|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
15-488 |
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: 883.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 15 EQPTGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEK 93
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 94 NIDLLAAVESLDNGKAISM-AKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAW 172
Cdd:cd07091 81 DRDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 173 KIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAA 252
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 253 ASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAA 332
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 333 DTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAI 412
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108935817 413 KLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-490 |
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: 839.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 12 GKYEQPTGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGSW-RQETPENRGKLLNNLANL 90
Cdd:cd07143 1 GKYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWgLKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 91 FEKNIDLLAAVESLDNGKAI-SMAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLM 169
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFgTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 170 WAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTIL 249
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 250 KAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDP 329
Cdd:cd07143 241 EAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 330 FAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKE 409
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 410 DAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
.
gi 108935817 490 L 490
Cdd:cd07143 481 L 481
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
18-489 |
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: 761.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 18 TGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GS-WRQETPENRGKLLNNLANLFEKNI 95
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSpWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 96 DLLAAVESLDNGKAISMAK-GDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKI 174
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 175 GPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAS 254
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 255 SNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADT 334
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 335 FQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKL 414
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108935817 415 GNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-490 |
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: 724.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 13 KYEQPTGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFE 92
Cdd:cd07144 3 SYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 93 KNIDLLAAVESLDNGKAISM-AKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWA 171
Cdd:cd07144 83 KNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 172 WKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKA 251
Cdd:cd07144 163 WKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 252 AAsSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKN-VVGDPF 330
Cdd:cd07144 243 AA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGG---KRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKT 407
Cdd:cd07144 322 DDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 408 KEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVS 487
Cdd:cd07144 402 YEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVH 481
|
...
gi 108935817 488 IRL 490
Cdd:cd07144 482 INL 484
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
16-486 |
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: 684.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 16 QPTGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAF-EGSWRQETPENRGKLLNNLANLFEKN 94
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFdEGPWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 95 IDLLAAVESLDNGKAISMAK-GDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWK 173
Cdd:cd07142 82 ADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 174 IGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAA 253
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 254 SSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAAD 333
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 334 TFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 414 LGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
15-490 |
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: 682.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 15 EQPTGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKN 94
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA-WAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 95 IDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDT-TPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWK 173
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 174 IGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAA 253
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 254 sSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAAD 333
Cdd:COG1012 242 -ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 334 TFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKR-KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAI 412
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 413 KLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLH-HQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-486 |
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: 669.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 26 FVKGqEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLD 105
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA-WRKTPAAERAAILRKAADLLEERKDELAELETLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 106 NGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVV 185
Cdd:pfam00171 79 NGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 186 LKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELG 265
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 266 GKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQF 345
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 346 DRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAA 425
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108935817 426 VHTKNLNTAIEVSNALKAGTVWVNTYNTLHH-QMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
18-486 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 647.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 18 TGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAF-EGSWRQETPENRGKLLNNLANLFEKNID 96
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 97 LLAAVESLDNGKAISM-AKGDISMCVGCLRYYGGWADKITGKVIDTtpDTFNYVK--KEPIGVCGQIIPWNFPLLMWAWK 173
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPA--DGPHHVQtlHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 174 IGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAA 253
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 254 SSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAAD 333
Cdd:PLN02466 296 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 334 TFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 414 LGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
18-486 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 612.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 18 TGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNID 96
Cdd:PLN02766 21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 97 LLAAVESLDNGKAISMAKG-DISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIG 175
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 176 PAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASS 255
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 256 NLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTF 335
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 336 QGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLG 415
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108935817 416 NASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:PLN02766 421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
58-488 |
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: 611.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 58 DIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGK 137
Cdd:cd07078 1 DAAVAAARAAFKA-WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 138 VI-DTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVI 216
Cdd:cd07078 80 VIpSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 217 SGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQC 296
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 297 CCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKR-KGDKGYF 375
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 376 IEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNT-L 454
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgA 398
|
410 420 430
....*....|....*....|....*....|....
gi 108935817 455 HHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07078 399 EPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
37-488 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 611.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKG 115
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEgGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 116 DISMCVGCLRYYGGWADKITGKVIDT-TPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPL 194
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVdKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 195 GGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFE 274
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 275 DADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQA 354
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 355 GKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKN 430
Cdd:cd07114 320 AREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 108935817 431 LNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-490 |
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: 610.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNIDLLA 99
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKK 259
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA-GNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQ 339
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 340 VSKVQFDRIMEYIQAGKDAGATVETGGKRKGD----KGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLG 415
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108935817 416 NASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
32-488 |
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: 603.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 32 GKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAI 110
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 111 SMA-KGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:cd07112 81 SDAlAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNLKKVTLELGGKSP 269
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDA-DIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRI 348
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 349 MEYIQAGKDAGATVETGGKR--KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAV 426
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108935817 427 HTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
37-490 |
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: 594.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKG- 115
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA-WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 116 DISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLG 195
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 196 GLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFED 275
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG-NLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAI 435
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 108935817 436 EVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
37-488 |
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: 578.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK-G 115
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG-WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 116 DISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLG 195
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 196 GLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFED 275
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKRKG----DKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNL 431
Cdd:cd07093 319 RAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 432 NTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
19-488 |
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: 558.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK-TWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKG-DISMCVGCLRYYGG--WADKITGKVIDTtpDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIG 175
Cdd:cd07559 81 AVAETLDNGKPIRETLAaDIPLAIDHFRYFAGviRAQEGSLSEIDE--DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 176 PAIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASs 255
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 256 NLKKVTLELGGKSPNIVFEDA-----DIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPF 330
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRK----GDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFK 406
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 407 TKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 108935817 487 SI 488
Cdd:cd07559 477 LV 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
17-488 |
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: 537.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 17 PTGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNI 95
Cdd:cd07140 5 PHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEnGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 96 DLLAAVESLDNGKAISMA-KGDISMCVGCLRYYGGWADKITGKVIDTTPDTFN----YVKKEPIGVCGQIIPWNFPLLMW 170
Cdd:cd07140 85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNrnltLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 171 AWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILK 250
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 251 AAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPF 330
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTK-- 408
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdv 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 409 EDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
37-486 |
0e+00 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 529.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR-WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKI---TGKVIDTTPDTFN-YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQT 192
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLdakAERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 193 PLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIV 272
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 273 FEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYI 352
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 353 QAGKDAGATVETGGKR--KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKN 430
Cdd:cd07110 319 ARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 108935817 431 LNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
38-488 |
0e+00 |
|
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: 526.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDkGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLG 195
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLgDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 196 GLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFED 275
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKR-KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTA 434
Cdd:cd07118 321 RAEGATLLLGGERlASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 108935817 435 IEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
20-492 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 521.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLF-EKNiDLL 98
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK-IWAAMTAMERSRILRRAVDILrERN-DEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAK-GDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPA 177
Cdd:PRK13252 87 AALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 178 IACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVaGAALSSHMDVDKVAFTGSTVVGRTILKAAASSnL 257
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS-L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 258 KKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQG 337
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 338 PQVSKVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 414 LGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRLGD 492
Cdd:PRK13252 405 RANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
37-488 |
0e+00 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 518.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGG 196
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 197 LVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFEDA 276
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 277 DIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGdPFAADTFQGPQVSKVQFDRIMEYIQAGK 356
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 357 DAGATVETGGKR---KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNT 433
Cdd:cd07109 319 ARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 108935817 434 AIEVSNALKAGTVWVNTYNTLHH-QMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-490 |
0e+00 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 517.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK-TWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKG-DISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPA 177
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 178 IACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNL 257
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 258 KKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQG 337
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 338 PQVSKVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 414 LGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
37-491 |
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: 516.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK-EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGG 196
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 197 LVAASLVKEAGFPPGVINVISGFGKVaGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDA 276
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 277 DIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGK 356
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 357 DAGATVETGGKR-----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNL 431
Cdd:cd07090 318 QEGAKVLCGGERvvpedGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 432 NTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRLG 491
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
37-488 |
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: 513.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK-TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKITGKVIDT-TPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLG 195
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 196 GLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFED 275
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAD-TVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAI 435
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 108935817 436 EVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
20-486 |
1.78e-179 |
|
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: 511.28 E-value: 1.78e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLA 99
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP-AWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AVESLDNGKAISMAKGD-ISMCVGCLRYYggwadkitgkvIDTTpDTFNY--------VKKEPIGVCGQIIPWNFPLLMW 170
Cdd:cd07138 80 QAITLEMGAPITLARAAqVGLGIGHLRAA-----------ADAL-KDFEFeerrgnslVVREPIGVCGLITPWNWPLNQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 171 AWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILK 250
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 251 AAASSnLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPF 330
Cdd:cd07138 228 AAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKG---DKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKT 407
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPeglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 408 KEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
21-484 |
9.63e-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: 507.04 E-value: 9.63e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFeGSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ-GEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAIS-MAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:TIGR01804 80 LETLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKK 259
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQ 339
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 340 VSKVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLG 415
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRpenvGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 416 NASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTK 484
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-496 |
8.21e-177 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 506.19 E-value: 8.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE----GSWRQETPENRGKLLNNLANLFEKN 94
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 95 IDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKV---IDTTPDTFN-YVKKEPIGVCGQIIPWNFPLLMW 170
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkapVSLPMETFKgYVLKEPLGVVGLITPWNYPLLMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 171 AWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILk 250
Cdd:PLN02467 169 TWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 251 AAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPF 330
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGD--KGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTK 408
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 409 EDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVTK 487
|
....*...
gi 108935817 489 RLGDALFG 496
Cdd:PLN02467 488 YISDEPWG 495
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
17-491 |
2.42e-176 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 504.06 E-value: 2.42e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 17 PTGLFINNEFVKGqEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNID 96
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE-WSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 97 LLAAVESLDNGKAISMAKGD-ISMCVGCLRYYGGWADKITGKVI-DTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKI 174
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGKAAgEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 175 GPAIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAS 254
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 255 SnLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADT 334
Cdd:PRK13473 239 S-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 335 FQGPQVSKVQFDRIMEYIQAGKDAG-ATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108935817 414 LGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRLG 491
Cdd:PRK13473 398 WANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
37-486 |
2.25e-174 |
|
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: 498.00 E-value: 2.25e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP-SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 -ISMCVGCLRYYGGWADKITGKVI-DTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPL 194
Cdd:cd07092 80 eLPGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 195 GGLVAASLVKEaGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFE 274
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 275 DADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIqA 354
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV-E 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 355 GKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTA 434
Cdd:cd07092 317 RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 108935817 435 IEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
19-480 |
6.05e-171 |
|
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: 490.37 E-value: 6.05e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE-SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAK-GDISMCVGCLRYYGGWADKItgkvidttpDTfNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPA 177
Cdd:cd07111 102 AVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLL---------DT-ELAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 178 IACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVaGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNl 257
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 258 KKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQG 337
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 338 PQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNA 417
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 418 STYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANY 480
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
62-488 |
6.42e-171 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 485.97 E-value: 6.42e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 62 AAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITG-KVID 140
Cdd:cd06534 1 AAARAAFKA-WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGpELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 141 TTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFG 220
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 221 KVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAG 300
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 301 SRVYVQESIYDKFVQKFKeraqknvvgdpfaadtfqgpqvskvqfdrimeyiqagkdagatvetggkrkgdkgyfiepTI 380
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 381 FSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHH-QMP 459
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpEAP 338
|
410 420
....*....|....*....|....*....
gi 108935817 460 FGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
37-488 |
2.99e-170 |
|
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: 487.42 E-value: 2.99e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG-WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYggwAD-KITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLG 195
Cdd:cd07106 80 VGGAVAWLRYT---ASlDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 196 GLVAASLVKEAgFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFED 275
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAI 435
Cdd:cd07106 314 KAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 108935817 436 EVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07106 394 AVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
20-486 |
1.04e-169 |
|
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: 486.70 E-value: 1.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAF-EGSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAIS-MAKGDISMCVGCLRYYGGWADKITgkVIDTTPDTFN---YVKKEPIGVCGQIIPWNFPLLMWAWKI 174
Cdd:cd07139 81 ARLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFP--FEERRPGSGGghvLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 175 GPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAS 254
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 255 sNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADT 334
Cdd:cd07139 238 -RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 335 FQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKR-KG-DKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAI 412
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108935817 413 KLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYnTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07139 397 RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
37-486 |
4.40e-168 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 482.13 E-value: 4.40e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAF-EGSWRQeTPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKG 115
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFdTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 116 -DISMCVGCLRYYGGWADKITGKVIDTTPDTFNY-----VKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSP 269
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIM 349
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 350 EYIQAGKDAGATVETGGKR--KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVH 427
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 428 TKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
21-486 |
1.48e-166 |
|
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: 478.68 E-value: 1.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA-WERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFN-YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILkAAASSNLKK 259
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIM-EAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQ 339
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 340 VSKVQFDRIMEYIQAGKDAGATVETGGKR-KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNAS 418
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRpEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108935817 419 TYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07088 399 EYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
37-488 |
4.27e-165 |
|
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: 474.54 E-value: 4.27e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAI-SMAKG 115
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPE-WAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 116 DISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLG 195
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 196 GLVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFED 275
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGI-FFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQA 354
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 355 GKDA-GATVETGGKRKGD----KGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTK 429
Cdd:cd07108 318 GLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 430 NLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELG-EDALANYTQTKTVSI 488
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
19-492 |
2.31e-160 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 463.89 E-value: 2.31e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:TIGR02299 2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK-RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKGDISMCVGCLRYYggwADKITGKVIDTT---PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIG 175
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQVIRAAENFRFF---ADKCEEAMDGRTypvDTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 176 PAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASS 255
Cdd:TIGR02299 158 PALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 256 nLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTF 335
Cdd:TIGR02299 238 -LKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 336 QGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGD-------KGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTK 408
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTfrgedlgRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 409 EDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
....
gi 108935817 489 RLGD 492
Cdd:TIGR02299 477 ALGP 480
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
19-489 |
1.09e-159 |
|
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: 461.53 E-value: 1.09e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKG-DISMCVGCLRYYGGWADKITGKVIDTTPDTFN------YVKKEPIGVCGQIIPWNFPLLMWA 171
Cdd:cd07113 81 AQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQgerytaFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 172 WKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVaGAALSSHMDVDKVAFTGSTVVGRTIlKA 251
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKI-GR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 252 AASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFA 331
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 332 ADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDA 411
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108935817 412 IKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
21-488 |
7.85e-158 |
|
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: 456.71 E-value: 7.85e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKtfDVINPSDES-VITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLA 99
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA-WRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAI 178
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTrPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 179 ACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILkAAASSNLK 258
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIA-AAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 259 KVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGP 338
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 339 QVSKVQFDRIMEYIQAGKDAGATVETGGKR--KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGN 416
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108935817 417 ASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNT-LHHQMPFGGYKESGIG-RELGEDALANYTQTKTVSI 488
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
37-490 |
4.02e-155 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 449.13 E-value: 4.02e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE-WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGG 196
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 197 LVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSnLKKVTLELGGKSPNIVFEDA 276
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 277 DIDNAISWVNFGIFFN-HGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07107 238 DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNL 431
Cdd:cd07107 318 KREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 432 NTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
18-490 |
3.72e-154 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 448.19 E-value: 3.72e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 18 TGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFE-GSWRQETPENRGKLLNNLANLFEKNID 96
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErGDWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 97 LLAAVESLDNGKAISMA-KGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIG 175
Cdd:PRK09847 100 ELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 176 PAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASS 255
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 256 NLKKVTLELGGKSPNIVFEDA-DIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADT 334
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 335 FQGPQVSKVQFDRIMEYIQAGKDAGaTVETGGKRKGDKGYfIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKL 414
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108935817 415 GNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:PRK09847 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
21-490 |
9.05e-152 |
|
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: 441.47 E-value: 9.05e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVkgQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:TIGR03216 4 FINGAFV--ESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGPWGKMTVAERADLLYAVADEIERRFDDFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKG-DISMCVGCLRYYggwADKITGKVID----TTPD---TFNYVKKEPIGVCGQIIPWNFPLLMWAW 172
Cdd:TIGR03216 82 AEVADTGKPRSLASHlDIPRGAANFRVF---ADVVKNAPTEcfemATPDgkgALNYAVRKPLGVVGVISPWNLPLLLMTW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 173 KIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGK-VAGAALSSHMDVDKVAFTGSTVVGRTILKA 251
Cdd:TIGR03216 159 KVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 252 AASSnLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFA 331
Cdd:TIGR03216 239 AADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 332 ADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGG-----KRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFK 406
Cdd:TIGR03216 318 PATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 407 TKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:TIGR03216 398 SEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNV 477
|
....
gi 108935817 487 SIRL 490
Cdd:TIGR03216 478 CIKL 481
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
21-484 |
7.13e-150 |
|
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: 436.88 E-value: 7.13e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE-AWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKG-DISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAaSSNLKK 259
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA-SENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFE------DADIDNAISwvNFGIF-FNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAA 332
Cdd:cd07116 241 VTLELGGKSPNIFFAdvmdadDAFFDKALE--GFVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 333 DTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKG-----DKGYFIEPTIFSNvtEDMKIVKEEIFGPVCSIAKFKT 407
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNElggllGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 408 KEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTK 484
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
56-488 |
2.17e-149 |
|
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: 433.50 E-value: 2.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 56 DVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLA---AVESldnGKAISMAKGDISMCVGCLRYYGGWAD 132
Cdd:cd07104 1 DVDRAYAAAAAAQK-AWAATPPQERAAILRKAAEILEERRDEIAdwlIRES---GSTRPKAAFEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 133 KITGKVIDT-TPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPL-GGLVAASLVKEAGFPP 210
Cdd:cd07104 77 RPEGEILPSdVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVtGGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 211 GVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTIlKAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIF 290
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHI-GELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 291 FNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKG 370
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 371 DkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNT 450
Cdd:cd07104 316 L---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 108935817 451 yNTLHH--QMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07104 393 -QTVNDepHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-488 |
1.17e-148 |
|
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: 433.70 E-value: 1.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSD-ESVITQVHEATEKDVDIAVAAARKAFeGSWRQETPENRGKLLNNLANLFEKNIDLLA 99
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAF-PEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAI 178
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 179 ACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNlK 258
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN-K 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 259 KVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGP 338
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 339 QVSKVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKL 414
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 415 GNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVN--TYNTLHHqMPFGGYKESGIG-RELGEDALANYTQTKTVSI 488
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGAEVH-LPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-486 |
4.31e-148 |
|
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: 431.38 E-value: 4.31e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAFEGS-WRQEtPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGD 116
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETdWAHD-PRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 117 ISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGG 196
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 197 LVAASLVKEA-GFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFED 275
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 276 ADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAG 355
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 356 KDAGATVETGGKRKGD---KGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLN 432
Cdd:cd07120 320 IAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 108935817 433 TAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
21-488 |
5.00e-147 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 430.27 E-value: 5.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP-SWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:PLN02278 107 LMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPfPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSnLKK 259
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT-VKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQ 339
Cdd:PLN02278 266 VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 340 VSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNAST 419
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTE 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 420 YGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:PLN02278 426 AGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
35-488 |
2.76e-145 |
|
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: 423.93 E-value: 2.76e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 35 FDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK 114
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK-EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMCVGCLRYYGGWADKITGKVI--DTTP---DTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIpfDASPggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAssnLKKVTLELGGKSP 269
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIM 349
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 350 EYIQAGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTK 429
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108935817 430 NLNTAIEVSNALKAGTVWVN---TYNTLHhqMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07149 394 DLQKALKAARELEVGGVMINdssTFRVDH--MPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
35-488 |
9.88e-145 |
|
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: 422.51 E-value: 9.88e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 35 FDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK 114
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP-AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMCVGCLRYYGGWADKITGKVIDT-TPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTP 193
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 194 LGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTIlKAAASSNLKKVTLELGGKSPNIVF 273
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREI-AEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 274 EDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQ 353
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 354 AGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNT 433
Cdd:cd07150 319 DAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 434 AIEVSNALKAGTVWVNTyNTLHH--QMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07150 396 AFKLAERLESGMVHIND-PTILDeaHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
24-488 |
7.88e-135 |
|
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: 397.83 E-value: 7.88e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 24 NEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAfEGSWRQETPENRGKLLNNLANLFEKN----IDLLA 99
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QKEWAATLPQERAEILEKAAQILEERrdeiVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AvESldnGKAISMAKGDISMCVGCLRYYGGWADKITGKVI-DTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAI 178
Cdd:cd07151 80 R-ES---GSTRIKANIEWGAAMAITREAATFPLRMEGRILpSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 179 ACGNTVVLKTAEQTPL-GGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTIlKAAASSNL 257
Cdd:cd07151 156 ALGNAVVLKPASDTPItGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHI-GELAGRHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 258 KKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQG 337
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 338 PQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNA 417
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 418 STYGLAAAVHTKNLNTAIEVSNALKAGTVWVN--TYNTLHHqMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEPH-VPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-488 |
3.02e-134 |
|
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: 396.55 E-value: 3.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVkGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFeGSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF-KEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKGD----ISMCvgclRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIG 175
Cdd:cd07086 80 LVSLEMGKILPEGLGEvqemIDIC----DYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 176 PAIACGNTVVLKTAEQTPLGGLVAASLVKEA----GFPPGVINVISGFGKVaGAALSSHMDVDKVAFTGSTVVGRTILKA 251
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 252 AASSNlKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFA 331
Cdd:cd07086 235 VARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 332 ADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKR--KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKE 409
Cdd:cd07086 314 EGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 410 DAIKLGNASTYGLAAAVHTKNLNTA--IEVSNALKAGTVWVNT-YNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07086 394 EAIAINNDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
..
gi 108935817 487 SI 488
Cdd:cd07086 474 TI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
35-488 |
6.01e-134 |
|
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: 395.18 E-value: 6.01e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 35 FDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK 114
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD-VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMCVGCLRYYGGWADKITGKVIDTTPDTFN-----YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSnLKKVTLELGGKSP 269
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIM 349
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 350 EYIQAGKDAGATVETGGKRkgDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTK 429
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 430 NLNTAIEVSNALKAGTVWVNTYNTLH-HQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRwDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-487 |
2.07e-133 |
|
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: 395.82 E-value: 2.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGqeGKTFDVINPSDES-VITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07124 35 LVIGGKEVRT--EEKIESRNPADPSeVLGTVQKATKEEAEAAVQAARAAFP-TWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAI 178
Cdd:cd07124 112 AAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 179 ACGNTVVLKTAEQTPLgglVAASLVK---EAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAS- 254
Cdd:cd07124 192 VTGNTVVLKPAEDTPV---IAAKLVEileEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 255 ----SNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPF 330
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGaTVETGGKR--KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTK 408
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 409 EDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNT--LHHQMPFGGYKESGIG-RELGEDALANYTQTKT 485
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITgaLVGRQPFGGFKMSGTGsKAGGPDYLLQFMQPKT 507
|
..
gi 108935817 486 VS 487
Cdd:cd07124 508 VT 509
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
57-488 |
8.06e-129 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 381.04 E-value: 8.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 57 VDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYYggwADKITG 136
Cdd:cd07100 1 IEAALDRAHAAFL-AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYY---AENAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 137 KVIDTTPDTFN---YVKKEPIGVCGQIIPWNFPLlmwaWKI----GPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFP 209
Cdd:cd07100 77 FLADEPIETDAgkaYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 210 PGV-INVISGFGKVAgaALSSHMDVDKVAFTGSTVVGRTIlKAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFG 288
Cdd:cd07100 153 EGVfQNLLIDSDQVE--AIIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 289 IFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKR 368
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 369 KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWV 448
Cdd:cd07100 310 PDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 108935817 449 NTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07100 390 NGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
38-486 |
8.56e-124 |
|
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: 369.24 E-value: 8.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDI 117
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA-WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 118 SMCVGCLRYYGGWADKITGK-VIDTTPDTFN---YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTP 193
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPrKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 194 LGGLVAASLVKEAGFPPGVINVISGFGKVaGAALSSHMdVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVF 273
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 274 EDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQ 353
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 354 AGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNT 433
Cdd:cd07099 317 DAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 108935817 434 AIEVSNALKAGTVWVN--TYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07099 397 AEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
18-489 |
1.31e-122 |
|
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: 366.84 E-value: 1.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 18 TGLFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDL 97
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP-AWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 98 LAAVESLDNGKAISMAKGDIS-------MCVGCLRYYGGWADKITGKVIDTtpdtfnYVKKEPIGVCGQIIPWNFPLLMW 170
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLrglevveFACSIPHLLKGEYLENVARGIDT------YSYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 171 AWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTILk 250
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIY- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 251 AAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPF 330
Cdd:cd07085 232 ERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 331 AADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFK 406
Cdd:cd07085 312 DPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGvkvpGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 407 TKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtyntlhhqMP---------FGGYKES--GIGRELGED 475
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN--------VPipvplaffsFGGWKGSffGDLHFYGKD 463
|
490
....*....|....
gi 108935817 476 ALANYTQTKTVSIR 489
Cdd:cd07085 464 GVRFYTQTKTVTSR 477
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
36-488 |
1.72e-120 |
|
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: 360.59 E-value: 1.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 36 DVINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKG 115
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN-RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 116 DISMCVGCLRYYGGWADKITGKVI--DTTPDTFN---YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAE 190
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIplDATQGSDNrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 191 QTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAssnLKKVTLELGGKSPN 270
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 271 IVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIME 350
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 351 YIQAGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKN 430
Cdd:cd07094 318 WVEEAVEAGARLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108935817 431 LNTAIEVSNALKAGTVWVN---TYNTLHhqMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNdssAFRTDW--MPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
56-488 |
6.58e-119 |
|
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: 355.73 E-value: 6.58e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 56 DVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKIT 135
Cdd:cd07105 1 DADQAVEAAAAAFP-AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 136 GKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVIN 214
Cdd:cd07105 80 GGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 215 VISGFGKVAGA---ALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFF 291
Cdd:cd07105 160 VVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 292 NHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAadtfqGPQVSKVQFDRIMEYIQAGKDAGATVETGGK-RKG 370
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGGLaDES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 371 DKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNT 450
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 108935817 451 yNTLH--HQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:cd07105 394 -MTVHdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
38-486 |
2.98e-117 |
|
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: 352.32 E-value: 2.98e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDI 117
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG-WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 118 SMCVGCLRYYGGWADKITGKVIDTTPDTFN-YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGG 196
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 197 LVAASLVKEAGFPPGVINVISGFGKVAGAALSSHmDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDA 276
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 277 DIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGK 356
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 357 DAGATVETGGKR---KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNT 433
Cdd:cd07102 318 AKGARALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 108935817 434 AIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07102 398 AEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-488 |
6.26e-117 |
|
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: 351.21 E-value: 6.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 45 VITQVHEATEKDVDIAVAAARKAfEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCL 124
Cdd:cd07152 3 VLGEVGVADAADVDRAAARAAAA-QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 125 RYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPL-GGLVAASLV 203
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVsGGVVIARLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 204 KEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTIlKAAASSNLKKVTLELGGKSPNIVFEDADIDNAIS 283
Cdd:cd07152 162 EEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKV-GEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 284 WVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVE 363
Cdd:cd07152 240 NGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 364 TGGKRkgdKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKA 443
Cdd:cd07152 320 AGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRT 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 108935817 444 GTVWVNTYNTLHH-QMPFGGYKESGIGRELGEDA-LANYTQTKTVSI 488
Cdd:cd07152 397 GMLHINDQTVNDEpHNPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
35-484 |
2.18e-115 |
|
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: 347.70 E-value: 2.18e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 35 FDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK 114
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR-PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMCVGCLRYYGGWADKITGKVI--DTTPDTFNY---VKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLplDISARGEGRqglVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAgAALSSHMDVDKVAFTGSTVVGRTiLKAAASSnlKKVTLELGGKSP 269
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWD-LKARAGK--KKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIM 349
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 350 EYIQAGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTK 429
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 108935817 430 NLNTAIEVSNALKAGTVWVNTYNTLH-HQMPFGGYKESGIGRELGEDALANYTQTK 484
Cdd:cd07147 393 DLEKALRAWDELEVGGVVINDVPTFRvDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
21-489 |
1.51e-113 |
|
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: 343.40 E-value: 1.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGqEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVI--DTTPDTFN---YVKKEPIGVCGQIIPWNFPLLMWAWKIG 175
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLpgDWFPGTKGkiaQVRREPLGVVLAIGPFNYPLNLTVSKLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 176 PAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAss 255
Cdd:cd07082 164 PALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 256 nLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTF 335
Cdd:cd07082 242 -MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 336 QGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGdkGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLG 415
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108935817 416 NASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYnTLH--HQMPFGGYKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:cd07082 399 NKSNYGLQASIFTKDINKARKLADALEVGTVNINSK-CQRgpDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
20-490 |
3.61e-113 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 343.84 E-value: 3.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGQEgkTFDVINPSDES-VITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:PRK03137 39 LIIGGERITTED--KIVSINPANKSeVVGRVSKATKELAEKAMQAALEAFE-TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKIT-GKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPA 177
Cdd:PRK03137 116 SAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLAdGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 178 IACGNTVVLKTAEQTPlggLVAASLV---KEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAS 254
Cdd:PRK03137 196 IVAGNTVLLKPASDTP---VIAAKFVevlEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 255 SN-----LKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDP 329
Cdd:PRK03137 273 VQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 330 fAADTFQGPQVSKVQFDRIMEYIQAGKDAGaTVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKE 409
Cdd:PRK03137 353 -EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 410 DAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNT-----LHhqmPFGGYKESGIGRELG-EDALANYTQT 483
Cdd:PRK03137 431 HALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTgaivgYH---PFGGFNMSGTDSKAGgPDYLLLFLQA 507
|
....*..
gi 108935817 484 KTVSIRL 490
Cdd:PRK03137 508 KTVSEMF 514
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
84-486 |
5.15e-113 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 340.18 E-value: 5.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 84 LNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIP 162
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDrPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 163 WNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGST 242
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 243 VVGRTILkAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQ 322
Cdd:PRK10090 161 SAGEKIM-AAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 323 KNVVGDPFAADTFQ-GPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCS 401
Cdd:PRK10090 240 AVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 402 IAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYT 481
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYL 399
|
....*
gi 108935817 482 QTKTV 486
Cdd:PRK10090 400 QTQVV 404
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
27-487 |
1.66e-112 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 342.63 E-value: 1.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 27 VKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAfEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDN 106
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 107 GKAISMAKGDISMCVGCLRYYGGWADKI------TGKVIDTTPDTFNYVkkePIGVCGQIIPWNFPLLMWAWKIGPAIAC 180
Cdd:PRK09407 105 GKARRHAFEEVLDVALTARYYARRAPKLlaprrrAGALPVLTKTTELRQ---PKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 181 GNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHmdVDKVAFTGSTVVGRTILKAAASsNLKKV 260
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-RLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 261 TLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQV 340
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 341 SKVQFDRIMEYIQAGKDAGATVETGGKRKGDKG-YFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNAST 419
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 420 YGLAAAVHTKNLNTAIEVSNALKAGTVWVN-----TYNTlhHQMPFGGYKESGIGRELGEDALANYTQTKTVS 487
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGS--VDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
21-490 |
1.36e-109 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 333.80 E-value: 1.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP-AWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVI-DTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:PRK11241 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIpGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLKK 259
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQ 339
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 340 VSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNAST 419
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108935817 420 YGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
38-487 |
3.07e-108 |
|
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: 329.27 E-value: 3.07e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAfEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDI 117
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAA-QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 118 SMCVGCLRYYGGWADKI--TGKVIDTTPD-TFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPL 194
Cdd:cd07101 80 LDVAIVARYYARRAERLlkPRRRRGAIPVlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 195 GGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHmdVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFE 274
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 275 DADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQA 354
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 355 GKDAGATVETGGKRKGDKG-YFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNT 433
Cdd:cd07101 317 AVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 434 AIEVSNALKAGTVWVN-----TYNTLhhQMPFGGYKESGIGRELGEDALANYTQTKTVS 487
Cdd:cd07101 397 GRRIAARLRAGTVNVNegyaaAWASI--DAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
37-488 |
2.15e-105 |
|
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: 322.00 E-value: 2.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 37 VINPSDESVITQVHEATEKDVD--IAVAAARKAfegswrQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK 114
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALReaLALAASYRS------TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMCVGCLRYYGGWADKITGKVIDTtPDTFN------YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKT 188
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSC-DLTANgkarkiFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 189 AEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTIlkaAASSNLKKVTLELGGKS 268
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 269 PNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRI 348
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 349 MEYIQAGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHT 428
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQGA---LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108935817 429 KNLNTAIEVSNALKAGTVWVNT---YNTLHhqMPFGGYKESGIG-RELGEDALANYTQTKTVSI 488
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEvpgFRSEL--SPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
20-487 |
8.30e-102 |
|
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: 314.50 E-value: 8.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKgQEGKtFDVINPSDES-VITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:TIGR01237 35 LVINGERVE-TENK-IVSINPCDKSeVVGTVSKASQEHAEHALQAAAKAFE-AWKKTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKIT-GKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPA 177
Cdd:TIGR01237 112 SALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAkGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 178 IACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAA---- 253
Cdd:TIGR01237 192 IVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 254 -SSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAA 332
Cdd:TIGR01237 272 gQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 333 DTFQGPQVSKVQFDRIMEYIQAGKDAGATVeTGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAI 412
Cdd:TIGR01237 352 DVYVGPVIDQKSFNKIMEYIEIGKAEGRLV-SGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEAL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108935817 413 KLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNT--LHHQMPFGGYKESGIGREL-GEDALANYTQTKTVS 487
Cdd:TIGR01237 431 EIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITgaIVGYQPFGGFKMSGTDSKAgGPDYLALFMQAKTVT 508
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
39-487 |
2.01e-101 |
|
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: 312.31 E-value: 2.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 39 NPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKA-ISMAKGDI 117
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQR-EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 118 SMCVGCLRY---YGGWADKITGKviDTTPDTF---NYVKKEPIGVCGQIIPWNFPL--LmwawkIGPAIAC---GNTVVL 186
Cdd:cd07098 81 LVTCEKIRWtlkHGEKALRPESR--PGGLLMFykrARVEYEPLGVVGAIVSWNYPFhnL-----LGPIIAAlfaGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 187 KTAEQT-----PLGGLVAASLvKEAGFPPGVINVISGFGKvAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSnLKKVT 261
Cdd:cd07098 154 KVSEQVawssgFFLSIIRECL-AACGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 262 LELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVS 341
Cdd:cd07098 231 LELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 342 KVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNA 417
Cdd:cd07098 311 PARFDRLEELVADAVEKGARLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108935817 418 STYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTY--NTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVS 487
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
31-491 |
9.84e-88 |
|
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: 277.17 E-value: 9.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 31 EGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAI 110
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK-EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 111 SMAKGD----ISMC---VGCLRyyggwadKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGN 182
Cdd:cd07130 89 PEGLGEvqemIDICdfaVGLSR-------QLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 183 TVVLKTAEQTPLGGL----VAASLVKEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASsNLK 258
Cdd:cd07130 162 VVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA-RFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 259 KVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGP 338
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 339 QVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSnVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNAS 418
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 419 TYGLAAAVHTKNLNTAIEVSNALKA--GTVWVNTyntlhhqmP---------FGGYKESGIGRELGEDALANYTQTKTVS 487
Cdd:cd07130 399 PQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNI--------GtsgaeiggaFGGEKETGGGRESGSDAWKQYMRRSTCT 470
|
....
gi 108935817 488 IRLG 491
Cdd:cd07130 471 INYS 474
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-488 |
5.62e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 274.69 E-value: 5.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDI 117
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR-DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 118 SMCVGCLRYYggwADKITGKVIDTTPD------TFNYVKKEPIGVCGQIIPWNFPLlmwaWKI----GPAIACGNTVVLK 187
Cdd:PRK09406 85 LKCAKGFRYY---AEHAEALLADEPADaaavgaSRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 188 TAEQTPLGGLVAASLVKEAGFPPGVI-NVISGFGKVAgaALSSHMDVDKVAFTGSTVVGRTIlKAAASSNLKKVTLELGG 266
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGAVE--AILRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 267 KSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFD 346
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 347 RIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAV 426
Cdd:PRK09406 315 EVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108935817 427 HTKNLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSI 488
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
20-487 |
9.38e-84 |
|
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: 267.52 E-value: 9.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGQEGKTfdVINPSDES-VITQVHEATEKDVDIAVAAARKAFeGSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFAPSeVVGTTAKADKAEAEAALEAAWAAF-KTWKDWPQEDRARLLLKAADLLRRRRREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGK--VIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGP 176
Cdd:cd07083 98 IATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPavEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 177 AIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAAS-- 254
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARla 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 255 ---SNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFA 331
Cdd:cd07083 258 pgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 332 ADTFQGPQVSKVQFDRIMEYIQAGKDAGaTVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKE-- 409
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfa 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 410 DAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNT--LHHQMPFGGYKESGIGRELG-EDALANYTQTKTV 486
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGTNAKTGgPHYLRRFLEMKAV 496
|
.
gi 108935817 487 S 487
Cdd:cd07083 497 A 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-473 |
1.25e-82 |
|
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: 265.21 E-value: 1.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 1 MTSVQLETPHSGKYEqpTGLFINNEFvkGQEGKTFDVINPSD-ESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPEN 79
Cdd:cd07125 18 ALADALKAFDEKEWE--AIPIINGEE--TETGEGAPVIDPADhERTIGEVSLADAEDVDAALAIAAAAFAG-WSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 80 RGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTTP-DTFNYVKKEPIGVCG 158
Cdd:cd07125 93 RAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPtGELNGLELHGRGVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 159 QIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAF 238
Cdd:cd07125 173 CISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 239 TGSTVVGRTILKAAASSNLKKVTL--ELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQK 316
Cdd:cd07125 253 TGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 317 FKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETgGKRKGDKGYFIEPTIFSNVTEDmkIVKEEIF 396
Cdd:cd07125 333 LKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAP-APLDDGNGYFVAPGIIEIVGIF--DLTTEVF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 397 GPVCSIAKFKTK--EDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTyNT----LHHQmPFGGYKESGIGR 470
Cdd:cd07125 410 GPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NItgaiVGRQ-PFGGWGLSGTGP 487
|
...
gi 108935817 471 ELG 473
Cdd:cd07125 488 KAG 490
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
20-489 |
2.61e-80 |
|
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: 257.89 E-value: 2.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFeGSWRQETPENRGKLLNNLANLFEKNIDLLA 99
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF-LTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKV---IDTTPDTFNYvkKEPIGVCGQIIPWNFPLLMWAWKIGP 176
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETstqVATRVDVYSI--RQPLGVCAGITPFNFPAMIPLWMFPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 177 AIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTILKaAASSN 256
Cdd:TIGR01722 160 AIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHT-TGSAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 257 LKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVyVQESIYDKFVQKFKERAQKNVVG---DPFAAd 333
Cdd:TIGR01722 238 GKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGpgdDPGAE- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 334 tfQGPQVSKVQFDRIMEYIQAGKDAGATV---ETGGKRKG-DKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKE 409
Cdd:TIGR01722 316 --MGPLITPQAKDRVASLIAGGAAEGAEVlldGRGYKVDGyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 410 DAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQM-PFGGYKESGIG--RELGEDALANYTQTKTV 486
Cdd:TIGR01722 394 EAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYfSFTGWKDSFFGdhHIYGKQGTHFYTRGKTV 473
|
...
gi 108935817 487 SIR 489
Cdd:TIGR01722 474 TTR 476
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
141-474 |
2.07e-73 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 238.67 E-value: 2.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 141 TTPDTFNYVKKEPIGVCGQIIPWNFPLLMwawKIGP---AIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVIS 217
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNL---AFGPlvsAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 218 GFGKVAGAALSshMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDADIDNA---ISWvnfGIFFNHG 294
Cdd:cd07134 164 GDAEVAQALLE--LPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAakkIAW---GKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 295 QCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQ-VSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKG 373
Cdd:cd07134 238 QTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARiVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 374 YfIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNT--Y 451
Cdd:cd07134 318 Y-IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvL 396
|
330 340
....*....|....*....|...
gi 108935817 452 NTLHHQMPFGGYKESGIGRELGE 474
Cdd:cd07134 397 HFLNPNLPFGGVNNSGIGSYHGV 419
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
148-486 |
2.16e-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: 236.25 E-value: 2.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 148 YVKKEPIGVCGQIIPWNFPLLMwawKIGP---AIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAG 224
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 225 AALSSHMDvdKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVY 304
Cdd:cd07136 171 ELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 305 VQESIYDKFVQKFKERAQKNVVGDPFAADTFqGPQVSKVQFDRIMEYIQAGKdagatVETGGKRKGDKGYfIEPTIFSNV 384
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNGK-----IVFGGNTDRETLY-IEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 385 TEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtyNTLHH----QMPF 460
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTIMHlanpYLPF 398
|
330 340
....*....|....*....|....*.
gi 108935817 461 GGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07136 399 GGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
36-469 |
1.61e-71 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 234.24 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 36 DVINPSDESVITQVHEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK- 114
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 ------GDISMCVGCLRYYGGwadkiTGKVIDTTPDTFN---YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVV 185
Cdd:cd07148 82 evtraiDGVELAADELGQLGG-----REIPMGLTPASAGriaFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 186 LKTAEQTPLGGLVAASLVKEAGFPPGVINVIsgfgkVAGAALSSHMDVD-KVA---FTGSTVVG-RTILKAAASSnlkKV 260
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAV-----PCENAVAEKLVTDpRVAffsFIGSARVGwMLRSKLAPGT---RC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 261 TLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQV 340
Cdd:cd07148 229 ALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 341 SKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYfiEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTY 420
Cdd:cd07148 309 RPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 108935817 421 GLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLHHQ-MPFGGYKESGIG 469
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
148-486 |
2.31e-70 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 230.49 E-value: 2.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 148 YVKKEPIGVCGQIIPWNFPLLMwawKIGP---AIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAG 224
Cdd:cd07087 95 YVIPEPLGVVLIIGPWNYPLQL---ALAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 225 AALSSHMDvdKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVY 304
Cdd:cd07087 171 ALLAEPFD--HIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 305 VQESIYDKFVQKFKEraqknvvgdpfAADTFQGPQ----------VSKVQFDRIMEYIQAGKdagatVETGGKR-KGDKg 373
Cdd:cd07087 248 VHESIKDELIEELKK-----------AIKEFYGEDpkespdygriINERHFDRLASLLDDGK-----VVIGGQVdKEER- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 374 yFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtyNT 453
Cdd:cd07087 311 -YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN--DV 387
|
330 340 350
....*....|....*....|....*....|....*..
gi 108935817 454 LHH----QMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07087 388 LLHaaipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-486 |
2.99e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 228.59 E-value: 2.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 38 INPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDI 117
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR-DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 118 SMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLlmwaWKI----GPAIACGNTVVLKTAEQTP 193
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 194 LGGLVAASLVKEAGFPPGVINVISgfgkvAGAALSSHMDVDK----VAFTGSTVVGRTIlKAAASSNLKKVTLELGGKSP 269
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLN-----ADNDGVSQMINDSriaaVTVTGSVRAGAAI-GAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIM 349
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 350 EYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTK 429
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 430 NLNTAIEVSNALKAGTVWVNTYNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
56-470 |
2.79e-68 |
|
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: 225.23 E-value: 2.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 56 DVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVG----CLRYYggwa 131
Cdd:cd07095 1 QVDAAVAAARAAFPG-WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGkidiSIKAY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 132 DKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLgglVAASLVK---EAGF 208
Cdd:cd07095 76 HERTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPA---VAELMVElweEAGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 209 PPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFG 288
Cdd:cd07095 153 PPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 289 IFFNHGQCCCAGSRVYVQESIY-DKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGK 367
Cdd:cd07095 232 AFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 368 RKGDKGYFIEPTIFsNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTV- 446
Cdd:cd07095 312 RLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVn 390
|
410 420
....*....|....*....|....
gi 108935817 447 WVNTYNTLHHQMPFGGYKESGIGR 470
Cdd:cd07095 391 WNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
53-486 |
6.22e-68 |
|
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: 224.41 E-value: 6.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 53 TEKDVDIAVAAARKAFEG------SWRQETpenrgklLNNLANLFEKNIDLLAAVESLDNGKA--------ISMAKGDIS 118
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSgktkdlEYRLWQ-------LKQLYWAVKDNEEAIVEALKKDLGRPpfetllteVSGVKNDIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 119 MCVGCLRyygGWA-DKitgKVIDTTPDTFN---YVKKEPIGVCGQIIPWNFPLLMwawKIGP---AIACGNTVVLKTAEQ 191
Cdd:cd07135 76 HMLKNLK---KWAkDE---KVKDGPLAFMFgkpRIRKEPLGVVLIIGPWNYPVLL---ALSPlvgAIAAGCTVVLKPSEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 192 TPLGGLVAASLVKEAgFPPGVINVISGFGKVAGAALSSHMDvdKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNI 271
Cdd:cd07135 147 TPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 272 VFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFqGPQVSKVQFDRIMEY 351
Cdd:cd07135 223 VTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 352 IQagkDAGATVETGGKRKGDKgYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNL 431
Cdd:cd07135 302 LD---TTKGKVVIGGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDK 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 108935817 432 NTAIEVSNALKAGTVWVNtyNTLHH----QMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07135 378 SEIDHILTRTRSGGVVIN--DTLIHvgvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
21-492 |
5.38e-67 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 226.55 E-value: 5.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAA 100
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP-LWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 101 VESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTTPDTFN-YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIA 179
Cdd:PLN02419 196 NITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDtYSIREPLGVCAGICPFNFPAMIPLWMFPVAVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 180 CGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGaALSSHMDVDKVAFTGSTVVGRTILKAAASSNlKK 259
Cdd:PLN02419 276 CGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKG-KR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 260 VTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYV---QESIYDKFVQKFKerAQKNVVGDPFAADTfq 336
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAK--ALKVTCGSEPDADL-- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 337 GPQVSKVQFDRIMEYIQAGKDAGATVETGGKR----KGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAI 412
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 413 KLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTynTLHHQMP---FGGYKESGIG--RELGEDALANYTQTKTVS 487
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGdlNFYGKAGVDFFTQIKLVT 587
|
....*
gi 108935817 488 IRLGD 492
Cdd:PLN02419 588 QKQKD 592
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-490 |
3.61e-66 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 221.55 E-value: 3.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAfEGSWrQETPEN-RGKLLNNLANLFEKNIDLLA 99
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKAW-AKTPLWkRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGK----VIDTTP----DTFNYVKKEPIGVCGQIIPWNFPLLMWA 171
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflVSDSFPgnerNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 172 WKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGstvvGRTILKA 251
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG----GDTGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 252 AASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPfA 331
Cdd:PLN00412 253 SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 332 ADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDkgyFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDA 411
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 412 IKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNTYNTLH-HQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGpDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINL 488
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
31-473 |
1.98e-64 |
|
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: 217.09 E-value: 1.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 31 EGKTFDVINPSD-ESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKA 109
Cdd:TIGR01238 49 DGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFP-TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 110 ISMAKGDISMCVGCLRYYGGWADkitgkvidttpDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:TIGR01238 128 IHNAIAEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNLKKVTL--ELGGK 267
Cdd:TIGR01238 197 EQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 268 SPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDR 347
Cdd:TIGR01238 277 NAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 348 IMEYIQAGKDAGATV---ETGGKRKGDKGYFIEPTIFSnvTEDMKIVKEEIFGPVCSIAKFKTKEDA--IKLGNASTYGL 422
Cdd:TIGR01238 357 LLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARELDqiVDQINQTGYGL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 108935817 423 AAAVHTKNLNTAIEVSNALKAGTVWVN--TYNTLHHQMPFGGYKESGIGRELG 473
Cdd:TIGR01238 435 TMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
31-469 |
2.74e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 225.90 E-value: 2.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 31 EGKTFDVINPSDES-VITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKA 109
Cdd:PRK11905 565 DGGTRPVLNPADHDdVVGTVTEASAEDVERALAAAQAAFP-EWSATPAAERAAILERAADLMEAHMPELFALAVREAGKT 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 110 ISMAKGDISMCVGCLRYYGgwadkitgkviDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:PRK11905 644 LANAIAEVREAVDFLRYYA-----------AQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPA 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNLKKVTL--ELGGK 267
Cdd:PRK11905 713 EQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQ 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 268 SPNIVFEDADIDNAISWVNFGIFFNHGQCCCAgSRV-YVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFD 346
Cdd:PRK11905 793 NAMIVDSSALPEQVVADVIASAFDSAGQRCSA-LRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQA 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 347 RIMEYIQAGKDAGATVETGGKRKG-DKGYFIEPTIFSnvTEDMKIVKEEIFGPVCSIAKFKTKE-----DAIklgNASTY 420
Cdd:PRK11905 872 NIEAHIEAMRAAGRLVHQLPLPAEtEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADEldrviDDI---NATGY 946
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 108935817 421 GLAAAVHTKNLNTAIEVSNALKAGTVWVNtyntlhHQM--------PFGGYKESGIG 469
Cdd:PRK11905 947 GLTFGLHSRIDETIAHVTSRIRAGNIYVN------RNIigavvgvqPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
29-488 |
8.71e-63 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 220.84 E-value: 8.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 29 GQEGKTFDVINPSD-ESVITQVHEATEKDVDIAVAAARKAFeGSWRQeTP-ENRGKLLNNLANLFEKNIDLLAAVESLDN 106
Cdd:PRK11904 558 NGEGEARPVVSPADrRRVVGEVAFADAEQVEQALAAARAAF-PAWSR-TPvEERAAILERAADLLEANRAELIALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 107 GKAISMAKGDISMCVGCLRYYGGWADKITGKVI---DTTPDTfNYVKKEPIGV--CgqIIPWNFPLLMWAWKIGPAIACG 181
Cdd:PRK11904 636 GKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEklpGPTGES-NELRLHGRGVfvC--ISPWNFPLAIFLGQVAAALAAG 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 182 NTVVLKTAEQTPlggLVAASLVK---EAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNLK 258
Cdd:PRK11904 713 NTVIAKPAEQTP---LIAAEAVKllhEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGP 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 259 KVTL--ELGGKSPNIVfeDAD------IDNAISwvnfGIFFNHGQCCCAgSRV-YVQESIYDKFVQKFKERAQKNVVGDP 329
Cdd:PRK11904 790 IVPLiaETGGQNAMIV--DSTalpeqvVDDVVT----SAFRSAGQRCSA-LRVlFVQEDIADRVIEMLKGAMAELKVGDP 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 330 FAADTFQGPQVSKVQFDRIMEYIQAGKDAG---ATVETGGkrKGDKGYFIEPTIFSnvTEDMKIVKEEIFGPVCSIAKFK 406
Cdd:PRK11904 863 RLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPA--GTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYK 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 407 TKE-----DAIklgNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtyntlHHQM-------PFGGYKESGIG-RELG 473
Cdd:PRK11904 939 ASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-----RNQIgavvgvqPFGGQGLSGTGpKAGG 1010
|
490
....*....|....*
gi 108935817 474 EDALANYTQTKTVSI 488
Cdd:PRK11904 1011 PHYLLRFATEKTVTV 1025
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
147-486 |
1.58e-62 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 210.03 E-value: 1.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 147 NYVKKEPIGVCGQIIPWNFPLLMwawKIGP---AIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVA 223
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGADVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 224 gAALSShMDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRV 303
Cdd:cd07133 171 -AAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 304 YVQESIYDKFVQKFKERAQKnvvgdpFAADTFQGPQ----VSKVQFDRIMEYIQAGKDAGATVET--------GGKRKgd 371
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAK------MYPTLADNPDytsiINERHYARLQGLLEDARAKGARVIElnpagedfAATRK-- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 372 kgyfIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNty 451
Cdd:cd07133 320 ----LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN-- 393
|
330 340 350
....*....|....*....|....*....|....*....
gi 108935817 452 NTL-H---HQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07133 394 DTLlHvaqDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
18-425 |
4.67e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 210.20 E-value: 4.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 18 TGLFINNEFVKGQeGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDL 97
Cdd:PRK09457 1 MTLWINGDWIAGQ-GEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA-WARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 98 LAAVESLDNGKAI--------SMA-KGDISmcvgcLRYYggwaDKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLL 168
Cdd:PRK09457 79 LAEVIARETGKPLweaatevtAMInKIAIS-----IQAY----HERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 169 MWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGRTI 248
Cdd:PRK09457 150 LPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 249 LKAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIY-DKFVQKFKERAQKNVVG 327
Cdd:PRK09457 229 HRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 328 DPFAADT-FQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFsNVTEDMKIVKEEIFGPVCSIAKFK 406
Cdd:PRK09457 309 RWDAEPQpFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYD 387
|
410
....*....|....*....
gi 108935817 407 TKEDAIKLGNASTYGLAAA 425
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAG 406
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
19-494 |
1.46e-60 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 206.99 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 19 GLFINNEFvkGQEGKTFDVINPSDESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLL 98
Cdd:PLN02315 22 GCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAK-IWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 AAVESLDNGKAISMAKGDISMCVGCLRYYGGWADKITGKVIDTT-PDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPA 177
Cdd:PLN02315 99 GRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 178 IACGNTVVLKTAEQTPLGGL----VAASLVKEAGFPPGVINVISGfGKVAGAALSSHMDVDKVAFTGSTVVGrTILKAAA 253
Cdd:PLN02315 179 LVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG-LMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 254 SSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAAD 333
Cdd:PLN02315 257 NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 334 TFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKGDKGYFIEPTIFSnVTEDMKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:PLN02315 337 TLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 414 LGNASTYGLAAAVHTKNLNTAIEVSNALKA--GTVWVNT-YNTLHHQMPFGGYKESGIGRELGEDALANYTQTKTVSIRL 490
Cdd:PLN02315 416 INNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINY 495
|
....
gi 108935817 491 GDAL 494
Cdd:PLN02315 496 GNEL 499
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
28-449 |
8.86e-59 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 209.79 E-value: 8.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 28 KGQEGKTFDVINPSDES-VITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDN 106
Cdd:COG4230 565 EAASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFP-AWSATPVEERAAILERAADLLEAHRAELMALLVREA 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 107 GKAISMAKGDISMCVGCLRYYGGWADKITGkvidttpdtfNYVKKEPIGVCGQIIPWNFPLlmwAWKIGP---AIACGNT 183
Cdd:COG4230 644 GKTLPDAIAEVREAVDFCRYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPL---AIFTGQvaaALAAGNT 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 184 VVLKTAEQTPLgglVAASLVK---EAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNLKKV 260
Cdd:COG4230 711 VLAKPAEQTPL---IAARAVRllhEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIV 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 261 TL--ELGGKSPNIVfeD---------ADI-----DNAiswvnfgiffnhGQCCCAgSRV-YVQESIYDKFVQKFKERAQK 323
Cdd:COG4230 788 PLiaETGGQNAMIV--DssalpeqvvDDVlasafDSA------------GQRCSA-LRVlCVQEDIADRVLEMLKGAMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 324 NVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVETGGKRKG-DKGYFIEPTIFSnvTEDMKIVKEEIFGPVCSI 402
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcANGTFVAPTLIE--IDSISDLEREVFGPVLHV 930
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 108935817 403 AKFKTKE-----DAIklgNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVN 449
Cdd:COG4230 931 VRYKADEldkviDAI---NATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
20-467 |
1.68e-55 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 193.85 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGqEGKTFDVINPSD-ESVITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRgkllnnlANLFEKNIDLL 98
Cdd:TIGR01236 34 LVIGGEEVYD-SNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDAKK-DWSNLPFYDR-------AAIFLKAADLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 99 A--------AVESLDNGKAISMAKGD-ISMCVGCLRYYGGWADKITGKVIDTTPDTFNYVKKEPI-GVCGQIIPWNFPLL 168
Cdd:TIGR01236 105 SgpyryeilAATMLGQSKTVYQAEIDaVAELIDFFRFNVKYARELYAQQPISAPGEWNRTEYRPLeGFVYAISPFNFTAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 169 MWAWKIGPAIAcGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTI 248
Cdd:TIGR01236 185 AGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 249 LKAAASS-----NLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQK 323
Cdd:TIGR01236 264 WKKVAQNldryhNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 324 NVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKDAGATVET--GGKRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCS 401
Cdd:TIGR01236 344 VKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEALTIlyGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLT 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 402 IAKF---KTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALK--AGTVWVNTYNT--LHHQMPFGGYKESG 467
Cdd:TIGR01236 424 VYVYpddKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINDKCTgaVVGQQPFGGARMSG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
60-489 |
3.62e-55 |
|
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: 190.90 E-value: 3.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 60 AVAAARKAFEgSWRQETPENRGKLLNNLANLFEKN-IDLLAAVESlDNGKA--------ISMAKGDISMCVGCLRyygGW 130
Cdd:cd07132 3 AVRRAREAFS-SGKTRPLEFRIQQLEALLRMLEENeDEIVEALAK-DLRKPkfeavlseILLVKNEIKYAISNLP---EW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 131 A-DKITGKVIDTTPDTFnYVKKEPIGVCGQIIPWNFPL-LMWAWKIGpAIACGNTVVLKTAEQTP-----LGGLVAASLV 203
Cdd:cd07132 78 MkPEPVKKNLATLLDDV-YIYKEPLGVVLIIGAWNYPLqLTLVPLVG-AIAAGNCVVIKPSEVSPataklLAELIPKYLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 204 KEAgFPpgvinVISGFGKVAGAALSSHMdvDKVAFTGSTVVGRTILKAAAsSNLKKVTLELGGKSPNIVFEDADIDNA-- 281
Cdd:cd07132 156 KEC-YP-----VVLGGVEETTELLKQRF--DYIFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDIDVAar 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 282 -ISWvnfGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFqGPQVSKVQFDRIMEYIQAGKdaga 360
Cdd:cd07132 227 rIAW---GKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDY-GRIINDRHFQRLKKLLSGGK---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 361 tVETGGkRKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNA 440
Cdd:cd07132 299 -VAIGG-QTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSN 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 108935817 441 LKAGTVWVNtyNTLHH----QMPFGGYKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:cd07132 377 TSSGGVCVN--DTIMHytldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
148-489 |
4.88e-55 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 191.78 E-value: 4.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 148 YVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAgFPPGVINVISGFGKVAGAAL 227
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 228 SSHMDVdkVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQE 307
Cdd:PTZ00381 183 KEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 308 SIYDKFVQKFKErAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIqagKDAGATVETGGK-RKGDKgyFIEPTIFSNVTE 386
Cdd:PTZ00381 260 SIKDKFIEALKE-AIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGEvDIENK--YVAPTIIVNPDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 387 DMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtyNTLHH----QMPFGG 462
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN--DCVFHllnpNLPFGG 411
|
330 340
....*....|....*....|....*..
gi 108935817 463 YKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:PTZ00381 412 VGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
20-467 |
4.31e-54 |
|
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: 189.72 E-value: 4.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 20 LFINNEFVKGqeGKTFDVINPSDES-VITQVHEATEKDVDIAVAAARKAfEGSWRQETPENRGKLLNNLANLF--EKNID 96
Cdd:cd07123 35 LVIGGKEVRT--GNTGKQVMPHDHAhVLATYHYADAALVEKAIEAALEA-RKEWARMPFEDRAAIFLKAADLLsgKYRYE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 97 LLAAVeSLDNGKAISMAKGDiSMCVGC--LRYYGGWADKITGKV-IDTTPDTFNYVKKEPI-GVCGQIIPWNF------- 165
Cdd:cd07123 112 LNAAT-MLGQGKNVWQAEID-AACELIdfLRFNVKYAEELYAQQpLSSPAGVWNRLEYRPLeGFVYAVSPFNFtaiggnl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 166 ---PLLMwawkigpaiacGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGST 242
Cdd:cd07123 190 agaPALM-----------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 243 VVGRTILKAAASS-----NLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKF 317
Cdd:cd07123 259 PTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 318 KERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGK-DAGATVETGGKRKGDKGYFIEPTIFsnVTED--MKIVKEE 394
Cdd:cd07123 339 LEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsDPEAEIIAGGKCDDSVGYFVEPTVI--ETTDpkHKLMTEE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 395 IFGPVCSI-----AKFKTKEDAIKlgNASTYGLAAAVHTKNLNTAIEVSNALK--AGTVWVNTYNT--LHHQMPFGGYKE 465
Cdd:cd07123 417 IFGPVLTVyvypdSDFEETLELVD--TTSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTgaVVGQQPFGGARA 494
|
..
gi 108935817 466 SG 467
Cdd:cd07123 495 SG 496
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
36-469 |
1.77e-53 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 194.42 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 36 DVINPSDES-VITQVHEATEKDVDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAK 114
Cdd:PRK11809 662 PVINPADPRdIVGYVREATPAEVEQALESAVNAAP-IWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMCVGCLRYYGGWADkitgkvidttpDTFNYVKKEPIG--VCgqIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQT 192
Cdd:PRK11809 741 AEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQT 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 193 PlggLVAASLVK---EAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAA---SSNLKKVTL--EL 264
Cdd:PRK11809 808 P---LIAAQAVRillEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIPLiaET 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 265 GGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQ 344
Cdd:PRK11809 885 GGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEA 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 345 FDRIMEYIQAGKDAGATV---ETGGKRKGDKGYFIEPTI--FSNVTEdmkiVKEEIFGPVCSIAKFKTKE-----DAIkl 414
Cdd:PRK11809 965 KANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRNQldeliEQI-- 1038
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 415 gNASTYGLAAAVHTKNLNTAIEVSNALKAGTVWVNtyntlhHQM--------PFGGYKESGIG 469
Cdd:PRK11809 1039 -NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN------RNMvgavvgvqPFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
61-486 |
1.97e-46 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 167.20 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 61 VAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKA--------ISMAKGDISMCVGCLryyGGWAD 132
Cdd:cd07137 5 VRELRETFR-SGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPsaesfrdeVSVLVSSCKLAIKEL---KKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 133 KITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTP-----LGGLVAASLVKEAg 207
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPatsalLAKLIPEYLDTKA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 208 fppgvINVISGfGKVAGAALSSHmDVDKVAFTGSTVVGRTILkAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNF 287
Cdd:cd07137 160 -----IKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIM-AAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 288 GIF-FNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQgPQVSKVQFDRIMEYIQAGKDAGATVEtGG 366
Cdd:cd07137 232 GKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS-RIVNSHHFQRLSRLLDDPSVADKIVH-GG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 367 KRKGDKGYfIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTV 446
Cdd:cd07137 310 ERDEKNLY-IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 108935817 447 WVNTyNTLH---HQMPFGGYKESGIGRELGEDALANYTQTKTV 486
Cdd:cd07137 389 TFND-TVVQyaiDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
110-496 |
1.87e-33 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 132.48 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 110 ISMAKGDISMCVGCLRyygGWADKITGKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTA 189
Cdd:PLN02174 72 VSLLRNSIKLALKQLK---NWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 190 EQTPLGGLVAASLVkEAGFPPGVINVISGFGKVAGAALSSHMdvDKVAFTGSTVVGRTILkAAASSNLKKVTLELGGKSP 269
Cdd:PLN02174 149 ELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW--DKIFYTGSSKIGRVIM-AAAAKHLTPVVLELGGKSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIF-FNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGDPFAADTFQgPQVSKVQFDRI 348
Cdd:PLN02174 225 VVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMS-RIVNSTHFDRL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 349 MEYIQAgKDAGATVETGGKrKGDKGYFIEPTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHT 428
Cdd:PLN02174 304 SKLLDE-KEVSDKIVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFT 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108935817 429 KNLNTAIEVSNALKAGTVWVNTYnTLH---HQMPFGGYKESGIGRELGEDALANYTQTKTVSIRlgdALFG 496
Cdd:PLN02174 382 HNKKLKERFAATVSAGGIVVNDI-AVHlalHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYR---SLFG 448
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
149-489 |
1.56e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 129.46 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 149 VKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTP-LGGLVAASLVKEagFPPGVINVISGfGKVAGAAL 227
Cdd:PLN02203 104 VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPaTSAFLAANIPKY--LDSKAVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 228 SSHmDVDKVAFTGSTVVGRTILKAAASsNLKKVTLELGGKSPNIV---FEDADIDNAISWVNFGIFFN-HGQCCCAGSRV 303
Cdd:PLN02203 181 LQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 304 YVQESIYDKFVQKFKERAQKNVVGDPFAADTFqGPQVSKVQFDRIMEYIQAGKDAGATVETGGKrkGDKGYFIEPTIFSN 383
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRESKSM-ARILNKKHFQRLSNLLKDPRVAASIVHGGSI--DEKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 384 VTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKAGTVwvnTYNTLHHQ-----M 458
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIQyacdsL 412
|
330 340 350
....*....|....*....|....*....|.
gi 108935817 459 PFGGYKESGIGRELGEDALANYTQTKTVSIR 489
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAVLRR 443
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-480 |
1.46e-28 |
|
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: 117.72 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 60 AVAAARKAfEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAkGDISMCVGCLRYYG--GWADKITGK 137
Cdd:cd07084 4 ALLAADIS-TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAfvIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 138 VIDTTPDTFNYVKKE---PIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAG-FPPGVI 213
Cdd:cd07084 82 PGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 214 NVISGFGKvAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSnlkKVTLELGGKSPNIVFEDADIDNAISW-VNFGIFFN 292
Cdd:cd07084 162 TLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 293 HGQCCCAGSRVYVQESIY-DKFVQKFKERAQKNVVGDpfaadTFQGPQVSKVQFDRIMEyiqAGKDAGATVETGGK---- 367
Cdd:cd07084 238 SGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIAH---MENLLGSVLLFSGKelkn 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 368 --RKGDKGYFIEPTIFSNVTEDMK---IVKEEIFGPVCSIAKFK-----TKEDAIKLGNAStygLAAAVHTKN------- 430
Cdd:cd07084 310 hsIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSNDpiflqel 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 108935817 431 -LNTAIE---VSNALKAGTVWVNTYNtlhhqmpFGGYKESGIGRELG-EDALANY 480
Cdd:cd07084 387 iGNLWVAgrtYAILRGRTGVAPNQNH-------GGGPAADPRGAGIGgPEAIKLV 434
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-437 |
8.63e-24 |
|
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: 104.27 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 21 FINNEFVKGQEGKTfDVINPSDESVITQVHEATeKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLAN-LFEKNIDLLA 99
Cdd:cd07128 4 YVAGQWHAGTGDGR-TLHDAVTGEVVARVSSEG-LDFAAAVAYAREKGGPALRALTFHERAAMLKALAKyLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 100 AveSLDNGKAISMAKGDISMCVGCLRYYGGWADK--------ITGKVIDTTPD-TFN----YVKKEpiGVCGQIIPWNFP 166
Cdd:cd07128 82 L--SAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDgTFVgqhiLTPRR--GVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 167 llmwAW----KIGPAIACGNTVVLKTAEQTplgGLVAASLVK---EAG-FPPGVINVISGfgkvAGAALSSHMDV-DKVA 237
Cdd:cd07128 158 ----VWgmleKFAPALLAGVPVIVKPATAT---AYLTEAVVKdivESGlLPEGALQLICG----SVGDLLDHLGEqDVVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 238 FTGSTVVGRTiLKAAASSNLKKVTLELGGKSPN--IVFEDADIDNAiswvNFGIFFNH---------GQCCCAGSRVYVQ 306
Cdd:cd07128 227 FTGSAATAAK-LRAHPNIVARSIRFNAEADSLNaaILGPDATPGTP----EFDLFVKEvaremtvkaGQKCTAIRRAFVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 307 ESIYDKFVQKFKERAQKNVVGDPFAADTFQGPQVSKVQFDRIMEYIQAGKdAGATVETGGK-------RKGDKGYFIEPT 379
Cdd:cd07128 302 EARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLL-AEAEVVFGGPdrfevvgADAEKGAFFPPT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 380 IF-SNVTEDMKIVKE-EIFGPVCSIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEV 437
Cdd:cd07128 381 LLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
39-482 |
2.39e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.86 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 39 NPSDESVITQVhEATEKDVDIAVAAARKAFEGSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDIS 118
Cdd:PRK11903 25 DPVTGEELVRV-SATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 119 MCVGCLRYYGGWADKITGK--VIDTTPDTfnyVKKEPI-----------GVCGQIIPWNFPllmwAW----KIGPAIACG 181
Cdd:PRK11903 104 GGIFTLGYYAKLGAALGDArlLRDGEAVQ---LGKDPAfqgqhvlvptrGVALFINAFNFP----AWglweKAAPALLAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 182 NTVVLKTAEQTplgGLVAASLVK---EAG-FPPGVINVISGfgkvAGAALSSH---MDVdkVAFTGSTVVGRTI------ 248
Cdd:PRK11903 177 VPVIVKPATAT---AWLTQRMVKdvvAAGiLPAGALSVVCG----SSAGLLDHlqpFDV--VSFTGSAETAAVLrshpav 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 249 LKAAASSNLKKVTLELGGKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKERAQKNVVGD 328
Cdd:PRK11903 248 VQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 329 PFAADTFQGPQVSKVQFDRIMEYIQAGKdAGATVETGGKR------KGDKGYFIEPTIF-SNVTEDMKIVKE-EIFGPVC 400
Cdd:PRK11903 328 PRNDGVRMGPLVSRAQLAAVRAGLAALR-AQAEVLFDGGGfalvdaDPAVAACVGPTLLgASDPDAATAVHDvEVFGPVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 401 SIAKFKTKEDAIKLGNASTYGLAAAVHTKNLNTAIEVSNALKA--GTVWVNTYNTLHHQ------MP---FGGYKESGIG 469
Cdd:PRK11903 407 TLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVISPDVAALHtghgnvMPqslHGGPGRAGGG 486
|
490
....*....|....
gi 108935817 470 RELGE-DALANYTQ 482
Cdd:PRK11903 487 EELGGlRALAFYHR 500
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
57-460 |
6.59e-22 |
|
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: 98.00 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 57 VDIAVAAARKAFEgSWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGCLRYY------GGW 130
Cdd:cd07129 1 VDAAAAAAAAAFE-SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFadlvreGSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 131 ADKitgkVIDTTPDTF----------NYVKKEPIGVCGqiiPWNFPLlmwAWKIG-----PAIACGNTVVLK-------T 188
Cdd:cd07129 80 LDA----RIDPADPDRqplprpdlrrMLVPLGPVAVFG---ASNFPL---AFSVAggdtaSALAAGCPVVVKahpahpgT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 189 AEQTplgGLVAASLVKEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGSTVVGRTILKAAASSNL-KKVTLELGGK 267
Cdd:cd07129 150 SELV---ARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 268 SPNIVFEDA------DIdnAISWVNfGIFFNHGQ-CCCAGSRVYVQESIYDKFVQKFKERAQKNVVG---DPFAADTFQg 337
Cdd:cd07129 227 NPVFILPGAlaergeAI--AQGFVG-SLTLGAGQfCTNPGLVLVPAGPAGDAFIAALAEALAAAPAQtmlTPGIAEAYR- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 338 pqvskvqfdrimEYIQAGKDAGATVETGGKRKGDKGYFIEPTIF----SNVTEDmKIVKEEIFGPVCSIAKFKTKEDAIK 413
Cdd:cd07129 303 ------------QGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFkvdaAAFLAD-PALQEEVFGPASLVVRYDDAAELLA 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108935817 414 L-----GNastygLAAAVH--TKNLNTAIEVSNAL--KAGTVWVNTYNT-------LHHQMPF 460
Cdd:cd07129 370 VaealeGQ-----LTATIHgeEDDLALARELLPVLerKAGRLLFNGWPTgvevcpaMVHGGPY 427
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
76-318 |
4.60e-12 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 67.63 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 76 TPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKGDISMCVGC-----------LRYYGGWADKITGKvidTTPD 144
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCsesklyknidtERGITASVGHIQDV---LLPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 145 TFN-YVKKEPIGVCGQIIPWNFPLLMwAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEA---GFPPGVINVISGFG 220
Cdd:cd07077 91 NGEtYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 221 KVAGAALSSHMDVDKVAFTGstvvGRTILKAAASSNLKKVTLELG-GKSPNIVFEDADIDNAISWVNFGIFFNhGQCCCA 299
Cdd:cd07077 170 DELAEELLSHPKIDLIVATG----GRDAVDAAVKHSPHIPVIGFGaGNSPVVVDETADEERASGSVHDSKFFD-QNACAS 244
|
250
....*....|....*....
gi 108935817 300 GSRVYVQESIYDKFVQKFK 318
Cdd:cd07077 245 EQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
57-450 |
8.30e-12 |
|
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: 66.91 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 57 VDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAVESLDNGKAISMAKgdISMCVGCLRY-YGGWADKIT 135
Cdd:cd07081 1 LDDAVAAAKVAQQG-LSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDK--VIKNHFAAEYiYNVYKDEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 136 GKVIDTTPDTFNYVKKEPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEA----GFPPG 211
Cdd:cd07081 78 CGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 212 VINVISGFGKVAGAALSSHMDVDKVAFTGstvvGRTILKAAASSNlkKVTLELG-GKSPNIVFEDADIDNAISWVNFGIF 290
Cdd:cd07081 158 LIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG--KPAIGVGaGNTPVVIDETADIKRAVQSIVKSKT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 291 FNHGQCCCAGSRVYVQESIYDKFVQKFKERaqknvvgdpfAADTFQGPQVSKVQfDRIMEYIQ-----AGKDAGATVETG 365
Cdd:cd07081 232 FDNGVICASEQSVIVVDSVYDEVMRLFEGQ----------GAYKLTAEELQQVQ-PVILKNGDvnrdiVGQDAYKIAAAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 366 GKR--KGDKGYFIEPTifsnVTEDMKIVKEEIFGPVCSIAKFKTKED----AIKLGNASTYGLAAAVHTKNLNTAIEV-- 437
Cdd:cd07081 301 GLKvpQETRILIGEVT----SLAEHEPFAHEKLSPVLAMYRAANFADadakALALKLEGGCGHTSAMYSDNIKAIENMnq 376
|
410
....*....|....
gi 108935817 438 -SNALKAGTVWVNT 450
Cdd:cd07081 377 fANAMKTSRFVKNG 390
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
55-440 |
1.87e-11 |
|
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: 65.72 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 55 KDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAvesldngkaisMAKGDISMcvgclryyGGWADKI 134
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ-YRKCTLADREKIIEAIREALLSNAEELAE-----------MAVEETGM--------GRVEDKI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 135 ---------TGKVIDTTPDTFN------YVKKEPIGVCGQIIPWNFPLlmwAWKIGPAI---ACGNTVVLKTAeqtPLGG 196
Cdd:cd07121 64 aknhlaaekTPGTEDLTTTAWSgdngltLVEYAPFGVIGAITPSTNPT---ETIINNSIsmlAAGNAVVFNPH---PGAK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 197 LVAASLV-------KEAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGstvvGRTILKAAASSNlKKVTLELGGKSP 269
Cdd:cd07121 138 KVSAYAVelinkaiAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSG-KKAIGAGAGNPP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 270 NIVFEDADIDNAISWVNFGIFFNHGQCCCAGSRVYVQESIYDKFVQKFKeRAQKNVVGDPFAADtfqgpQVSKVQFDRIM 349
Cdd:cd07121 213 VVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLNDEQAEQ-----LLEVVLLTNKG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 350 EYIQ---AGKDAG-----ATVETGGKRKgdkgyfiepTIFSNVTEDMKIVKEEIFGPVCSIAKFKTKEDAIKLGNASTYG 421
Cdd:cd07121 287 ATPNkkwVGKDASkilkaAGIEVPADIR---------LIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHG 357
|
410 420 430
....*....|....*....|....*....|.
gi 108935817 422 L--AAAVHTKN----------LNTAIEVSNA 440
Cdd:cd07121 358 NrhTAIIHSKNvenltkmaraMQTTIFVKNG 388
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
36-440 |
1.35e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.83 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 36 DVINPSDESVITQVHE-ATEKDVDIAVAAARKAFEGsWRQETPENRGKLLNNLANLFEKNIDLLAAvesldngkaisMAK 114
Cdd:PRK15398 16 EMLSSQTVSPPAAVGEmGVFASVDDAVAAAKVAQQR-YQQKSLAMRQRIIDAIREALLPHAEELAE-----------LAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 115 GDISMcvgclryyGGWADKI---------TGKVIDTTPDTFN------YVKKEPIGVCGQIIPWNFPLlmwAWKIGPAI- 178
Cdd:PRK15398 84 EETGM--------GRVEDKIaknvaaaekTPGVEDLTTEALTgdngltLIEYAPFGVIGAVTPSTNPT---ETIINNAIs 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 179 --ACGNTVVLKTAeqtPLGGLVAASLVK-------EAGFPPGVINVISGFGKVAGAALSSHMDVDKVAFTGstvvGRTIL 249
Cdd:PRK15398 153 mlAAGNSVVFSPH---PGAKKVSLRAIEllneaivAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 250 KAAASSNlKKVTLELGGKSPNIVFEDADIDNA-ISWVNfGIFFNHGQCCCAGSRVYVQESIYDKFVQKFK---------- 318
Cdd:PRK15398 226 KAAMKSG-KKAIGAGAGNPPVVVDETADIEKAaRDIVK-GASFDNNLPCIAEKEVIVVDSVADELMRLMEkngavlltae 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 319 --ERAQKNVVGDPFAADTfqgpqvskvqfdrimEYIqaGKDAGATVETGGKrKGDKGyfiEPTIFSNVTEDMKIVKEEIF 396
Cdd:PRK15398 304 qaEKLQKVVLKNGGTVNK---------------KWV--GKDAAKILEAAGI-NVPKD---TRLLIVETDANHPFVVTELM 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 397 GPVCSIAKFKTKEDAIKL------GNASTyglaAAVHTKN----------LNTAIEVSNA 440
Cdd:PRK15398 363 MPVLPVVRVKDVDEAIALavklehGNRHT----AIMHSRNvdnlnkmaraIQTSIFVKNG 418
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
152-320 |
1.24e-06 |
|
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: 50.57 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 152 EPIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVL-----------KTAEqtplggLVAASLVKeAGFPPGVINVISGFG 220
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFsphprakkcsiEAAK------IMREAAVA-AGAPEGLIQWIEEPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 221 KVAGAALSSHMDVDKVAFTGstvvGRTILKAAASSNlkKVTLELG-GKSPNIVFEDADIDNAISWVNFGIFFNHGQCCCA 299
Cdd:cd07122 167 IELTQELMKHPDVDLILATG----GPGMVKAAYSSG--KPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
170 180
....*....|....*....|.
gi 108935817 300 GSRVYVQESIYDKFVQKFKER 320
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRR 261
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
153-409 |
3.11e-05 |
|
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: 46.33 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 153 PIGVCGQIIPWNFPLLMWAWKIGPAIACGNTVVLKTAEQTPLGGLVAASLVKEAGFPPGVINVISGFGKVAGAALSShMD 232
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-AN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 233 VDKVAFTGSTVVGrtilkaaassnlKKVTLELGGKspnIVFEDADID-----------NAISWV-NFGIFFNHGQCCCAG 300
Cdd:cd07126 221 PRMTLFTGSSKVA------------ERLALELHGK---VKLEDAGFDwkilgpdvsdvDYVAWQcDQDAYACSGQKCSAQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935817 301 SRVYVQESIYDK-FVQKFKERAQKNVVgdpfaADTFQGPqVSKVQFDRIMEYIQA-GKDAGATVETGGKRKGDKGY---- 374
Cdd:cd07126 286 SILFAHENWVQAgILDKLKALAEQRKL-----EDLTIGP-VLTWTTERILDHVDKlLAIPGAKVLFGGKPLTNHSIpsiy 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 108935817 375 -FIEPT-IF-----SNVTEDMKIVKEEIFGPVCSIAKFKTKE 409
Cdd:cd07126 360 gAYEPTaVFvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQ 401
|
|
| |
