|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
9-412 |
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: 596.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRSN 210
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEagfppgvvnvvpgygptagaaisshpdidkvaftgsteVGKLIQQAAGKSN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQ--------------------------GGAPSSSGYV--P-----VPSGQRTApalshR----GPRDR------VDLA 327
Cdd:cd07141 329 GPQideeqfkkileliesgkkegaklecgGKRHGDKGYFiqPtvfsdVTDDMRIA-----KeeifGPVQQifkfktIDEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 328 VQCAHQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 407
Cdd:cd07141 404 IERANNTTY-------GLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
....*
gi 1331431699 408 TVTIK 412
Cdd:cd07141 477 TVTIK 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
5-411 |
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: 519.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 5 FPG*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADLVER 84
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 85 DRAILATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAW 164
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 165 KLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAA 206
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEagfppgvvnivpgfgptagaaisshmdvdkiaftgstaVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 207 SRSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDV 286
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 287 RTEQGPQ--------------------------GGAPSSSGY-------VPVPSGQRTA------PALSHRGPRDrVDLA 327
Cdd:cd07091 321 DTFQGPQvskaqfdkilsyiesgkkegatlltgGERHGSKGYfiqptvfTDVKDDMKIAkeeifgPVVTILKFKT-EDEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 328 VQCAHQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 407
Cdd:cd07091 400 IERANDTEY-------GLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
....
gi 1331431699 408 TVTI 411
Cdd:cd07091 473 AVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
9-409 |
1.16e-142 |
|
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: 414.97 E-value: 1.16e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGsAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRSN 210
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEaglpdgvlnivtgfgptagaaiashmdvdkvaftgsteVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQ--------------------------GGAPSSSGYVPVPS-------GQRTA------PALSHRGPRDrVDLAVQCA 331
Cdd:cd07142 325 GPQvdkeqfekilsyiehgkeegatlitgGDRIGSKGYYIQPTifsdvkdDMKIArdeifgPVQSILKFKT-VDEVIKRA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331431699 332 HQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:cd07142 404 NNSKY-------GLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-413 |
4.82e-141 |
|
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: 411.15 E-value: 4.82e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 2 TTSFPG*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgSAWRRLDAPS-RGHLLHQLAD 80
Cdd:cd07143 2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLKVSGSkRGRCLSKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 81 LVERDRAILATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLL 160
Cdd:cd07143 80 LMERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 161 MLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLV 202
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEagfppgvinvvsgygrtcgnaisshmdidkvaftgstlVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 203 KEAASRSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGD 282
Cdd:cd07143 240 MEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 283 PFDVRTEQGPQGGAPSSSGYVP-VPSGQRTAPALSHRGPRdrvdlavqCAHQGVFFNQG--QCCTAASRVFVEE------ 353
Cdd:cd07143 320 PFAEDTFQGPQVSQIQYERIMSyIESGKAEGATVETGGKR--------HGNEGYFIEPTifTDVTEDMKIVKEEifgpvv 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 354 ------------------------QVYAEFVRRSVEFAKKR------INCYNAIYAQAPFGGFKMSGNGRELGEYALAEY 403
Cdd:cd07143 392 avikfkteeeaikrandstyglaaAVFTNNINNAIRVANALkagtvwVNCYNLLHHQVPFGGYKQSGIGRELGEYALENY 471
|
490
....*....|
gi 1331431699 404 TEVKTVTIKL 413
Cdd:cd07143 472 TQIKAVHINL 481
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
6-413 |
5.67e-135 |
|
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: 396.01 E-value: 5.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 6 PG*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgSAWRRLDAPSRGHLLHQLADLVERD 85
Cdd:cd07144 7 PTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 86 RAILATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWK 165
Cdd:cd07144 85 RDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 166 LAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAAS 207
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEagfppgvvniipgygavagsalaehpdvdkiaftgstaTGRLVMKAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 208 rSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKR-PVGDPFDV 286
Cdd:cd07144 245 -QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 287 RTEQGPQ-------------------------GGAPSSSG-----YVP------VPSGQRT------APALSHRGPRDrV 324
Cdd:cd07144 324 DTVVGPQvsktqydrvlsyiekgkkegaklvyGGEKAPEGlgkgyFIPptiftdVPQDMRIvkeeifGPVVVISKFKT-Y 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 325 DLAVQCAhqgvffNQGQCCTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYT 404
Cdd:cd07144 403 EEAIKKA------NDTTYGLAAA-VFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYT 475
|
....*....
gi 1331431699 405 EVKTVTIKL 413
Cdd:cd07144 476 QTKAVHINL 484
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-413 |
7.45e-135 |
|
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: 395.26 E-value: 7.45e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 1 MTTSfPG*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLAD 80
Cdd:COG1012 1 MTTP-EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 81 LVERDRAILATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPL 159
Cdd:COG1012 77 LLEERREELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 160 LMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKL 201
Cdd:COG1012 156 ALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEaglpagvlnvvtgdgsevgaalvahpdvdkisftgstaVGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 202 VKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVG 281
Cdd:COG1012 236 IAAAAAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 282 DPFDVRTEQGPqggapsssgyvpvpsgqrtapaLSHRGPRDRVDLAVQCAHQ----------------------GVFFNq 339
Cdd:COG1012 315 DPLDPGTDMGP----------------------LISEAQLERVLAYIEDAVAegaelltggrrpdgeggyfvepTVLAD- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 340 gqcCTAASRVFVEEQ------------------------------VYAEFVRRSVEFAKK------RINCYNAIY-AQAP 382
Cdd:COG1012 372 ---VTPDMRIAREEIfgpvlsvipfddeeeaialandteyglaasVFTRDLARARRVARRleagmvWINDGTTGAvPQAP 448
|
490 500 510
....*....|....*....|....*....|.
gi 1331431699 383 FGGFKMSGNGRELGEYALAEYTEVKTVTIKL 413
Cdd:COG1012 449 FGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
20-409 |
3.12e-132 |
|
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: 388.04 E-value: 3.12e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 20 SGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGK 99
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 100 PFLHAFFiDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVK 179
Cdd:pfam00171 82 PLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 180 PAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRsNLKRVTLELGGK 221
Cdd:pfam00171 161 PSELTPLTALLLAELFEEaglpagvlnvvtgsgaevgealvehpdvrkvsftgstaVGRHIAEAAAQ-NLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 222 NPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPqggapsssg 301
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGP--------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 302 yvpvpsgqrtapaLSHRGPRDRV----DLAV----QCAHQG-------------VFFNqgqcCTAASRVFVEE------- 353
Cdd:pfam00171 311 -------------LISKAQLERVlkyvEDAKeegaKLLTGGeagldngyfveptVLAN----VTPDMRIAQEEifgpvls 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 354 -----------------------QVYAEFVRRSVEFAKK------RINCYNAIYA-QAPFGGFKMSGNGRELGEYALAEY 403
Cdd:pfam00171 374 virfkdeeeaieiandteyglaaGVFTSDLERALRVARRleagmvWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEY 453
|
....*.
gi 1331431699 404 TEVKTV 409
Cdd:pfam00171 454 TEVKTV 459
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-414 |
2.39e-128 |
|
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: 378.96 E-value: 2.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGE-WPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPA 169
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 170 LCCGNTIVVKPAEQTPLTTLHLGSLIQEV--------------------------------------GKLVKEAASRsNL 211
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAglpagvvnlvtgsgatvgaelaespdvdlvsftggtatGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 212 KRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQG 291
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 292 P--------------QGGApsSSGYVPVPSGQRTAPALSHRG----PR--DRVDLAVQCAHQGVFfnqGQCCTA------ 345
Cdd:cd07119 318 PlvsaehrekvlsyiQLGK--EEGARLVCGGKRPTGDELAKGyfvePTifDDVDRTMRIVQEEIF---GPVLTVerfdte 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 346 --------------ASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07119 393 eeairlandtpyglAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
...
gi 1331431699 412 KLE 414
Cdd:cd07119 473 NLS 475
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-415 |
5.64e-127 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 377.23 E-value: 5.64e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGP-WPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRSN 210
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEaglppgvlnvvsgfgptagaalashmdvdklaftgstdTGKIVLELAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQ--------------------------GGAPSSSGYVPVPS-------GQRTA------PALSHRGPRDrVDLAVQCA 331
Cdd:PLN02466 379 GPQidseqfekilryiksgvesgatlecgGDRFGSKGYYIQPTvfsnvqdDMLIAqdeifgPVQSILKFKD-LDEVIRRA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 332 HQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:PLN02466 458 NNTRY-------GLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 530
|
....
gi 1331431699 412 KLED 415
Cdd:PLN02466 531 PLKN 534
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
21-411 |
2.19e-116 |
|
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: 347.67 E-value: 2.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 21 GKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKP 100
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 101 FLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKP 180
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 181 AEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRSNLKRVTLELGGKN 222
Cdd:cd07112 160 AEQSPLTALRLAELALEaglpagvlnvvpgfghtagealglhmdvdalaftgsteVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 223 PCIVCADA-DLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP---QGGAPS 298
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAlvsEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 299 SSGYvpVPSGQRTAPALSHRGPRDRVDlavqcaHQGVF-----FNQgqcCTAASRVFVEE-------------------- 353
Cdd:cd07112 320 VLGY--IESGKAEGARLVAGGKRVLTE------TGGFFveptvFDG---VTPDMRIAREEifgpvlsvitfdseeeaval 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331431699 354 ----------QVYAEFVRRSVEFAKK------RINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07112 389 andsvyglaaSVWTSDLSRAHRVARRlragtvWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
9-418 |
3.52e-116 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 348.35 E-value: 3.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGP-WPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQ--------------------------------------EVGKLVKEAASRSN 210
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKlagvpdgvinvvtgfgptagaaiashmdvdkvsftgstEVGRKIMQAAATSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQ-------------------------GGAPS-SSGYVPVPS-------------GQRTAPALSHRGPRDrVDLAVQCA 331
Cdd:PLN02766 342 GPQvdkqqfekilsyiehgkregatlltGGKPCgDKGYYIEPTiftdvtedmkiaqDEIFGPVMSLMKFKT-VEEAIKKA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 332 hqgvffNQGQCCTAASRVFVEEQVyAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:PLN02766 421 ------NNTKYGLAAGIVTKDLDV-ANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVT 493
|
....*..
gi 1331431699 412 KLEDkSP 418
Cdd:PLN02766 494 PLYN-SP 499
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
47-411 |
6.95e-116 |
|
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: 345.35 E-value: 6.95e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 47 DMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHAFFIDLEGCVKTLRYFAGWADKI 126
Cdd:cd07078 1 DAAVAAARAAFK---AWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 127 QGKTIPTDD-NVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------- 197
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEaglppgvl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 ------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQ 247
Cdd:cd07078 157 nvvtgdgdevgaalashprvdkisftgstaVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 248 GQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQGGAPSS---SGYV--PVPSGQRTApALSHRGPRD 322
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLdrvLAYIedAKAEGAKLL-CGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 323 R-----------VDLAVQCAHQGVF--------F----------NQGQCCTAASrVFVEEQVYAEFVRRSVEFAKKRINC 373
Cdd:cd07078 315 KgyfvpptvltdVDPDMPIAQEEIFgpvlpvipFkdeeeaielaNDTEYGLAAG-VFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 1331431699 374 YNA-IYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07078 394 YSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
2-412 |
1.40e-114 |
|
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: 343.71 E-value: 1.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 2 TTSFPG*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADL 81
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGE-WGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 82 VERDRAILATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTD----DNVVCFTRHEPVGVCGAITPWNF 157
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 158 PLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHL--------------------GSLI------------------QEVG 199
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFaeltvkagfpkgvinilpgsGSLVgqrlsdhpdvrklgftgsTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 200 KLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRP 279
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 280 VGDPFDVRTEQGPQ------------------GGAPSSSGYVPVP-SGQRTAPAL-------------SHRGP------- 320
Cdd:cd07140 320 IGDPLDRSTDHGPQnhkahldklveycergvkEGATLVYGGKQVDrPGFFFEPTVftdvedhmfiakeESFGPimiiskf 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 321 -RDRVDLAVQCAHQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYA 399
Cdd:cd07140 400 dDGDVDGVLQRANDTEY-------GLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEA 472
|
490
....*....|...
gi 1331431699 400 LAEYTEVKTVTIK 412
Cdd:cd07140 473 LNEYLKTKTVTIE 485
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-413 |
2.22e-111 |
|
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: 334.41 E-value: 2.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSAwrrLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAF 105
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSA---MDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTP 185
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 186 LTTLHLGSLIQEVG---------------------------------------KLVKEAAsrSNLKRVTLELGGKNPCIV 226
Cdd:cd07115 158 LSALRIAELMAEAGfpagvlnvvtgfgevagaalvehpdvdkitftgstavgrKIMQGAA--GNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 227 CADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQ------------- 293
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLvsqaqfdrvldyv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 294 -------------GGAPSSSG-YVP------VPSGQRTA------PALSHRGPRDRVDlAVQCAHqgvffnqGQCCTAAS 347
Cdd:cd07115 316 dvgreegarlltgGKRPGARGfFVEptifaaVPPEMRIAqeeifgPVVSVMRFRDEEE-ALRIAN-------GTEYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331431699 348 RVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 413
Cdd:cd07115 388 GVWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
26-411 |
6.35e-111 |
|
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: 333.36 E-value: 6.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqRGSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHAF 105
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FIDLEGCVKTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQT 184
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 185 PLTTLHLGSLIQE--------------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIV 226
Cdd:cd07114 159 PASTLELAKLAEEagfppgvvnvvtgfgpetgealvehplvakiaftggteTGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 227 CADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPqggapsssgyvpvp 306
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGP-------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 307 sgqrtapaLSHRGPRDR----VDLAVQ---------CAHQGVFFNQGQ--------CCTAASRVFVEE------------ 353
Cdd:cd07114 304 --------LATERQLEKveryVARAREegarvltggERPSGADLGAGYffeptilaDVTNDMRIAQEEvfgpvlsvipfd 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 354 ------------------QVYAEFVRRSVEFAKKR------INCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:cd07114 376 deeeaialandseyglaaGIWTRDLARAHRVARAIeagtvwVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
..
gi 1331431699 410 TI 411
Cdd:cd07114 456 WI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-411 |
1.31e-108 |
|
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: 327.21 E-value: 1.31e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAF 105
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTP 185
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 186 LTTLHLGSLIQEVG------------------KLVK--------------------EAASRsNLKRVTLELGGKNPCIVC 227
Cdd:cd07093 158 LTAWLLAELANEAGlppgvvnvvhgfgpeagaALVAhpdvdlisftgetatgrtimRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 228 ADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQggaPSSSGYVPVPS 307
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPL---ISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 308 GQRTAPALSHR----GPRDR-----------------VDLAVQCAHQGVFfnqGQCCTAASrvFVEEQ------------ 354
Cdd:cd07093 314 YVELARAEGATiltgGGRPElpdleggyfveptvitgLDNDSRVAQEEIF---GPVVTVIP--FDDEEeaielandtpyg 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331431699 355 ----VYAEFVRRSVEFAKKR------INCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07093 389 laayVWTRDLGRAHRVARRLeagtvwVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
51-411 |
8.78e-103 |
|
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: 309.54 E-value: 8.78e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 51 EAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHAFFIDLEGCVKTLRYFAGWADKIQGKT 130
Cdd:cd06534 1 AAARAAFK---AWAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 131 IP-TDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE------------ 197
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEaglppgvvnvvp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 --------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCC 251
Cdd:cd06534 157 gggdevgaallshprvdkisftgstaVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 252 TAASRVFVEEQVYAEFVRRSVEFakKRPVGDPFDVRTEQ--GPQggapsssgyVPVpsgqrtapalshrGPRDRVDLAVQ 329
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLVTV--LVDVDPDMPIAQEEifGPV---------LPV-------------IRFKDEEEAIA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 330 CAhqgvffNQGQCCTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAIY-AQAPFGGFKMSGNGRELGEYALAEYTEVKT 408
Cdd:cd06534 292 LA------NDTEYGLTAG-VFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKNSGIGREGGPYGLEEYTRTKT 364
|
...
gi 1331431699 409 VTI 411
Cdd:cd06534 365 VVI 367
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-411 |
8.57e-95 |
|
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: 291.74 E-value: 8.57e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF 106
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFP---GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 iDLEGCVKTLRYFAGWAdkIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPL 186
Cdd:cd07106 79 -EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 187 TTLHLGSLIQEV------------------------------------GKLVKEAASrSNLKRVTLELGGKNPCIVCADA 230
Cdd:cd07106 156 CTLKLGELAQEVlppgvlnvvsggdelgpaltshpdirkisftgstatGKKVMASAA-KTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 231 DLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP------------------ 292
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPvqnkmqydkvkelvedak 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 -------QGGAP-SSSGY-VP------VPSGQR---------TAPALSHRGPRDRVDLAvqcahqgvffNQGQCCTAASr 348
Cdd:cd07106 315 akgakvlAGGEPlDGPGYfIPptivddPPEGSRivdeeqfgpVLPVLKYSDEDEVIARA----------NDSEYGLGAS- 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 349 VFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07106 384 VWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
9-413 |
4.55e-94 |
|
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: 290.90 E-value: 4.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQ-------------------------------------EVGKLVKEAASRsNL 211
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQdvlpkgvvnivtgkgsksgeyllnhpgldklaftgstEVGRDVAIAAAK-KL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 212 KRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQG 291
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 292 PQGGAPS------------SSGYVPVPSGQRTAPALSHRG----PR--DRVDLAVQCAHQGVF--------FNQGQCCTA 345
Cdd:cd07117 319 AQVNKDQldkilsyvdiakEEGAKILTGGHRLTENGLDKGffiePTliVNVTNDMRVAQEEIFgpvatvikFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331431699 346 ---------ASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 413
Cdd:cd07117 399 mandseyglGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-411 |
2.45e-93 |
|
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: 288.07 E-value: 2.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF 106
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADKIQGKT----IPtddNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAE 182
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 183 QTPLTTLHLGSLIQEV-------------------------------------GKLVKEAASRsNLKRVTLELGGKNPCI 225
Cdd:cd07092 156 TTPLTTLLLAELAAEVlppgvvnvvcgggasagdalvahprvrmvsltgsvrtGKKVARAAAD-TLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 226 VCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP------------- 292
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPlnsaaqrervagf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 ------------QGGAPSSSGYVPVP---SGQRTAPALSHR---GPR------DRVDLAVQCAHqGVFFNqgqcctAASR 348
Cdd:cd07092 315 verapaharvltGGRRAEGPGYFYEPtvvAGVAQDDEIVQEeifGPVvtvqpfDDEDEAIELAN-DVEYG------LASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 349 VFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
10-413 |
5.15e-93 |
|
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: 288.09 E-value: 5.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPA 169
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 170 LCCGNTIVVKPAEQTPLTTLHLGSLIQ-------------------------------------EVGKLVKEAASRsNLK 212
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGdllpkgvvnvvtgfgseagkplashpriaklaftgstTVGRLIMQYAAE-NLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 213 RVTLELGGKNPCIVCADA-----DLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVR 287
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 288 TEQGPQGGAPSSS---GYVPVpsGQRTAPALSHRGPRDRVDLAVQCAH--QGVFFNQgqccTAASRVFVEE--------- 353
Cdd:cd07559 320 TMMGAQVSKDQLEkilSYVDI--GKEEGAEVLTGGERLTLGGLDKGYFyePTLIKGG----NNDMRIFQEEifgpvlavi 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 354 --QVYAEFVR-------------------------RSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEV 406
Cdd:cd07559 394 tfKDEEEAIAiandteyglgggvwtrdinralrvaRGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQT 473
|
....*..
gi 1331431699 407 KTVTIKL 413
Cdd:cd07559 474 KNILVSY 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
10-414 |
2.91e-91 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 283.34 E-value: 2.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSkSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PRK13473 6 LINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTipTDDNVVCFT---RHEPVGVCGAITPWNFPLLMLAWKL 166
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 167 APALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEAASRS 209
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADilppgvlnvvtgrgatvgdalvghpkvrmvsltgsiaTGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 210 nLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTE 289
Cdd:PRK13473 240 -VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 290 QGPQ---------------------------GGAPSSSGYVPVPS-----GQRTA--------PALSHRgPRDRVDLAVQ 329
Cdd:PRK13473 319 LGPLisaahrdrvagfverakalghirvvtgGEAPDGKGYYYEPTllagaRQDDEivqrevfgPVVSVT-PFDDEDQAVR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 330 CAhqgvffNQGQCCTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:PRK13473 398 WA------NDSDYGLASS-VWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
....*
gi 1331431699 410 TIKLE 414
Cdd:PRK13473 471 MVKHT 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
10-411 |
4.12e-90 |
|
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: 280.31 E-value: 4.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK---AWERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQEV--------------------------------------GKLVKEAASRsN 210
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAglpagvlnivtgrgsvvgdalvahpkvgmisltgsteaGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQ-------------------------GGAPSSSG----YVP-VPSGQRTAPALSHR---GP------RDRVDLAVQCA 331
Cdd:cd07088 316 GPLvneaaldkveemveraveagatlltGGKRPEGEkgyfYEPtVLTNVRQDMEIVQEeifGPvlpvvkFSSLDEAIELA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 332 HQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07088 396 NDSEY-------GLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-409 |
1.01e-89 |
|
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: 279.52 E-value: 1.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKkfATYNPSTL-EKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTsDVVGKYARASAEDADAAIAAAAAAF---PAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGKTIP-TDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLA 167
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 168 PALCCGNTIVVKPAEQTPLTTLHL--------------------GSLI------------------QEVGKLVKEAASrS 209
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALveileeaglpagvfnlvmgsGSEVgqalvehpdvdavsftgsTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 210 NLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTE 289
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 290 QGP------------------QGGAPSSSGYVPVPSGQR---TAPAL------SHRGPRDRV-------------DLAVQ 329
Cdd:cd07097 317 IGPvvserqlekdlryieiarSEGAKLVYGGERLKRPDEgyyLAPALfagvtnDMRIAREEIfgpvaavirvrdyDEALA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 330 CAHQGVF-FNQGQCCTAASRVFveeqvyaEFVRRsVEFAKKRINCYNAIYA-QAPFGGFKMSGNG-RELGEYALAEYTEV 406
Cdd:cd07097 397 IANDTEFgLSAGIVTTSLKHAT-------HFKRR-VEAGVVMVNLPTAGVDyHVPFGGRKGSSYGpREQGEAALEFYTTI 468
|
...
gi 1331431699 407 KTV 409
Cdd:cd07097 469 KTV 471
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-411 |
2.41e-89 |
|
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: 277.78 E-value: 2.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFf 106
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK---TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADKIQGKTIPTDD-NVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTP 185
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 186 LTTLHLGSLIQE--------------------------------------VGKLVKEAASrSNLKRVTLELGGKNPCIVC 227
Cdd:cd07103 158 LSALALAELAEEaglpagvlnvvtgspaeigealcasprvrkisftgstaVGKLLMAQAA-DTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 228 ADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPqggapsssgyvpvps 307
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGP--------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 308 gqrtapaLSHRGPRDRVDLAVQCA---------------HQGVFF------NqgqcCTAASRVFVEEQ------------ 354
Cdd:cd07103 302 -------LINERAVEKVEALVEDAvakgakvltggkrlgLGGYFYeptvltD----VTDDMLIMNEETfgpvapiipfdt 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 355 ------------------VYAEFVRRSVEFAKK------RINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:cd07103 371 edeviarandtpyglaayVFTRDLARAWRVAEAleagmvGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
.
gi 1331431699 411 I 411
Cdd:cd07103 451 L 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
26-409 |
4.36e-89 |
|
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: 277.26 E-value: 4.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAF 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK---EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 fIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTP 185
Cdd:cd07090 78 -VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 186 LTTLHLGSLIQE-------------------------------------VGKLVKEAASrSNLKRVTLELGGKNPCIVCA 228
Cdd:cd07090 157 LTALLLAEILTEaglpdgvfnvvqgggetgqllcehpdvakvsftgsvpTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 229 DADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP---------------- 292
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGAliseehlekvlgyies 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 --QGGAPSSSGYVPVP------SGQRTAPAL------SHR-------GPR------DRVDLAVQCAHQGVFfnqgqccTA 345
Cdd:cd07090 316 akQEGAKVLCGGERVVpedgleNGFYVSPCVltdctdDMTivreeifGPVmsilpfDTEEEVIRRANDTTY-------GL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331431699 346 ASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:cd07090 389 AAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
10-407 |
5.87e-89 |
|
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: 277.46 E-value: 5.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPA 169
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 170 LCCGNTIVVKPAEQTPLTTLHLGSLIQEVG---------------------------------------KLVKEAAsrSN 210
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGlpkgvfnvvqgdgaevgpllvnhpdvakvsftggvptgkKIMAAAA--GH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:TIGR01804 236 LKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQGGAPSSS---GYVPVpsGQRTAPALSHRGPR-DRVDLAVQCAHQGVFFNQgqcCTAASRVfVEEQVY---------- 356
Cdd:TIGR01804 316 GPLISAAHRDkvlSYIEK--GKAEGATLATGGGRpENVGLQNGFFVEPTVFAD---CTDDMTI-VREEIFgpvmtvltfs 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331431699 357 --AEFVRRS-------------------------VEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 407
Cdd:TIGR01804 390 deDEVIARAndteyglaggvftadlgrahrvadqLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-411 |
8.37e-89 |
|
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: 276.42 E-value: 8.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGsaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFf 106
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPL 186
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 187 TTLHLGSLIQE--------------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCA 228
Cdd:cd07109 159 TALRLAELAEEaglpagalnvvtglgaeagaalvahpgvdhisftgsveTGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 229 DADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFD-------VRTEQ----------G 291
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEdpdlgplISAKQldrvegfvarA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 292 PQGGA-----------PSSSGYV-------PVPSGQRTA------PALSHRgPRDRVDLAVQCAH-------QGVFFNQG 340
Cdd:cd07109 318 RARGArivaggriaegAPAGGYFvaptlldDVPPDSRLAqeeifgPVLAVM-PFDDEAEAIALANgtdyglvAGVWTRDG 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331431699 341 QCCTAASRVFVEEQVYaefvrrsvefakkrINCYNA---IyaQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07109 397 DRALRVARRLRAGQVF--------------VNNYGAgggI--ELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-410 |
1.93e-88 |
|
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: 275.77 E-value: 1.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHAF 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FIDLEGCVKTLRYFAGWADKI---QGKTIPTDDN-VVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPA 181
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRsNLKRVTLELGGKNP 223
Cdd:cd07110 157 ELTSLTELELAEIAAEaglppgvlnvvtgtgdeagaplaahpgidkisftgstaTGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 224 CIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP----------- 292
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPlvsqaqyekvl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 ---------------QGGAPSSSG---------YVPVPSGQRT------APALSHRGPRDRvDLAVQCAhqgvffNQGQC 342
Cdd:cd07110 316 sfiargkeegarllcGGRRPAHLEkgyfiaptvFADVPTDSRIwreeifGPVLCVRSFATE-DEAIALA------NDSEY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331431699 343 CTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:cd07110 389 GLAAA-VISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-411 |
1.60e-87 |
|
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: 273.06 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 40 EGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCVKTLRYF 119
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EIEGAADLWRYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 120 AGWADKIQGKTIPT-DDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE- 197
Cdd:cd07118 93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 -------------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAH 240
Cdd:cd07118 173 glpagvvnivtgygatvgqamtehpdvdmvsftgstrVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 241 QGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP---QGGAPSSSGYvpVPSGQRTAPALSH 317
Cdd:cd07118 252 FGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAiinEAQLAKITDY--VDAGRAEGATLLL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 318 RGprDRVDLAVQCAHQGVFFNQgqcCTAASRVFVEE------------------------------QVYAEFVRRSVEFA 367
Cdd:cd07118 330 GG--ERLASAAGLFYQPTIFTD---VTPDMAIAREEifgpvlsvltfdtvdeaialandtvyglsaGVWSKDIDTALTVA 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1331431699 368 KK------RINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07118 405 RRiragtvWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-414 |
2.43e-87 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 274.08 E-value: 2.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 7 G*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRLDAPSRGHLLHQLADLVERDR 86
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 87 AILATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKL 166
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 167 APALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASR 208
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEaglpdgvlnvvtgfgheagqalsrhndidaiaftgstrTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 209 SNLKRVTLELGGKNPCIVCADA-DLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVR 287
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 288 TEQGP---QGGAPSSSGYVPVPSGQ-------RTAPALSHRGPR--DRVDLAVQCAHQGVFfnqgQCCTAASRVFVEEQ- 354
Cdd:PRK09847 339 TTMGTlidCAHADSVHSFIREGESKgqllldgRNAGLAAAIGPTifVDVDPNASLSREEIF----GPVLVVTRFTSEEQa 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 355 --------------VYAEFVRRSVEFAKKR------INCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLE 414
Cdd:PRK09847 415 lqlandsqyglgaaVWTRDLSRAHRMSRRLkagsvfVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
10-415 |
1.86e-86 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 271.37 E-value: 1.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLV-ERDRAi 88
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ---KIWAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLG-----------------------------------SLIQEV--GKLVKEAASRSnL 211
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAeiyteaglpdgvfnvvqgdgrvgawltehpdiakvSFTGGVptGKKVMAAAAAS-L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 212 KRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQG 291
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 292 PQGGAPSSS---GYvpVPSGQRTAPALSHRGPR-DRVDLAVQCAHQGVFFNQgqcCTAASRVfVEEQVY----------- 356
Cdd:PRK13252 325 PLVSFAHRDkvlGY--IEKGKAEGARLLCGGERlTEGGFANGAFVAPTVFTD---CTDDMTI-VREEIFgpvmsvltfdd 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 357 -AEFVRRS--VEFAK---------KR--------------INCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:PRK13252 399 eDEVIARAndTEYGLaagvftadlSRahrvihqleagicwINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
....*
gi 1331431699 411 IKLED 415
Cdd:PRK13252 479 VEMGP 483
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
10-411 |
2.52e-86 |
|
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: 270.76 E-value: 2.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKIC-DVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLA 167
Cdd:cd07131 79 LARLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 168 PALCCGNTIVVKPAEQTPLTTLHL----------------------------------------GSLiqEVGKLVKEAAS 207
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLvelfaeaglppgvvnvvhgrgeevgealvehpdvdvvsftGST--EVGERIGETCA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 208 RSNlKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVR 287
Cdd:cd07131 236 RPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 288 TEQGP---QGGAPSSSGYVPVpsGQRTAPALSHRGPR-DRVDLAVQC-AHQGVFFNQgqccTAASRVFVEE--------- 353
Cdd:cd07131 315 TDMGPlinEAQLEKVLNYNEI--GKEEGATLLLGGERlTGGGYEKGYfVEPTVFTDV----TPDMRIAQEEifgpvvali 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 354 ---------------------QVYAEFVRRSVEFAKK---RINCYNA--IYAQA--PFGGFKMSGNG-RELGEYALAEYT 404
Cdd:cd07131 389 evssleeaieiandteyglssAIYTEDVNKAFRARRDleaGITYVNAptIGAEVhlPFGGVKKSGNGhREAGTTALDAFT 468
|
....*..
gi 1331431699 405 EVKTVTI 411
Cdd:cd07131 469 EWKAVYV 475
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-410 |
2.31e-82 |
|
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: 260.13 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAG------WADKIQGKTIptddnvvcftRHEPVGVCGAITPWNFPLLML 162
Cdd:cd07138 78 LAQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VREPIGVCGLITPWNWPLNQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 163 AWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKE 204
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEaglpagvfnlvngdgpvvgealsahpdvdmvsftgstrAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 205 AASRSnLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPF 284
Cdd:cd07138 228 AAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 285 DVRTEQGP------------------QGGAPSSSGYVPVPSGQRT------------------------APALSHRgPRD 322
Cdd:cd07138 307 DPATTLGPlasaaqfdrvqgyiqkgiEEGARLVAGGPGRPEGLERgyfvkptvfadvtpdmtiareeifGPVLSII-PYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 323 RVDLAVQCAHQGVFFNQGqcctaasrvfveeQVYAEFVRRSVEFAKK------RINcYNAIYAQAPFGGFKMSGNGRELG 396
Cdd:cd07138 386 DEDEAIAIANDTPYGLAG-------------YVWSADPERARAVARRlragqvHIN-GAAFNPGAPFGGYKQSGNGREWG 451
|
490
....*....|....
gi 1331431699 397 EYALAEYTEVKTVT 410
Cdd:cd07138 452 RYGLEEFLEVKSIQ 465
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
28-411 |
3.07e-81 |
|
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: 256.90 E-value: 3.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 28 NPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFI 107
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 108 DLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLT 187
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 188 TLHLGSLIQ-------------------------------------EVGKLV-KEAASRsnLKRVTLELGGKNPCIVCAD 229
Cdd:cd07108 160 VLLLAEILAqvlpagvlnvitgygeecgaalvdhpdvdkvtftgstEVGKIIyRAAADR--LIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 230 ADLDLAVQCAHQGV-FFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP---QGGAPSSSGYvpV 305
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAiisEKQFAKVCGY--I 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 306 PSGQRTAPALSHRGPRDRVDLAVQCA--HQGVFFNQgqcCTAASRVFVEE---------------QVYA-----EF---- 359
Cdd:cd07108 316 DLGLSTSGATVLRGGPLPGEGPLADGffVQPTIFSG---VDNEWRLAREEifgpvlcaipwkdedEVIAmandsHYglaa 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331431699 360 ------VRRSVEFAKK------RINCYNAIYAQAPFGGFKMSGNGRELG-EYALAEYTEVKTVTI 411
Cdd:cd07108 393 yvwtrdLGRALRAAHAleagwvQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-403 |
3.11e-79 |
|
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: 252.70 E-value: 3.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKtiptddnvvcFTRHEPVGVCGAITPWNFPLLMLAWKLAPA 169
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTE----------LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 170 LCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEAASRSNlK 212
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEaglppgvlnivtgngsfgsalanhpgvdkvaftgsteVGRALRRATAGTG-K 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 213 RVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP 292
Cdd:cd07111 251 KLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 QG------------------GA---------PSSSGYVP------VPSGQRTA------P---ALSHRGPRDRVDLAvqc 330
Cdd:cd07111 331 IVdpaqlkrirelveegraeGAdvfqpgadlPSKGPFYPptlftnVPPASRIAqeeifgPvlvVLTFRTAKEAVALA--- 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 331 ahqgvffNQGQCCTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEY 403
Cdd:cd07111 408 -------NNTPYGLAAS-VWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
10-412 |
3.33e-79 |
|
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: 252.36 E-value: 3.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgSAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTI------PTDDNVVCFTRHEPVGVCGAITPWNFPLLMLA 163
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 164 WKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEAA 206
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEagipdgvlnvvngkgavgaqlishpdvakvsftgsvaTGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 207 SrSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDV 286
Cdd:cd07113 241 A-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 287 RTEQGP--------------------------QGGAPSSSGYVPVP---SGQRTAPALSHR---GP------RDRVDLAV 328
Cdd:cd07113 320 SVMFGPlanqphfdkvcsylddaraegdeivrGGEALAGEGYFVQPtlvLARSADSRLMREetfGPvvsfvpYEDEEELI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 329 QcahqgvFFNQGQCCTAASrvfveeqVYAEFVRRSVEFAKK------RINCYNAIYAQAPFGGFKMSGNGRELGEYALAE 402
Cdd:cd07113 400 Q------LINDTPFGLTAS-------VWTNNLSKALRYIPRieagtvWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDD 466
|
490
....*....|
gi 1331431699 403 YTEVKTVTIK 412
Cdd:cd07113 467 YTELKSVMIR 476
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
27-409 |
3.59e-79 |
|
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: 251.78 E-value: 3.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSaWRRlDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF 106
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGD-WST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVC-----FTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPA 181
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRsNLKRVTLELGGKNP 223
Cdd:cd07089 160 PDTPLSALLLGEIIAEtdlpagvvnvvtgsdnavgealttdprvdmvsftgstaVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 224 CIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQ---------- 293
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLisaaqrdrve 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 294 ----------------GGAPSS--SGY-------VPVPSGQRTA------PALSHRGPRDrVDLAVQCAHQGVFFNQGqc 342
Cdd:cd07089 319 gyiargrdegarlvtgGGRPAGldKGFyveptlfADVDNDMRIAqeeifgPVLVVIPYDD-DDEAVRIANDSDYGLSG-- 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 343 ctaasrvfveeQVYAEFVRRSVEFAKK-R-----INCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:cd07089 396 -----------GVWSADVDRAYRVARRiRtgsvgINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-410 |
3.89e-79 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 253.12 E-value: 3.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 1 MTTSFPG-*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQR--GSAWRRLDAPSRGHLLHQ 77
Cdd:PLN02467 1 MAIPVPRrQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 78 LADLVERDRAILATLETMDTGKPFLHAFF--IDLEGCVKtlrYFAGWADKIQGK-----TIPtDDNVVCFTRHEPVGVCG 150
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAAWdmDDVAGCFE---YYADLAEALDAKqkapvSLP-METFKGYVLKEPLGVVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 151 AITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEV-------------------------------- 198
Cdd:PLN02467 157 LITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVglppgvlnvvtglgteagaplashpgvdkiaf 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 199 ------GKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSV 272
Cdd:PLN02467 237 tgstatGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 273 EFAKKRPVGDPFdvrtEQGPQGGAPSSSG-------YVPVpsGQRTAPALSHRGPRDRVdlavqcaHQGVFFNQGQ---C 342
Cdd:PLN02467 316 KWAKNIKISDPL----EEGCRLGPVVSEGqyekvlkFIST--AKSEGATILCGGKRPEH-------LKKGFFIEPTiitD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 343 CTAASRVFVEEqVYA------EFVR--RSVEFAK------------------KR-----------INCYNAIYAQAPFGG 385
Cdd:PLN02467 383 VTTSMQIWREE-VFGpvlcvkTFSTedEAIELANdshyglagavisndlercERvseafqagivwINCSQPCFCQAPWGG 461
|
490 500
....*....|....*....|....*
gi 1331431699 386 FKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:PLN02467 462 IKRSGFGRELGEWGLENYLSVKQVT 486
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
10-409 |
4.56e-78 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 249.99 E-value: 4.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTDD-NVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:PLN02278 105 AQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRSn 210
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQagippgvlnvvmgdapeigdallaspkvrkitftgstaVGKKLMAGAAAT- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQ 290
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 291 GPQGGAPS------------SSGYVPVPSGQRTAPALSHRGPR--DRVDLAVQCAHQGVFfnqGQccTAASRVFVEEQ-- 354
Cdd:PLN02278 343 GPLINEAAvqkveshvqdavSKGAKVLLGGKRHSLGGTFYEPTvlGDVTEDMLIFREEVF---GP--VAPLTRFKTEEea 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331431699 355 --------------VYAEFVRRSVEFAKKR------INCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:PLN02278 418 iaiandteaglaayIFTRDLQRAWRVSEALeygivgVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
26-413 |
2.82e-77 |
|
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: 246.90 E-value: 2.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHAF 105
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTP 185
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 186 LTTLHLGSLIQEV-------------------------------------GKLVKEAASRSnLKRVTLELGGKNPCIVCA 228
Cdd:cd07107 157 LSALRLAELAREVlppgvfnilpgdgatagaalvrhpdvkrialigsvptGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 229 DADLDLAVQCAHQGVFFN-QGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQG---------------- 291
Cdd:cd07107 236 DADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGplvsrqqydrvmhyid 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 292 ---------------PQGGAPSSSGYVP------VPSGQRTA------PALSHRGPRDRVDLAVQCahQGVFFnqGQCCT 344
Cdd:cd07107 316 sakregarlvtgggrPEGPALEGGFYVEptvfadVTPGMRIAreeifgPVLSVLRWRDEAEMVAQA--NGVEY--GLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331431699 345 aasrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 413
Cdd:cd07107 392 ----IWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
10-411 |
1.46e-76 |
|
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: 245.55 E-value: 1.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSkSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK---EWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAF-----FIDLegCvktlRYFAGWADKIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLMLA 163
Cdd:cd07086 78 GRLVSLEMGKILPEGLgevqeMIDI--C----DYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 164 WKLAPALCCGNTIVVKPAEQTPLTTL-----------------HLGSLIQ------------------------EVGKLV 202
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIavtkilaevleknglppGVVNLVTgggdggellvhdprvplvsftgstEVGRRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 203 KEAASRSNlKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGD 282
Cdd:cd07086 232 GETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 283 PFDVRTEQGP-------------------QGGAPSSSGYVPV--PSGQRTAPALShRGPRDrvDLAVqcAHQGVF----- 336
Cdd:cd07086 311 PLDEGTLVGPlinqaavekylnaieiaksQGGTVLTGGKRIDggEPGNYVEPTIV-TGVTD--DARI--VQEETFapily 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 337 ------FNQ--------GQCCTAAsrvfveeqVYAEFVRRSVEFAKKRINCYNAIY---------AQAPFGGFKMSGNGR 393
Cdd:cd07086 386 vikfdsLEEaiainndvPQGLSSS--------IFTEDLREAFRWLGPKGSDCGIVNvniptsgaeIGGAFGGEKETGGGR 457
|
490
....*....|....*...
gi 1331431699 394 ELGEYALAEYTEVKTVTI 411
Cdd:cd07086 458 ESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-411 |
4.95e-75 |
|
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: 240.69 E-value: 4.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 24 FATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLH 103
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 104 AFFiDLEGCVKTLRYFAGWADKIQGKTIPTDDN-VVCFTRHEPVGVCGAITPWNFPLLmLAWK-LAPALCCGNTIVVKPA 181
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLI-LATKkVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASRsNLKRVTLELGGKNP 223
Cdd:cd07150 156 EETPVIGLKIAEIMEEaglpkgvfnvvtgggaevgdelvddprvrmvtftgstaVGREIAEKAGR-HLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 224 CIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP----------- 292
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPlisprqverik 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 --------QGGAPSSSGYVpvpSGQRTAPALSHRGPRD------------RVDLAVQCAHQGVFFNQGQCCTAASRVFVE 352
Cdd:cd07150 315 rqvedavaKGAKLLTGGKY---DGNFYQPTVLTDVTPDmrifreetfgpvTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331431699 353 EQVYAEFVRRSVEFAKKRINCyNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07150 392 DLQRAFKLAERLESGMVHIND-PTILdeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
27-411 |
2.08e-74 |
|
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: 239.42 E-value: 2.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSAWRRLDapsRGHLLHQLADLVERDRAILATLETMDTGKPfLHAFF 106
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYE---RAEILERAAQLLEERREEFARTIALEAGKP-IKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPA 181
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASrsnLKRVTLELGGKNP 223
Cdd:cd07149 160 SQTPLSALKLAELLLEaglpkgalnvvtgsgetvgdalvtdprvrmisftgspaVGEAIARKAG---LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 224 CIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP----------- 292
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPmiseaeaerie 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 --------------QGGAPSSSGYVP-----VPSGQRT------APALSHRgPRDRVDLAVQCA-------HQGVFFNQG 340
Cdd:cd07149 317 ewveeaveggarllTGGKRDGAILEPtvltdVPPDMKVvceevfAPVVSLN-PFDTLDEAIAMAndspyglQAGVFTNDL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331431699 341 QCCTAASRvfvEEQVYAEFVRRSVEFakkRINcynaiyaQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07149 396 QKALKAAR---ELEVGGVMINDSSTF---RVD-------HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
24-411 |
1.00e-73 |
|
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: 237.63 E-value: 1.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 24 FATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLH 103
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 104 AFfIDLEGCVKTLRYFAGWADKIQGKTIPTDD-----NVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVV 178
Cdd:cd07145 78 SR-VEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 179 KPAEQTPLTTLHLGSLIQEVG---------------------------------------KLVKEAASRsnLKRVTLELG 219
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGlppgvinvvtgygsevgdeivtnpkvnmisftgstavglLIASKAGGT--GKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 220 GKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP------- 292
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPlispeav 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 ------------QGG-------APSSSGYVPVPSGQRT--------------APALSHRGPRDRVDLAvqcahqgvffNQ 339
Cdd:cd07145 315 ermenlvndaveKGGkilyggkRDEGSFFPPTVLENDTpdmivmkeevfgpvLPIAKVKDDEEAVEIA----------NS 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 340 GQCCTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAI-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07145 385 TEYGLQAS-VFTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
45-411 |
1.95e-73 |
|
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: 235.89 E-value: 1.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 45 DVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWAD 124
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 125 KIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLmLAWK-LAPALCCGNTIVVKPAEQTPLTT-------------- 188
Cdd:cd07104 77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLI-LAMRsVAPALALGNAVVLKPDSRTPVTGglliaeifeeaglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 189 ---LHL----GSLIQE------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGV 243
Cdd:cd07104 156 kgvLNVvpggGSEIGDalvehprvrmisftgstaVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 244 FFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPqggapsssgyvpvpsgqrtapaLSHRGPRDR 323
Cdd:cd07104 235 FLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGP----------------------LINERQVDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 324 VDLAVQCA------------HQGVFF------NqgqcCTAASRVFVEE------------------------------QV 355
Cdd:cd07104 293 VHAIVEDAvaagarlltggtYEGLFYqptvlsD----VTPDMPIFREEifgpvapvipfdddeeavelandteyglsaAV 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 356 YAEFVRRSVEFAKK------RINCYNAI-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07104 369 FTRDLERAMAFAERletgmvHINDQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
9-411 |
5.33e-73 |
|
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: 235.93 E-value: 5.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGsAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAG------WADKIQGKTipTDDNVVcftRHEPVGVCGAITPWNFPLLML 162
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAAlardfpFEERRPGSG--GGHVLV---RREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 163 AWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEA 205
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEaglppgvvnvvpadrevgeylvrhpgvdkvsftgstaAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 206 ASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFD 285
Cdd:cd07139 235 CGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 286 VRTEQGP--------------QGGapSSSGYVPVPSGQRtaPALSHRG------------------------------PR 321
Cdd:cd07139 314 PATQIGPlasarqrervegyiAKG--RAEGARLVTGGGR--PAGLDRGwfveptlfadvdndmriaqeeifgpvlsviPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 322 DRVDLAVQCAHQGVFFNQGQCCTAAsrvfvEEQVYAefVRRSVEFAKKRINCYnAIYAQAPFGGFKMSGNGRELGEYALA 401
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTAD-----VERGLA--VARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLD 461
|
490
....*....|
gi 1331431699 402 EYTEVKTVTI 411
Cdd:cd07139 462 AYLETKSIYL 471
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
10-413 |
3.08e-70 |
|
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: 229.22 E-value: 3.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSksGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAfQRGSaWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA-LKGP-WGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAgwaDKIqgKTIPTD---------DNVVCFTRHEPVGVCGAITPWNFPLL 160
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFA---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 161 MLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVG----------------------------------------K 200
Cdd:TIGR03216 155 LMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGvpkgvynvvhgfgpdsagefltrhpgvdaitftgetrtgsA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 201 LVKEAAsrSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPV 280
Cdd:TIGR03216 235 IMKAAA--DGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 281 GDPFDVRTEQGP-------------------QGGAPSSSGYVPVPSGQRTAPA------------------------LSH 317
Cdd:TIGR03216 313 GVPDDPATNMGPlisaehrdkvlsyyalaveEGATVVTGGGVPDFGDALAGGAwvqptiwtglpdsarvvteeifgpCCH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 318 RGPRDRVDLAVQCAHQGVFfnqGQCCTaasrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGE 397
Cdd:TIGR03216 393 IAPFDSEEEVIALANDTPY---GLAAS----VWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGV 465
|
490
....*....|....*.
gi 1331431699 398 YALAEYTEVKTVTIKL 413
Cdd:TIGR03216 466 HSLEFYTELTNVCIKL 481
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-411 |
3.38e-68 |
|
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: 223.08 E-value: 3.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 28 NPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFfI 107
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 108 DLEGCVKTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAE 182
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 183 QTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASrsnLKRVTLELGGKNPC 224
Cdd:cd07094 161 KTPLSALELAKILVEagvpegvlqvvtgerevlgdafaadervamlsftgsaaVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 225 IVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQ----------- 293
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLiseeaaerver 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 294 --------------GGAPSSSGYVP-----VPsgqRTAPALSHR--GP------RDRVDLAVQCA-------HQGVFfnq 339
Cdd:cd07094 318 wveeaveagarllcGGERDGALFKPtvledVP---RDTKLSTEEtfGPvvpiirYDDFEEAIRIAnstdyglQAGIF--- 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331431699 340 gqccTAASRVFVEeqvyaefVRRSVEFAKKRINCYNAIYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07094 392 ----TRDLNVAFK-------AAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-411 |
9.18e-68 |
|
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: 222.71 E-value: 9.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPA 169
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 170 LCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEAASRsNLK 212
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDllppgvvnvvngfgleagkplasskriakvaftgettTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 213 RVTLELGGKNPCIVCA------DADLDLAVQCAhqGVF-FNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFD 285
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 286 VRTEQGPQ-------------------------GGAPSSSG-------YVP--VPSGQRT--------APALSHRGPRDR 323
Cdd:cd07116 318 TETMIGAQasleqlekilsyidigkeegaevltGGERNELGgllgggyYVPttFKGGNKMrifqeeifGPVLAVTTFKDE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 324 VDlAVQCAHQGVFfnqgqccTAASRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEY 403
Cdd:cd07116 398 EE-ALEIANDTLY-------GLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHY 469
|
....*...
gi 1331431699 404 TEVKTVTI 411
Cdd:cd07116 470 QQTKNLLV 477
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
9-410 |
1.98e-66 |
|
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: 220.17 E-value: 1.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHgsKSGKKFATYNPS-TLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRA 87
Cdd:cd07124 35 LVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 88 ILATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLA 167
Cdd:cd07124 110 ELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 168 PALCCGNTIVVKPAEQTPLTTLHLGSLIQEVG------------------KLVK--------------------EAASR- 208
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGlppgvvnflpgpgeevgdYLVEhpdvrfiaftgsrevglriyERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 209 ----SNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPF 284
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 285 DVRTEQGP------------------------QGGAPSSSG----YVP------VPSGQRTA------PALSHRGPRDrV 324
Cdd:cd07124 349 DPEVYMGPvidkgardrirryieigksegrllLGGEVLELAaegyFVQptifadVPPDHRLAqeeifgPVLAVIKAKD-F 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 325 DLAVQCAHQGVFfnqgqCCTAAsrVFVEEQVYAEFVRRSVEFAKKRIN--CYNAIYAQAPFGGFKMSG-NGRELGEYALA 401
Cdd:cd07124 428 DEALEIANDTEY-----GLTGG--VFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLL 500
|
....*....
gi 1331431699 402 EYTEVKTVT 410
Cdd:cd07124 501 QFMQPKTVT 509
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
26-410 |
1.43e-65 |
|
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: 216.44 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 26 TYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqRGSAWRRlDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAF 105
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FiDLEGCVKTLRYFAGWADKIQGKTI-PTDDNVVCFTRhEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQT 184
Cdd:cd07120 79 F-EISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 185 PLTTLHLGSLIQEV---------------------------------------GKLVKEAASrSNLKRVTLELGGKNPCI 225
Cdd:cd07120 157 AQINAAIIRILAEIpslpagvvnlftesgsegaahlvaspdvdvisftgstatGRAIMAAAA-PTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 226 VCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP------------- 292
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPlidranvdrvdrm 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 ------QG------GAPSSSGYvpvPSGQRTAPAL-SHRGPRDRV------------------DLAVQCAHQGVFfnqGq 341
Cdd:cd07120 316 veraiaAGaevvlrGGPVTEGL---AKGAFLRPTLlEVDDPDADIvqeeifgpvltletfddeAEAVALANDTDY---G- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331431699 342 ccTAASrVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:cd07120 389 --LAAS-VWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
27-407 |
6.68e-61 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 203.82 E-value: 6.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAff 106
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAF---KTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 idlEGCVKT----LRYFAGWADKIQGKTIPT--DDNVVCFTRhEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKP 180
Cdd:TIGR01780 77 ---KGEILYaasfLEWFAEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 181 AEQTPLTTLHLGSLIQE---------------------------------------VGK-LVKEAAsrSNLKRVTLELGG 220
Cdd:TIGR01780 153 AEQTPLSALALARLAEQagipkgvlnvitgsrakevgnvlttsplvrkisftgstnVGKiLMKQSA--STVKKVSMELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 221 KNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP-------- 292
Cdd:TIGR01780 231 NAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPlinekave 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 ----QGGAPSSSGYVPVPSGQRT-------APA-LSHrgprdrVDLAVQCAHQGVFfnqGQCCTAASRVFVEEQV----- 355
Cdd:TIGR01780 311 kvekHIADAVEKGAKVVTGGKRHelggnffEPTvLSN------VTADMLVSKEETF---GPLAPVFKFDDEEEVIaiand 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331431699 356 ---------YAEFVRRSVEFAKK----RINCYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVK 407
Cdd:TIGR01780 382 tevglaayfFSRDLSRIWRVAEAleygMVGINTGLISnvVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
46-411 |
6.70e-60 |
|
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: 200.76 E-value: 6.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 46 VDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF-IDLegCVKTLRYFAGWAD 124
Cdd:cd07100 1 IEAALDRAHAAFL---AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 125 K-IQGKTIPTDDNVvCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVG---- 199
Cdd:cd07100 76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGfpeg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 200 ------------------KLVK-------EAASRS-------NLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQ 247
Cdd:cd07100 155 vfqnllidsdqveaiiadPRVRgvtltgsERAGRAvaaeagkNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 248 GQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPqggapsssgyvpvpsgqrtapaLSHRGPRDRVDLA 327
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGP----------------------LARKDLRDELHEQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 328 VQCA---------------HQGVFF------NqgqcCTAASRVFVEE------QVY-----AEFVR-------------- 361
Cdd:cd07100 293 VEEAvaagatlllggkrpdGPGAFYpptvltD----VTPGMPAYDEElfgpvaAVIkvkdeEEAIAlandspfglggsvf 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331431699 362 -----RSVEFAKK------RINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07100 369 ttdleRAERVARRleagmvFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
13-412 |
3.73e-59 |
|
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: 199.84 E-value: 3.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 13 NEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAfQRgsAWRRLDAPSRGHLLHQLADLVERDRAILATL 92
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 93 ETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTD----DNVVcftRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:cd07151 78 LIRESGSTRIKAN-IEWGAAMAITREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLT----------------------------------TLHLGSLIQ-----EVGKLVKEAASRs 209
Cdd:cd07151 154 ALALGNAVVLKPASDTPITgglllakifeeaglpkgvlnvvvgagseigdafvEHPVPRLISftgstPVGRHIGELAGR- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 210 NLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTE 289
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 290 QGPQGGAPSSSGYVPVPSGQRTAPA-LSHRGPRDrvDLAVqcaHQGVFFNqgqcCTAASRVFVEE--------------- 353
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGAtLLVGGEAE--GNVL---EPTVLSD----VTNDMEIAREEifgpvapiikaddee 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 354 ---------------QVYAEFVRRSVEFAkKRINC----YNAI----YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:cd07151 384 ealelandteyglsgAVFTSDLERGVQFA-RRIDAgmthINDQpvndEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
..
gi 1331431699 411 IK 412
Cdd:cd07151 463 VQ 464
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
27-411 |
3.15e-57 |
|
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: 194.36 E-value: 3.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHAFF 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQ---RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADKIQGKT-IPTDD---NVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAE 182
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVLAPRkVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 183 QTPLTTLHLGSLIQEV------------------------------------GKLVKEAASRsNLKRVTLELGGKNPCIV 226
Cdd:cd07099 157 VTPLVGELLAEAWAAAgppqgvlqvvtgdgatgaalidagvdkvaftgsvatGRKVMAAAAE-RLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 227 CADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP-----Q-------- 293
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPmttarQldivrrhv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 294 ------------GGAPSSSG--YVP------VPSG-----QRT-APALSHRGPRDrVDLAVQCAhqgvffNQGQCCTAAS 347
Cdd:cd07099 316 ddavakgakaltGGARSNGGgpFYEptvltdVPHDmdvmrEETfGPVLPVMPVAD-EDEAIALA------NDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331431699 348 rVFVEEQVYAEFVRRSVEFAKKRINC--YNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07099 389 -VFSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-411 |
3.30e-57 |
|
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: 194.11 E-value: 3.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 28 NPSTLEKICDVEEGDKPDVDMAVEAARAafQRGsawrRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFi 107
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALAAS--YRS----TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 108 DLEGCVKTLRYFAGWADKIQGKTIPTDDNV-----VCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAE 182
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 183 QTPLTTLHLGSLIQE--------------------------------------VGKLVKEAASrsnLKRVTLELGGKNPC 224
Cdd:cd07146 158 KTPLSAIYLADLLYEaglppdmlsvvtgepgeigdelithpdvdlvtftggvaVGKAIAATAG---YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 225 IVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP------------ 292
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTvideeaaiqien 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 ------QGGAPSSSGyvPVPSGQRTAPALSHRGPRD----------------RV---DLAVQCAHQGVFFNQGQCCT--- 344
Cdd:cd07146 315 rveeaiAQGARVLLG--NQRQGALYAPTVLDHVPPDaelvteetfgpvapviRVkdlDEAIAISNSTAYGLSSGVCTndl 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331431699 345 -AASRVFVEEQVYAEFVRRSVEFAKKRIncynaiyaqaPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 411
Cdd:cd07146 393 dTIKRLVERLDVGTVNVNEVPGFRSELS----------PFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
45-411 |
4.66e-55 |
|
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: 188.17 E-value: 4.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 45 DVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWAD 124
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 125 KIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE------ 197
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEaglpkg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 -----------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQG 242
Cdd:cd07105 157 vlnvvthspedapevvealiahpavrkvnftgstrVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 243 VFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGD--PFDVRTEQG------------------PQGGAPSSSgy 302
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPvvLGSLVSAAAadrvkelvddalskgaklVVGGLADES-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 303 vpvPSGQRTAPA-LSHR------------GPR------DRVDLAVQCAhqgvffNQGQCCTAASrVFVEEQVYAEFVRRS 363
Cdd:cd07105 314 ---PSGTSMPPTiLDNVtpdmdiyseesfGPVvsiirvKDEEEAVRIA------NDSEYGLSAA-VFTRDLARALAVAKR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1331431699 364 VEFAKKRINCYNaIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07105 384 IESGAVHINGMT-VHdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
9-292 |
2.77e-54 |
|
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: 187.01 E-value: 2.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 9 IFINNEWHGSkSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgSAWRRLDAPSRGHLLHQLADLVERDRAI 88
Cdd:cd07082 4 YLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPVGVCGAITPWNFPLLMLA 163
Cdd:cd07082 81 VANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 164 WKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQ--------------------------------------EVGKLVKEA 205
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHdagfpkgvvnvvtgrgreigdplvthgridvisftgstEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 206 ASRsnlKRVTLELGGKNPCIVCADADLDLAVQ-CAHQGVFFNqGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPF 284
Cdd:cd07082 240 HPM---KRLVLELGGKDPAIVLPDADLELAAKeIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
....*...
gi 1331431699 285 DVRTEQGP 292
Cdd:cd07082 316 DNGVDITP 323
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-411 |
1.96e-53 |
|
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: 184.03 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 45 DVDMAVEAARAAfQRgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWAD 124
Cdd:cd07152 14 DVDRAAARAAAA-QR--AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAAIGELHEAAGLPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 125 KIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLT----------------- 187
Cdd:cd07152 90 QPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviarlfeeaglpag 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 188 TLHL-----------------------GSliQEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVF 244
Cdd:cd07152 170 VLHVlpggadagealvedpnvamisftGS--TAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASNGAWGAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 245 FNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPqggapsssgyvpvpsgqrtapaLSHRGPRDRV 324
Cdd:cd07152 247 LHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGP----------------------LINARQLDRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 325 DLAVQCA------------HQGVFFN----QGqcCTAASRVFVEE---QVYAEFVRRSVEFAKKRINC--YN---AIY-- 378
Cdd:cd07152 305 HAIVDDSvaagarleaggtYDGLFYRptvlSG--VKPGMPAFDEEifgPVAPVTVFDSDEEAVALANDteYGlsaGIIsr 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331431699 379 ---------------------------AQAPFGGFKMSGNGRELGEYA-LAEYTEVKTVTI 411
Cdd:cd07152 383 dvgramaladrlrtgmlhindqtvndePHNPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-410 |
1.77e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 183.54 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 18 SKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAfQRgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDT 97
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QR--AWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 98 GKPFLHAF--FIDLegcVKTLRYFAGWADKI------QGkTIPTDDNVVcfTRHEPVGVCGAITPWNFPLLMLAWKLAPA 169
Cdd:PRK09407 105 GKARRHAFeeVLDV---ALTARYYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 170 LCCGNTIVVKPAEQTPLTTLHLGSLIQE------------------------------------VGKLVKEAASRsNLKR 213
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEaglprdlwqvvtgpgpvvgtalvdnadylmftgstaTGRVLAEQAGR-RLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 214 VTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQ 293
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 294 GGAP---SSSGYV--------PVPSGQR------------------TAPALSHR----GP------RDRVDLAVQCAHQG 334
Cdd:PRK09407 338 ISEAqleTVSAHVddavakgaTVLAGGKarpdlgplfyeptvltgvTPDMELAReetfGPvvsvypVADVDEAVERANDT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 335 VF-FNqgqcctaASrvfveeqVYAEFVRRSVEFAkKRINC--------YNAIYA--QAPFGGFKMSGNGRELGEYALAEY 403
Cdd:PRK09407 418 PYgLN-------AS-------VWTGDTARGRAIA-ARIRAgtvnvnegYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKY 482
|
....*..
gi 1331431699 404 TEVKTVT 410
Cdd:PRK09407 483 TESQTIA 489
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-292 |
3.86e-52 |
|
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: 181.56 E-value: 3.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP---AWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAffidlEGCVktLR-----YFA-GWADKIQGKTIP-TDDNVVCFTRHEPVGVCGAITPWNFPLLML 162
Cdd:cd07085 81 ARLITLEHGKTLADA-----RGDV--LRglevvEFAcSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 163 AWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEA 205
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEaglpdgvlnvvhggkeavnalldhpdikavsfvgstpVGEYIYER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 206 ASRSNlKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFD 285
Cdd:cd07085 234 AAANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
....*..
gi 1331431699 286 VRTEQGP 292
Cdd:cd07085 313 PGADMGP 319
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
27-411 |
4.90e-52 |
|
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: 180.52 E-value: 4.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF 106
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP---MRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 iDLEGCVKTLRYFAGWADKIQGKTIPTD-----DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPA 181
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQE-------------------------------------VGKLVKEAASRsnlKRVTLELGGKNPC 224
Cdd:cd07147 160 SRTPLSALILGEVLAEtglpkgafsvlpcsrddadllvtderikllsftgspaVGWDLKARAGK---KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 225 IVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP---QGGAPSSSG 301
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPmisESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 302 YV--PVPSGQRTAPALSHRGPR------DRVDLAVQCAHQGVFfnqgqcctaASRVFVEEqvYAEFvrrsvEFAKKRIN- 372
Cdd:cd07147 317 WVneAVDAGAKLLTGGKRDGALleptilEDVPPDMEVNCEEVF---------GPVVTVEP--YDDF-----DEALAAVNd 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331431699 373 -------------CYNAIYA--------------------QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:cd07147 381 skfglqagvftrdLEKALRAwdelevggvvindvptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
29-410 |
2.34e-51 |
|
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: 178.66 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 29 PSTLEKICDVEEGDKPDVDMAVEAARAAfQRgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFfID 108
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QR--AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 109 LEGCVKTLRYFAGWADKI-----QGKTIPT-DDNVVCftrHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAE 182
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 183 QTPLTTLHLGSLIQE------------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIV 226
Cdd:cd07101 156 QTALTALWAVELLIEaglprdlwqvvtgpgsevggaivdnadyvmftgstaTGRVVAERAGR-RLIGCSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 227 CADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP---QGGAPSSSGYV 303
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSlisQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 304 --PVPSGqrtapALSHRGPRDRVDLavqcahqGVFF----------NQGQCCT--------AASRVFVEEQ--------- 354
Cdd:cd07101 315 ddAVAKG-----ATVLAGGRARPDL-------GPYFyeptvltgvtEDMELFAeetfgpvvSIYRVADDDEaielandtd 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331431699 355 ------VYAEFVRRSVEFAkKRINC--------YNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:cd07101 383 yglnasVWTRDGARGRRIA-ARLRAgtvnvnegYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
2-413 |
2.49e-51 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 179.33 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 2 TTSFPG*IFINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADL 81
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 82 VERDRAILATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGKTIP---TDDNVVCFTrhEPVGVCGAITPWNFP 158
Cdd:PRK11241 83 MMEHQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPghqADKRLIVIK--QPIGVTAAITPWNFP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 159 LLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQ--------------------------------------EVGK 200
Cdd:PRK11241 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIragipagvfnvvtgsagavggeltsnplvrklsftgstEIGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 201 LVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPV 280
Cdd:PRK11241 240 QLMEQCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 281 GDPFDVRTEQGP-------------------------QGGAPSSSG--------YVPVPSGQRTAPALSHrGP------- 320
Cdd:PRK11241 319 GDGLEKGVTIGPlidekavakveehiadalekgarvvCGGKAHELGgnffqptiLVDVPANAKVAKEETF-GPlaplfrf 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 321 RDRVDLAVQCahqgvffNQGQCCTAA-------SRVFVeeqvyaefVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGR 393
Cdd:PRK11241 398 KDEADVIAQA-------NDTEFGLAAyfyardlSRVFR--------VGEALEYGIVGINTGIISNEVAPFGGIKASGLGR 462
|
490 500
....*....|....*....|
gi 1331431699 394 ELGEYALAEYTEVKTVTIKL 413
Cdd:PRK11241 463 EGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
12-292 |
9.74e-48 |
|
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: 169.69 E-value: 9.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 12 NNEWHGSksGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILAT 91
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK---EWRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 92 LETMDTGKPFLHAF-----FIDLegCvktlRYFAGWADKIQGKTIPTD--DNVVCFTRHePVGVCGAITPWNFPLLMLAW 164
Cdd:cd07130 79 LVSLEMGKILPEGLgevqeMIDI--C----DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 165 KLAPALCCGNTIVVKPAEQTPLTTL-----------------HLGSLIQ------------------------EVGKLVK 203
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIavtkivarvleknglpgAIASLVCggadvgealvkdprvplvsftgstAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 204 EAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDP 283
Cdd:cd07130 232 QAVAA-RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
....*....
gi 1331431699 284 FDVRTEQGP 292
Cdd:cd07130 311 LDDGTLVGP 319
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-413 |
2.87e-47 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 169.35 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 11 INNEWhgSKSGKKFATYNPS-TLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PRK03137 41 IGGER--ITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFA----GWADKIQGKTIPTDDNvvcFTRHEPVGVCGAITPWNFPLLMLAWK 165
Cdd:PRK03137 116 SAWLVKEAGKPWAEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 166 LAPALCCGNTIVVKPAEQTPLTTLHL----------------------------------------GSLiqEVGKLVKEA 205
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFvevleeaglpagvvnfvpgsgsevgdylvdhpktrfitftGSR--EVGLRIYER 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 206 ASRSN-----LKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPV 280
Cdd:PRK03137 270 AAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 281 GDPFDVR-----------------TEQGPQ-------GGAPSSSGYV--P-----VPSGQRTA------PALSHRGPRDr 323
Cdd:PRK03137 350 GNPEDNAymgpvinqasfdkimsyIEIGKEegrlvlgGEGDDSKGYFiqPtifadVDPKARIMqeeifgPVVAFIKAKD- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 324 VDLAVQCAHqgvffNQGQCCTAAsrvfveeqVYAEfVRRSVEFAKKRI---------NCYNAIYAQAPFGGFKMSGNGRE 394
Cdd:PRK03137 429 FDHALEIAN-----NTEYGLTGA--------VISN-NREHLEKARREFhvgnlyfnrGCTGAIVGYHPFGGFNMSGTDSK 494
|
490 500
....*....|....*....|.
gi 1331431699 395 LG--EYaLAEYTEVKTVTIKL 413
Cdd:PRK03137 495 AGgpDY-LLLFLQAKTVSEMF 514
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-298 |
9.06e-47 |
|
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: 166.65 E-value: 9.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQ-LADLVERDRAILATLETMdTGKPFLHAF 105
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK---GWRAVPLEERKAIVTRaVELLAANTDEIAEELTWQ-MGRPIAQAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 FiDLEGCVKTLRYFAGWADK-IQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQT 184
Cdd:cd07102 77 G-EIRGMLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 185 PLTTLHLGSLIQEVG-----------------KLVKEA-------------------ASRSNLKRVTLELGGKNPCIVCA 228
Cdd:cd07102 156 PLCGERFAAAFAEAGlpegvfqvlhlshetsaALIADPridhvsftgsvaggraiqrAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 229 DADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGPQGGAPS 298
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARA 305
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-411 |
8.82e-45 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 161.44 E-value: 8.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 25 ATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPfLHA 104
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 105 FFIDLEGCVKTLRYFAGWADKIQGKTiPTDDNVV----CFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKP 180
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 181 AEQTPLTTLHLGSLIQEVG--------KLV---------------------KEAASRS-------NLKRVTLELGGKNPC 224
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGfpdgcfqtLLVgsgaveailrdprvaaatltgSEPAGRAvaaiagdEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 225 IVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP----QG------ 294
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPlateQGrdevek 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 295 --------GA--------PSSSG--YVPVPSGQRTAPALSHR----GP------RDRVDLAVQCAHQGVFfnqgqccTAA 346
Cdd:PRK09406 319 qvddavaaGAtilcggkrPDGPGwfYPPTVITDITPDMRLYTeevfGPvaslyrVADIDEAIEIANATTF-------GLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331431699 347 SRVFVEEQVYAEFVRRSVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 411
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
20-409 |
1.70e-44 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 161.09 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 20 SGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgSAWRRlDAPSRGHLLHQLADLVERDRAILATLETMDTGK 99
Cdd:TIGR04284 13 SAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSR-DTALRVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 100 PFLHAFFIDLEGCVKTLRYFAGWADKIQGKT---------IPTDDNVvcftRHEPVGVCGAITPWNFPLLMLAWKLAPAL 170
Cdd:TIGR04284 91 PRMLTAGAQLEGPVDDLGFAADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 171 CCGNTIVVKPAEQTPLTTLHLGSLIQE------------------VGKLVKE--------------------AASRSNLK 212
Cdd:TIGR04284 167 AAGNTVVLKPAPDTPWCAAVLGELIAEhtdfppgvvnivtssdhrLGALLAKdprvdmvsftgstatgravmADAAATLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 213 RVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP 292
Cdd:TIGR04284 247 KVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 293 -------------------QGGAPSSSGYVPV--PSGQRTAPAL------SHRGPRDRVDLAVQC--AHQGVffNQGQCC 343
Cdd:TIGR04284 327 visarqrdrvqsyldlavaEGGRFACGGGRPAdrDRGFFVEPTViagldnNARVAREEIFGPVLTviAHDGD--DDAVRI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331431699 344 TAASRVFVEEQVYAEFVRRSVEFAKK----RINCYNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:TIGR04284 405 ANDSPYGLSGTVFGADPERAAAVAARvrtgTVNVNGGVWysADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
23-410 |
5.85e-43 |
|
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: 157.33 E-value: 5.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 23 KFATYNPS-TLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPF 101
Cdd:TIGR01237 47 KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFE---AWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 102 LHAFfIDLEGCVKTLRYFAGWADKIQGK----TIPTDDNVVCFTrhePVGVCGAITPWNFPLLMLAWKLAPALCCGNTIV 177
Cdd:TIGR01237 124 NEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 178 VKPAEQTP---------------------------------LTTLHLGSLI-----QEVGKLVKEAASR-----SNLKRV 214
Cdd:TIGR01237 200 LKPAEAAPviaakfveileeaglpkgvvqfvpgsgsevgdyLVDHPKTSLItftgsREVGTRIFERAAKvqpgqKHLKRV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 215 TLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRT------ 288
Cdd:TIGR01237 280 IAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVyvgpvi 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 289 ------------EQGPQ-------GGAPSSSGYVPVPS----GQRTAPALSHR--GPRDRV------DLAVQCAHQGVFF 337
Cdd:TIGR01237 360 dqksfnkimeyiEIGKAegrlvsgGCGDDSKGYFIGPTifadVDRKARLAQEEifGPVVAFirasdfDEALEIANNTEYG 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331431699 338 NQGQCCTaASRVFVeEQVYAEFVRRSVEFAKkriNCYNAIYAQAPFGGFKMSGNGRELG--EYaLAEYTEVKTVT 410
Cdd:TIGR01237 440 LTGGVIS-NNRDHI-NRAKAEFEVGNLYFNR---NITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQAKTVT 508
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
116-283 |
1.16e-41 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 151.81 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 116 LRYFAGWADKIQGKTIPTD---DNVVCFTRhePVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLG 192
Cdd:PRK10090 41 IDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 193 SLIQEV--------------------------------------GKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 234
Cdd:PRK10090 119 KIVDEIglpkgvfnlvlgrgetvgqelagnpkvamvsmtgsvsaGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331431699 235 AVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDP 283
Cdd:PRK10090 198 AVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNP 246
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
27-410 |
3.88e-40 |
|
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: 148.99 E-value: 3.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF 106
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 ID-LEGCVKtLRYFAGWADK-IQGKTIPTddNVVCFTR-----HEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVK 179
Cdd:cd07098 78 GEiLVTCEK-IRWTLKHGEKaLRPESRPG--GLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 180 PAEQTPLTTLHLGSLIQE-----------------------------------------VGKLVKEAASRSnLKRVTLEL 218
Cdd:cd07098 155 VSEQVAWSSGFFLSIIREclaacghdpdlvqlvtclpetaealtshpvidhitfigsppVGKKVMAAAAES-LTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 219 GGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRteqgPQGGAPS 298
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGD----VDVGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 299 SSGYV---------PVPSGQRTApALSHRGPRDR--------------VDLAVQCAHQGVF---------FNQGQCCTAA 346
Cdd:cd07098 310 SPARFdrleelvadAVEKGARLL-AGGKRYPHPEypqghyfpptllvdVTPDMKIAQEEVFgpvmvvmkaSDDEEAVEIA 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331431699 347 --------SRVFVEEQVYAEFVRRSVEFAKKRINCYNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 410
Cdd:cd07098 389 nsteyglgASVFGKDIKRARRIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
49-268 |
4.65e-36 |
|
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: 136.89 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 49 AVEAARAAFQRGS----AWRRldapsrgHLLHQLADLV-ERDRAILATLETmDTGKPFLHAFFIDLEGCVK----TLRYF 119
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRK-------AQLKALKRMLtENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGeidhALKHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 120 AGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLI---- 195
Cdd:cd07087 75 KKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIpkyf 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 196 -------------------------------QEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVF 244
Cdd:cd07087 155 dpeavavveggvevatallaepfdhifftgsPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
250 260
....*....|....*....|....
gi 1331431699 245 FNQGQCCTAASRVFVEEQVYAEFV 268
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDELI 257
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
27-292 |
5.90e-36 |
|
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: 138.10 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 27 YNPSTLEK-ICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAF 105
Cdd:cd07125 51 IDPADHERtIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 106 -----FIDLegcvktLRYFAGWADKIQGKTI---PTD--DNVVCftrhEPVGVCGAITPWNFPLLMLAWKLAPALCCGNT 175
Cdd:cd07125 128 aevreAIDF------CRYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 176 IVVKPAEQTPLT----------------TLHLgsLI---QEVGK-LVK-------------EAASRSNLKR-------VT 215
Cdd:cd07125 198 VIAKPAEQTPLIaaravellheagvprdVLQL--VPgdgEEIGEaLVAhpridgviftgstETAKLINRALaerdgpiLP 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331431699 216 L--ELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP 292
Cdd:cd07125 276 LiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGP 354
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
28-409 |
1.32e-35 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 136.53 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 28 NPSTLEKICDVEEGDKPDVDMAVEAARAAFQRgsaWRRLDAPSRGHLLHQLADLVeRDRAI-LATLETMDTGKPFLHAff 106
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSEeMAQMITREMGKPINQA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 idlEGCVKTLRYFAGWADKiQG----KTIPT-DDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPA 181
Cdd:PRK13968 87 ---RAEVAKSANLCDWYAE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQEVG-----------------KLVKE-------------------AASRSNLKRVTLELGGKNPCI 225
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGipqgvygwlnadndgvsQMINDsriaavtvtgsvragaaigAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 226 VCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDP------------FDVRTEQGPQ 293
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrdeenalgpmarFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 294 GGAPSSSG----------------YVPVPSGQRTAPALSHR----GPRDRVDLAVQCAHQGVFFNQGQCCTAASRVFVEE 353
Cdd:PRK13968 323 VEATLAEGarlllggekiagagnyYAPTVLANVTPEMTAFReelfGPVAAITVAKDAEHALELANDSEFGLSATIFTTDE 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331431699 354 QVYAEFVRRsVEFAKKRINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 409
Cdd:PRK13968 403 TQARQMAAR-LECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-292 |
1.38e-35 |
|
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: 136.39 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 28 NPSTLEKICDVEEGDKPDVDMAVEAARAAFQRGSAWrrLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFF- 106
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 ----ID-LEGCVKTLRYFAGwaDKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPA 181
Cdd:cd07148 83 vtraIDgVELAADELGQLGG--REIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 182 EQTPLTTLHLGSLIQEVG-----------------KLVKEAAS---------------RSNLK---RVTLELGGKNPCIV 226
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGlpegwcqavpcenavaeKLVTDPRVaffsfigsarvgwmlRSKLApgtRCALEHGGAAPVIV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331431699 227 CADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP 292
Cdd:cd07148 241 DRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGP 306
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-292 |
2.69e-34 |
|
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: 132.40 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 45 DVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAffidlEGCVKTLryfagwAD 124
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-----QTEVAAM------AG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 125 KIQ-----------GKTIPTDdNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGS 193
Cdd:cd07095 67 KIDisikayhertgERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 194 LIQEVG------KLVK------EAASRSN----------------LKRVT---------LELGGKNPCIVCADADLDLAV 236
Cdd:cd07095 146 LWEEAGlppgvlNLVQggretgEALAAHEgidgllftgsaatgllLHRQFagrpgkilaLEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331431699 237 QCAHQGVFFNQGQCCTAASRVFVEE-QVYAEFVRRSVEFAKKRPVGDPFDVRTEQGP 292
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGP 282
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
7-410 |
4.76e-32 |
|
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: 126.92 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 7 G*IFINNEWHGSKSGKkfATYNPS-TLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADLVERD 85
Cdd:cd07083 19 YPLVIGGEWVDTKERM--VSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 86 RAILATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGK-----TIPTDDNVvcfTRHEPVGVCGAITPWNFPLL 160
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPavevvPYPGEDNE---SFYVGLGAGVVISPWNFPVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 161 MLAWKLAPALCCGNTIVVKPAEQTPLTT------LH----------------------------------LGSLiqEVGK 200
Cdd:cd07083 170 IFTGMIVAPVAVGNTVIAKPAEDAVVVGykvfeiFHeagfppgvvqflpgvgeevgaylteherirginfTGSL--ETGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 201 LVKEAASR-----SNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFA 275
Cdd:cd07083 248 KIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 276 KKRPVGDPFDVRTEQGP-------------------------QGGAPSSSGY-------------VPVPSGQRTAPALS- 316
Cdd:cd07083 328 ERLSVGPPEENGTDLGPvidaeqeakvlsyiehgknegqlvlGGKRLEGEGYfvaptvveevppkARIAQEEIFGPVLSv 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 317 HRGPRDRVDLAVQCAHQ-------GVFFNQGQCCTAASRVFVEEQVYaeFVRRSVefakkrincyNAIYAQAPFGGFKMS 389
Cdd:cd07083 408 IRYKDDDFAEALEVANStpygltgGVYSRKREHLEEARREFHVGNLY--INRKIT----------GALVGVQPFGGFKLS 475
|
490 500
....*....|....*....|..
gi 1331431699 390 G-NGRELGEYALAEYTEVKTVT 410
Cdd:cd07083 476 GtNAKTGGPHYLRRFLEMKAVA 497
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
10-285 |
5.15e-32 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 126.61 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHgSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFF--------IDLEgcvktlryFAGWADKIQGKTIPTDDNVVCFtRHEPVGVCGAITPWNFPLLM 161
Cdd:PRK09457 80 AEVIARETGKPLWEAATevtaminkIAIS--------IQAYHERTGEKRSEMADGAAVL-RHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 162 LAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVG------KLV---KE-----AASR----------SNL------ 211
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGlpagvlNLVqggREtgkalAAHPdidgllftgsANTgyllhr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 212 -------KRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAE-FVRRSVEFAKKRPVGDP 283
Cdd:PRK09457 231 qfagqpeKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRW 310
|
..
gi 1331431699 284 FD 285
Cdd:PRK09457 311 DA 312
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
51-270 |
4.82e-31 |
|
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: 123.11 E-value: 4.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 51 EAARAAFQRgsaWRRLDAPSRGHLLHQLADLVERDRA-ILATLETmDTGKPFLHAFFIDLEGCVK----TLRYFAGWADK 125
Cdd:cd07134 5 AAQQAHALA---LRASTAAERIAKLKRLKKAILARREeIIAALAA-DFRKPAAEVDLTEILPVLSeinhAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 126 IQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------- 197
Cdd:cd07134 81 KRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREafdedeva 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 ---------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQC 250
Cdd:cd07134 161 vfegdaevaqallelpfdhifftgspaVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQT 239
|
250 260
....*....|....*....|
gi 1331431699 251 CTAASRVFVEEQVYAEFVRR 270
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEH 259
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
10-285 |
1.02e-30 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 123.33 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAfQRgsAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QK--AWAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAF--------FIDL---EGCvktlRYFAgwadkiQGKTIPTDD------NVVCFTRHEPVGVCGAI 152
Cdd:PLN00412 96 AECLVKEIAKPAKDAVtevvrsgdLISYtaeEGV----RILG------EGKFLVSDSfpgnerNKYCLTSKIPLGVVLAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 153 TPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHL----------GSLIQ-------EVGKLVKE----------- 204
Cdd:PLN00412 166 PPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMvhcfhlagfpKGLIScvtgkgsEIGDFLTMhpgvncisftg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 205 ------AASRSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKR 278
Cdd:PLN00412 246 gdtgiaISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
....*..
gi 1331431699 279 PVGDPFD 285
Cdd:PLN00412 326 TVGPPED 332
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-270 |
3.71e-30 |
|
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: 120.79 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 45 DVDMAVEAARAAFQRGsawRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFIDLEGC-------VKTLR 117
Cdd:cd07135 6 EIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVkndilhmLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 118 YFAgwadkiqgKTIPTDDNVVCF------TRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHL 191
Cdd:cd07135 83 KWA--------KDEKVKDGPLAFmfgkprIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 192 GSLIQE-----------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAV 236
Cdd:cd07135 155 AELVPKyldpdafqvvqggvpettalleqkfdkifytgsgrVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAA 233
|
250 260 270
....*....|....*....|....*....|....
gi 1331431699 237 QCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRR 270
Cdd:cd07135 234 KRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEE 267
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
49-277 |
8.53e-30 |
|
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: 120.02 E-value: 8.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 49 AVEAARAAFQRGsawRRLDAPSRGHLLHQLADLV-ERDRAILATLEtMDTGKPFLHAFFIDLEGCVKTLRY----FAGWA 123
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 124 -DKIQGKTIPT--DDnvvCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLI----- 195
Cdd:cd07132 79 kPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyld 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 196 ------------------------------QEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFF 245
Cdd:cd07132 156 kecypvvlggveettellkqrfdyifytgsTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFI 234
|
250 260 270
....*....|....*....|....*....|..
gi 1331431699 246 NQGQCCTAASRVFVEEQVYAEFvrrsVEFAKK 277
Cdd:cd07132 235 NAGQTCIAPDYVLCTPEVQEKF----VEALKK 262
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
139-277 |
1.07e-29 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 120.13 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 139 CFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTP-------------------------------LT 187
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPhtsklmaklltkyldpsyvrvieggvevtteLL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 188 TLHLGSLI----QEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQV 263
Cdd:PTZ00381 183 KEPFDHIFftgsPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
170
....*....|....
gi 1331431699 264 YAEFVRRSVEFAKK 277
Cdd:PTZ00381 262 KDKFIEALKEAIKE 275
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
142-278 |
5.49e-29 |
|
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: 117.59 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 142 RHEPVGVCGAITPWNFPLlMLAwkLAP---ALCCGNTIVVKPAEQTPLTTLHLGSLIQE--------------------- 197
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPL-YLA--LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEyfdedevavvtggadvaaafs 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 --------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQV 263
Cdd:cd07133 175 slpfdhllftgstaVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDK 253
|
170
....*....|....*
gi 1331431699 264 YAEFVRRSVEFAKKR 278
Cdd:cd07133 254 LEEFVAAAKAAVAKM 268
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
144-285 |
1.09e-28 |
|
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: 116.83 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 144 EPVGVCGAITPWNFPLLMLawkLAP---ALCCGNTIVVKPAEQTPLTTLHLGSLIQE----------------------- 197
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEEtfdeeyvavveggveenqelldq 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 ------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYA 265
Cdd:cd07136 176 kfdyifftgsvrVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKE 254
|
170 180
....*....|....*....|
gi 1331431699 266 EFVRRSVEFAKKRPVGDPFD 285
Cdd:cd07136 255 KFIKELKEEIKKFYGEDPLE 274
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-292 |
1.15e-28 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 117.63 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSksGKKFATYNPSTLEKICDVEEGDKPDVDmavEAARAAFQRGSAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PLN02315 24 YVGGEWRAN--GPLVSSVNPANNQPIAEVVEASLEDYE---EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKpFLHAFFIDLEGCVKTLRYFAGWADKIQGKTIPTD-DNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAP 168
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 169 ALCCGNTIVVKPAEQTPLTTLHLGSLIQEV----------------GKLVKEAASR------------------------ 208
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknnlpgaiftsfcgGAEIGEAIAKdtriplvsftgsskvglmvqqtvn 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 209 SNLKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRT 288
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGT 337
|
....
gi 1331431699 289 EQGP 292
Cdd:PLN02315 338 LLGP 341
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
10-292 |
1.62e-27 |
|
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: 113.82 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFlhaffIDLEGCV----KTLRYFAGWADKIQGKTIPT-DDNVVCFTRHEPVGVCGAITPWNFPLLMLAW 164
Cdd:TIGR01722 81 AELITAEHGKTH-----SDALGDVarglEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 165 KLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE-------------------------------------VGKLVKEAAS 207
Cdd:TIGR01722 156 MFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEagapdgvlnvvhgdkeavdrllehpdvkavsfvgstpIGRYIHTTGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 208 RSNlKRVTLELGGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVyAEFVRRSVEFAKKRPVGDPFDVR 287
Cdd:TIGR01722 236 AHG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPG 313
|
....*
gi 1331431699 288 TEQGP 292
Cdd:TIGR01722 314 AEMGP 318
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
52-261 |
3.48e-22 |
|
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: 98.08 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 52 AARAAFQRGSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFFIDleGCVKTLRYFA--GWADKIQGK 129
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENIC--GDQVQLRARAfvIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 130 TIPTDDNVVCFTRHE---PVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVGKLVKEAA 206
Cdd:cd07084 82 PGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 207 S---------------------------------RSNLK--RVTLELGGKNPCIVCADADL--DLAVQCAhQGVFFNQGQ 249
Cdd:cd07084 162 TlingdgktmqalllhpnpkmvlftgssrvaeklALDAKqaRIYLELAGFNWKVLGPDAQAvdYVAWQCV-QDMTACSGQ 240
|
250
....*....|..
gi 1331431699 250 CCTAASRVFVEE 261
Cdd:cd07084 241 KCTAQSMLFVPE 252
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
50-261 |
3.68e-21 |
|
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: 94.79 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 50 VEAARAAFQ----RGSAWRRLDapsrghlLHQLADLV-ERDRAILATLETmDTGKPFLHAFFIDL----EGCVKTLRYFA 120
Cdd:cd07137 5 VRELRETFRsgrtRSAEWRKSQ-------LKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVsvlvSSCKLAIKELK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 121 GWAD----KIQGKTIPTDDNVVCftrhEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQ 196
Cdd:cd07137 77 KWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 197 E-----------------------------------VGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVQCAHQ 241
Cdd:cd07137 153 EyldtkaikvieggvpettalleqkwdkifftgsprVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
|
250 260
....*....|....*....|.
gi 1331431699 242 GVF-FNQGQCCTAASRVFVEE 261
Cdd:cd07137 232 GKWgCNNGQACIAPDYVLVEE 252
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
10-199 |
1.49e-20 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 94.55 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWH-------GSKSGKKFATYNPS-TLEKICDVEEGDKPDVDMAVEAARAAFQrgsAWRRLDAPSRGHLLHQLADL 81
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 82 VERDRAILATLETMDTGKPFLHAffID-LEGCVKTLRYFAGwadkiQGKTIPTDDnvvcftRHEPVGVCGAITPWNFPLL 160
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANA--IAeVREAVDFLRYYAA-----QARRLLNGP------GHKPLGPVVCISPWNFPLA 691
|
170 180 190
....*....|....*....|....*....|....*....
gi 1331431699 161 MLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVG 199
Cdd:PRK11905 692 IFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAG 730
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
38-292 |
2.75e-20 |
|
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: 92.67 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 38 VEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFlHAFFIDLEGCVKTLR 117
Cdd:TIGR01238 68 VFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAIAEVREAVDFCR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 118 YFAGWADKiqgkTIPTDDnvvcftrHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQE 197
Cdd:TIGR01238 144 YYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 198 VG--------------------------------------KLVKEAASRSNLKRVTL--ELGGKNPCIVCADADLDLAVQ 237
Cdd:TIGR01238 213 AGfpagtiqllpgrgadvgaaltsdpriagvaftgstevaQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVR 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331431699 238 CAHQGVFFNQGQCCTAASRVFVEEQVyAEFVRRSVEFAKKR-PVGDPFDVRTEQGP 292
Cdd:TIGR01238 293 DVLRSAFDSAGQRCSALRVLCVQEDV-ADRVLTMIQGAMQElKVGVPHLLTTDVGP 347
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
38-199 |
3.07e-20 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 93.46 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 38 VEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHA---------Ffid 108
Cdd:COG4230 587 VVEATAADVEAALAAAQAAF---PAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAiaevreavdF--- 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 109 legcvktLRYFAGwadkiQGKTIPTDDnvvcfTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPLTT 188
Cdd:COG4230 661 -------CRYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIA 723
|
170
....*....|.
gi 1331431699 189 LHLGSLIQEVG 199
Cdd:COG4230 724 ARAVRLLHEAG 734
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
38-186 |
3.68e-20 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 92.95 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 38 VEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAffID-LEGCVKTL 116
Cdd:PRK11904 579 VAFADAEQVEQALAAARAAF---PAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA--IAeVREAVDFC 653
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331431699 117 RYFAGWADKIQGKTI----PT-DDNVVcftRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPL 186
Cdd:PRK11904 654 RYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPL 725
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
18-257 |
8.12e-20 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 91.73 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 18 SKSGKKFATYNPSTLEKICDVEEGDKPDVDMAVEAARAAFqrgSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDT 97
Cdd:PLN02419 125 SQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF---PLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQ 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 98 GKPFLHAFFIDLEGcVKTLRYFAGWADKIQGKTIPTDDNVV-CFTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTI 176
Cdd:PLN02419 202 GKTLKDSHGDIFRG-LEVVEHACGMATLQMGEYLPNVSNGVdTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 177 VVKPAEQTPLTTLHLGSLIQEVG--------------------------------------KLVKEAASRSnlKRVTLEL 218
Cdd:PLN02419 281 ILKPSEKDPGASVILAELAMEAGlpdgvlnivhgtndtvnaicddediravsfvgsntagmHIYARAAAKG--KRIQSNM 358
|
250 260 270
....*....|....*....|....*....|....*....
gi 1331431699 219 GGKNPCIVCADADLDLAVQCAHQGVFFNQGQCCTAASRV 257
Cdd:PLN02419 359 GAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV 397
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
28-186 |
2.03e-15 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 78.48 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 28 NPSTLEKICD-VEEGDKPDVDMAVEAARAAfqrGSAWRRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPFLHAFf 106
Cdd:PRK11809 665 NPADPRDIVGyVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 107 IDLEGCVKTLRYFAGWADkiqgktiPTDDNvvcfTRHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPL 186
Cdd:PRK11809 741 AEVREAVDFLRYYAGQVR-------DDFDN----DTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPL 809
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
34-288 |
2.42e-13 |
|
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: 71.46 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 34 KICDVEEGDKPDVDMAVEAARAAfqrGSAWRRLDAPSRGHLLHQLADLVE---RDRAILATLetMDTGKPFLHAFfIDlE 110
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQAE-ID-A 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 111 GC--VKTLRYFAGWADKI-QGKTIPTDDNVVCFTRHEPV-GVCGAITPWNFPLLMLAWKLAPALCcGNTIVVKPAEQTPL 186
Cdd:cd07123 132 ACelIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 187 TTLHLGSLIQEVG---------------------------------------KLVKEAASR----SNLKRVTLELGGKNP 223
Cdd:cd07123 211 SNYLVYKILEEAGlppgvinfvpgdgpvvgdtvlasphlaglhftgstptfkSLWKQIGENldryRTYPRIVGETGGKNF 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331431699 224 CIVCADADLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKKRPVGDPFDVRT 288
Cdd:cd07123 291 HLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSN 355
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-283 |
1.13e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 69.35 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSkSGKKFATYNPSTLEKICDVEeGDKPDVDMAVEAARAafQRGSAWRRLDAPSRGHLLHQLADLVERDRAIL 89
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 90 ATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGKTIPTDDNVVCFTR-------HEPV---GVCGAITPWNFPL 159
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKdpafqgqHVLVptrGVALFINAFNFPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 160 LMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVGKLVKEAAS-------------------------------R 208
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAGALSvvcgssaglldhlqpfdvvsftgsaetaavlR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 209 SNLK------RVTLELGGKNPCIVCADAD-----LDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFAKK 277
Cdd:PRK11903 243 SHPAvvqrsvRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAK 322
|
....*.
gi 1331431699 278 RPVGDP 283
Cdd:PRK11903 323 TTVGNP 328
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
39-262 |
1.51e-12 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 68.99 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 39 EEGDKPDVDMAVEAARAAFQRGS----AWRRldAPSRGhLLHQLADlveRDRAILATLETmDTGKPFLHAFFIDLEGCVK 114
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESGRtrslEWRK--SQLKG-LLRLLKD---NEEAIFKALHQ-DLGKHRVEAYRDEVGVLTK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 115 TLRY----FAGWADKIQGK----TIPTDDNVVcftrHEPVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKPAEQTPL 186
Cdd:PLN02203 74 SANLalsnLKKWMAPKKAKlplvAFPATAEVV----PEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 187 TTLHLGSLI-----------------------------------QEVGKLVKEAASRsNLKRVTLELGGKNPCIV-CADA 230
Cdd:PLN02203 150 TSAFLAANIpkyldskavkvieggpavgeqllqhkwdkifftgsPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1331431699 231 --DLDLAVQ---------CAhqgvffnqGQCCTAASRVFVEEQ 262
Cdd:PLN02203 229 srDTKVAVNrivggkwgsCA--------GQACIAIDYVLVEER 263
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
96-262 |
3.24e-12 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 68.15 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 96 DTGKPFLHAFFID---LEGCVK-TLRYFAGWADKIQGKTIPTDDNVVCFTRHEPVGVCGAITPWNFPLLMLAWKLAPALC 171
Cdd:PLN02174 59 DLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 172 CGNTIVVKPAEQTPLTTLHLGSLIQE-----------------------------------VGKLVKEAASRsNLKRVTL 216
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQyldssavrvvegavtettalleqkwdkifytgsskIGRVIMAAAAK-HLTPVVL 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1331431699 217 ELGGKNPCIVCADADLDLAVQCAHQGVF-FNQGQCCTAASRVFVEEQ 262
Cdd:PLN02174 218 ELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKE 264
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-292 |
9.69e-11 |
|
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: 63.44 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 10 FINNEWHGSkSGKKFATYNPSTLEKICDVEeGDKPDVDMAVEAARAAfqRGSAWRRLDAPSRGHLLHQLAD-LVERDRAI 88
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREK--GGPALRALTFHERAAMLKALAKyLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 89 LATleTMDTGKPFLHAFfIDLEGCVKTLRYFAGWADK--------IQGKTIPTDDNVVCFTRHEPV---GVCGAITPWNF 157
Cdd:cd07128 80 YAL--SAATGATRRDSW-IDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGTFVGQHILTprrGVAVHINAFNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 158 PLLMLAWKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEVGKLVK---------------------------EAASRSN 210
Cdd:cd07128 157 PVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEgalqlicgsvgdlldhlgeqdvvaftgSAATAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 211 LK----------RVTLELGGKNPCIVCADA-----DLDLAVQCAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEFA 275
Cdd:cd07128 237 LRahpnivarsiRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARL 316
|
330
....*....|....*..
gi 1331431699 276 KKRPVGDPFDVRTEQGP 292
Cdd:cd07128 317 AKVVVGDPRLEGVRMGP 333
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
51-292 |
5.81e-10 |
|
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: 60.70 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 51 EAARAAfQRGSAwrRLDAPSRGHLLHQLADLVERDRAILATLETMDTGKPF--LHAFFIDLEGCVK--------TLRYFA 120
Cdd:cd07077 1 ESAKNA-QRTLA--VNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCSEsklyknidTERGIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 121 GWADKIQGKTIPtdDNVVCFTRHEPVGVCGAITPWNFPLLMLAwKLAPALCCGNTIVVKPAEQTPLTTLHLGSLIQEV-- 198
Cdd:cd07077 78 ASVGHIQDVLLP--DNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAAda 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 199 ------------------------------------GKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVQCAHQG 242
Cdd:cd07077 155 ahgpkilvlyvphpsdelaeellshpkidlivatggRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331431699 243 VFFNQGQCCTAASRVFVE---EQVYAEFVRRSVEFAKKRPVG-----------DPFDVRTEQGP 292
Cdd:cd07077 235 KFFDQNACASEQNLYVVDdvlDPLYEEFKLKLVVEGLKVPQEtkplskettpsFDDEALESMTP 298
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
145-282 |
1.66e-04 |
|
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: 43.64 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 145 PVGVCGAITPWNFPLLMLAWKLAPALCCGNTIVVKP-------AEQ------------TPLTTLHLGSliQEVGKLVKEA 205
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVdskvsvvMEQflrllhlcgmpaTDVDLIHSDG--PTMNKILLEA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331431699 206 ASRSNL--------KRVTLELGGKnpcIVCADADLD-------------LAVQCaHQGVFFNQGQCCTAASRVFVEEQ-V 263
Cdd:cd07126 220 NPRMTLftgsskvaERLALELHGK---VKLEDAGFDwkilgpdvsdvdyVAWQC-DQDAYACSGQKCSAQSILFAHENwV 295
|
170
....*....|....*....
gi 1331431699 264 YAEFVRRSVEFAKKRPVGD 282
Cdd:cd07126 296 QAGILDKLKALAEQRKLED 314
|
|
| |
