGNTMVLKPAEQTPLTALYLGSLIKE-AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnL 274
Cdd:TIGR04284 167 AAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAAT-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 354
Cdd:TIGR04284 246 KKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 355 PQIDQKQFDKILELIESGKKEGAKLECGGS--AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRA 432
Cdd:TIGR04284 326 PVISARQRDRVQSYLDLAVAEGGRFACGGGrpADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52788258 433 NSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:TIGR04284 406 NDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
53-504 |
3.73e-107 |
|
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: 327.33 E-value: 3.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFi 132
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQRE---WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 133 dleGCIRTLryfagwADKIQ-----G----KTIPTDDNVVCFTR-----HEPIGVCGAITPWNFPLLMLVWKLAPALCCG 198
Cdd:cd07098 78 ---GEILVT------CEKIRwtlkhGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 199 NTMVLKPAEQTPLTALYLGSLIKEA----GFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnL 274
Cdd:cd07098 149 NAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 354
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 355 PQIDQKQFDKILELIESGKKEGAKLECGGS----AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 430
Cdd:cd07098 307 AMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788258 431 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07098 387 IANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
50-505 |
5.19e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 306.28 E-value: 5.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 50 ATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPfLHA 129
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 130 FFIDLEGCIRTLRYFAGWADKIQGKTiPTDDNVV----CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKP 205
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 206 AEQTPLTALYLGSLIKEAGFPPGVVNIVpgfgpTVGA----AISSHPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLEL 281
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSgaveAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQ 361
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 362 FDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTA 441
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52788258 442 AVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
37-508 |
1.37e-95 |
|
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: 297.97 E-value: 1.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 37 NNEWheSKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAA 116
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 117 LETMDTGKPFLHAF-----FIDLegCirtlRYFAGWADKIQGKTIPTD--DNVVCFTRHePIGVCGAITPWNFPLLMLVW 189
Cdd:cd07130 79 LVSLEMGKILPEGLgevqeMIDI--C----DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 190 KLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEA----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLV 265
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 266 KEAASRsNLKRVTLELGGKNPCIVCADADLDLAVecahQGVFF----NQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKR 341
Cdd:cd07130 231 GQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 342 PVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFsEVTDNMRIAKEEIFGPVQPILK 421
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 422 FKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCyNALYAQA----PFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQY 463
|
490
....*....|.
gi 52788258 498 TEVKTVTIKLG 508
Cdd:cd07130 464 MRRSTCTINYS 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
34-504 |
1.31e-94 |
|
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: 296.41 E-value: 1.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 34 IFINNEWHESKSGKkfATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:cd07083 21 LVIGGEWVDTKERM--VSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKT---WKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFfIDLEGCIRTLRYFAGWADKIQGK-----TIPTDDNVvcfTRHEPIGVCGAITPWNFPLLML 187
Cdd:cd07083 96 ELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPavevvPYPGEDNE---SFYVGLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 188 VWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 267
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 268 AASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRP 342
Cdd:cd07083 252 AAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 343 VGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKF 422
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 423 KSIE--EVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGFKMSG-NGRELGEYALAEY 497
Cdd:cd07083 411 KDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGtNAKTGGPHYLRRF 490
|
....*..
gi 52788258 498 TEVKTVT 504
Cdd:cd07083 491 LEMKAVA 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-505 |
3.67e-85 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 272.15 E-value: 3.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESKSGKkfATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07125 36 IINGEETETGEGA--PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 114 LAALETMDTGKPFLHAffiDLEgcIRT----LRYFAGWADKIQGKTI---PTD--DNVVCftrhEPIGVCGAITPWNFPL 184
Cdd:cd07125 111 LIALAAAEAGKTLADA---DAE--VREaidfCRYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFPL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 185 LMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKL 264
Cdd:cd07125 182 AIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 265 VKEAASRSNLKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRP 342
Cdd:cd07125 262 INRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 343 VGDPFDVKTEQGPQIDQKQFDKILELIESGKKEgAKLECGGSAMEDKGLFIKPTVFSEVTDNMRiaKEEIFGPVQPILKF 422
Cdd:cd07125 342 VGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 423 KS--IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYN---ALYAQAPFGGFKMSGNGRELG--EYaLA 495
Cdd:cd07125 419 KAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNitgAIVGRQPFGGWGLSGTGPKAGgpNY-LL 496
|
490
....*....|
gi 52788258 496 EYTEVKTVTI 505
Cdd:cd07125 497 RFGNEKTVSL 506
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
53-505 |
1.60e-83 |
|
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: 266.21 E-value: 1.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSPWrrLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFF- 131
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 132 ----ID-LEGCIRTLRYFAGwaDKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPA 206
Cdd:cd07148 83 vtraIDgVELAADELGQLGG--REIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 207 EQTPLTALYLGSLIKEAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVkeaasRSNLK---RVTLELGG 283
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFD 363
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 364 KILELIESGKKEGAKLECGGSAMEDKGLfiKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAV 443
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52788258 444 FTKNLDKALKLASALESGTVWINCYNALYAQ-APFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07148 393 FTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
33-507 |
1.96e-83 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 267.01 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAffidLEGCIRT---LRYFAGWADKI--QGKTIPTDD------NVVCFTRHEPIGVCGAITPWN 181
Cdd:PLN00412 94 PIAECLVKEIAKPAKDA----VTEVVRSgdlISYTAEEGVRIlgEGKFLVSDSfpgnerNKYCLTSKIPLGVVLAIPPFN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 182 FPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGStEV 261
Cdd:PLN00412 170 YPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 262 GKLVKEAASRSNLKrvtLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKR 341
Cdd:PLN00412 249 GIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 342 PVGDPFDvKTEQGPQIDQKQFDKILELIESGKKEGAKLEcggSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILK 421
Cdd:PLN00412 326 TVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 422 FKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEV 500
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKV 481
|
....*..
gi 52788258 501 KTVTIKL 507
Cdd:PLN00412 482 KSTVINL 488
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
53-503 |
7.06e-81 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 259.41 E-value: 7.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVeRDRA-TLAALETMDTGKPFLHAff 131
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSeEMAQMITREMGKPINQA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 132 idlEGCIRTLRYFAGWADKiQG----KTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPA 206
Cdd:PRK13968 87 ---RAEVAKSANLCDWYAE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 207 EQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISShPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNP 286
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKIL 366
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 367 ELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 446
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 447 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
74-505 |
7.77e-81 |
|
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: 258.22 E-value: 7.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 74 AVEAAQVAFQRGS----PWRR--LDALSRGrllhqladLVERDRATLAALETmDTGKPFLHAFFIDLEGCIR----TLRY 143
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRKaqLKALKRM--------LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGeidhALKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 144 FAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEA 223
Cdd:cd07087 74 LKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 224 gFPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAH 303
Cdd:cd07087 154 -FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 304 QGVFFNQGQCCTAASRVFVEEQVYSEFVrrsvEYAKKRpvgdpfdVKTEQGPQ----------IDQKQFDKILELIESGK 373
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELI----EELKKA-------IKEFYGEDpkespdygriINERHFDRLASLLDDGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 374 kegakLECGGSAmEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALK 453
Cdd:cd07087 299 -----VVIGGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQER 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 454 LASALESGTVwinCYNALYAQA-----PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07087 373 VLAETSSGGV---CVNDVLLHAaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-503 |
1.62e-79 |
|
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: 254.84 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 164 CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGfGPTVGAA 243
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 244 ISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:cd07134 172 LLELP-FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 324 EQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQI-DQKQFDKILELIESGKKEGAKLECGGsAMEDKGLFIKPTVFSEVT 402
Cdd:cd07134 250 ESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIvNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 403 DNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGF 480
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdvVLHFLNPNLPFGGV 408
|
330 340
....*....|....*....|...
gi 52788258 481 KMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07134 409 NNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
70-498 |
1.78e-79 |
|
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: 254.89 E-value: 1.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 70 DVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFF--------IDLEgcIRTL 141
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 142 RYFAGwadkiqGKTIPTDdNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIK 221
Cdd:cd07095 76 HERTG------ERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 222 EAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVEC 301
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 302 AHQGVFFNQGQCCTAASRVFVEE-QVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLE 380
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 381 CGGSAMEDKGLFIKPTVFsEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALES 460
Cdd:cd07095 308 LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 52788258 461 GTV-WINCYNALYAQAPFGGFKMSGNGRELGEYAlAEYT 498
Cdd:cd07095 387 GIVnWNRPTTGASSTAPFGGVGLSGNHRPSAYYA-ADYC 424
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
33-504 |
5.99e-75 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 244.41 E-value: 5.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 113 TLAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWADKIQGKTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 192 APALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEVGKLVKEAASR 271
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 272 SNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVySEFVRRSVEYAKKRPVGDPFDVKT 351
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 352 EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGL----FIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 427
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 428 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCynALYAQAP---FGGFKMS--GNGRELGEYALAEYTEVKT 502
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGKT 472
|
..
gi 52788258 503 VT 504
Cdd:TIGR01722 473 VT 474
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
169-492 |
2.03e-72 |
|
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: 237.02 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGfGPTVGAAISSHP 248
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELLDQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 249 qINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYS 328
Cdd:cd07136 177 -FDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 329 EFVRRSVEYAKKRPVGDPFDVKtEQGPQIDQKQFDKILELIESGKkegakLECGGSAmEDKGLFIKPTVFSEVTDNMRIA 408
Cdd:cd07136 255 KFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNGK-----IVFGGNT-DRETLYIEPTILDNVTWDDPVM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 409 KEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcyNALYAQA----PFGGFKMSG 484
Cdd:cd07136 328 QEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTIMHLAnpylPFGGVGNSG 405
|
....*...
gi 52788258 485 NGRELGEY 492
Cdd:cd07136 406 MGSYHGKY 413
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
70-503 |
2.50e-72 |
|
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: 236.35 E-value: 2.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 70 DVDKAVEAAQVAFQRGS----PWRRLDalsrgrlLHQLADLVERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFA 145
Cdd:cd07135 6 EIDSIHSRLRATFRSGKtkdlEYRLWQ-------LKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 146 G----WAdkiqgKTIPTDDNVVCF------TRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALY 215
Cdd:cd07135 79 KnlkkWA-----KDEKVKDGPLAFmfgkprIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 216 LGSLIKEAgFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADL 295
Cdd:cd07135 154 LAELVPKY-LDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 296 DLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDvKTEQGPQIDQKQFDKILELIESGKke 375
Cdd:cd07135 230 ELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTK-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 376 gAKLECGGSaMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKnlDKALK-- 453
Cdd:cd07135 307 -GKVVIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTD--DKSEIdh 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 52788258 454 -LASALESGTVWINCY-NALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07135 383 iLTRTRSGGVVINDTLiHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
56-505 |
1.54e-70 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 243.18 E-value: 1.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 56 TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAffIDlE 135
Cdd:PRK11904 572 RRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA--IA-E 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 136 gcIRT----LRYFAGWADKIQGKTI----PT-DDNVVcftRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPA 206
Cdd:PRK11904 646 --VREavdfCRYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 207 EQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEA-ASRSNlKRVTL--ELGG 283
Cdd:PRK11904 721 EQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTlAARDG-PIVPLiaETGG 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVYS---EFVRRSVEYAKkrpVGDPFDVKTEQGPQIDQ 359
Cdd:PRK11904 800 QNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RVlFVQEDIADrviEMLKGAMAELK---VGDPRLLSTDVGPVIDA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 360 KQFDKILELIESGKKEG---AKLECGGSAmeDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPILKFKS--IEEVIKRANS 434
Cdd:PRK11904 876 EAKANLDAHIERMKREArllAQLPLPAGT--ENGHFVAPTAF-EI-DSISQLEREVFGPILHVIRYKAsdLDKVIDAINA 951
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52788258 435 TDYGLTAAVFTKNLDKALKLASALESGTVWINcYNALYA----QaPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:PRK11904 952 TGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ-PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1025
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
53-490 |
3.34e-70 |
|
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: 232.49 E-value: 3.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 53 NPST-REQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFlHAFF 131
Cdd:TIGR01238 57 NPADrRDIVGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 132 IDLEGCIRTLRYFAGWADKiqgkTIPTDDnvvcftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPL 211
Cdd:TIGR01238 133 AEVREAVDFCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 212 TALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTL--ELGGKNPCIV 289
Cdd:TIGR01238 202 IAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 290 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 369
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 370 ESGKKEG---AKLECGGSAMEDKGLFIKPTVFSevTDNMRIAKEEIFGPVQPILKFKS--IEEVIKRANSTDYGLTAAVF 444
Cdd:TIGR01238 362 EHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVH 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 52788258 445 TKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGFKMSGNGRELG 490
Cdd:TIGR01238 440 SRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
167-503 |
2.41e-68 |
|
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: 225.83 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 167 RHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGfGPTVGAAISS 246
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 247 HPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQV 326
Cdd:cd07133 176 LP-FDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 327 YSEFVRRSVEYAKKR-PvgdpfDVKTeqGPQ----IDQKQFDKILELIESGKKEGAKL-ECGGSAMEDKGL-FIKPTVFS 399
Cdd:cd07133 254 LEEFVAAAKAAVAKMyP-----TLAD--NPDytsiINERHYARLQGLLEDARAKGARViELNPAGEDFAATrKLPPTLVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 400 EVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcyNALY--AQ--A 475
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--DTLLhvAQddL 404
|
330 340
....*....|....*....|....*...
gi 52788258 476 PFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07133 405 PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
42-486 |
2.87e-68 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 237.91 E-value: 2.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 42 ESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETM 120
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 121 DTGKPFLHAffIDlEgcIRT----LRYFAGwadkiQGKTIPTDDnvvcfTRHEPIGVCGAITPWNFPLLMLVWKLAPALC 196
Cdd:COG4230 642 EAGKTLPDA--IA-E--VREavdfCRYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 197 CGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVkeaaSRSNLKR 276
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----NRTLAAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 277 ----VTL--ELGGKNPCIV---------CADadldlAVECAhqgvFFNQGQCCTAAsRV-FVEEQVYSEFVRRSVEYAKK 340
Cdd:COG4230 783 dgpiVPLiaETGGQNAMIVdssalpeqvVDD-----VLASA----FDSAGQRCSAL-RVlCVQEDIADRVLEMLKGAMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 341 RPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKL-ECGGSAMEDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPI 419
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-EI-DSISDLEREVFGPVLHV 930
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52788258 420 LKFKS--IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYNALYA----QaPFGGFKMSGNG 486
Cdd:COG4230 931 VRYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-484 |
1.03e-67 |
|
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: 226.70 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 11 GQPDRKppALPRPIRNLEVKFTKI--FINNEwhESKSGKKFATCNPSTREQ-ICEVEEGDKPDVDKAVEAAQVAfqRGSp 87
Cdd:cd07123 12 GSPERA--KLQEALAELKSLTVEIplVIGGK--EVRTGNTGKQVMPHDHAHvLATYHYADAALVEKAIEAALEA--RKE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 88 WRRLDALSRGRLLHQLADLVE-RDRATLAALETMDTGKPFLHAFfIDlEGC--IRTLRYFAGWADKI-QGKTIPTDDNVV 163
Cdd:cd07123 85 WARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQAE-ID-AACelIDFLRFNVKYAEELyAQQPLSSPAGVW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 164 CFTRHEPI-GVCGAITPWNFPLLMLVWKLAPALCcGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGA 242
Cdd:cd07123 163 NRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 243 AISSHPQINKIAFTGSTEVGK-LVKEAASR----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAA 317
Cdd:cd07123 242 TVLASPHLAGLHFTGSTPTFKsLWKQIGENldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 318 SRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKE-GAKLECGGSAMEDKGLFIKPT 396
Cdd:cd07123 322 SRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 397 VFsEVTD-NMRIAKEEIFGPVQPIL-----KFKSIEEVIKraNSTDYGLTAAVFTKNlDKALKLAS-ALE--SGTVWIN- 466
Cdd:cd07123 402 VI-ETTDpKHKLMTEEIFGPVLTVYvypdsDFEETLELVD--TTSPYALTGAIFAQD-RKAIREATdALRnaAGNFYINd 477
|
490
....*....|....*....
gi 52788258 467 -CYNALYAQAPFGGFKMSG 484
Cdd:cd07123 478 kPTGAVVGQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
35-486 |
1.81e-67 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 235.53 E-value: 1.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWH-------ESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADL 106
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 107 VERDRATLAALETMDTGKPFLHAffIDlEgcIRT----LRYFAGwadkiQGKTIPTDDnvvcftRHEPIGVCGAITPWNF 182
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANA--IA-E--VREavdfLRYYAA-----QARRLLNGP------GHKPLGPVVCISPWNF 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 183 PLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVG 262
Cdd:PRK11905 689 PLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVA 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 263 KLV-KEAASRSNlKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVYSEFVRRSVEYA 338
Cdd:PRK11905 769 RLIqRTLAKRSG-PPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVlCLQEDVADRVLTMLKGAM 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 339 KKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKL-ECGGSAMEDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQ 417
Cdd:PRK11905 847 DELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLI-EI-DSISDLEREVFGPVL 924
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 418 PILKFKS--IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYNALYA----QaPFGGFKMSGNG 486
Cdd:PRK11905 925 HVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
35-497 |
3.40e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 224.45 E-value: 3.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESkSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKPFLHAffidlegciRTlrYFAGWADKIQ-----------GKTIPTDDNVVCFtRHEPIGVCGAITPWNFP 183
Cdd:PRK09457 80 AEVIARETGKPLWEA---------AT--EVTAMINKIAisiqayhertgEKRSEMADGAAVL-RHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 184 LLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGK 263
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 264 LV-KEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSE-FVRRSVEYAKKR 341
Cdd:PRK09457 227 LLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 342 PVGDPFDvkTEQ---GPQIDQKQFDKILE----LIESGKK---EGAKLECGGSamedkglFIKPTVFsEVTDNMRIAKEE 411
Cdd:PRK09457 306 TVGRWDA--EPQpfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 412 IFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTV-WINCYNALYAQAPFGGFKMSGNGRELG 490
Cdd:PRK09457 376 YFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSA 455
|
....*..
gi 52788258 491 EYAlAEY 497
Cdd:PRK09457 456 YYA-ADY 461
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
35-512 |
6.73e-67 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 223.94 E-value: 6.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWheSKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfqrGSPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA---AKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 115 AALETMDTGKpFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 194 ALCCGNTMVLKPAEQTPLTALYLGSLIKEA----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAA 269
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 270 SrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDV 349
Cdd:PLN02315 257 N-ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 350 KTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFsEVTDNMRIAKEEIFGPVQPILKFKSIEEVI 429
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 430 KRANSTDYGLTAAVFTKNLDKALKLASALES--GTVWINC-YNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTIN 494
|
....*.
gi 52788258 507 LGDKNP 512
Cdd:PLN02315 495 YGNELP 500
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
18-509 |
5.39e-64 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 218.85 E-value: 5.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 18 PALPRPIRNLevkftkifINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRG 97
Cdd:PLN02419 108 PQMPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 98 RLLHQLADLVERDRATLAALETMDTGKPfLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVV-CFTRHEPIGVCGA 176
Cdd:PLN02419 177 RVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVdTYSIREPLGVCAG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 177 ITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFT 256
Cdd:PLN02419 256 ICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 257 GSTEVG-KLVKEAASRSnlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR-VFVEEQVYSEfvRRS 334
Cdd:PLN02419 335 GSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAKSWE--DKL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 335 VEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAM----EDKGLFIKPTVFSEVTDNMRIAKE 410
Cdd:PLN02419 411 VERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 411 EIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcynaLYAQAPFGGFKMSGNGREL- 489
Cdd:PLN02419 491 EIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN----VPIPVPLPFFSFTGNKASFa 566
|
490 500
....*....|....*....|....*.
gi 52788258 490 ------GEYALAEYTEVKTVTIKLGD 509
Cdd:PLN02419 567 gdlnfyGKAGVDFFTQIKLVTQKQKD 592
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
87-506 |
8.26e-61 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 207.57 E-value: 8.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 87 PWRR--LDALSRGrllhqladLVERDRATLAALETmDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVV- 163
Cdd:PTZ00381 29 EFRKqqLRNLLRM--------LEENKQEFSEAVHK-DLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVFg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 164 ---CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAgFPPGVVNIVPGfGPTV 240
Cdd:PTZ00381 100 pgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 241 GAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRV 320
Cdd:PTZ00381 178 TTELLKEP-FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 321 FVEEQVYSEFVrRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESgkkEGAKLECGGSAMEDKgLFIKPTVFSE 400
Cdd:PTZ00381 256 LVHRSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDIEN-KYVAPTIIVN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 401 VTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFG 478
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFG 410
|
410 420
....*....|....*....|....*...
gi 52788258 479 GFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
73-506 |
6.96e-57 |
|
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: 195.90 E-value: 6.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 73 KAVEAAQVAFQRGspwRRLDALSRGRLLHQLADLV-ERDRATLAALEtMDTGKPFLHAFFIDLEGCIRTLRY----FAGW 147
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 148 A-DKIQGKTIPT--DDnvvCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLI---- 220
Cdd:cd07132 78 MkPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 221 -KEAgFPpgVVNivpgfgptvgAAISSHPQI-----NKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADAD 294
Cdd:cd07132 155 dKEC-YP--VVL----------GGVEETTELlkqrfDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 295 LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVrrsvEYAK---KRPVGDpfDVKTEQ--GPQIDQKQFDKILELI 369
Cdd:cd07132 221 IDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV----EALKktlKEFYGE--DPKESPdyGRIINDRHFQRLKKLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 370 ESGKkegakLECGGSaMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLD 449
Cdd:cd07132 295 SGGK-----VAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52788258 450 KALKLASALESGTVwinCYN-----ALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07132 369 VINKILSNTSSGGV---CVNdtimhYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
69-503 |
1.21e-52 |
|
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: 184.15 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 69 PDVDKAVEAAQVAFQRGSPWRrldaLSRGRLLHQLADlvERDRATLAALETmDTGKPFLHAFFIDL----EGCIRTLRYF 144
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWR----KSQLKGLLRLVD--ENEDDIFAALRQ-DLGKPSAESFRDEVsvlvSSCKLAIKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 145 AGWAD----KIQGKTIPTDDNVVCftrhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLI 220
Cdd:cd07137 76 KKWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 221 KEAgFPPGVVNIVPGfGPTVGAAISSHpQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVE 300
Cdd:cd07137 152 PEY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 301 CAHQGVF-FNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQgpQIDQKQFDKILELIESGKKEGAKL 379
Cdd:cd07137 228 RIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS--RIVNSHHFQRLSRLLDDPSVADKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 380 ECGGSAMEDKgLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALE 459
Cdd:cd07137 306 VHGGERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 52788258 460 SGTVWINCYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07137 385 SGGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
52-486 |
2.03e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 182.87 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 52 CNPS-TREQICEVEEGDKPDVDKAVEAAQVAfqrGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAF 130
Cdd:PRK11809 664 INPAdPRDIVGYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 131 fidleGCIRT----LRYFAGWADkiqgktiPTDDNvvcfTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPA 206
Cdd:PRK11809 741 -----AEVREavdfLRYYAGQVR-------DDFDN----DTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 207 EQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASR-SNLKRVT---LEL 281
Cdd:PRK11809 805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAGRlDPQGRPIpliAET 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYS---EFVRRSV-EYAkkrpVGDPFDVKTEQGPQI 357
Cdd:PRK11809 885 GGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADrtlKMLRGAMaECR----MGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 358 DQKQFDKILELIESGKKEGAK---LECGGSAMEDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPILKFKS--IEEVIKRA 432
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLI-EL-DSFDELKREVFGPVLHVVRYNRnqLDELIEQI 1038
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 52788258 433 NSTDYGLTAAVFTKNLDKALKLASALESGTVWI--NCYNALYAQAPFGGFKMSGNG 486
Cdd:PRK11809 1039 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
169-504 |
2.79e-39 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 149.11 E-value: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKeAGFPPGVVNIVPGfGPTVGAAISSHP 248
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 249 QiNKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV-CADA--DLDLAVE---------CAhqgvffnqGQCCTA 316
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSSsrDTKVAVNrivggkwgsCA--------GQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 317 ASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTeQGPQIDQKQFDKILELIESgKKEGAKLECGGSAMEDKgLFIKPT 396
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDEKK-LFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 397 VFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYA--Q 474
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdS 411
|
330 340 350
....*....|....*....|....*....|
gi 52788258 475 APFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
71-466 |
2.17e-37 |
|
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: 142.76 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 71 VDKAVEAAQVAfqrGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDleGCIRTLRYFA--GWA 148
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENIC--GDQVQLRARAfvIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 149 DKIQGKTIPTDDNVVCFTRHE---PIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAG- 224
Cdd:cd07084 76 YRIPHEPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 225 FPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGklvkeAASRSNLK--RVTLELGGKNPCIVCADADL--DLAVE 300
Cdd:cd07084 156 LPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQAvdYVAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 301 CAhQGVFFNQGQCCTAASRVFVEEQVYSE-FVRRSVEYAKKRPVGDpfdvkTEQGPQIdqkQFDKILELIESGKKEGAKL 379
Cdd:cd07084 230 CV-QDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQ---TFTTLAMIAHMENLLGSVL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 380 ECGGSAM------EDKGLFIKPTVFSEVTDNMRIAK---EEIFGPVQPILKFKSIEE--VIKRANSTDYGLTAAVFTKNL 448
Cdd:cd07084 301 LFSGKELknhsipSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDP 380
|
410
....*....|....*....
gi 52788258 449 DKALKLASALES-GTVWIN 466
Cdd:cd07084 381 IFLQELIGNLWVaGRTYAI 399
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
84-503 |
1.37e-34 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 135.94 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 84 RGSPWRrldaLSRgrlLHQLADLVERDRATLAALETMDTGKPFLHAFFID---LEGCIR-TLRYFAGWADKIQGKTIPTD 159
Cdd:PLN02174 29 RGYEWR----VTQ---LKKLMIICDNHEPEIVAALRDDLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 160 DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIkEAGFPPGVVNIVPGFGPT 239
Cdd:PLN02174 102 FPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 240 VGAAISShpQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVF-FNQGQCCTAAS 318
Cdd:PLN02174 181 TTALLEQ--KWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 319 RVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKtEQGPQIDQKQFDKILELIESgKKEGAKLECGGSAmEDKGLFIKPTVF 398
Cdd:PLN02174 258 YILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDE-KEVSDKIVYGGEK-DRENLKIAPTIL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 399 SEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN---CYNALYAqA 475
Cdd:PLN02174 335 LDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHT-L 413
|
410 420
....*....|....*....|....*...
gi 52788258 476 PFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PLN02174 414 PFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
35-459 |
1.42e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 121.74 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESkSGKKFATCNPSTREQICEVEeGDKPDVdkaveAAQVAFQR---GSPWRRLDALSRGRLLHQLADLVERDR 111
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDL-----AAAFAFAReqgGAALRALTYAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 112 ATLAALETMDTGKPFLHAFFiDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPI----------GVCGAITPWN 181
Cdd:PRK11903 81 DAYYDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 182 FPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAG-FPPGVVNIVPGfgptVGAAISSHPQ-INKIAFTGST 259
Cdd:PRK11903 160 FPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 260 EVGKLVKE--AASRSNLkRVTLELGGKNPCIVCADAD-----LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVR 332
Cdd:PRK11903 236 ETAAVLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 333 RSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIEsGKKEGAKLECGGSAME------DKGLFIKPTVF--SEVTDN 404
Cdd:PRK11903 315 ALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 52788258 405 MRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKnlDKALKLASALE 459
Cdd:PRK11903 394 TAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSD--DAAFLAAAALE 446
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
35-458 |
5.42e-27 |
|
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: 113.90 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 35 FINNEWHESkSGKKFATCNPSTREQICEVEeGDKPDVDKAVEAAQvafQRGSP-WRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAR---EKGGPaLRALTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 114 LAALETmDTGKPFLHAFfIDLEGCIRTLRYFAGWADK--------IQGKTIPTDDNVVCFTRH--EPI-GVCGAITPWNF 182
Cdd:cd07128 79 LYALSA-ATGATRRDSW-IDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGTFVGQHilTPRrGVAVHINAFNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 183 PLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAG-FPPGVVNIVPGfGPtvgAAISSH--PQiNKIAFTGST 259
Cdd:cd07128 157 PVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG-SV---GDLLDHlgEQ-DVVAFTGSA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 260 EVG-KLVKEAASRSNLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRR 333
Cdd:cd07128 232 ATAaKLRAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 334 SVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME------DKGLFIKPTVF-SEVTDNMR 406
Cdd:cd07128 312 LKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEvvgadaEKGAFFPPTLLlCDDPDAAT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 52788258 407 IAKE-EIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASAL 458
Cdd:cd07128 392 AVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
71-459 |
2.81e-21 |
|
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: 96.46 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 71 VDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPflhaffidlEGCI-----RT---LR 142
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP---------EARLqgelgRTtgqLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 143 YFA------GWADKI------QGKTIPTDDNVVCFTRHEPIGVCGAItpwNFPLLMLVW--KLAPALCCGNTMVLKPAEQ 208
Cdd:cd07129 69 LFAdlvregSWLDARidpadpDRQPLPRPDLRRMLVPLGPVAVFGAS---NFPLAFSVAggDTASALAAGCPVVVKAHPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 209 TPLTALYLGSLI----KEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGK-LVKEAASRSNLKRVTLELGG 283
Cdd:cd07129 146 HPGTSELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 284 KNPCIVCADADLDLAVECAhQG----VFFNQGQCCTAASRVFV-EEQVYSEFVRRSVEYAKKRPVGdpfdvkTEQGPQId 358
Cdd:cd07129 226 VNPVFILPGALAERGEAIA-QGfvgsLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAAAPAQ------TMLTPGI- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 359 QKQFDKILELIESGKkeGAKLECGGSAMEDKGLFiKPTVFSEVTDNMR---IAKEEIFGPVQPILKFKSIEEVIKRANST 435
Cdd:cd07129 298 AEAYRQGVEALAAAP--GVRVLAGGAAAEGGNQA-APTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAEAL 374
|
410 420
....*....|....*....|....*.
gi 52788258 436 DYGLTAAVF--TKNLDKALKLASALE 459
Cdd:cd07129 375 EGQLTATIHgeEDDLALARELLPVLE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
96-479 |
1.61e-16 |
|
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: 81.50 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 96 RGRLLHQLADLVERDRATLAALETMDTGKPF--LHAFFIDLEGC--------IRTLRYFAGWADKIQGKTIPtdDNVVCF 165
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCsesklyknIDTERGITASVGHIQDVLLP--DNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 166 TRHEPIGVCGAITPWNFPLLMlVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEA---GFPPGVVNIVPGFGPTVGA 242
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 243 AISSHPQINKIAFTGSTEVgklVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCctaasrvFV 322
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC-------AS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 323 EEQVYSefvrrsveyakkrpVGDPFDVKTEQgpqidqkqfdkileLIESGKKEGAKLECGgsamedkglfIKPtVFSEVT 402
Cdd:cd07077 245 EQNLYV--------------VDDVLDPLYEE--------------FKLKLVVEGLKVPQE----------TKP-LSKETT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 403 DNMRIAKEEIFGPVQPILKFKSIEEVIKRA----NSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFG 478
Cdd:cd07077 286 PSFDDEALESMTPLECQFRVLDVISAVENAwmiiESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAG 365
|
.
gi 52788258 479 G 479
Cdd:cd07077 366 K 366
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
170-443 |
8.67e-15 |
|
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: 76.77 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAIS-SHP 248
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 249 QInkIAFTGSTEVGklvkEAASRSNLKRVTLELGGKNPCIVCAD-ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQ-V 326
Cdd:cd07126 222 RM--TLFTGSSKVA----ERLALELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 327 YSEFVRRSVEYAKKRPVGDpfdvkTEQGP------QIDQKQFDKILELiesgkkEGAKLECGGS------------AMED 388
Cdd:cd07126 296 QAGILDKLKALAEQRKLED-----LTIGPvltwttERILDHVDKLLAI------PGAKVLFGGKpltnhsipsiygAYEP 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 389 KGLFIkPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE--VIKRANSTDYGLTAAV 443
Cdd:cd07126 365 TAVFV-PLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAV 420
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
70-459 |
4.16e-14 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 74.55 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 70 DVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDLegcIRTLRYFAGWAD 149
Cdd:PRK15398 37 SVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKN---VAAAEKTPGVED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 150 KIqgKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSL----IKEAGF 225
Cdd:PRK15398 111 LT--TEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELlneaIVAAGG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 226 PPGVVNIVPGfgPTVGAA--ISSHPQINKIAFTGstevGKLVKEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAH 303
Cdd:PRK15398 189 PENLVVTVAE--PTIETAqrLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETADIEKAARDIV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 304 QGVFFNQGQCCTAASRVFVEEQVYSEFVRRsveyakkrpvgdpfdVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG 383
Cdd:PRK15398 262 KGASFDNNLPCIAEKEVIVVDSVADELMRL---------------MEKNGAVLLTAEQAEKLQKVVLKNGGTVNKKWVGK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 384 SA---MEDKGLFIKPTV---FSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGL--TAAVFTKNLDKALKLA 455
Cdd:PRK15398 327 DAakiLEAAGINVPKDTrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMA 406
|
....
gi 52788258 456 SALE 459
Cdd:PRK15398 407 RAIQ 410
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
170-459 |
2.79e-13 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 71.50 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSL----IKEAGFPPGVVNIVPGfgPTVGAA-- 243
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELinkaIAEAGGPDNLVVTVEE--PTIETTne 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 244 ISSHPQINKIAFTGSTEVGKlvkeaASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:cd07121 175 LMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 324 EQVYSEFVRRsveyakkrpvgdpfdVKTEQGPQIDQKQFDKILELIESGKKEGA---KLEcGGSA---MEDKGLFIKPT- 396
Cdd:cd07121 250 DSVADYLIAA---------------MQRNGAYVLNDEQAEQLLEVVLLTNKGATpnkKWV-GKDAskiLKAAGIEVPADi 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52788258 397 --VFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGL--TAAVFTKNLDKALKLASALE 459
Cdd:cd07121 314 rlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
71-466 |
1.47e-10 |
|
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: 63.05 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 71 VDKAVEAAQVAfQRGSPWRRLDAlsRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDlegcirtlRYFAG---- 146
Cdd:cd07081 1 LDDAVAAAKVA-QQGLSCKSQEM--VDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIK--------NHFAAeyiy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 147 --WADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKP----AEQTPLTALYLGSLI 220
Cdd:cd07081 70 nvYKDEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 221 KEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGstevGKLVKEAAsRSNLKRVTLELGGKNPCIVCADADLDLAVE 300
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAA-YSSGKPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 301 CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRsveyakkrpvgdpfdVKTEQGPQIDQKQFDKILELIESGKKEGAKL- 379
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRL---------------FEGQGAYKLTAEELQQVQPVILKNGDVNRDIv 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 380 -ECGGSAMEDKGLFIKPT---VFSEVT--DNMRIAKEEIFGPVQPILKFKSIEEVIKRA----NSTDYGLTAAVFTKNL- 448
Cdd:cd07081 290 gQDAYKIAAAAGLKVPQEtriLIGEVTslAEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIk 369
|
410 420
....*....|....*....|
gi 52788258 449 --DKALKLASALESGTVWIN 466
Cdd:cd07081 370 aiENMNQFANAMKTSRFVKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
169-467 |
7.49e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.34 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKP----AEQTPLTALYLGSLIKEAGFPPGVVNIVPgfGPTVGA-- 242
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhpraKKCSIEAAKIMREAAVAAGAPEGLIQWIE--EPSIELtq 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 243 AISSHPQINKIAFTGStevGKLVKEAASRSnlkrvTLELG---GKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR 319
Cdd:cd07122 172 ELMKHPDVDLILATGG---PGMVKAAYSSG-----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 320 VFVEEQVYSEFVRRSVEY-------AKKRPVGDP-FDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGgsamEDKGl 391
Cdd:cd07122 244 VIVDDEIYDEVRAELKRRgayflneEEKEKLEKAlFDDGGTLNPDIVGKSAQKIAELAGIEVPEDTKVLVA----EETG- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 392 fikptvfseVTDNMRIAKEEIFgPVQPILKFKSIEEVIKRANS-TDY---GLTAAVFTKNLDKALKLASALESGTVWINC 467
Cdd:cd07122 319 ---------VGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMPVSRILVNT 388
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
67-322 |
1.55e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 47.47 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 67 DKPDVDKAVEAAQVAFQRgspWRRLDALSR-GRLLHQLADLVERDRAtLAALETMDTGKPFLHAF------FIDlegciR 139
Cdd:cd07127 82 PQCDPDALLAAARAAMPG---WRDAGARARaGVCLEILQRLNARSFE-MAHAVMHTTGQAFMMAFqaggphAQD-----R 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 140 TLRYFAgWADKIQGKTIPTDDNVVCFTRHEPI-----------GV-----CGAITPWN-FPLLMlvwklaPALCCGNTMV 202
Cdd:cd07127 153 GLEAVA-YAWREMSRIPPTAEWEKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNPVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52788258 203 LKPAeqtPLTALYLGSLIK-------EAGFPPGVVNIV---PGFGptVGAAISSHPQINKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07127 226 VKPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ- 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 52788258 273 nlKRVTLELGGKNPCIVcaDADLDLAVECAHQGVFFN--QGQCCTAASRVFV 322
Cdd:cd07127 300 --AQVYTEKAGVNTVVV--DSTDDLKAMLRNLAFSLSlySGQMCTTPQNIYV 347
|
|
| |
