|
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 ... |
34-514 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 1004.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 34 TPDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSPWRRMDASERGRLLYRLAD 113
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 114 LMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGpTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKK 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH-GDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 433 LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
..
gi 20129399 513 VK 514
Cdd:cd07141 480 IK 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
40-511 |
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: 869.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSpWRRMDASERGRLLYRLADLMERDQ 119
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGN 278
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGpTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 279 TNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNT 358
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 359 EQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH-GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
37-512 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 743.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 37 ILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADLME 116
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 117 RDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMA 196
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 197 WKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLA 275
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGpTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFD 355
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 356 LNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDE 435
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI-GSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-512 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 706.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 9 ALLRSQAKNF--AAAVANYSS----LPQPQTTP-DILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDI 81
Cdd:PLN02466 20 ALLRSRGRNGgrGRGIRRFSTaaaaVEEPITPPvQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 82 AVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHG 161
Cdd:PLN02466 100 AVAAARKAFDEG-PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 162 KTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVV 241
Cdd:PLN02466 179 LTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 242 PGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQC 320
Cdd:PLN02466 259 SGFGpTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQC 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 321 CCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpEGLPGYF 400
Cdd:PLN02466 339 CCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR-FGSKGYY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 401 VQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA 480
Cdd:PLN02466 418 IQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFD 497
|
490 500 510
....*....|....*....|....*....|..
gi 20129399 481 AQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:PLN02466 498 AAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
43-514 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 674.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:COG1012 9 FIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTN 280
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGsEVGAALVAHPDVDKISFTGSTAVGRRI-AAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERA 440
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 441 NNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA-AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-515 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 672.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRR-MDASERGRLLYRLADLMERD 118
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 119 QVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWK 198
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 199 LGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASG 277
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGrTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 278 NTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVI 437
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKR-HGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVKV 515
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-511 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 661.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 48 WHKSKSGKIfETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLET 127
Cdd:pfam00171 1 WVDSESETI-EVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 128 LDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGN 207
Cdd:pfam00171 77 LENGKPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 208 TIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGnTNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGaEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 287 ELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNE 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 367 EQMEKILGMIKTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYG 446
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLD-NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 447 LAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAA-QAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
40-511 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 659.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQ 119
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASGN 278
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAvAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 279 tNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRT-VGNPFDLN 357
Cdd:cd07144 246 -NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGS-RPEGL-PGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDE 435
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkAPEGLgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
35-512 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 636.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 35 PDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADL 114
Cdd:PLN02766 16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 115 MERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILM 194
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 195 MAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQ 273
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGpTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 274 LASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNP 353
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 354 FDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGsRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKL 433
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGG-KPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 434 DEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
80-513 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 619.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 80 DIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKN 159
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 160 HGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVV 238
Cdd:cd07078 77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 239 NVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNM 317
Cdd:cd07078 157 NVVTGDGdEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 318 GQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP 397
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 398 GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYN 477
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 20129399 478 VLA-AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07078 396 VGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
59-513 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 614.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYS--- 135
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRetr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 136 --MSYnvdlptAIKNLRYFAGWADKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLK 212
Cdd:cd07114 80 aqVRY------LAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 213 PAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGK 291
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGpETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 292 SPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLA 448
Cdd:cd07114 313 VERYVARAREEGARVLTGGERPSGADlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 449 AAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-511 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 613.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 54 GKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSpWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKP 133
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 134 YSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKP 213
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 214 AEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKS 292
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGhTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 293 PNIILSDT-DMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGGSR--PEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAA 449
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTET-GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129399 450 AVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-511 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 611.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI-QLASGNtn 280
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGaTVGAELAESPDVDLVSFTGGTATGRSImRAAAGN-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEG---LPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVI 437
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399 438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
59-515 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 603.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVG-KLIQLASGntNLKRVTLELGGKSPNII 296
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGeVAGAALVEHPDVDKITFTGSTAVGrKIMQGAAG--NLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 297 LSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMI 376
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 377 KTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDL 456
Cdd:cd07115 316 DVGREEGARLLTGGKRP-GARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 457 DKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVKV 515
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-513 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 578.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNt 279
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGsEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NLKRVTLELGGKSPNIILSD-----TDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPF 354
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 355 DLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR---PEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 20129399 512 IV 513
Cdd:cd07559 477 LV 478
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
59-513 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 576.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIIL 297
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGpEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIK 377
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 378 TGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07093 317 LARAEGATILTGGGRPELPDlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
43-513 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 564.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLM-ERDQVy 121
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNL 281
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKV-MAAAAASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSR--PEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGGERltEGGFAnGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:PRK13252 405 RANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
43-514 |
0e+00 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 550.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWNFPILMMAWK 198
Cdd:cd07140 88 ATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 199 LGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASG 277
Cdd:cd07140 168 MAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSlVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 278 NTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:cd07140 248 VSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEgLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK--KLDE 435
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD-RPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDVDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-513 |
0e+00 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 550.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSy 138
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILS 298
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKT 378
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 GKKQGAKLVAGGSRPEGLP----GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEDglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
43-509 |
0e+00 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 544.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGaEVGPLLVNHPDVAKVSFTGGVPTGKKI-MAAAAGHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGlqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVK 509
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-513 |
0e+00 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 537.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNt 279
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGsKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTE 359
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 360 QGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR--PEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEV 436
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltENGLDkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 437 IERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
60-513 |
0e+00 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 535.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 vDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSL 219
Cdd:cd07109 80 -DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 220 TALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILS 298
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGaEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDlNTEQGPQVNEEQMEKILGMIKT 378
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 GKKQGAKLVAGGSRPEGLP--GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDL 456
Cdd:cd07109 317 ARARGARIVAGGRIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 457 DKANYIVGGLRAGTVWVNTYNVLAA-QAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
43-512 |
0e+00 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 526.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAG------WADKNHGKTIpmdgdfftytRHEPVGVCGQIIPWNFPILMMA 196
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 197 WKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLA 275
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGpVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGNTnLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFD 355
Cdd:cd07138 229 AADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 356 LNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGS-RPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKL 433
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgRPEGLErGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 434 DEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNtYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
60-511 |
1.13e-180 |
|
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: 515.06 E-value: 1.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 -VDLptAIKNLRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQT 217
Cdd:cd07103 79 eVDY--AASFLEWFAEEARRIYGRTIPsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 218 SLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGK-LIQLASgnTNLKRVTLELGGKSPNI 295
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEiGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 296 ILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGM 375
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 376 IKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKD 455
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRL-GLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 456 LDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
43-513 |
3.11e-179 |
|
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: 512.12 E-value: 3.11e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTI---PMDGDffTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERrpgSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNt 279
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTE 359
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 360 QGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYnVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-512 |
7.93e-179 |
|
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: 510.36 E-value: 7.93e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSy 138
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP---RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWA---DKNHGKTIPM-DGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPA 214
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 215 EQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSP 293
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDeAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD-IKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 294 NIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKIL 373
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 374 GMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVF 452
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEkGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 453 TKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-511 |
2.61e-177 |
|
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: 506.49 E-value: 2.61e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 vDLPTAIKNLRYFAGWADKNHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07118 81 -EIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIIL 297
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGaTVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIK 377
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 378 TGKKQGAKLVAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLD 457
Cdd:cd07118 319 AGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 20129399 458 KANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
60-513 |
7.16e-175 |
|
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: 500.62 E-value: 7.16e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRrMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADKNHGK-TIPMDGDFFTYT----RHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPA 214
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 215 EQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSP 293
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDnAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT-LKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 294 NIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKIL 373
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 374 GMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVF 452
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLDkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399 453 TKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
43-514 |
1.12e-174 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 500.59 E-value: 1.12e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSkSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PRK13473 6 LINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGK-TIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKaAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTN 280
Cdd:PRK13473 162 ALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGaTVGDALVGHPKVRMVSLTGSIATGKHV-LSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQG-AKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIER 439
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG-KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 440 ANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
41-505 |
1.71e-172 |
|
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: 495.38 E-value: 1.71e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKnhgktipMDGDFftyTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07111 100 LFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTEL---AGWKPVGVVGQIVPWNFPLLMLAWKIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTN 280
Cdd:cd07111 170 PALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 lKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGA-KLVAGGSRPEglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIER 439
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGAdVFQPGADLPS--KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 440 ANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNY 505
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
60-513 |
5.01e-172 |
|
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: 493.00 E-value: 5.01e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADKNHGktiPMDGDFF----TYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAE 215
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 216 QTSLTALYIAQLVKEaGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSPN 294
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGaSAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT-LKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 295 IILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILG 374
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 375 MIkTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07092 314 FV-ERAPAHARVLTGGRRAEG-PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
84-513 |
4.96e-168 |
|
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: 479.42 E-value: 4.96e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 84 QAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKT 163
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 164 IP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVP 242
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 243 GFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCC 321
Cdd:cd06534 157 GGGdEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 322 CAGSRTFVEDKIYDEFVERSAerakkrtvgnpfdlnteqgpqvneeqmekilgmiktgkkqgaklvaggsrpeglpgyfv 401
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 402 qpTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA- 480
Cdd:cd06534 257 --TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVg 334
|
410 420 430
....*....|....*....|....*....|...
gi 20129399 481 AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
41-511 |
1.09e-165 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 478.84 E-value: 1.09e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFK--LGSPWRRMDASERGRLLYRLADLMERD 118
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 119 QVYLASLETLDNGKPYSMSyNVDLPTAIKNLRYFAGWADKNHGK-----TIPMDgDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTeAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 qLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:PLN02467 247 -MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
60-511 |
1.70e-165 |
|
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: 476.25 E-value: 1.70e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSyN 139
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADKNhgKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSL 219
Cdd:cd07106 78 FEVGGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 220 TALYIAQLVKEAgFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNLKRVTLELGGKSPNIILSD 299
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKV-MASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 300 TDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTG 379
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 380 KKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKA 459
Cdd:cd07106 314 KAKGAKVLAGGEPLDG-PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 20129399 460 NYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
43-513 |
1.56e-161 |
|
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: 467.21 E-value: 1.56e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINP-TTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07131 79 LARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNT 279
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGeEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NlKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTE 359
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 360 QGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEG---LPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEV 436
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 437 IERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA-AQAPFGGYKMSGHG-RENGEYALSNYTEVKSVIV 513
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAeVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
43-511 |
1.76e-161 |
|
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: 467.11 E-value: 1.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKifETINPT-TAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPysmsynvdLPTAIKN-------LRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:cd07097 79 LARLLTREEGKT--------LPEARGEvtragqiFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:cd07097 151 IPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEvGQALVEHPDVDAVSFTGSTAVGRRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07097 231 AAAAAA-RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR-PEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:cd07097 310 ALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNV-LAAQAPFGGYKMSGHG-RENGEYALSNYTEVK 509
Cdd:cd07097 390 DYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
..
gi 20129399 510 SV 511
Cdd:cd07097 470 TV 471
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
40-511 |
4.08e-157 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 456.67 E-value: 4.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSpWRRMDASERGRLLYRLADLMERDQ 119
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGN 278
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 279 TNLKRVTLELGGKSPNIILSDT-DMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGgsRPEGLPGYfVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVI 437
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399 438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-513 |
4.50e-157 |
|
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: 455.28 E-value: 4.50e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAgFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIIL 297
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEeCGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGL-FFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMI 376
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 377 KTGKK-QGAKLVAGGSRPEGL---PGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVF 452
Cdd:cd07108 316 DLGLStSGATVLRGGPLPGEGplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129399 453 TKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENG-EYALSNYTEVKSVIV 513
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
43-513 |
5.94e-157 |
|
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: 455.76 E-value: 5.94e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI-QLASgnTN 280
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGlEAGKPLASSKRIAKVAFTGETTTGRLImQYAS--EN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDM------DYAVETahFGLF-FNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNP 353
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADVMDaddaffDKALEG--FVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 354 FDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR---PEGLPGYFVQPTVFADvQDDMTIAREEIFGPVQQLIRF 430
Cdd:cd07116 316 LDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 431 KKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKS 510
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474
|
...
gi 20129399 511 VIV 513
Cdd:cd07116 475 LLV 477
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-513 |
3.57e-156 |
|
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: 453.26 E-value: 3.57e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFT-YTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTN 280
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGsVVGDALVAHPKVGMISLTGSTEAGQKI-MEAAAEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERA 440
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 441 NNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-514 |
5.45e-155 |
|
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: 450.74 E-value: 5.45e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKT----IP-MDGDFFT-YTRHEPVGVCGQIIPWNFPILM 194
Cdd:cd07113 79 ELAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPsMQGERYTaFTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 195 MAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQl 274
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIG- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 275 ASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPF 354
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 355 DLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLD 434
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAG-EGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 435 EVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-513 |
6.16e-151 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 439.50 E-value: 6.16e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NvDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07107 78 G-DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSPNIIL 297
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGaTAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFN-MGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMI 376
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 377 KTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFT 453
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 454 KDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
57-513 |
1.05e-148 |
|
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: 433.68 E-value: 1.05e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 57 FETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSM 136
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 137 SYnVDLPTAIKNLRYFAGWADKNHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAE 215
Cdd:cd07150 78 AW-FETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 216 QTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPN 294
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 295 IILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILG 374
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 375 MIKTGKKQGAKLVAGGSRpeglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKY----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVL-AAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
78-513 |
5.71e-147 |
|
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: 428.49 E-value: 5.71e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 78 DIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSyNVDLPTAIKNLRYFAGWAD 157
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 158 KNHGKTIPMDGD-FFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLT-ALYIAQLVKEAGFPE 235
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 236 GVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLF 314
Cdd:cd07104 157 GVLNVVPGGGsEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 315 FNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpE 394
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-E 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 395 GLpgyFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN 474
Cdd:cd07104 315 GL---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 20129399 475 TYNVL-AAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07104 392 DQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-511 |
8.39e-143 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 420.25 E-value: 8.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIPM-DGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:PLN02278 105 AQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLIQLASGNTn 280
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEiGDALLASPKVRKITFTGSTAVGKKLMAGAAAT- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERA 440
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKR-HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399 441 NNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
43-511 |
3.40e-142 |
|
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: 419.32 E-value: 3.40e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSksGKIFETINP-TTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:cd07124 36 VIGGKEVRT--EEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:cd07124 111 LAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVG-----KLIQLA 275
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGeEVGDYLVEHPDVRFIAFTGSREVGlriyeRAAKVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGNTNLKRVTLELGGKSPNIILSDTDMDYAVE---TAHFGLffnMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07124 270 PGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEgivRSAFGF---QGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGaKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN---TYNVLAAQaPFGGYKMSG-HGRENGEYALSNYTE 507
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALVGRQ-PFGGFKMSGtGSKAGGPDYLLQFMQ 504
|
....
gi 20129399 508 VKSV 511
Cdd:cd07124 505 PKTV 508
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-513 |
9.43e-142 |
|
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: 415.84 E-value: 9.43e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 57 FETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGspwRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSM 136
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 137 SYN-VDlpTAIKNLRYFAGWADKNHGKTIPMDG-----DFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIV 210
Cdd:cd07149 78 ARKeVD--RAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 211 LKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGntnLKRVTLELG 289
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGeTVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 290 GKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQM 369
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 370 EKILGMIKTGKKQGAKLVAGGSRpeglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAA 449
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 450 AVFTKDLDKANYIVGGLRAGTVWVN---TYNVlaAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMINdssTFRV--DHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-513 |
1.76e-141 |
|
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: 415.21 E-value: 1.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 57 FETINPTTAEVIAEIQCADKEDIDIAVQAARNAFklgSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSM 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAK---DVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 137 SyNVDLPTAIKNLRYFAGWADKNHGKTIPMDG-----DFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVL 211
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 212 KPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGG 290
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGsEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 291 KSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQME 370
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 371 KILGMIKTGKKQGAKLVAGGSRPEglpGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAA 450
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDE---GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399 451 VFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQA-PFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
43-513 |
3.11e-141 |
|
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: 415.42 E-value: 3.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSkSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:cd07086 78 GRLVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEA----GFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASG 277
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 278 NTNlKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:cd07086 237 RRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEG-LPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEV 436
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 437 IERANNSEYGLAAAVFTKDLDKANYIVG--GLRAGTVWVNTYNVLA-AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNVNIPTSGAeIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
59-511 |
1.43e-138 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 407.89 E-value: 1.43e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRmDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSy 138
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTI-PMDGDFFTYTRhEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQT 217
Cdd:cd07120 78 RFEISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 218 SLTALYIAQLVKEA-GFPEGVVNVVPGFGTAGAA-LANHCDVDKVAFTGSTDVGKLIQlASGNTNLKRVTLELGGKSPNI 295
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAhLVASPDVDVISFTGSTATGRAIM-AAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 296 ILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGM 375
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 376 IKTGKKQGAK-LVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFT 453
Cdd:cd07120 316 VERAIAAGAEvVLRGGPVTEGLAkGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 454 KDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-514 |
7.75e-132 |
|
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: 390.90 E-value: 7.75e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 46 NEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLME--RDQ-VYL 122
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQK---EWAATLPQERAEILEKAAQILEerRDEiVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETldnGKPYSMSyNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFT-YTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:cd07151 78 LIRES---GSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDVPGKEnRVYREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTA-LYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLI-QLASGN 278
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEiGDAFVEHPVPRLISFTGSTPVGRHIgELAGRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 279 tnLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNT 358
Cdd:cd07151 234 --LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 359 EQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSrPEGLpgyFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGGE-AEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVL-AAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
79-513 |
9.65e-129 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 381.81 E-value: 9.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 79 IDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMS-YNVDLPTAIknLRYFAgwad 157
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEArAEVEKCAWI--CRYYA---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 158 kNHG------KTIPMDGDFfTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEA 231
Cdd:cd07100 72 -ENAeafladEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 232 GFPEGV-VNVVPGFGTAGAALANHcDVDKVAFTGSTDVGKLIQLASGnTNLKRVTLELGGKSPNIILSDTDMDYAVETAH 310
Cdd:cd07100 150 GFPEGVfQNLLIDSDQVEAIIADP-RVRGVTLTGSERAGRAVAAEAG-KNLKKSVLELGGSDPFIVLDDADLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 311 FGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGG 390
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 391 SRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGT 470
Cdd:cd07100 308 KRPDG-PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 20129399 471 VWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
58-513 |
3.50e-124 |
|
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: 371.00 E-value: 3.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 58 ETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMS 137
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 138 yNVDLPTAIKNLRYFAGWADKNHGKTIPMD-----GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLK 212
Cdd:cd07094 79 -RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 213 PAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGntnLKRVTLELGGK 291
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 292 SPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGGSRpeglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAV 451
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGER----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 452 FTKDLDKANYIVGGLRAGTVWVNTYNVLAAQA-PFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
43-514 |
6.76e-122 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 366.07 E-value: 6.76e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQlASGNTNL 281
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIY-ERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 282 KRVTLELGGKSPNIILSDTDMDYAVE---TAHFGlffNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNT 358
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANalvGAAFG---AAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 359 EQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGS--RPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDE 435
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRgvKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNT-YNVLAAQAPFGGYKMS--GHGRENGEYALSNYTEVKSVI 512
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVpIPVPLAFFSFGGWKGSffGDLHFYGKDGVRFYTQTKTVT 475
|
..
gi 20129399 513 VK 514
Cdd:cd07085 476 SR 477
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-513 |
9.36e-122 |
|
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: 364.62 E-value: 9.36e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYn 139
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADK----NHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAE 215
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRvlapRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 216 QTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHcDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSPNI 295
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER-LIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 296 ILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGM 375
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 376 IKTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKD 455
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNG-GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 456 LDKANYIVGGLRAGTVWVN--TYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07099 394 LARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
44-511 |
2.53e-121 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 365.80 E-value: 2.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 44 INNEWHKSKsGKIfETINPT-TAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PRK03137 41 IGGERITTE-DKI-VSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSyNVDLPTAIKNLRYFAGWADK-NHGKTI-PMDGDFFTYtRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:PRK03137 116 SAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKlADGKPVeSRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGMTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLI-----QL 274
Cdd:PRK03137 194 AAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEvGDYLVDHPKTRFITFTGSREVGLRIyeraaKV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 275 ASGNTNLKRVTLELGGKSPNIILSDTDMDYAVE---TAHFGlfFNmGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVG 351
Cdd:PRK03137 274 QPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAEsivASAFG--FS-GQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 352 NPFDlNTEQGPQVNEEQMEKILGMIKTGKKQGaKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:PRK03137 351 NPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDS-KGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN---TYNVLAAQaPFGGYKMSGHGRENG--EYaLSNYT 506
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVGYH-PFGGFNMSGTDSKAGgpDY-LLLFL 505
|
....*
gi 20129399 507 EVKSV 511
Cdd:PRK03137 506 QAKTV 510
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-513 |
1.77e-118 |
|
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: 356.17 E-value: 1.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 57 FETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSM 136
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 137 SyNVDLPTAIKNLRYFAGWADKNHGKTIPMDGD-----FFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVL 211
Cdd:cd07147 78 A-RGEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 212 KPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtnlKRVTLELGGK 291
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 292 SPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGGSRpeglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAV 451
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKR----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 452 FTKDLDKANYIVGGLRAGTVWVN---TYNVlaAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVINdvpTFRV--DHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-513 |
2.05e-117 |
|
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: 353.54 E-value: 2.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQR---AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIkNLRYFAGWA-----DKNHGKTIPmdgdFFTYTR--HEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLK 212
Cdd:cd07101 78 EVLDVAI-VARYYARRAerllkPRRRRGAIP----VLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 213 PAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVdkVAFTGSTDVGKLIQLASGNtNLKRVTLELGGK 291
Cdd:cd07101 153 PDSQTALTALWAVELLIEAGLPRDLWQVVTGPGsEVGGAIVDNADY--VMFTGSTATGRVVAERAGR-RLIGCSLELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 292 SPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07101 230 NPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGG-SRPEGLPgYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAA 450
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGrARPDLGP-YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 451 VFTKDLDKANYIVGGLRAGTVWVNTYNVLA---AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
66-494 |
7.73e-115 |
|
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: 346.59 E-value: 7.73e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 66 EVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGK-PYSMSYNVDLpt 144
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSiRPKAGFEVGA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 145 AIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTA-LY 223
Cdd:cd07152 77 AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 224 IAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMD 303
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 304 YAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQG 383
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 384 AKLVAGGSRpEGLpgyFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIV 463
Cdd:cd07152 316 ARLEAGGTY-DGL---FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|..
gi 20129399 464 GGLRAGTVWVNTYNVL-AAQAPFGGYKMSGHG 494
Cdd:cd07152 392 DRLRTGMLHINDQTVNdEPHNPFGGMGASGNG 423
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
60-511 |
1.01e-113 |
|
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: 344.23 E-value: 1.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 vDLPTAIKNLRYFAGWADKN-HGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07102 78 -EIRGMLERARYMISIAEEAlADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILS 298
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKT 378
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 GKKQGAKLVAGGSR-PEG-LPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDL 456
Cdd:cd07102 316 AIAKGARALIDGALfPEDkAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 457 DKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07102 396 ARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
51-511 |
4.18e-113 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 344.94 E-value: 4.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 51 SKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDN 130
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQR---AWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 131 GKPYSMSYNVDLPTAIkNLRYFAGWA-----DKNHGKTIPMDGDffTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALAT 205
Cdd:PRK09407 105 GKARRHAFEEVLDVAL-TARYYARRApkllaPRRRAGALPVLTK--TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 206 GNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVdkVAFTGSTDVGKLIQLASGNtNLKRV 284
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGpVVGTALVDNADY--LMFTGSTATGRVLAEQAGR-RLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 285 TLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQV 364
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 365 NEEQMEKILGMIKTGKKQGAKLVAGG-SRPEGLPgYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNS 443
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGkARPDLGP-LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDT 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 444 EYGLAAAVFTKDLDKANYIVGGLRAGTVWVN-----TYNvlAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PRK09407 418 PYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWG--SVDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
58-513 |
1.57e-111 |
|
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: 338.56 E-value: 1.57e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 58 ETINPTTAEVIAEIQCADKEDIDIAVQAARNafklgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMS 137
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAAS------YRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 138 -YNVDlpTAIKNLRYFAGWADKNHGKTIPMD-----GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVL 211
Cdd:cd07146 76 rYEVG--RAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 212 KPAEQTSLTALYIAQLVKEAGFPEGVVNVVPG-FGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGntnLKRVTLELGG 290
Cdd:cd07146 154 KPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGePGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 291 KSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQME 370
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 371 KILGMIKTGKKQGAKLVAGGSRpeglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAA 450
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGNQR----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 451 VFTKDLDKANYIVGGLRAGTVWVNT---YNVlaAQAPFGGYKMSGHG-RENGEYALSNYTEVKSVIV 513
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVNEvpgFRS--ELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
43-514 |
2.77e-111 |
|
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: 338.39 E-value: 2.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSkSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSY-NVDlpTAIKNLRYFAGWADKNHGKTIPMDGDFFT-----YTRHEPVGVCGQIIPWNFPILMMA 196
Cdd:cd07082 82 ANLLMWEIGKTLKDALkEVD--RTIDYIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 197 WKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLA 275
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGrEIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGntnLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLF-FNmGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPF 354
Cdd:cd07082 240 HP---MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALsYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 355 DLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGsrpEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLD 434
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG---GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 435 EVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTY-----NVLaaqaPFGGYKMSGHGRENGEYALSNYTEVK 509
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQGIGDALRSMTRRK 468
|
....*
gi 20129399 510 SVIVK 514
Cdd:cd07082 469 GIVIN 473
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-509 |
6.42e-111 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 338.03 E-value: 6.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFklgSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:PRK11241 91 ARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPG-FGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTN 280
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQL-MEQCAKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGsRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERA 440
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGG-KAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 441 NNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVK 509
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
78-513 |
2.15e-110 |
|
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: 334.93 E-value: 2.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 78 DIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMS-YNVDLptAIKNLRYFAGWA 156
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAgFNVDL--AAGMLREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 157 DKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPE 235
Cdd:cd07105 76 TQIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 236 GVVNVV-------PGFGTAgaaLANHCDVDKVAFTGSTDVGKLI-QLASgnTNLKRVTLELGGKSPNIILSDTDMDYAVE 307
Cdd:cd07105 156 GVLNVVthspedaPEVVEA---LIAHPAVRKVNFTGSTRVGRIIaETAA--KHLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 308 TAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNpfdlnTEQGPQVNEEQMEKILGMIKTGKKQGAKLV 387
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 388 AGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLR 467
Cdd:cd07105 306 VGGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 20129399 468 AGTVWVNTYNVL-AAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07105 386 SGAVHINGMTVHdEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
61-513 |
3.43e-106 |
|
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: 325.41 E-value: 3.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 61 NPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPysmsyNV 140
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQR---EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT-----MV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 141 D------LPTAIKnLRYFAGWADKnHGKTIPMDGDFFTYTR-----HEPVGVCGQIIPWNFPILMMawkLGPALA---TG 206
Cdd:cd07098 74 DaslgeiLVTCEK-IRWTLKHGEK-ALRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNL---LGPIIAalfAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 207 NTIVLKPAEQTSLTALYIAQLVKEA----GFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLK 282
Cdd:cd07098 149 NAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 283 RVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGP 362
Cdd:cd07098 228 PVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 363 QVNEEQMEKILGMIKTGKKQGAKLVAGGSR---PEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIER 439
Cdd:cd07098 308 MISPARFDRLEELVADAVEKGARLLAGGKRyphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 440 ANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNV--LAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07098 388 ANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVnyYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
43-511 |
8.97e-105 |
|
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: 323.36 E-value: 8.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKsGKIfETINPT-TAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:TIGR01237 36 VINGERVETE-NKI-VSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFE---AWKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPYSMSyNVDLPTAIKNLRYFAGWADK--NHGKTIPMDGDFFTYTrHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIElaKGKPVNSREGETNQYV-YTPTGVTVVISPWNFPFAIMVGMT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLI-----Q 273
Cdd:TIGR01237 189 VAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSeVGDYLVDHPKTSLITFTGSREVGTRIferaaK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 274 LASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNP 353
Cdd:TIGR01237 269 VQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 354 FDLNTEQGPQVNEEQMEKILGMIKTGKKQGaKLVAGGSrPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKL 433
Cdd:TIGR01237 349 DSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGC-GDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 434 DEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN---TYNVLAAQaPFGGYKMSGHGRENG--EYaLSNYTEV 508
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrniTGAIVGYQ-PFGGFKMSGTDSKAGgpDY-LALFMQA 504
|
...
gi 20129399 509 KSV 511
Cdd:TIGR01237 505 KTV 507
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
149-511 |
1.91e-99 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 305.89 E-value: 1.91e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 149 LRYFAGWADKNHGKTIPMD---GDFFTYTRhePVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIA 225
Cdd:PRK10090 41 IDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 226 QLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNLKRVTLELGGKSPNIILSDTDMDY 304
Cdd:PRK10090 119 KIVDEIGLPKGVFNLVLGRGeTVGQELAGNPKVAMVSMTGSVSAGEKI-MAAAAKNITKVCLELGGKAPAIVMDDADLDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 305 AVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNT-EQGPQVNEEQMEKILGMIKTGKKQG 383
Cdd:PRK10090 198 AVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 384 AKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIV 463
Cdd:PRK10090 278 ARVALGGKAVEG-KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAI 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 20129399 464 GGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PRK10090 357 KGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVV 404
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
59-511 |
3.35e-91 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 286.25 E-value: 3.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSmSY 138
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA-SA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGwadknHGKTI----PMD----GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIV 210
Cdd:PRK09406 81 KAEALKCAKGFRYYAE-----HAEALladePADaaavGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 211 LKPAEQTSLTALYIAQLVKEAGFPEGV-VNVVPGFGTAGAALANHcDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELG 289
Cdd:PRK09406 156 LKHASNVPQTALYLADLFRRAGFPDGCfQTLLVGSGAVEAILRDP-RVAAATLTGSEPAGRAVAAIAGD-EIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 290 GKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQM 369
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 370 EKILGMIKTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAA 449
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPDG-PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129399 450 AVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
41-505 |
6.26e-86 |
|
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: 273.31 E-value: 6.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFiNNEWhkSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07130 1 GVY-DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMS------------YNVDLPTAIknlryfagwadknHGKTIPMD-GDFFTYTRHEPVGVCGQIIP 187
Cdd:cd07130 75 ALGKLVSLEMGKILPEGlgevqemidicdFAVGLSRQL-------------YGLTIPSErPGHRMMEQWNPLGVVGVITA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 188 WNFPILMMAWKLGPALATGNTIVLKPAEQTSLTAL----YIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFT 263
Cdd:cd07130 142 FNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 264 GSTDVGKLIQLASgNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAE 343
Cdd:cd07130 222 GSTAVGRQVGQAV-AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 344 RAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGlPGYFVQPTVfADVQDDMTIAREEIFGP 423
Cdd:cd07130 301 AYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDG-PGNYVEPTI-VEGLSDAPIVKEETFAP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 424 VQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVG--GLRAGTVWVNTYNVLAA-QAPFGGYKMSGHGRENGEY 500
Cdd:cd07130 379 ILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGpkGSDCGIVNVNIGTSGAEiGGAFGGEKETGGGRESGSD 458
|
....*
gi 20129399 501 ALSNY 505
Cdd:cd07130 459 AWKQY 463
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
43-511 |
1.29e-80 |
|
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: 260.20 E-value: 1.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIfeTINP-TTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:cd07083 22 VIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTI------PMDGDFFtytrHEPVGVCGQIIPWNFPILMM 195
Cdd:cd07083 97 LIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESF----YVGLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 196 AWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI-- 272
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGeEVGAYLTEHERIRGINFTGSLETGKKIye 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 ---QLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRT 349
Cdd:cd07083 252 aaaRLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 350 VGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGaKLVAGGSRPEGLpGYFVQPTVFADVQDDMTIAREEIFGPVQQLIR 429
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGE-GYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 430 FK--KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN--TYNVLAAQAPFGGYKMSGHG-RENGEYALSN 504
Cdd:cd07083 410 YKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNaKTGGPHYLRR 489
|
....*..
gi 20129399 505 YTEVKSV 511
Cdd:cd07083 490 FLEMKAV 496
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
17-498 |
1.36e-80 |
|
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: 260.59 E-value: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 17 NFAAAVANYSSlPQPQTTPdiLYTGVFINNEWHKsksgkifETINPT-TAEVIAEIQCADKEDIDIAVQAARNAFklgSP 95
Cdd:cd07125 18 ALADALKAFDE-KEWEAIP--IINGEETETGEGA-------PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 96 WRRMDASERGRLLYRLADLMERDQ---VYLASLE---TLDNGKPysmsynvDLPTAIKNLRYFAGWADKNHGKTIpMDGD 169
Cdd:cd07125 85 WSATPVEERAEILEKAADLLEANRgelIALAAAEagkTLADADA-------EVREAIDFCRYYAAQARELFSDPE-LPGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 170 FF---TYTRHEP-VGVCgqIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG 245
Cdd:cd07125 157 TGelnGLELHGRgVFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 246 -TAGAALANHCDVDKVAFTGSTDVGKLIQ--LASGNTNLKRVTLELGGKSPNIILSDTDMDYAV----ETAhfglFFNMG 318
Cdd:cd07125 235 eEIGEALVAHPRIDGVIFTGSTETAKLINraLAERDGPILPLIAETGGKNAMIVDSTALPEQAVkdvvQSA----FGSAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 319 QCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQgAKLVAGGSRPEGlPG 398
Cdd:cd07125 311 QRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDG-NG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 399 YFVQPTVFADVQDDmTIaREEIFGPVQQLIRFKK--LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN-- 474
Cdd:cd07125 389 YFVAPGIIEIVGIF-DL-TTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrn 466
|
490 500
....*....|....*....|....*
gi 20129399 475 -TYNVLAAQaPFGGYKMSGHGRENG 498
Cdd:cd07125 467 iTGAIVGRQ-PFGGWGLSGTGPKAG 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-501 |
1.75e-76 |
|
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: 247.18 E-value: 1.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 78 DIDIAVQAARNAFklgSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPY--------SMSYNVDLptAIKNL 149
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqtevaAMAGKIDI--SIKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 150 RYFAGwadknhGKTIPMdGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVK 229
Cdd:cd07095 76 HERTG------ERATPM-AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 230 EAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETA 309
Cdd:cd07095 149 EAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 310 HFGLFFNMGQCCCAGSRTFVEDKIY-DEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILgmiktgkKQGAKLVA 388
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYL-------LAQQDLLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 389 GGSRP----EGLP--GYFVQP-----TVFADVQDdmtiarEEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLD 457
Cdd:cd07095 302 LGGEPllamERLVagTAFLSPgiidvTDAADVPD------EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 20129399 458 KANYIVGGLRAGTV-WVNTYNVLAAQAPFGGYKMSGHGRENGEYA 501
Cdd:cd07095 376 LFERFLARIRAGIVnWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
58-494 |
9.13e-75 |
|
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: 243.48 E-value: 9.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 58 ETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSPWrrMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYsMS 137
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPL-VD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 138 YNVDLPTAIKNLRYFAGWADKNHGKTIPMD-----GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLK 212
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 213 PAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLI--QLASGNtnlkRVTLELGG 290
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLrsKLAPGT----RCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 291 KSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQME 370
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 371 KILGMIKTGKKQGAKLVAGGSRpegLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAA 450
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKR---LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 20129399 451 VFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQ-APFGGYKMSGHG 494
Cdd:cd07148 392 VFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
43-501 |
2.60e-73 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 240.63 E-value: 2.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSkSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFklgSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPY--------SMSYNVDLptAIKnlryfaGWADKNHGKTIPMdGDFFTYTRHEPVGVCGQIIPWNFPILM 194
Cdd:PRK09457 80 AEVIARETGKPLweaatevtAMINKIAI--SIQ------AYHERTGEKRSEM-ADGAAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 195 MAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLI-- 272
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLhr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLAsGNTNlKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIY-DEFVERSAERAKKRTVG 351
Cdd:PRK09457 231 QFA-GQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 352 NPFDlnTEQ---GPQVNEEQMEKILgmiktgKKQgAKLVAGGSRP--------EGLPgyFVQP-----TVFADVQDdmti 415
Cdd:PRK09457 309 RWDA--EPQpfmGAVISEQAAQGLV------AAQ-AQLLALGGKSllemtqlqAGTG--LLTPgiidvTGVAELPD---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 416 arEEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTV-WVNTYNVLAAQAPFGGYKMSGHG 494
Cdd:PRK09457 374 --EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNH 451
|
....*..
gi 20129399 495 RENGEYA 501
Cdd:PRK09457 452 RPSAYYA 458
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
96-504 |
1.01e-72 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 237.51 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 96 WRRMDASERGRLLYRLADLME--RDQVYLASLEtlDNGKPYSmsyNVDL----PT------AIKNLRyfaGW-ADKNHGK 162
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILarREEIIAALAA--DFRKPAA---EVDLteilPVlseinhAIKHLK---KWmKPKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 163 TIPMDGDFfTYTRHEPVGVCGQIIPWNFPiLMMAwkLGP---ALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVN 239
Cdd:cd07134 86 PLLLFGTK-SKIRYEPKGVCLIISPWNYP-FNLA--FGPlvsAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 240 VVPGfgtaGAALANH---CDVDKVAFTGSTDVGKLIqLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFN 316
Cdd:cd07134 161 VFEG----DAEVAQAlleLPFDHIFFTGSPAVGKIV-MAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 317 MGQCCCAGSRTFVEDKIYDEFVERsAERAKKRTVGNpfDLNTEQGPQ----VNEEQMEKILGMIKTGKKQGAKLVAGGSR 392
Cdd:cd07134 236 AGQTCIAPDYVFVHESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 393 PEGlpGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVW 472
Cdd:cd07134 313 DAA--QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVV 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 20129399 473 VNT--YNVLAAQAPFGGYKMSGHGRENGEY---ALSN 504
Cdd:cd07134 391 VNDvvLHFLNPNLPFGGVNNSGIGSYHGVYgfkAFSH 427
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
43-511 |
1.39e-72 |
|
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: 238.63 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFklgSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:TIGR01722 81 AELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNL 281
Cdd:TIGR01722 160 AIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYI-HTTGSAHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSrTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGS--RPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRgyKVDGYEeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNT-YNVLAAQAPFGGYKMSGHGREN--GEYALSNYTEVKSV 511
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVpIPVPLPYFSFTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
59-511 |
4.64e-71 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 233.99 E-value: 4.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 -NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRhePVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQT 217
Cdd:PRK13968 88 aEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYR--PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 218 SLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSPNIIL 297
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIK 377
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 378 TGKKQGAKLVAGGSRPEGLPGYFVqPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLD 457
Cdd:PRK13968 325 ATLAEGARLLLGGEKIAGAGNYYA-PTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 20129399 458 KANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
77-512 |
5.11e-70 |
|
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: 230.57 E-value: 5.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 77 EDIDIAVQAARNAFKLGspwRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNV-------DLPTAIKNL 149
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTevsgvknDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 150 RyfaGWADKNHGKTIPMDGDFF-TYTRHEPVGVCGQIIPWNFPILMMawkLGP---ALATGNTIVLKPAEQTSLTALYIA 225
Cdd:cd07135 82 K---KWAKDEKVKDGPLAFMFGkPRIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 226 QLVKEAgFPEGVVNVVPGfGTA--GAALAnhCDVDKVAFTGSTDVGKLIQLASgNTNLKRVTLELGGKSPNIILSDTDMD 303
Cdd:cd07135 156 ELVPKY-LDPDAFQVVQG-GVPetTALLE--QKFDKIFYTGSGRVGRIIAEAA-AKHLTPVTLELGGKSPVIVTKNADLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 304 YAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERsAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKkqg 383
Cdd:cd07135 231 LAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEE-LKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 384 AKLVAGGSRPEGLpgYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIV 463
Cdd:cd07135 307 GKVVIGGEMDEAT--RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHIL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 20129399 464 GGLRAGTVWVN--TYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07135 385 TRTRSGGVVINdtLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-494 |
2.62e-68 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 237.40 E-value: 2.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 12 RSQAKNFAAAVANYSSlPQPQTTPdilytgvFINNewhkskSGKIFETINPT-TAEVIAEIQCADKEDIDIAVQAARNAF 90
Cdd:PRK11904 533 RSELEPLAAAIAAFLE-KQWQAGP-------IING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAF 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 91 KLgspWRRMDASERGRLLYRLADLMERDQ---VYLASLE---TLDNGkpysmsynVD-LPTAIKNLRYFAGWADKNHGKT 163
Cdd:PRK11904 599 PA---WSRTPVEERAAILERAADLLEANRaelIALCVREagkTLQDA--------IAeVREAVDFCRYYAAQARRLFGAP 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 164 IPMDGdfFT----YTRHEPVGV--CgqIIPWNFPIlmmAWKLGP---ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFP 234
Cdd:PRK11904 668 EKLPG--PTgesnELRLHGRGVfvC--ISPWNFPL---AIFLGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIP 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 235 EGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTL--ELGGKspNIILSDTD------MDYA 305
Cdd:PRK11904 741 KDVLQLLPGDGaTVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQ--NAMIVDSTalpeqvVDDV 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 306 VETAhfglFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQgAK 385
Cdd:PRK11904 819 VTSA----FRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-AR 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 386 LVAGGSRPEGLP-GYFVQPTVFAdvQDDMTIAREEIFGPVQQLIRFKK--LDEVIERANNSEYGLAAAVFTKDLDKANYI 462
Cdd:PRK11904 894 LLAQLPLPAGTEnGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRI 971
|
490 500 510
....*....|....*....|....*....|....*.
gi 20129399 463 VGGLRAGTVWVNTyNVLAA----QaPFGGYKMSGHG 494
Cdd:PRK11904 972 ADRVRVGNVYVNR-NQIGAvvgvQ-PFGGQGLSGTG 1005
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
82-513 |
3.00e-68 |
|
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: 225.48 E-value: 3.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 82 AVQAARNAFKLGS----PWRRmdasERGRLLYRLadLMERDQVYLASLETlDNGKPYSMSY-------NVDLPTAIKNLR 150
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRK----AQLKALKRM--LTENEEEIAAALYA-DLGKPPAEAYlteiavvLGEIDHALKHLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 151 yfaGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMawkLGP---ALATGNTIVLKPAEQTSLTALYIAQL 227
Cdd:cd07087 76 ---KWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 228 VKEAgFPEGVVNVVPGFGTAGAALANHCdVDKVAFTGSTDVGKLI-QLASgnTNLKRVTLELGGKSPNIILSDTDMDYAV 306
Cdd:cd07087 150 IPKY-FDPEAVAVVEGGVEVATALLAEP-FDHIFFTGSPAVGKIVmEAAA--KHLTPVTLELGGKSPCIVDKDANLEVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 307 ETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERsAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKkqgakL 386
Cdd:cd07087 226 RRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEE-LKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK-----V 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 387 VAGGSRPEGLPgyFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGL 466
Cdd:cd07087 300 VIGGQVDKEER--YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAET 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 20129399 467 RAGTVWVN--TYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07087 378 SSGGVCVNdvLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
43-513 |
7.42e-67 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 223.86 E-value: 7.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYS------------MSYnvdlpTAIKNLRYFAgwadknHGKTIPMDG------DFFTYTRHEPVGVCGQ 184
Cdd:PLN00412 96 AECLVKEIAKPAKdavtevvrsgdlISY-----TAEEGVRILG------EGKFLVSDSfpgnerNKYCLTSKIPLGVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 185 IIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFT 263
Cdd:PLN00412 165 IPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEiGDFLTMHPGVNCISFT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 264 GStDVGKLIQLASGNTNLKrvtLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAE 343
Cdd:PLN00412 245 GG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 344 RAKKRTVGNPFDlNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLpgyfVQPTVFADVQDDMTIAREEIFGP 423
Cdd:PLN00412 321 KVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNL----IWPLLLDNVRPDMRIAWEEPFGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 424 VQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNtynvlAAQA------PFGGYKMSGHGREN 497
Cdd:PLN00412 396 VLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIGSQG 470
|
490
....*....|....*.
gi 20129399 498 GEYALSNYTEVKSVIV 513
Cdd:PLN00412 471 ITNSINMMTKVKSTVI 486
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-511 |
2.24e-66 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 225.40 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 1 MLRVlkTGALLRSQAKNFAAAVANY-SSLP----QPQTTPDI--LYTGVFInnewhKSKSGKIFETINPTTAEVIAEIQC 73
Cdd:PLN02419 75 LLRI--SGNNLRPLRPQFLALRSSWlSTSPeqstQPQMPPRVpnLIGGSFV-----ESQSSSFIDVINPATQEVVSKVPL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 74 ADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNvDLPTAIKNLRYFA 153
Cdd:PLN02419 148 TTNEEFKAAVSAAKQAFPL---WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-DIFRGLEVVEHAC 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 154 GWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAG 232
Cdd:PLN02419 224 GMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 233 FPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFG 312
Cdd:PLN02419 304 LPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHI-YARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 313 LFFNMGQCCCAGSR-TFVED--KIYDEFVERSaeRAKKRTVGNPFDlnTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAG 389
Cdd:PLN02419 383 GFGAAGQRCMALSTvVFVGDakSWEDKLVERA--KALKVTCGSEPD--ADLGPVISKQAKERICRLIQSGVDDGAKLLLD 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 390 GsRPEGLPGY----FVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGG 465
Cdd:PLN02419 459 G-RDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMD 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 20129399 466 LRAGTVWVNTynVLAAQAP---FGGYKMSGHGREN--GEYALSNYTEVKSV 511
Cdd:PLN02419 538 IEAGQIGINV--PIPVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-494 |
4.29e-65 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 229.05 E-value: 4.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 50 KSKSGKIFETINPT-TAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQ---VYLASL 125
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRaelMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 126 E---TLDNGkpysmsynVD-LPTAIKNLRYFAGWADKnhgktipmdgDFFTYTRHEPVGVCGQIIPWNFPIlmmAWKLGP 201
Cdd:COG4230 642 EagkTLPDA--------IAeVREAVDFCRYYAAQARR----------LFAAPTVLRGRGVFVCISPWNFPL---AIFTGQ 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ---ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI--QLA 275
Cdd:COG4230 701 vaaALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGeTVGAALVADPRIAGVAFTGSTETARLInrTLA 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGNTNLkrVTL--ELGGKspNIILSDT---------DmdyAVETAhfglFFNMGQCCCAGSRTFVEDKIYDEFVERSAER 344
Cdd:COG4230 781 ARDGPI--VPLiaETGGQ--NAMIVDSsalpeqvvdD---VLASA----FDSAGQRCSALRVLCVQEDIADRVLEMLKGA 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 345 AKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGaKLVAGGSRPEGLP-GYFVQPTVF--ADVqDDMTiarEEIF 421
Cdd:COG4230 850 MAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLPEECAnGTFVAPTLIeiDSI-SDLE---REVF 924
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 422 GPVQQLIRFK--KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTyNVLAA----QaPFGGYKMSGHG 494
Cdd:COG4230 925 GPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR-NIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
66-509 |
2.37e-64 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 217.47 E-value: 2.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 66 EVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNvDLPTA 145
Cdd:TIGR01238 63 DIVGQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIA-EVREA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 146 IKNLRYFAGWADknhgktipmdgDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIA 225
Cdd:TIGR01238 139 VDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 226 QLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQ--LASGNTNLKRVTLELGGKSPNIILSDTDM 302
Cdd:TIGR01238 208 ELMQEAGFPAGTIQLLPGRGaDVGAALTSDPRIAGVAFTGSTEVAQLINqtLAQREDAPVPLIAETGGQNAMIVDSTALP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 303 DYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQ 382
Cdd:TIGR01238 288 EQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 383 G---AKLVAGGSRpEGLPGYFVQPTVFAdvQDDMTIAREEIFGPVQQLIRFK--KLDEVIERANNSEYGLAAAVFTKDLD 457
Cdd:TIGR01238 368 QkkiAQLTLDDSR-ACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIET 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 458 KANYIVGGLRAGTVWVNTYNVLAAQA--PFGGYKMSGHG-RENGEYALSNYTEVK 509
Cdd:TIGR01238 445 TYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
145-514 |
9.16e-62 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 208.90 E-value: 9.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 145 AIKNLRYfagWADKNHGKTiPMdGDFFT--YTRHEPVGVCGQIIPWNFPILMMawkLGP---ALATGNTIVLKPAEQTSL 219
Cdd:cd07136 70 AIKHLKK---WMKPKRVKT-PL-LNFPSksYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 220 TALYIAQLVKEAgFPEGVVNVVPGFGTAGAALANHCdVDKVAFTGSTDVGKLI-QLASgnTNLKRVTLELGGKSPNIILS 298
Cdd:cd07136 142 TSKVIAKIIEET-FDEEYVAVVEGGVEENQELLDQK-FDYIFFTGSVRVGKIVmEAAA--KHLTPVTLELGGKSPCIVDE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDlNTEQGPQVNEEQMEKILGMIKT 378
Cdd:cd07136 218 DANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 GKkqgakLVAGG-SRPEGLpgyFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLD 457
Cdd:cd07136 297 GK-----IVFGGnTDRETL---YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKK 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 458 KANYIVGGLRAGTVWVN--TYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSvIVK 514
Cdd:cd07136 369 VEKKVLENLSFGGGCINdtIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKS-ILK 426
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
175-496 |
9.38e-62 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 208.49 E-value: 9.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 175 RHEPVGVCGQIIPWNFPILMMawkLGP---ALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFGTAGAAL 251
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGADVAAAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 252 AnHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFV-E 330
Cdd:cd07133 174 S-SLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVpE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 331 DKIyDEFVERSAERAKKR---TVGNPfdlntEQGPQVNEEQMEKILGMIKTGKKQGAKLV----AGGSRPEG--LPgyfv 401
Cdd:cd07133 252 DKL-EEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIelnpAGEDFAATrkLP---- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 402 qPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN--TYNVL 479
Cdd:cd07133 322 -PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtLLHVA 400
|
330 340
....*....|....*....|.
gi 20129399 480 AAQAPFGGYKMSG----HGRE 496
Cdd:cd07133 401 QDDLPFGGVGASGmgayHGKE 421
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
60-494 |
3.51e-60 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 214.73 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INP-TTAEVIAEIQCADKEDIDIAVQAARNAFklgSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKpySMSY 138
Cdd:PRK11905 572 LNPaDHDDVVGTVTEASAEDVERALAAAQAAF---PEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK--TLAN 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVD-LPTAIKNLRYFAGWADknhgktipmdgDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQT 217
Cdd:PRK11905 647 AIAeVREAVDFLRYYAAQAR-----------RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQT 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 218 SLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQ--LASgntNLKR-VTL--ELGGK 291
Cdd:PRK11905 716 PLIAARAVRLLHEAGVPKDALQLLPGDGrTVGAALVADPRIAGVMFTGSTEVARLIQrtLAK---RSGPpVPLiaETGGQ 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 292 SPNII----LSDTDMDYAVETAhfglFFNMGQCCCAGSRTFVEDKIYDEFVE--RSAERAkkRTVGNPFDLNTEQGPQVN 365
Cdd:PRK11905 793 NAMIVdssaLPEQVVADVIASA----FDSAGQRCSALRVLCLQEDVADRVLTmlKGAMDE--LRIGDPWRLSTDVGPVID 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 366 EEQMEKILGMIKTGKKQGAKLVAGGSRPEGLPGYFVQPTVFAdvQDDMTIAREEIFGPVQQLIRFK--KLDEVIERANNS 443
Cdd:PRK11905 867 AEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKadELDRVIDDINAT 944
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 444 EYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTyNVLAA----QaPFGGYKMSGHG 494
Cdd:PRK11905 945 GYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
41-505 |
1.18e-54 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 191.59 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 41 GVFINNEWhkSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQV 120
Cdd:PLN02315 22 GCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPysmsynvdLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTR--H------EPVGVCGQIIPWNFPI 192
Cdd:PLN02315 97 YLGRLVSLEMGKI--------LAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERpnHmmmevwNPLGIVGVITAFNFPC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 193 LMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEA----GFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDV 268
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 269 GKLIQLASgNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKR 348
Cdd:PLN02315 249 GLMVQQTV-NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 349 TVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGlPGYFVQPTVfADVQDDMTIAREEIFGPVQQLI 428
Cdd:PLN02315 328 KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIES-EGNFVQPTI-VEISPDADVVKEELFGPVLYVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 429 RFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVG--GLRAGTVWVNT-YNVLAAQAPFGGYKMSGHGRENGEYALSNY 505
Cdd:PLN02315 406 KFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGplGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
74-514 |
1.63e-52 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 185.62 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 74 ADKEDIDIAVQAARNAFKLGS----PWRRmdasERGRLLYRLADLMErDQVYLASLETLDNGKPYSMSYNVDLPTA---- 145
Cdd:PTZ00381 4 DNPEIIPPIVKKLKESFLTGKtrplEFRK----QQLRNLLRMLEENK-QEFSEAVHKDLGRHPFETKMTEVLLTVAeieh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 146 -IKNLRyfaGWADKnhgKTIPMDGDFF---TYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTA 221
Cdd:PTZ00381 79 lLKHLD---EYLKP---EKVDTVGVFGpgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 222 LYIAQLVKEAgFPEGVVNVVPGfgtaGAALANHC---DVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILS 298
Cdd:PTZ00381 153 KLMAKLLTKY-LDPSYVRVIEG----GVEVTTELlkePFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAErAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKT 378
Cdd:PTZ00381 227 SCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKE-AIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 gkKQGaKLVAGGSrpEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDK 458
Cdd:PTZ00381 306 --HGG-KVVYGGE--VDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRH 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 459 ANYIVGGLRAGTVWVN--TYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:PTZ00381 381 KELVLENTSSGAVVINdcVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
82-514 |
3.67e-52 |
|
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: 183.19 E-value: 3.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 82 AVQAARNAFKLGspwRRMDASERGRLLYRLAD-LMERDQVYLASLEtLDNGKPYSMSY-------NVDLPTAIKNLRYFA 153
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEFRIQQLEALLRmLEENEDEIVEALA-KDLRKPKFEAVlseillvKNEIKYAISNLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 154 gwADKNHGKTIP--MDGdffTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLV--- 228
Cdd:cd07132 79 --KPEPVKKNLAtlLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpky 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 229 --KEAgFPegvvnVVPGFGTAGAALANHcDVDKVAFTGSTDVGKLIQLASgNTNLKRVTLELGGKSPNIILSDTDMDYAV 306
Cdd:cd07132 154 ldKEC-YP-----VVLGGVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAA-AKHLTPVTLELGGKSPCYVDKSCDIDVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 307 ETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVErSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKtgkkqGAKL 386
Cdd:cd07132 226 RRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVE-ALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 387 VAGGSRPEGlpGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGL 466
Cdd:cd07132 300 AIGGQTDEK--ERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 20129399 467 RAGTVWVN------TYNVLaaqaPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:cd07132 378 SSGGVCVNdtimhyTLDSL----PFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
60-494 |
9.41e-52 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 190.18 E-value: 9.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 60 INP-TTAEVIAEIQCADKEDIDIAVQAARNAfklGSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSmsy 138
Cdd:PRK11809 664 INPaDPRDIVGYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFS--- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NV--DLPTAIKNLRYFAGWADknhgktipmdgDFFTYTRHEPVG--VCgqIIPWNFPILMMAWKLGPALATGNTIVLKPA 214
Cdd:PRK11809 738 NAiaEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 215 EQTSLTAlyiAQLVK---EAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQ--LASGNTNLKRVT--- 285
Cdd:PRK11809 805 EQTPLIA---AQAVRillEAGVPAGVVQLLPGRGeTVGAALVADARVRGVMFTGSTEVARLLQrnLAGRLDPQGRPIpli 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 286 LELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVE--RSAERakKRTVGNPFDLNTEQGPQ 363
Cdd:PRK11809 882 AETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKmlRGAMA--ECRMGNPDRLSTDIGPV 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 364 VNEEQMEKILGMIKTGKKQGAKlVAGGSRPEGLP---GYFVQPTVFA-DVQDDMTiarEEIFGPVQQLIRFKK--LDEVI 437
Cdd:PRK11809 960 IDAEAKANIERHIQAMRAKGRP-VFQAARENSEDwqsGTFVPPTLIElDSFDELK---REVFGPVLHVVRYNRnqLDELI 1035
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399 438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTyNVLAA----QaPFGGYKMSGHG 494
Cdd:PRK11809 1036 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
44-492 |
1.09e-47 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 173.43 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 44 INNEwHKSKSGKIFETINPTT-AEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLME---RDQ 119
Cdd:TIGR01236 36 IGGE-EVYDSNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDAKK---DWSNLPFYDRAAIFLKAADLLSgpyRYE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLetLDNGK-PYSMSYNVdLPTAIKNLRYFAGWADKNHGKT-IPMDGDFFTyTRHEPV-GVCGQIIPWNFPILMMA 196
Cdd:TIGR01236 112 ILAATM--LGQSKtVYQAEIDA-VAELIDFFRFNVKYARELYAQQpISAPGEWNR-TEYRPLeGFVYAISPFNFTAIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 197 WKLGPALaTGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLI--Q 273
Cdd:TIGR01236 188 LAGAPAL-MGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQvSDQVLADPDLAGIHFTGSTNTFKHLwkK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 274 LASG---NTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTV 350
Cdd:TIGR01236 267 VAQNldrYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 351 GNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKL-VAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLI- 428
Cdd:TIGR01236 347 GDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEALtILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYv 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 429 ----RFKKLDEVIEraNNSEYGLAAAVFTKDLDKANYIVGGLR--AGTVWVN---TYNVLAAQaPFGGYKMSG 492
Cdd:TIGR01236 427 ypddKYKEILDLVD--STSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkcTGAVVGQQ-PFGGARMSG 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
106-513 |
1.33e-45 |
|
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: 165.28 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 106 RLLYRLADlmERDQVYLASLETlDNGKPYSMSYNVDLPT-------AIKNLRyfaGWADKNHGK----TIPMDGDFFTyt 174
Cdd:cd07137 28 KGLLRLVD--ENEDDIFAALRQ-DLGKPSAESFRDEVSVlvsscklAIKELK---KWMAPEKVKtpltTFPAKAEIVS-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 175 rhEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEgVVNVVPGFGTAGAALANH 254
Cdd:cd07137 100 --EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTK-AIKVIEGGVPETTALLEQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 255 cDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLF-FNMGQCCCAGSRTFVEDKI 333
Cdd:cd07137 177 -KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 334 YDEFVERSAERAKKRTVGNPfdLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEglPGYFVQPTVFADVQDDM 413
Cdd:cd07137 255 APTLIDALKNTLEKFFGENP--KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDE--KNLYIEPTILLDPPLDS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 414 TIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVN--TYNVLAAQAPFGGYKMS 491
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQYAIDTLPFGGVGES 410
|
410 420
....*....|....*....|..
gi 20129399 492 GHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07137 411 GFGAYHGKFSFDAFSHKKAVLY 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
65-492 |
8.75e-45 |
|
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: 165.07 E-value: 8.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 65 AEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLME---RDQVYLASLetLDNGKpysmsyNV- 140
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARK---EWARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGK------NVw 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 141 ----DLPT-AIKNLRYFAGWADK-NHGKTIPMDGDFFTYTRHEPV-GVCGQIIPWNFPILMMAWKLGPALaTGNTIVLKP 213
Cdd:cd07123 126 qaeiDAACeLIDFLRFNVKYAEElYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 214 AEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI-QLASGNT----NLKRVTLE 287
Cdd:cd07123 205 SDTAVLSNYLVYKILEEAGLPPGVINFVPGDGpVVGDTVLASPHLAGLHFTGSTPTFKSLwKQIGENLdryrTYPRIVGE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 288 LGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEE 367
Cdd:cd07123 285 TGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 368 QMEKILGMIKTGKKQ-GAKLVAGGSrPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRF--KKLDEVIERANN-S 443
Cdd:cd07123 365 AFDRIKGYIDHAKSDpEAEIIAGGK-CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYpdSDFEETLELVDTtS 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 444 EYGLAAAVFTKD---LDKANyivGGLR--AGTVWVN---TYNVLAAQaPFGGYKMSG 492
Cdd:cd07123 444 PYALTGAIFAQDrkaIREAT---DALRnaAGNFYINdkpTGAVVGQQ-PFGGARASG 496
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
43-466 |
1.73e-36 |
|
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: 141.64 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHkSKSGKIFETINPTTAEVIAEIQcADKEDIDIAVQAARNAfklGSP-WRRMDASERGRLLYRLAD-LMER-DQ 119
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREK---GGPaLRALTFHERAAMLKALAKyLMERkED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLET----LDNGkpysmsynVDLPTAIKNLRYFAGWA-----DKN---HGKTIPM--DGDFFTytRHEPV---GVC 182
Cdd:cd07128 79 LYALSAATgatrRDSW--------IDIDGGIGTLFAYASLGrrelpNAHflvEGDVEPLskDGTFVG--QHILTprrGVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 183 GQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAG-FPEGVVNVVpgFGTAGAALANHCDVDKVA 261
Cdd:cd07128 149 VHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLI--CGSVGDLLDHLGEQDVVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 262 FTGSTDVGKLIQlasGNTNLK----RVTLElgGKSPN-IILSDtdmDYAVETAHFGLFF-----NM----GQCCCAGSRT 327
Cdd:cd07128 227 FTGSAATAAKLR---AHPNIVarsiRFNAE--ADSLNaAILGP---DATPGTPEFDLFVkevarEMtvkaGQKCTAIRRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 328 FVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTgKKQGAKLVAGG---SRPEGLP---GYFV 401
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGpdrFEVVGADaekGAFF 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 402 QPTVF-ADVQDDMTIARE-EIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGL 466
Cdd:cd07128 378 PPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
84-494 |
2.50e-36 |
|
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: 140.07 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 84 QAARNAFKLGSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNH--- 160
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPhep 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 161 GKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAG-FPEGVVN 239
Cdd:cd07084 83 GNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 240 VVPGFGTAGAALANHCDVDKVAFTGSTDVG-KLIQLASgntnLKRVTLELGGKSPNIILSDTD-MDYAVETAHFGLFFNM 317
Cdd:cd07084 163 LINGDGKTMQALLLHPNPKMVLFTGSSRVAeKLALDAK----QARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 318 GQCCCAGSRTFV-EDKIYDEFVERSAERAKKRTVGnpfdlnteqGPQVNEEQMEKILGMIKT-GKKQGAKLVAGGS---- 391
Cdd:cd07084 239 GQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLE---------DLLLGPVQTFTTLAMIAHmENLLGSVLLFSGKelkn 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 392 -RPEGLPGYFVQPTVF--ADVQDDMTIA-REEIFGPVQQLIRFKKLDE--VIERANNSEYGLAAAVFTKDldkanYIVGG 465
Cdd:cd07084 310 hSIPSIYGACVASALFvpIDEILKTYELvTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSND-----PIFLQ 384
|
410 420
....*....|....*....|....*....
gi 20129399 466 LRAGTVWVNTYNVLAAQAPFGGYKMSGHG 494
Cdd:cd07084 385 ELIGNLWVAGRTYAILRGRTGVAPNQNHG 413
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
74-512 |
9.39e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 139.09 E-value: 9.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 74 ADKEDIDIAVQAARNAFKLGS----PWRRmdaSERGRLLYRLADlmERDQVYLASLETLdnGKPYSMSYNVDLPTAIKNL 149
Cdd:PLN02203 3 APGETLEGSVAELRETYESGRtrslEWRK---SQLKGLLRLLKD--NEEAIFKALHQDL--GKHRVEAYRDEVGVLTKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 150 RY----FAGWADKNHGK----TIPMDGDFFTytrhEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTA 221
Cdd:PLN02203 76 NLalsnLKKWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 222 LYIAQLVKeAGFPEGVVNVVPGfgtaGAALANH---CDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNI--- 295
Cdd:PLN02203 152 AFLAANIP-KYLDSKAVKVIEG----GPAVGEQllqHKWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIvds 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 296 ILSDTDMDYAVETAHFGLFFN-MGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTeQGPQVNEEQMEKILG 374
Cdd:PLN02203 226 LSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 375 MIKTGKKQgAKLVAGGS-RPEGLpgyFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFT 453
Cdd:PLN02203 305 LLKDPRVA-ASIVHGGSiDEKKL---FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399 454 KDLDKANYIVGGLRAGTVwvnTYNVLAAQ-----APFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:PLN02203 381 NNEKLKRRILSETSSGSV---TFNDAIIQyacdsLPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
61-494 |
3.10e-31 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 126.74 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 61 NPTTAEVIAEiqcADKEDIDIAVQAARNAFKLGSPWRRMDASERGRLLYRLADLM--ERDQVYLASLEtldNGKPYSMSY 138
Cdd:PRK11903 25 DPVTGEELVR---VSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLqaNRDAYYDIATA---NSGTTRNDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGD--------------FFTYTRhepvGVCGQIIPWNFPILMMAWKLGPALA 204
Cdd:PRK11903 99 AVDIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpafqgqhVLVPTR----GVALFINAFNFPAWGLWEKAAPALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 205 TGNTIVLKPAEQTSLTALYIAQLVKEAG-FPEGVVNVVPGfgtAGAALANH---CDVdkVAFTGSTDVGKLIQlASGNTN 280
Cdd:PRK11903 175 AGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAGLLDHlqpFDV--VSFTGSAETAAVLR-SHPAVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPN--IILSDTDMDyaveTAHFGLFF---------NMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRT 349
Cdd:PRK11903 249 QRSVRVNVEADSLNsaLLGPDAAPG----SEAFDLFVkevvremtvKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 350 VGNPFDLNTEQGPQVNEEQMEKILGMIKTgKKQGAKLVAGGSR--PEGLP---GYFVQPTVF-ADVQDDMTIARE-EIFG 422
Cdd:PRK11903 325 VGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGfaLVDADpavAACVGPTLLgASDPDAATAVHDvEVFG 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399 423 PVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRA--GTVWVNTYNVLAAQapfggykmSGHG 494
Cdd:PRK11903 404 PVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVISPDVAALH--------TGHG 469
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
145-514 |
2.01e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 124.00 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 145 AIKNLR-YFAGWADKNHGKTIPMDGDFFTytrhEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALY 223
Cdd:PLN02174 82 ALKQLKnWMAPEKAKTSLTTFPASAEIVS----EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 224 IAQLVkEAGFPEGVVNVVPGFGTAGAALANHcDVDKVAFTGSTDVGKLIqLASGNTNLKRVTLELGGKSPNIILSDTDMD 303
Cdd:PLN02174 158 LAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-KWDKIFYTGSSKIGRVI-MAAAAKHLTPVVLELGGKSPVVVDSDTDLK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 304 YAVETAHFGLF-FNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDlNTEQGPQVNEEQMEKILGMIKTgKKQ 382
Cdd:PLN02174 235 VTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDE-KEV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 383 GAKLVAGGSRP-EGLPgyfVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANY 461
Cdd:PLN02174 313 SDKIVYGGEKDrENLK---IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKER 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 462 IVGGLRAGTVWVNTYNVLAA--QAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:PLN02174 390 FAATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
79-495 |
1.71e-18 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 87.98 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 79 IDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLME--RDQ-VYLASLETldnGKPySMSYNVDLPTAIKNLRYFAGW 155
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEalGDElVARAHAET---GLP-EARLQGELGRTTGQLRLFADL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 156 ADKN--HGKTI-PMDGDFFTYTRHE---------PVGVCGqiiPWNFPIlmmAWKLG-----PALATGNTIVLK-----P 213
Cdd:cd07129 74 VREGswLDARIdPADPDRQPLPRPDlrrmlvplgPVAVFG---ASNFPL---AFSVAggdtaSALAAGCPVVVKahpahP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 214 AeqTS-LTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGK-LIQLASGNTNLKRVTLELGG 290
Cdd:cd07129 148 G--TSeLVARAIRAALRATGLPAGVFSLLQGGGREvGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 291 KSPNIILSDTDMDYAVETAHfGLF----FNMGQ-CCCAGSRTFVEDKIYDEFVERSAERAKkrtvgnpfdlntEQGPQVn 365
Cdd:cd07129 226 VNPVFILPGALAERGEAIAQ-GFVgsltLGAGQfCTNPGLVLVPAGPAGDAFIAALAEALA------------AAPAQT- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 366 eeqM--EKILGMIKTGKKQ-----GAKLVAGGSRPEGlpGYFVQPTVFA-DVQD--DMTIAREEIFGPVQQLIRFKKLDE 435
Cdd:cd07129 292 ---MltPGIAEAYRQGVEAlaaapGVRVLAGGAAAEG--GNQAAPTLFKvDAAAflADPALQEEVFGPASLVVRYDDAAE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 436 VIERANNSEYGLAAAVF--TKDLDKANYIVGGL--RAGTVWVNTY----NVLAAQAPFGGYKMSGHGR 495
Cdd:cd07129 367 LLAVAEALEGQLTATIHgeEDDLALARELLPVLerKAGRLLFNGWptgvEVCPAMVHGGPYPATTDPR 434
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
43-472 |
1.63e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 79.08 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 43 FINNEWHKSKsgKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLG--SPWRrmdASER----GRLLYRLADLME 116
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhNPLK---NPERyllyGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 117 RDQV--YLASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHE---PVGVCGQIIPWNFP 191
Cdd:cd07126 77 KPEVedFFARLIQRVAPKSDAQALG-EVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 192 ILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVG-K 270
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAeR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 271 LIQLASGntnlkRVTLELGGKSPNIILSD-TDMDYAVETAHFGLFFNMGQCCCAGSRTFV-EDKIYDEFVERSAERAKKR 348
Cdd:cd07126 236 LALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWVQAGILDKLKALAEQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 349 -----TVGNPFDLNTEQgpqvNEEQMEKILGMiktgkkQGAKLVAGG------SRPEGLPGYfvQPT-VFADVQ-----D 411
Cdd:cd07126 311 kledlTIGPVLTWTTER----ILDHVDKLLAI------PGAKVLFGGkpltnhSIPSIYGAY--EPTaVFVPLEeiaieE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 412 DMTIAREEIFGPVQQLIRFKK--LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVW 472
Cdd:cd07126 379 NFELVTTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
77-340 |
2.83e-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: 62.24 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 77 EDIDIAVQAARNA-FKLGSPWRRMDASERGRLLYRLA----DLMERDQVYLASLetldngkpysmsynvdlptaIKNLRY 151
Cdd:cd07077 16 EQRDLIINAIANAlYDTRQRLASEAVSERGAYIRSLIanwiAMMGCSESKLYKN--------------------IDTERG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 152 FAGWADKNHGKTIPMDGDffTYTRHEPVGVCGQIIPWNFPILMMAwKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEA 231
Cdd:cd07077 76 ITASVGHIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 232 GFPEGVVNVVPGFGTAGAALAN----HCDVDKVAFTGSTDVgklIQLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVE 307
Cdd:cd07077 153 DAAHGPKILVLYVPHPSDELAEellsHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASG 229
|
250 260 270
....*....|....*....|....*....|....
gi 20129399 308 TAHFGLFFNmgQCCCAGSRT-FVEDKIYDEFVER 340
Cdd:cd07077 230 SVHDSKFFD--QNACASEQNlYVVDDVLDPLYEE 261
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
75-455 |
1.84e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 56.72 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 75 DKEDIDIAVQAARNAFKlgsPWRrmDASERGR------LLYRLADL-MErdqvyLASLETLDNGKPYSMSYNVDLPTA-- 145
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARagvcleILQRLNARsFE-----MAHAVMHTTGQAFMMAFQAGGPHAqd 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 146 --IKNLRY----------FAGWaDKNHGKTIP--MDGDFFTYTRhepvGV-----CGQIIPWN-FPILMmawklgPALAT 205
Cdd:cd07127 152 rgLEAVAYawremsrippTAEW-EKPQGKHDPlaMEKTFTVVPR----GValvigCSTFPTWNgYPGLF------ASLAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 206 GNTIVLKPAEQTSLTA---LYIAQLV-KEAGFPEGVVNVV---PGFGTAGaALANHCDVDKVAFTGSTDVGK-LIQLASG 277
Cdd:cd07127 221 GNPVIVKPHPAAILPLaitVQVAREVlAEAGFDPNLVTLAadtPEEPIAQ-TLATRPEVRIIDFTGSNAFGDwLEANARQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 278 ntnlKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCA---------GSRTFVEDKIYDEFVERSAeRAKKR 348
Cdd:cd07127 300 ----AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTpqniyvprdGIQTDDGRKSFDEVAADLA-AAIDG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 349 TVGNPFDLNTEQGPQVNEEQMEKIlgmiktGKKQGAKLVAGGSRPEG---LPGYFVQ-PTVFADVQDDMTIAREEIFGPV 424
Cdd:cd07127 375 LLADPARAAALLGAIQSPDTLARI------AEARQLGEVLLASEAVAhpeFPDARVRtPLLLKLDASDEAAYAEERFGPI 448
|
410 420 430
....*....|....*....|....*....|....
gi 20129399 425 QQLIRFKKLDEVIERANNS--EYG-LAAAVFTKD 455
Cdd:cd07127 449 AFVVATDSTDHSIELARESvrEHGaMTVGVYSTD 482
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
167-475 |
4.25e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 55.35 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 167 DGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKP----AEQTSLTALYIAQLVKEAGFPEGVVNVV- 241
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWId 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 242 -PGFGTAgAALANHCDVDKVAFTGSTDVGKliqlaSGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQC 320
Cdd:cd07081 164 nPSIELA-QRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 321 CCAGSRTFVEDKIYDEFVERSAERakkrtvgNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKL--VAGGSRPEGLPG 398
Cdd:cd07081 238 CASEQSVIVVDSVYDEVMRLFEGQ-------GAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIaaAAGLKVPQETRI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 399 YFVQPTVFADVQddmtIAREEIFGPVQQLIRFKKLDEVIERA----NNSEYGLAAAVFT---KDLDKANYIVGGLRAGTV 471
Cdd:cd07081 311 LIGEVTSLAEHE----PFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSdniKAIENMNQFANAMKTSRF 386
|
....
gi 20129399 472 WVNT 475
Cdd:cd07081 387 VKNG 390
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
162-460 |
1.02e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 54.17 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 162 KTIPMDGDF-FTYTRHEPVGVCGQIIPWNFP--------ILMmawklgpaLATGNTIVLKP---AEQTSLTAL-YIAQLV 228
Cdd:cd07121 80 TTTAWSGDNgLTLVEYAPFGVIGAITPSTNPtetiinnsISM--------LAAGNAVVFNPhpgAKKVSAYAVeLINKAI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 229 KEAGFPEGVVNVV--PGFGTAgAALANHCDVDKVAFTGSTDVGKLIqLASGntnlKRVtLELGGKSPNIILSDT-DMDYA 305
Cdd:cd07121 152 AEAGGPDNLVVTVeePTIETT-NELMAHPDINLLVVTGGPAVVKAA-LSSG----KKA-IGAGAGNPPVVVDETaDIEKA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 306 VETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERsaerakkrtvgnpfdLNTEQGPQVNEEQMEKILGMIKTGKKQGA- 384
Cdd:cd07121 225 ARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA---------------MQRNGAYVLNDEQAEQLLEVVLLTNKGATp 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 385 --KLV----------AGGSRPEGLpgyfvqPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGL--AAA 450
Cdd:cd07121 290 nkKWVgkdaskilkaAGIEVPADI------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAI 363
|
330
....*....|
gi 20129399 451 VFTKDLDKAN 460
Cdd:cd07121 364 IHSKNVENLT 373
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
177-475 |
9.56e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.34 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 177 EPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKP---AEQTSLTAL-YIAQLVKEAGFPEGVVNVVPGFGTAGA-AL 251
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEEPSIELTqEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 252 ANHCDVDKVAFTGStdvGKLIQLA--SGNTNlkrvtleLG---GKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSR 326
Cdd:cd07122 174 MKHPDVDLILATGG---PGMVKAAysSGKPA-------IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 327 TFVEDKIYDEFVERSAERakkrtvGNPFdLNTEQgpqvnEEQMEKIlgMIKTGKKQGAKLV----------AGGSRPEGL 396
Cdd:cd07122 244 VIVDDEIYDEVRAELKRR------GAYF-LNEEE-----KEKLEKA--LFDDGGTLNPDIVgksaqkiaelAGIEVPEDT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 397 pgyfvqpTVFA----DVQDDMTIAREEIFgPVQQLIRFKKLDEVIERA----NNSEYGLAAAVFTKDLDKANYIVGGLRA 468
Cdd:cd07122 310 -------KVLVaeetGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPV 381
|
....*..
gi 20129399 469 GTVWVNT 475
Cdd:cd07122 382 SRILVNT 388
|
|
| |
