|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
40-516 |
0e+00 |
|
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: 944.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 40 VKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEI 119
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 120 AKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKR 279
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVG-EAKKWLPELVEHAKNLRVNAGDQPGADLGPL 358
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 359 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 438
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11095441 439 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 516
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
40-516 |
0e+00 |
|
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: 892.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 40 VKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEI 119
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 120 AKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKR 279
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 359
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 360 TPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 439
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11095441 440 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 516
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
38-532 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 674.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 38 PTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLK 117
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHG 277
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 278 KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGP 357
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 358 LITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQI 437
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 438 VNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWK 517
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|....*
gi 11095441 518 EEDATLSspaVVMPT 532
Cdd:PLN02419 592 DIHSPFS---LAIPI 603
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
38-516 |
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: 553.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 38 PTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLK 117
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRH 276
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 277 GKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADL 355
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 356 GPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAI 435
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 436 QIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDtnFYGKQGIQFYTQLKTITSQ 515
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIR 478
|
.
gi 11095441 516 W 516
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-512 |
3.15e-177 |
|
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: 507.07 E-value: 3.15e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 48 FVESKSDKwIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQ 127
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 128 GKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGA 286
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 287 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAK 364
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSR-LLVHEsiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 365 ERVCNLIDSGTKEGASILLDGRKikvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 444
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11095441 445 NGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
43-513 |
1.25e-135 |
|
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: 401.73 E-value: 1.25e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 201
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 359
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 360 TPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 439
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 440 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKT 511
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKA 472
|
..
gi 11095441 512 IT 513
Cdd:cd07131 473 VY 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
80-513 |
1.10e-134 |
|
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: 397.73 E-value: 1.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 80 DAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGET 159
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 160 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 239
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 240 G-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM 318
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 319 ALStAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkiKVKGYENG 396
Cdd:cd07078 241 AAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 397 NFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 476
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 11095441 477 VPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07078 397 GAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
43-512 |
1.38e-122 |
|
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: 368.12 E-value: 1.38e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKwiDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 201
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 359
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 360 TPQAKERVCNLIDSGTKEGASILLDGRKIkvKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 439
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERL--KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 440 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVP-----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKT 511
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKT 470
|
.
gi 11095441 512 I 512
Cdd:cd07097 471 V 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
43-474 |
2.95e-119 |
|
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: 359.57 E-value: 2.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKwIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKL 122
Cdd:cd07086 2 VIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVC 202
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 203 GNTFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGK 278
Cdd:cd07086 161 GNTVVWKPSETTPltaiAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 279 RVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGP 357
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 358 LITPQAKERVCNLIDSGTKEGASILLDGRKIkvKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQI 437
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 11095441 438 VNNNPYGNGTAIFTTNGATARKY--AHLVDVGQVGVNVP 474
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIP 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
59-513 |
9.50e-115 |
|
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: 347.25 E-value: 9.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAE-GD 137
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 VFRGLQVVEHACSVTSLMMGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 218 TMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 375 TKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 454
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 11095441 455 ATARKYAHLVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
61-513 |
2.91e-113 |
|
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: 343.26 E-value: 2.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFR 140
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 141 GLQVV----EHACSVTslmmGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVP 215
Cdd:cd07103 83 AASFLewfaEEARRIY----GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 216 GATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAknHG--VV 292
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 293 MPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNL 370
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 371 IDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIF 450
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11095441 451 TTNGATARKYAHLVDVGQVGVNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 513
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-512 |
1.51e-109 |
|
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: 334.62 E-value: 1.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKL 122
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 201
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLG 356
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 357 PLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQ 436
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11095441 437 IVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-512 |
9.05e-105 |
|
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: 321.40 E-value: 9.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDV 138
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 139 FRGLQVVEHACSVtslmmgeTMPSI----TKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 214
Cdd:cd07106 81 GGAVAWLRYTASL-------DLPDEviedDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 215 PGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMP 294
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 295 DANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLID 372
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 373 SGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTT 452
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 453 NGATARKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 512
Cdd:cd07106 388 DLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQSGIGVE--FGIEGLKEYTQTQVI 444
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-472 |
3.35e-102 |
|
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: 316.17 E-value: 3.35e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAM 200
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 201 VCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKR 279
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGP 357
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 358 LITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQI 437
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 11095441 438 VNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
87-513 |
7.24e-100 |
|
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: 306.08 E-value: 7.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 87 KRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKD 166
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 167 MDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAV 245
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 246 NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVL 325
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 326 VGEAkkwlpelvehaknlrvnagdqpgadlgplITPQAKERVCnlidsgtkegasilldgrkikvkgyengnfvgpTIIS 405
Cdd:cd06534 243 VHES-----------------------------IYDEFVEKLV---------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 406 NVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFT 485
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*...
gi 11095441 486 GSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd06534 341 GVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-513 |
3.04e-99 |
|
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: 307.89 E-value: 3.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQG--KTLAdAEGDVFRGLQVVEHACSVTSLMMGETMPSITKdmdlySYRLPLGVCAGIAPFNFPA-MIPLWMFPm 198
Cdd:cd07138 81 AITLEMGapITLA-RAAQVGLGIGHLRAAADALKDFEFEERRGNSL-----VVREPIGVCGLITPWNWPLnQIVLKVAP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 199 AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHG 277
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 278 KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKkwLPELVEHAK----NLRVNAGDQPGA 353
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAAaaaeAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 354 DLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDE 433
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 434 AIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPL-PmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 512
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQS--GNGREWGRYGLEEFLEVKSI 464
|
.
gi 11095441 513 T 513
Cdd:cd07138 465 Q 465
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
39-513 |
3.68e-99 |
|
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: 309.15 E-value: 3.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 39 TVKLFIGGKFVESkSDKwIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLK 117
Cdd:cd07124 32 EYPLVIGGKEVRT-EEK-IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFER---- 272
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERaakv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 273 --GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA-KKWLPELVEHAKNLRVNAGD 349
Cdd:cd07124 269 qpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 350 QPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 429
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 430 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMF-SFTGSRSSfrGDTnfyGKQG-----I 503
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMS--GTG---SKAGgpdylL 500
|
490
....*....|
gi 11095441 504 QFyTQLKTIT 513
Cdd:cd07124 501 QF-MQPKTVT 509
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
43-510 |
2.08e-97 |
|
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: 303.27 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKL 122
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 123 ITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMMGETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 201
Cdd:TIGR01804 81 ETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPL 358
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSN-GTRVFVHKKikERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 359 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 438
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11095441 439 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTynLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
37-513 |
7.74e-97 |
|
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: 301.82 E-value: 7.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 37 VPTvKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTSVLSRQQVLLRYQQLIKE 114
Cdd:cd07091 2 QPT-GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 115 NLKEIAKLITLEQGKTL-ADAEGDVfrglqvvehACSVTSL---------MMGETMPSITKDMDlYSYRLPLGVCAGIAP 184
Cdd:cd07091 81 DRDELAALESLDNGKPLeESAKGDV---------ALSIKCLryyagwadkIQGKTIPIDGNFLA-YTRREPIGVCGQIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 185 FNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSN 263
Cdd:cd07091 151 WNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 264 KAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHA 340
Cdd:cd07091 231 AVGRTIMEAAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFVQESiyDEFVEKFKARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 341 KNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFG 420
Cdd:cd07091 310 EKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 421 PVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGK 500
Cdd:cd07091 386 PVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGREL--GE 462
|
490
....*....|...
gi 11095441 501 QGIQFYTQLKTIT 513
Cdd:cd07091 463 EGLEEYTQVKAVT 475
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
59-512 |
1.01e-96 |
|
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: 301.01 E-value: 1.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 216
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 217 ATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPD 295
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 296 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 373
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 374 GTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 453
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 11095441 454 GATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-512 |
1.47e-96 |
|
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: 300.76 E-value: 1.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDV 138
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 139 FRGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 219 MLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANK 298
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 299 ENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSN-GTRVFVQRSikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 375 TKEGASILLDGRKIKVK-GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 453
Cdd:cd07090 317 KQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11095441 454 GATARKYAHLVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-472 |
1.08e-95 |
|
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: 298.72 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESkSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADT-SVLSRQQVLLRYQQLIKENLKEI 119
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 120 AKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSY----RLPLGVCAGIAPFNFP------A 189
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIaqvrREPLGVVLAIGPFNYPlnltvsK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 190 MIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEY 268
Cdd:cd07082 162 LIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 269 IFERGSRhgKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVN 346
Cdd:cd07082 236 LKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHEsvADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 347 AGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkikvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVL 426
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPII 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 11095441 427 ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07082 387 RVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
42-513 |
2.00e-95 |
|
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: 298.20 E-value: 2.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF-PAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGKTLAdaegdVFRGLQVvehACSVTSL---------MMGETM-PSIT----KDMDLYSYRLPLGVCAGIAPFN 186
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEV---GQSANFLryfagwatkINGETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 187 FPAMIPLWMFPMAMVCGNTFLMKPSERVPgATML-LAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKA 265
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 266 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCmALSTAVLVGEAKkwLPELVEHAK---- 341
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSK--FDELVTKLKqals 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 342 NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGP 421
Cdd:cd07113 310 SFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 422 VLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQ 501
Cdd:cd07113 386 VVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSA 462
|
490
....*....|..
gi 11095441 502 GIQFYTQLKTIT 513
Cdd:cd07113 463 FIDDYTELKSVM 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-512 |
1.30e-94 |
|
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: 295.50 E-value: 1.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG-DVF 139
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 140 RGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 219
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 220 LLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANK 298
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 299 ENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTK 376
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 377 EGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGAT 456
Cdd:cd07115 321 EGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11095441 457 ARKYAHLVDVGQVGVNVpipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 512
Cdd:cd07115 397 AHRVAAALKAGTVWINT--------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
58-513 |
7.14e-94 |
|
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: 293.47 E-value: 7.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 58 DIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGD 137
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 VFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 218 TMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NkentLNQLVG-AAFGA---AGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVC 368
Cdd:cd07150 242 D----LDYAVRaAAFGAfmhQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 369 NLIDSGTKEGASILldgrkikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTA 448
Cdd:cd07150 315 RQVEDAVAKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11095441 449 IFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
78-513 |
2.31e-93 |
|
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: 291.36 E-value: 2.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 78 EMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMG 157
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 158 ETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGTLN 236
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 237 IIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 315
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 316 RCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGAsilldgrKIKVK 391
Cdd:cd07104 241 ICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGA-------RLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 392 GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGV 471
Cdd:cd07104 311 GTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 11095441 472 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07104 391 NDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-510 |
7.81e-93 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 292.36 E-value: 7.81e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKL 122
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 201
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPL 358
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 359 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKgyenGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 438
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11095441 439 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-513 |
1.47e-92 |
|
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: 290.27 E-value: 1.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVFRGLQVVEHACSVTSLMMGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIP-----FDAspggegrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGsrhG-KRVQANMG 285
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 286 AKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKK--WLPELVEHAKNLRVnaGD--QPGADLGPLITP 361
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 362 QAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNN 441
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 442 PYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPipvplpmfsftgsrSSFRGDTNFYG--------KQGIQF----YTQL 509
Cdd:cd07149 383 PYGLQAGVFTNDLQKALKAARELEVGGVMINDS--------------STFRVDHMPYGgvkesgtgREGPRYaieeMTEI 448
|
....
gi 11095441 510 KTIT 513
Cdd:cd07149 449 KLVC 452
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
42-513 |
3.34e-92 |
|
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: 289.86 E-value: 3.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTSVLSRQQVLLRYQQLIKENLKEI 119
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 120 AKLITLEQGKTLA--------------DAEGDVFRGLQVVEHacsVTSLMMGETMPSitkdmdlysyRLPLGVCAGIAPF 185
Cdd:cd07139 81 ARLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEER---RPGSGGGHVLVR----------REPVGVVAAIVPW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 186 NFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKA 265
Cdd:cd07139 148 NAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 266 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKK--WLPELVEHAKNL 343
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYdeVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 344 RVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVL 423
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 424 VVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVP-LPmfsFTGSRSSfrGDTNFYGKQG 502
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQS--GIGREGGPEG 459
|
490
....*....|.
gi 11095441 503 IQFYTQLKTIT 513
Cdd:cd07139 460 LDAYLETKSIY 470
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-513 |
1.35e-91 |
|
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: 287.59 E-value: 1.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWA-DTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGD 137
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 VFRGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 218 TMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLIDS 373
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 374 GTKEGASILLDGRKIKVKgYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 453
Cdd:cd07109 317 ARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11095441 454 GATARKYAHLVDVGQVGVNVPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-472 |
4.18e-90 |
|
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: 283.86 E-value: 4.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVFRGLQVVEHACSVTSLMMGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 212
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 213 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGV 291
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 292 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERV 367
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 368 CNLIDSGTKEGASILLDGRKIKvkgyenGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGT 447
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420
....*....|....*....|....*
gi 11095441 448 AIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-513 |
5.14e-90 |
|
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: 283.46 E-value: 5.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGD 137
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 VFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 218 TMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NKENTLNqlvGAAFGA---AGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCN 369
Cdd:cd07118 242 DLDAAAD---AVVFGVyfnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 370 LIDSGTKEGASILLDGRKIkvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAI 449
Cdd:cd07118 316 YVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11095441 450 FTTNGATARKYAHLVDVGQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-512 |
1.16e-89 |
|
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: 283.53 E-value: 1.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 38 PTvKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA-WADTSVLSRQQVLLRYQQLIKENL 116
Cdd:cd07144 7 PT-GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 117 KEIAKLITLEQGKTL-ADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWM 195
Cdd:cd07144 86 DLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGS 274
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 275 RHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAK-NLRVNAGDQP 351
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 352 GADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETL 431
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 432 DEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYT 507
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYT 475
|
....*
gi 11095441 508 QLKTI 512
Cdd:cd07144 476 QTKAV 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
38-512 |
3.48e-87 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 277.15 E-value: 3.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 38 PTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLK 117
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMF 196
Cdd:PRK13252 85 ELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 197 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRH 276
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 277 GKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK--WLPELVEHAKNLRVnaGD--QPG 352
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSIKaaFEARLLERVERIRI--GDpmDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 353 ADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLD 432
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 433 EAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYTQIK 475
|
..
gi 11095441 511 TI 512
Cdd:PRK13252 476 SV 477
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-514 |
7.52e-87 |
|
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: 275.36 E-value: 7.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDV 138
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 139 FRGlqVVEH-------ACSVTSLMMGETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPS 211
Cdd:cd07092 81 LPG--AVDNfrffagaARTLEGPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 212 ERVPGATMLLAKLLQDsGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHG 290
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 291 VVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVC 368
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 369 NLIDsGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTA 448
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 449 IFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 514
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
42-472 |
3.14e-86 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 275.66 E-value: 3.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKsDKwIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:PRK03137 39 LIIGGERITTE-DK-IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGKTLADAEGDVFRGLQVVE-HACSVTSLMMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEyYARQMLKLADGKPVESRPGEHNRYFYI-PLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFER------ 272
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERaakvqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 273 GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA-KKWLPELVEHAKNLRVNAGDQP 351
Cdd:PRK03137 276 GQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVyDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 352 gADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETL 431
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 11095441 432 DEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
41-513 |
4.02e-86 |
|
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: 274.23 E-value: 4.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF---PAWADTSVLSRQQVLLRYQQLIKENLK 117
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMMGETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLW 194
Cdd:cd07141 88 YLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 195 MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERG 273
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 274 SRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQ 350
Cdd:cd07141 245 GKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 351 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETET 430
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 431 LDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVK 476
|
...
gi 11095441 511 TIT 513
Cdd:cd07141 477 TVT 479
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
57-513 |
6.87e-85 |
|
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: 270.46 E-value: 6.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVFRGLQVVEHACSVTSLMMGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 212
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 213 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSrhGKRVQANMGAKNHGV 291
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 292 VMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNL 370
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 371 IDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIF 450
Cdd:cd07094 319 VEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11095441 451 TTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 513
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-515 |
1.15e-83 |
|
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: 267.63 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 46 GKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITL 125
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 126 EQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNT 205
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 206 FLMKPSERVP--GATmLLAKLLQDSGAPDGTLNIIHGqheAVNFICD----HPDIKAISFVGSNKAGEYIFERGSRHGKR 279
Cdd:cd07151 161 VVLKPASDTPitGGL-LLAKIFEEAGLPKGVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVnaGDQ--PGADL 355
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 356 GPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAI 435
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 436 QIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITS 514
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISV 463
|
.
gi 11095441 515 Q 515
Cdd:cd07151 464 Q 464
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-512 |
3.62e-83 |
|
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: 266.03 E-value: 3.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWA-DTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG- 136
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 ------DVFRGlqVVEHACS--------VTSLMMGETMPSITKDmdlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVC 202
Cdd:cd07089 81 qvdgpiGHLRY--FADLADSfpwefdlpVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 203 GNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQ 281
Cdd:cd07089 151 GNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 282 ANMGAKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAVLVGEAKKwlPELVEHAKN----LRVNAGDQPGA 353
Cdd:cd07089 231 LELGGKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVPRSRY--DEVVEALAAafeaLPVGDPADPGT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 354 DLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDE 433
Cdd:cd07089 304 VMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 434 AIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTnfYGKQGIQFYTQL 509
Cdd:cd07089 382 AVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP-----FGGYKQSGLGRE--NGIEGLEEFLET 454
|
...
gi 11095441 510 KTI 512
Cdd:cd07089 455 KSI 457
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
80-513 |
4.03e-83 |
|
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: 264.82 E-value: 4.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 80 DAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGET 159
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 160 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 239
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 240 GQ----HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 315
Cdd:cd07105 163 HSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 316 RCMalSTA-VLVGE--AKKWLPELVEHAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRkikVKG 392
Cdd:cd07105 243 ICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGL---ADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 393 YENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 11095441 473 VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07105 393 GMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-513 |
5.73e-83 |
|
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: 265.38 E-value: 5.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTL-ADAEGD 137
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 VFRGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 218 TMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYgEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NKENTLNQLV-GAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLI 371
Cdd:cd07108 239 DLDDAVDGAIaGMRFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 372 DSGTKE-GASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIF 450
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11095441 451 TTNGATARKYAHLVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 513
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-512 |
6.11e-83 |
|
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: 265.93 E-value: 6.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 40 VKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTSVLSRQQVLLRYQQLIKENLK 117
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKT-LADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMF 196
Cdd:cd07143 87 YLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLT-YTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 197 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSR 275
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 276 HG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPG 352
Cdd:cd07143 246 SNlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQEGiyDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 353 ADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLD 432
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 433 EAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 512
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFGGYKQSGIGRE--LGEYALENYTQIKAV 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-472 |
1.64e-82 |
|
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: 264.24 E-value: 1.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDV 138
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 139 FRGLQVVEHACSVTSLMMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 219 MLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDAN 297
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 298 KENTLNQLV-GAAFGAAGQRCMALSTAvLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 375 TKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 454
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410
....*....|....*...
gi 11095441 455 ATARKYAHLVDVGQVGVN 472
Cdd:cd07107 398 SQAHRTARRVEAGYVWIN 415
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-512 |
2.85e-81 |
|
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: 261.51 E-value: 2.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSVTSLMMGETMPSitkdmdlYSYRLPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07559 82 VAETLDNGKpiretLAADipLAIDHFRYFAGVIRAQEGSLSEIDEDTLS-------YHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFER 272
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 273 GSRHGKRVQANMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRCMALSTAvLVGEA--KKWLPELVEHAKNLRV 345
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVCTCPSRA-LVQESiyDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 346 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVV 425
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 426 LETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGI 503
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyhQYPAHAP---FGGYKKSGIGRETH--KMML 467
|
....*....
gi 11095441 504 QFYTQLKTI 512
Cdd:cd07559 468 DHYQQTKNI 476
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-513 |
1.51e-79 |
|
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: 256.51 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDV 138
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 139 ---------FRGL--QVVEHAcsvtslmmGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:cd07110 81 ddvagcfeyYADLaeQLDAKA--------ERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGA 286
Cdd:cd07110 153 LKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTgDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 287 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAK 364
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 365 ERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 444
Cdd:cd07110 312 EKVLSFIARGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 445 NGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 513
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
58-512 |
1.92e-79 |
|
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: 256.38 E-value: 1.92e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 58 DIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADA- 134
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 135 EGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 214
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 215 PGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSR-HGKRVQANMGAKNHGVV 292
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 293 MPDA-NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERV 367
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 368 CNLIDSGTKEGASILLDGRKIKVKGyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGT 447
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11095441 448 AIFTTNGATARKYAHLVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-512 |
7.06e-79 |
|
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: 255.46 E-value: 7.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSVTSLMMGETMPSITKdmdlysyRLPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07117 82 MVETLDNGKpiretRAVDipLAADHFRYFAGVIRAEEGSANMIDEDTLSIVL-------REPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFER 272
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 273 GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQ 350
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiyDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 351 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETET 430
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 431 LDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQ 508
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGRETH--KSMLDAYTQ 467
|
....
gi 11095441 509 LKTI 512
Cdd:cd07117 468 MKNI 471
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
66-516 |
1.30e-78 |
|
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: 253.76 E-value: 1.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 66 EVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVV 145
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 146 EHACSVTSLMMGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKL 224
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 225 LQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQ 304
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 305 LVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIL 382
Cdd:cd07152 241 GAWGAFLHQGQICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 383 LDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAH 462
Cdd:cd07152 320 AGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 11095441 463 LVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 516
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
57-513 |
2.30e-78 |
|
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: 253.05 E-value: 2.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASckrafpAWADTSVLSRQQ---VLLRYQQLIKENLKEIAKLITLEQGKTLAD 133
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAL------AASYRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 134 AEGDVFRGLQVVEHACSVTSLMMGETMPS-IT---KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 209
Cdd:cd07146 75 TRYEVGRAADVLRFAAAEALRDDGESFSCdLTangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 210 PSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSrhGKRVQANMGAKN 288
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 289 HGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAK 364
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 365 ERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 444
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11095441 445 NGTAIFTTNGATARKYAHLVDVGQVGVNvpiPVP---LPMFSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 513
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
39-476 |
2.59e-78 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 253.68 E-value: 2.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 39 TVKLFIGGKFVESKSDKWiDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKE 118
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 119 IAKLITLEQGK----TLAD---AEGDVFR---GLqvvehACSVTSLMMGETMPSITkdmdlySY--RLPLGVCAGIAPFN 186
Cdd:PRK13473 81 FARLESLNCGKplhlALNDeipAIVDVFRffaGA-----ARCLEGKAAGEYLEGHT------SMirRDPVGVVASIAPWN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 187 FPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKA 265
Cdd:PRK13473 150 YPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 266 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNL 343
Cdd:PRK13473 229 GKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiyDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 344 RVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG-ASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPV 422
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 11095441 423 LVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 476
Cdd:PRK13473 384 VSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-499 |
2.18e-77 |
|
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: 250.63 E-value: 2.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVFRGLQVVEHACSVTSLMMGETMPsitkdMDLYS---------YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLP-----LDISArgegrqglvRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRhgKRVQANMGAK 287
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 288 NHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQA 363
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKT--GDpkDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 364 KERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPY 443
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 11095441 444 GNGTAIFTTNGATARKYAHLVDVGQVGVN-VPipvplpmfsftgsrsSFRGDTNFYG 499
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVINdVP---------------TFRVDHMPYG 425
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-513 |
2.97e-77 |
|
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: 250.22 E-value: 2.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVF 139
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 140 RGLQVVEHACSVTSLMMGE---TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 216
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 217 ATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPdIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 375 TKEGASILLDGRKIKVKGyengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 454
Cdd:cd07099 319 VAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 455 ATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
79-472 |
1.92e-76 |
|
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: 247.37 E-value: 1.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 79 MDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQV----VEHACSvtsL 154
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWIcryyAENAEA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 155 MMGETMPsiTKDMDLYSYRLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSG 229
Cdd:cd07100 78 LADEPIE--TDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 230 APDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 309
Cdd:cd07100 151 FPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 310 FGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDG 385
Cdd:cd07100 231 LQNAGQSCIA-AKRFIVHEdvYDEFLEKFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 386 RKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVD 465
Cdd:cd07100 308 KRPDGPGA----FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
....*..
gi 11095441 466 VGQVGVN 472
Cdd:cd07100 384 AGMVFIN 390
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
41-512 |
5.14e-76 |
|
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: 247.79 E-value: 5.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFP--AWADTSVLSRQQVLLRYQQLIKENLKE 118
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 119 IAKLITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMMGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWM 195
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNF-ICDHPDIKAISFVGSNKAGEYIFERGS 274
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 275 RHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEakKWLPELVEHAKN--LRVNAGD-- 349
Cdd:cd07142 242 KSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpf 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 350 QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 429
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 430 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQL 509
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQV 471
|
...
gi 11095441 510 KTI 512
Cdd:cd07142 472 KAV 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
61-513 |
2.14e-72 |
|
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: 237.63 E-value: 2.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 61 NPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTSVLsRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDV 138
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 139 FRGLQVVEHACSVTSLMMGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVL-REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 219 MLLAKLLQD-SGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07120 161 AAIIRILAEiPSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 297 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSR-VLVQRsiADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 375 TKEGASILLDGRKIkVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 454
Cdd:cd07120 320 IAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 11095441 455 ATARKYAHLVDVGQVGVNVPIPVpLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
42-472 |
5.73e-72 |
|
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: 237.29 E-value: 5.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMmgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAM 200
Cdd:cd07111 104 LESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL----------DTELAGWK-PVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 201 VCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPL 358
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 359 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 438
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430
....*....|....*....|....*....|....
gi 11095441 439 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
37-476 |
6.89e-72 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 237.71 E-value: 6.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 37 VPTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA-----WADTSVLSRQQVLLRYQQL 111
Cdd:PLN02467 5 VPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 112 IKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRL---PLGVCAGIAPFNFP 188
Cdd:PLN02467 85 ITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVlkePLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 189 AMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGE 267
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 268 YIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRV 345
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 346 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVV 425
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 11095441 426 LETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 476
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
37-472 |
1.66e-71 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 236.64 E-value: 1.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 37 VPTV---KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFP--AWADTSVLSRQQVLLRYQQL 111
Cdd:PLN02766 15 VPEIkftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 112 IKENLKEIAKLITLEQGKTLADAEG-DVFRGLQVVEHACSVTSLMMGETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAM 190
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 191 IPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYI 269
Cdd:PLN02766 174 MFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 270 FERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVN 346
Cdd:PLN02766 254 MQAAATSNlKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 347 AGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVL 426
Cdd:PLN02766 333 DPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGY----YIEPTIFTDVTEDMKIAQDEIFGPVMSLM 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 11095441 427 ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:PLN02766 409 KFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
57-474 |
8.99e-71 |
|
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: 234.02 E-value: 8.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP- 215
Cdd:cd07130 94 EVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPl 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 216 ---GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGkRVQANMGAKNHGV 291
Cdd:cd07130 174 taiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAvAARFG-RSLLELGGNNAII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 292 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERV 367
Cdd:cd07130 253 VMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGTLVGPLHTKAAVDNY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 368 CNLIDSGTKEGASILLDGRKIKvkgyENGNFVGPTIISnVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGT 447
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420
....*....|....*....|....*....
gi 11095441 448 AIFTTNGATARKY--AHLVDVGQVGVNVP 474
Cdd:cd07130 405 SIFTTDLRNAFRWlgPKGSDCGIVNVNIG 433
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
41-517 |
2.88e-68 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 229.31 E-value: 2.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFP--AWADTSVLSRQQVLLRYQQLIKENLKE 118
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 119 IAKLITLEQGKTLADAEG-DVFRGLQVVEHACSVTSLMMGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWM 195
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPA---DGPHHVQTLhePIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGS 274
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 275 RHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAvLVGEakKWLPELVEHAKN--LRVNAGD-- 349
Cdd:PLN02466 296 KSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RVYDEFVEKAKAraLKRVVGDpf 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 350 QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 429
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 430 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN------VPIPvplpmfsFTGSRSSFRGDTNfyGKQGI 503
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIGREK--GIYSL 519
|
490
....*....|....
gi 11095441 504 QFYTQLKTITSQWK 517
Cdd:PLN02466 520 NNYLQVKAVVTPLK 533
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
41-512 |
5.76e-68 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 227.09 E-value: 5.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTSVLSRQQVLLRYQQLIKENLKE 118
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 119 IAKLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIF-ERGSR 275
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 276 HGKRVQANMGAKNHGVVMPDANKentLNQLVGAA----FGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGD 349
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 350 QPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnfVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 429
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 430 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQ 504
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALE 481
|
....*...
gi 11095441 505 FYTQLKTI 512
Cdd:PRK09847 482 KFTELKTI 489
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
60-512 |
1.50e-66 |
|
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: 222.12 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVF 139
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 140 RGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 219
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 220 LLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKE 299
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 300 NTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 377
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 378 GASILLDGRKIKVkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATA 457
Cdd:cd07102 320 GARALIDGALFPE-DKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 11095441 458 RKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 512
Cdd:cd07102 399 EALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRGVT--LSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-510 |
7.45e-66 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 221.32 E-value: 7.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKL 122
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 201
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 280
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM-ALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 359
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 360 TPQAKERVCNLIDSGTKEGASILLDGRKIKVkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 439
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11095441 440 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-514 |
1.25e-65 |
|
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: 219.87 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVF 139
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 140 RGLQVVEH-ACSVTSLMMGE----TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 214
Cdd:cd07101 81 DVAIVARYyARRAERLLKPRrrrgAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 215 PGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVM 293
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 294 PDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLI 371
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 372 DSGTKEGASILLDGRKIKVKG---YEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTA 448
Cdd:cd07101 315 DDAVAKGATVLAGGRARPDLGpyfYE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11095441 449 IFTTNGATARKYAHLVDVGQVGVNVPI-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 514
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEGYaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-476 |
1.04e-64 |
|
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: 216.75 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 78 EMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVfrGLQVVEHACSVTSLMmg 157
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEV--AAMAGKIDISIKAYH-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 158 ETMPSITKDMD----LYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDG 233
Cdd:cd07095 77 ERTGERATPMAqgraVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 234 TLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 312
Cdd:cd07095 156 VLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 313 AGQRCMALSTAVLVG--EAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKv 390
Cdd:cd07095 236 AGQRCTCARRLIVPDgaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 391 kgyENGNFVGPTIIsNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 470
Cdd:cd07095 315 ---AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
....*.
gi 11095441 471 VNVPIP 476
Cdd:cd07095 391 WNRPTT 396
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
43-475 |
1.01e-63 |
|
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: 216.68 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKfvESKSDKWIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQGKTLADAEGDV--------FRGLQVVEhacsvtsLMMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07125 114 LAAAEAGKTLADADAEVreaidfcrYYAAQARE-------LFSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFE- 271
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 272 RGSRHGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAG 348
Cdd:cd07125 266 LAERDGPILPliAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 349 DQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgrKIKVKGYENGNFVGPTIISNVKPNmtCYKEEIFGPVLVVL-- 426
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLI-----APAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrf 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 11095441 427 ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI 475
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-515 |
2.41e-63 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 215.51 E-value: 2.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 49 VESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQG 128
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 129 KTLADAEGDVfrgLQVVehacsVTSLMMGETMPSITKD----------MDLYSYRLPLGVCAGIAPFNFPA------MIP 192
Cdd:PRK09407 106 KARRHAFEEV---LDVA-----LTARYYARRAPKLLAPrrragalpvlTKTTELRQPKGVVGVISPWNYPLtlavsdAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 193 lwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIkaISFVGSNKAGEYIFE 271
Cdd:PRK09407 178 ------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVLAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 272 RGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQ 350
Cdd:PRK09407 250 QAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESiYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 351 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG---YEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLE 427
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE------PTVLTGVTPDMELAREETFGPVVSVYP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 428 TETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpvpLPMFSFTGSRSSFRGDTNF---YGKQGIQ 504
Cdd:PRK09407 404 VADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---AAAWGSVDAPMGGMKDSGLgrrHGAEGLL 480
|
490
....*....|.
gi 11095441 505 FYTQLKTITSQ 515
Cdd:PRK09407 481 KYTESQTIATQ 491
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
60-472 |
8.31e-62 |
|
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: 210.23 E-value: 8.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAegdvf 139
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 140 rglqvvehacsvtslMMGETMPSITKdMD-------------------LYSYRL------PLGVCAGIAPFNFP------ 188
Cdd:cd07098 76 ---------------SLGEILVTCEK-IRwtlkhgekalrpesrpgglLMFYKRarveyePLGVVGAIVSWNYPfhnllg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 189 AMIPlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNK 264
Cdd:cd07098 140 PIIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 265 AGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKN 342
Cdd:cd07098 214 VGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKiyDKLLEILTDRVQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 343 LRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPV 422
Cdd:cd07098 293 LRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 11095441 423 LVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07098 373 MVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
110-517 |
2.46e-61 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 207.28 E-value: 2.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 110 QLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA 189
Cdd:PRK10090 6 AGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 190 -MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGE 267
Cdd:PRK10090 86 fLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 268 YIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC-MALSTAVLVGEAKKWLPELVEHAKNLRV- 345
Cdd:PRK10090 165 KIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 346 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVV 425
Cdd:PRK10090 245 NPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 426 LETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvpipvplpmfsftgsRSSFRGDTNFY------- 498
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---------------RENFEAMQGFHagwrksg 385
|
410 420
....*....|....*....|....
gi 11095441 499 -----GKQGIQFYTQLKTITSQWK 517
Cdd:PRK10090 386 iggadGKHGLHEYLQTQVVYLQSD 409
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
42-472 |
1.69e-57 |
|
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: 199.73 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKSDKWIdiHNP-ATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07083 21 LVIGGEWVDTKERMVS--VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMG--ETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPM 198
Cdd:cd07083 99 ATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 199 AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHG 277
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 278 ------KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKKWLPELVEHAKNLRVNAGDQ 350
Cdd:cd07083 258 pgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 351 PGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVL--ET 428
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKD 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 11095441 429 ETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07083 413 DDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
41-516 |
3.11e-56 |
|
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: 195.79 E-value: 3.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTSVLSRQQVLLRYQQLIKENLKE 118
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 119 IAKLITLEQGK--TLAdAEGDVFRGLQVVEHACSVTSLMMGETMP--SITKDMDL-YSYRLPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07140 87 LATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFER 272
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 273 GSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGD 349
Cdd:cd07140 246 CAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 350 QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVV--LE 427
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIIskFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 428 TETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPMFSFtgSRSSFRGDtnfYGKQGIQF 505
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPFGGF--KQSGFGKD---LGEEALNE 475
|
490
....*....|.
gi 11095441 506 YTQLKTITSQW 516
Cdd:cd07140 476 YLKTKTVTIEY 486
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
41-472 |
7.25e-56 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 194.60 E-value: 7.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWiDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWAdTSVLSRQQVLLRYQQLIKENLKE 118
Cdd:TIGR04284 2 RLLIDGKLVAGSAGTF-PTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWS-RDTALRVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 119 IAKLITLEQGKTLADAEGDVFRG-LQVVEHACSVTSLMMGETMPSITKDMDLYSYRL----PLGVCAGIAPFNFPAMIPL 193
Cdd:TIGR04284 80 LRELTIAEVGAPRMLTAGAQLEGpVDDLGFAADLAESYAWTTDLGVASPMGIPTRRTlrreAVGVVGAITPWNFPHQINL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHEAVNFICDHPDIKAISFVGSNKAGEYIFE 271
Cdd:TIGR04284 160 AKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 272 RGSRHGKRVQANMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAVLVGEAKkwLPELVEHAK----NLR 344
Cdd:TIGR04284 240 DAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVPRAR--YDEAVAAAAatmgSIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 345 VNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLV 424
Cdd:TIGR04284 314 PGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 11095441 425 VLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:TIGR04284 392 VIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
61-512 |
9.40e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 193.80 E-value: 9.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVF- 139
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 140 --RGLQ-VVEHAcsvTSLMMGET--MPSITKDMDLYSYRlPLGVCAGIAPFNFPamipLWM---FPM-AMVCGNTFLMKP 210
Cdd:PRK09406 87 caKGFRyYAEHA---EALLADEPadAAAVGASRAYVRYQ-PLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 211 SERVPGATMLLAKLLQDSGAPDG---TLNIIHGQHEAvnfICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAK 287
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGcfqTLLVGSGAVEA---ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 288 NHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL---VGEAkkWLPELVEHAKNLRVNAGDQPGADLGPLITPQAK 364
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadVYDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 365 ERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 444
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11095441 445 NGTAIFTTNGATARKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTI 512
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
61-472 |
1.27e-55 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 193.54 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFR 140
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 141 GLQV----VEHACSvtslmMGETMPSITKDMD-LYSYRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKP 210
Cdd:PRK13968 93 SANLcdwyAEHGPA-----MLKAEPTLVENQQaVIEYR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 211 SERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHG 290
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 291 VVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCN 369
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 370 LIDSGTKEGASILLDGRKIKVKGyengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAI 449
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAGAG----NYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATI 397
|
410 420
....*....|....*....|...
gi 11095441 450 FTTNGATARKYAHLVDVGQVGVN 472
Cdd:PRK13968 398 FTTDETQARQMAARLECGGVFIN 420
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
42-444 |
3.07e-54 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 190.55 E-value: 3.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 42 LFIGGKFVESKSDKwIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:PRK09457 3 LWINGDWIAGQGEA-FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQGKTLADAegdvfrglqvvehACSVTSlMMGETMPSITKdmdlYSYRL-----------------PLGVCAGIAP 184
Cdd:PRK09457 82 VIARETGKPLWEA-------------ATEVTA-MINKIAISIQA----YHERTgekrsemadgaavlrhrPHGVVAVFGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 185 FNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNK 264
Cdd:PRK09457 144 YNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 265 AGeYIFER--GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK---WLPELVEH 339
Cdd:PRK09457 224 TG-YLLHRqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQgdaFLARLVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 340 AKNLRVNAGD-QPGADLGPLITPQAKERVC----NLIDSgtkeGASILLDGRKIKvkgyENGNFVGPTIIsnvkpNMTCY 414
Cdd:PRK09457 302 AKRLTVGRWDaEPQPFMGAVISEQAAQGLVaaqaQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII-----DVTGV 368
|
410 420 430
....*....|....*....|....*....|....
gi 11095441 415 K----EEIFGPVLVVLETETLDEAIQIVNNNPYG 444
Cdd:PRK09457 369 AelpdEEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
43-472 |
3.63e-54 |
|
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: 189.97 E-value: 3.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKL 122
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 123 ITLEQGKTLADAEG-------DVFRGLQVVEHACSvtslmmgETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWM 195
Cdd:cd07116 84 ETWDNGKPVRETLAadiplaiDHFRYFAGCIRAQE-------GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGS 274
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 275 RHGKRVQANMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTAvLVGEA--KKWLPELVEHAKNLRVNA 347
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA-LIQESiyDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 348 GDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKpNMTCYKEEIFGPVLVVLE 427
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 11095441 428 TETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
61-474 |
5.79e-51 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 181.96 E-value: 5.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFR 140
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 141 GLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----G 216
Cdd:PLN02315 120 IIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 217 ATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGKRVqANMGAKNHGVVMPD 295
Cdd:PLN02315 200 MTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 296 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 373
Cdd:PLN02315 279 ADIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 374 GTKEGASILLDGRKIKvkgyENGNFVGPTIISnVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 453
Cdd:PLN02315 358 IKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
410 420
....*....|....*....|...
gi 11095441 454 GATARKY--AHLVDVGQVGVNVP 474
Cdd:PLN02315 433 PETIFKWigPLGSDCGIVNVNIP 455
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
41-503 |
1.71e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 169.55 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA 120
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 121 KLITLEQGKTLADAEGDVFRGLQVVEHAC-------SVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPL 193
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVG-------SNKA 265
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGgdtgiaiSKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 266 GEYifergsrhgkRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAVLVGE--AKKWLPELVEHAKNL 343
Cdd:PLN00412 257 GMV----------PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VVLVMEsvADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 344 RVNAGDQpGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVL 423
Cdd:PLN00412 326 TVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 424 VVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPiPVPLP-MFSFTGSRSSfrgdtnFYGKQG 502
Cdd:PLN00412 398 PVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQG 470
|
.
gi 11095441 503 I 503
Cdd:PLN00412 471 I 471
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
57-505 |
3.35e-43 |
|
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: 159.51 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF-------PAWAdtsvlsRQQVLLRYQQLIKENLKEIAKLITLEQGK 129
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrnnwlPAHE------RIAILERLADLMEERADELALLIAREGGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 130 TLADAEGDVFRGLQVVEHACSVTSLMMGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmA 199
Cdd:cd07148 75 PLVDAKVEVTRAIDGVELAADELGQLGGREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-A 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN-IIHGQHEAVNFICDhPDIKAISFVGSNKAGEYIFERGSRhGK 278
Cdd:cd07148 149 IAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 279 RVqanmgAKNHG-----VVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-VLVGEAKKWLPELVEHAKNLRVnaGDQ-- 350
Cdd:cd07148 227 RC-----ALEHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVfVPAEIADDFAQRLAAAAEKLVV--GDPtd 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 351 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLETET 430
Cdd:cd07148 300 PDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDD 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11095441 431 LDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 505
Cdd:cd07148 374 LDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
40-450 |
2.35e-42 |
|
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: 158.52 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 40 VKLFIGGKfvESKSDKWIDIHNPAT-NEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLK- 117
Cdd:cd07123 33 IPLVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 118 EIAKLITLEQGKTLADAEGDV-------FR----------GLQVVEHACSVTSLMmgetmpsitkdmdlySYRlPL-GVC 179
Cdd:cd07123 111 ELNAATMLGQGKNVWQAEIDAacelidfLRfnvkyaeelyAQQPLSSPAGVWNRL---------------EYR-PLeGFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 180 AGIAPFNFPAM------IPLWMfpmamvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHP 252
Cdd:cd07123 175 YAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 253 DIKAISFVGSNKAGEYIFER-GSRHGK-----RVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-VL 325
Cdd:cd07123 248 HLAGLHFTGSTPTFKSLWKQiGENLDRyrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAyVP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 326 VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRKIKVKGYengnFVGPTII 404
Cdd:cd07123 328 ESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY----FVEPTVI 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 11095441 405 SNVKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNN-NPYGNGTAIF 450
Cdd:cd07123 404 ETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
56-472 |
5.87e-41 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 158.44 E-value: 5.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 56 WIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADA 134
Cdd:PRK11904 563 ARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 135 EGDVfRglqvvE-------HACSVTSLM-MGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTF 206
Cdd:PRK11904 643 IAEV-R-----EavdfcryYAAQARRLFgAPEKLPGPTGESNELRLH-GRGVFVCISPWNFPLAIFLGQVAAALAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 207 LMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIfERG--SRHGKRVQ-- 281
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARII-NRTlaARDGPIVPli 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 282 ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStaVL-VGE--AKKWLPELVEHAKNLRVnaGD--QPGADLG 356
Cdd:PRK11904 795 AETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR--VLfVQEdiADRVIEMLKGAMAELKV--GDprLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 357 PLITPQAKERVCNLIDSGTKEG---ASILLDGrkikvkGYENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETETL 431
Cdd:PRK11904 871 PVIDAEAKANLDAHIERMKREArllAQLPLPA------GTENGHFVAPTAFE--IDSISQLEREVFGPILHVIryKASDL 942
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 11095441 432 DEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:PRK11904 943 DKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
59-472 |
9.98e-38 |
|
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: 145.44 E-value: 9.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPAT-NEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGD 137
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 VFRGLQVVEHACSvtslmmgetmpSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:TIGR01238 135 VREAVDFCRYYAK-----------QVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 218 TMLLAKLLQDSGAPDGTLNIIHGQHEAVN-FICDHPDIKAISFVGSNKAGEYI----FERGSRHGKRVqANMGAKNHGVV 292
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 293 MPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHA-KNLRVNAGDQPGADLGPLITPQAKERVCNLI 371
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 372 DSGTKEGASILLDGRKIKVKgYENGNFVGPTIISnvKPNMTCYKEEIFGPVL--VVLETETLDEAIQIVNNNPYGNGTAI 449
Cdd:TIGR01238 362 EHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGV 438
|
410 420
....*....|....*....|...
gi 11095441 450 FTTNGATARKYAHLVDVGQVGVN 472
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVN 461
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
101-472 |
2.89e-37 |
|
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: 142.67 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 101 RQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAE-GDVFRGLQVVEHAC----------SV-TSLMMGETMPSITKDmd 168
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALkhlkkwmkprRVsVPLLLQPAKAYVIPE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 169 lysyrlPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGtLNIIHGQHEAVN 246
Cdd:cd07087 100 ------PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEVAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 247 FICDHP-DIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVL 325
Cdd:cd07087 171 ALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 326 VGEAKKwlPELVEHAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGTkegasILLDGRKIKVKGYengnfVGP 401
Cdd:cd07087 248 VHESIK--DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11095441 402 TIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCVN 385
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
86-472 |
1.83e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 138.62 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 86 CKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLadaegdvfRGLQVVEHACSVTSLmmgetmPSITK 165
Cdd:PTZ00381 16 LKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHP--------FETKMTEVLLTVAEI------EHLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 166 DMDLY----------------SY--RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqD 227
Cdd:PTZ00381 82 HLDEYlkpekvdtvgvfgpgkSYiiPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-T 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 228 SGAPDGTLNIIHGQHEAVNFICDHP-DIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLV 306
Cdd:PTZ00381 161 KYLDPSYVRVIEGGVEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 307 GAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLrvnAGDQP--GADLGPLITPQAKERVCNLIDSgtkegasil 382
Cdd:PTZ00381 239 WGKFLNAGQTCVAPDY-VLVHRSikDKFIEALKEAIKEF---FGEDPkkSEDYSRIVNEFHTKRLAELIKD--------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 383 lDGRKIKVKGY--ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKY 460
Cdd:PTZ00381 306 -HGGKVVYGGEvdIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELV 384
|
410
....*....|..
gi 11095441 461 AHLVDVGQVGVN 472
Cdd:PTZ00381 385 LENTSSGAVVIN 396
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-472 |
8.29e-35 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 139.69 E-value: 8.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 50 ESKSDKWIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQG 128
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 129 KTLADAEGDVfRglqvvE-------HACSVTSLMMGETmpsitkdmdlySYRlPLGVCAGIAPFNFP---------Amip 192
Cdd:COG4230 645 KTLPDAIAEV-R-----EavdfcryYAAQARRLFAAPT-----------VLR-GRGVFVCISPWNFPlaiftgqvaA--- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 193 lwmfpmAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAge 267
Cdd:COG4230 704 ------ALAAGNTVLAKPAEQTP----LIAaravRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTET-- 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 268 yifergsrhGKRVQANMGAKNHGVVMPDAnkEnT--LN-----------QLVG----AAFGAAGQRCMALStaVL-VGE- 328
Cdd:COG4230 772 ---------ARLINRTLAARDGPIVPLIA--E-TggQNamivdssalpeQVVDdvlaSAFDSAGQRCSALR--VLcVQEd 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 329 -AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgRKIKV-KGYENGNFVGPTI--I 404
Cdd:COG4230 838 iADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLpEECANGTFVAPTLieI 913
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 405 SNVKPnmtcYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 472
Cdd:COG4230 914 DSISD----LEREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
80-472 |
4.01e-34 |
|
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: 133.89 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 80 DAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKtlADAEGDVFRGLQVVE---HACS------ 150
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK--PAAEVDLTEILPVLSeinHAIKhlkkwm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 151 -----VTSLMMGETMPSITKDmdlysyrlPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAK 223
Cdd:cd07134 79 kpkrvRTPLLLFGTKSKIRYE--------PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 224 LLQDSGAPDgTLNIIHGQHEAVNFICDHPdIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLN 303
Cdd:cd07134 149 IIREAFDED-EVAVFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 304 QLVGAAFGAAGQRCMALSTaVLVGEAKKwlPELVEH-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG 378
Cdd:cd07134 227 KIAWGKFLNAGQTCIAPDY-VFVHESVK--DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 379 ASILLDGrkikvKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATAR 458
Cdd:cd07134 304 AKVEFGG-----QFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVN 378
|
410
....*....|....
gi 11095441 459 KYAHLVDVGQVGVN 472
Cdd:cd07134 379 KVLARTSSGGVVVN 392
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
59-444 |
6.24e-33 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 134.22 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 59 IHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGD 137
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 138 V--------FRGLQVvehacsvtslmmgetmpsitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 209
Cdd:PRK11905 651 VreavdflrYYAAQA--------------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 210 PSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIfER--GSRHGKRVQ- 281
Cdd:PRK11905 711 PAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPl 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 282 -ANMGAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRCMALStaVL-VGE--AKKWLPELVEHAKNLRVNAGDQPGA 353
Cdd:PRK11905 786 iAETGGQNAMIVDSSALPE----QVVADviasAFDSAGQRCSALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLST 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 354 DLGPLITPQAKERVCNLIDSGTKEGASIlldgRKIKV-KGYENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETET 430
Cdd:PRK11905 860 DVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADE 933
|
410
....*....|....
gi 11095441 431 LDEAIQIVNNNPYG 444
Cdd:PRK11905 934 LDRVIDDINATGYG 947
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
58-444 |
1.35e-32 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 133.18 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 58 DIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEG 136
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 137 DVfRglQVVE----HACSVTSlmmgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 212
Cdd:PRK11809 742 EV-R--EAVDflryYAGQVRD------------DFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 213 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGS---------NKAGeyifeRGSRHGKRVQ- 281
Cdd:PRK11809 806 QTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGStevarllqrNLAG-----RLDPQGRPIPl 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 282 -ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLI 359
Cdd:PRK11809 881 iAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 360 TPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETETLDEAIQI 437
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVryNRNQLDELIEQ 1037
|
....*..
gi 11095441 438 VNNNPYG 444
Cdd:PRK11809 1038 INASGYG 1044
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
175-451 |
2.74e-29 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 120.02 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 175 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHEAVNFICDHPDI 254
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 255 KaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKkwLP 334
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 335 ELVEHAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSgTKegASILLDGRKIKVKgyengNFVGPTIISNVKPNM 411
Cdd:cd07135 263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT-TK--GKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 11095441 412 TCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFT 451
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
81-434 |
2.96e-28 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 117.34 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 81 AAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKT---LADAEGDV--FRGLQVVEHACSVTSLM 155
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPHEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 156 MGEtmPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGT 234
Cdd:cd07084 83 GNH--LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 235 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGsrHGKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGAA 313
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 314 GQRCMALStAVLVGEAKKWLPeLVEHAKNLRVNAGDQpGADLGPLITPQAKERvcnlIDSGTKEGASILLDGRKIkVKGY 393
Cdd:cd07084 239 GQKCTAQS-MLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAM----IAHMENLLGSVLLFSGKE-LKNH 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 11095441 394 ENGNFVGPTIISNV----KPNMTCYK---EEIFGPVLVVLETETLDEA 434
Cdd:cd07084 311 SIPSIYGACVASALfvpiDEILKTYElvtEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
170-459 |
8.18e-28 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 116.06 E-value: 8.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 170 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNF 247
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 248 IC----DHpdikaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 323
Cdd:cd07136 172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 324 VLVGEAKK--WLPELVEHAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGrkikvKGYENGNFV 399
Cdd:cd07136 246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYI 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11095441 400 GPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNGATARK 459
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
77-512 |
2.53e-26 |
|
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: 111.35 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 77 AEMDAAIASCKRAFPAWadtsvlsRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAegdvFRG-LQVVEHACSVTSLM 155
Cdd:cd07137 6 RELRETFRSGRTRSAEW-------RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAES----FRDeVSVLVSSCKLAIKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 156 MGETMPSITKDMDLYSYRL-------PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ-- 226
Cdd:cd07137 75 LKKWMAPEKVKTPLTTFPAkaeivsePLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPey 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 227 -DSGApdgtLNIIHGQHEAVNFICDHPDIKaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQL 305
Cdd:cd07137 155 lDTKA----IKVIEGGVPETTALLEQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 306 VGAAFGA-AGQRCMALSTaVLVGEakKWLPELVEHAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgTKEGASI 381
Cdd:cd07137 230 AGGKWGCnNGQACIAPDY-VLVEE--SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 382 LLDGRKIkvkgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYA 461
Cdd:cd07137 306 VHGGERD-----EKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 11095441 462 HLVDVGQVGVN-VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 512
Cdd:cd07137 381 AETSSGGVTFNdTVVQYAIDTLPFGGVGES--GFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
175-472 |
6.36e-23 |
|
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: 101.41 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 175 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHE------AV 245
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 246 NFicDHpdikaISFVGSnkageyifergSRHGKRVQAN-----------MGAKNHGVVMPDANKENTLNQLVGAAFGAAG 314
Cdd:cd07133 177 PF--DH-----LLFTGS-----------TAVGRHVMRAaaenltpvtleLGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 315 QRCMAlSTAVLVGEAKkwLPELVEHAKNL------RVNAGDqpgaDLGPLITPQAKERVCNLIDSGTKEGASI------- 381
Cdd:cd07133 239 QTCVA-PDYVLVPEDK--LEEFVAAAKAAvakmypTLADNP----DYTSIINERHYARLQGLLEDARAKGARVielnpag 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 382 --LLDGRKIkvkgyengnfvGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNG 454
Cdd:cd07133 312 edFAATRKL-----------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDK 375
|
330
....*....|....*...
gi 11095441 455 ATARKYAHLVDVGQVGVN 472
Cdd:cd07133 376 AEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
168-440 |
9.84e-22 |
|
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: 97.68 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 168 DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEA- 244
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 245 --VNFICDHpdikaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA--- 319
Cdd:cd07132 171 elLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdy 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 320 -LSTavlvgeaKKWLPELVEHAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSGtkegasilldgrKIKVKGY-- 393
Cdd:cd07132 246 vLCT-------PEVQEKFVEALKKtLKEFYGEDPkeSPDYGRIINDRHFQRLKKLLSGG------------KVAIGGQtd 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 11095441 394 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNN 440
Cdd:cd07132 307 EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINS 353
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
175-512 |
2.49e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 90.88 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 175 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHEAVNFICDHPDI 254
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 255 KaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTAVlvgEAKKWL 333
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYIL---TTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 334 PELVEHAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgtKEGASILLDGRKikvKGYENGNfVGPTIISNVKPN 410
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 411 MTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTGSRS 489
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
|
330 340
....*....|....*....|...
gi 11095441 490 SFRGdtNFYGKQGIQFYTQLKTI 512
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
77-459 |
2.76e-16 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 81.31 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 77 AEMDAAIASCKRAFPAWadtsvlsRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAegdvFRG-LQVVEHACSVTSLM 155
Cdd:PLN02203 13 AELRETYESGRTRSLEW-------RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEA----YRDeVGVLTKSANLALSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 156 MGETMPSITKDMDLYSYRL-------PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ 226
Cdd:PLN02203 82 LKKWMAPKKAKLPLVAFPAtaevvpePLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 227 ---DSGApdgtLNIIHGQHEAVNFICDHPDIKaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENT-- 301
Cdd:PLN02203 160 kylDSKA----VKVIEGGPAVGEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 302 -LNQLVGAAFGA-AGQRCMALSTaVLVGEakKWLPELVEHAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSgTK 376
Cdd:PLN02203 235 aVNRIVGGKWGScAGQACIAIDY-VLVEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 377 EGASIL----LDGRKIkvkgyengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTT 452
Cdd:PLN02203 311 VAASIVhggsIDEKKL---------FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTN 381
|
....*..
gi 11095441 453 NGATARK 459
Cdd:PLN02203 382 NEKLKRR 388
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
43-438 |
2.75e-13 |
|
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: 72.14 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESKsdKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLL------RYQQLIKENL 116
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLLygdvshRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 117 KE--IAKLITLEQGKTLADAEGDVFRGLQVVEHAC--SVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIP 192
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 193 LWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKageyIFER 272
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSK----VAER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 273 GSR--HGKrVQANMGAKNHGVVMPDANKENTLN-QLVGAAFGAAGQRCMALStavLVGEAKKWLPE-LVEHAKNLrvnAG 348
Cdd:cd07126 236 LALelHGK-VKLEDAGFDWKILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS---ILFAHENWVQAgILDKLKAL---AE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 349 DQPGADL--GPLITpQAKERVCNLIDSGTK-EGASILLDGRKIK------VKG-YENGNFVGPTIISNVKPNMTCYKEEI 418
Cdd:cd07126 309 QRKLEDLtiGPVLT-WTTERILDHVDKLLAiPGAKVLFGGKPLTnhsipsIYGaYEPTAVFVPLEEIAIEENFELVTTEV 387
|
410 420
....*....|....*....|
gi 11095441 419 FGPVLVVleTETLDEAIQIV 438
Cdd:cd07126 388 FGPFQVV--TEYKDEQLPLV 405
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
80-466 |
3.70e-13 |
|
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: 71.42 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 80 DAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQG-----------------KTLADA--EGDVFR 140
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLFADLvrEGSWLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 141 GlqVVEHAcsvtslmmgetMPSITKD--MDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMKP 210
Cdd:cd07129 82 A--RIDPA-----------DPDRQPLprPDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 211 SERVPGATMLLAKL----LQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSR--HGKRVQAN 283
Cdd:cd07129 143 HPAHPGTSELVARAiraaLRATGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 284 MGAKNHGVVMPDANKEN--TLNQ-LVGAAFGAAGQRCmaLSTAVLVGEAKKWLPELVEHAKNLrvnAGDQPGadlGPLIT 360
Cdd:cd07129 223 LGSVNPVFILPGALAERgeAIAQgFVGSLTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTMLT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 361 PqakeRVCNLIDSGTKE-----GASILLDGRkikvkGYENGNFVGPTI--------ISNVKpnmtcYKEEIFGPVLVVLE 427
Cdd:cd07129 295 P----GIAEAYRQGVEAlaaapGVRVLAGGA-----AAEGGNQAAPTLfkvdaaafLADPA-----LQEEVFGPASLVVR 360
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 11095441 428 TETLDEAIQIVNNNPyGNGTA-IFTTNGATArKYAHLVDV 466
Cdd:cd07129 361 YDDAAELLAVAEALE-GQLTAtIHGEEDDLA-LARELLPV 398
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
76-493 |
2.32e-09 |
|
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: 59.80 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 76 KAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLI--TLEQGKTLADAEGDVF---RGLQVVEHACS 150
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVmhTTGQAFMMAFQAGGPHaqdRGLEAVAYAWR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 151 VTSLMMGETM---PSITKD---MDLYSYRLPLGVCAGIAPFNFPAmiplW-----MFPmAMVCGNTFLMKPServPGATM 219
Cdd:cd07127 163 EMSRIPPTAEwekPQGKHDplaMEKTFTVVPRGVALVIGCSTFPT----WngypgLFA-SLATGNPVIVKPH---PAAIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 220 LLA-------KLLQDSG-APD-GTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIfERGSRhGKRVQANMGAKNHG 290
Cdd:cd07127 235 PLAitvqvarEVLAEAGfDPNlVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANAR-QAQVYTEKAGVNTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 291 VVmpdankENTlNQLVGA----AFGAA---GQRCMAlSTAVLV-------GEAKKWLPELVEH-AKNLRVNAGDQPGAD- 354
Cdd:cd07127 313 VV------DST-DDLKAMlrnlAFSLSlysGQMCTT-PQNIYVprdgiqtDDGRKSFDEVAADlAAAIDGLLADPARAAa 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 355 -LGPLITPQAKERVcnlidSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDE 433
Cdd:cd07127 385 lLGAIQSPDTLARI-----AEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDH 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11095441 434 AIQIVNNNPYGNGT---AIFTTNGATARKYAHLVDvgQVGVNVPIPVPLPMF-SFTGSRSSFRG 493
Cdd:cd07127 460 SIELARESVREHGAmtvGVYSTDPEVVERVQEAAL--DAGVALSINLTGGVFvNQSAAFSDFHG 521
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
177-461 |
9.57e-09 |
|
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: 57.66 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 177 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQheaVNFICDHPDIK 255
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 256 -AISFVGSNKAGEYIfeRGS----RHGKRVQANMGAKNHGVVMPDAnKENT------LNQLVGAAFGAAGQRCMALSTAv 324
Cdd:cd07128 223 dVVAFTGSAATAAKL--RAHpnivARSIRFNAEADSLNAAILGPDA-TPGTpefdlfVKEVAREMTVKAGQKCTAIRRA- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 325 LVGEAKkwLPELVE--HAKNLRVNAGD--QPGADLGPLITPQAKERVCNLIDSgTKEGASILL---DGRKIKVKGYENGN 397
Cdd:cd07128 299 FVPEAR--VDAVIEalKARLAKVVVGDprLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFggpDRFEVVGADAEKGA 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11095441 398 FVGPTII--SNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNnpyGNG---TAIFTTNGATARKYA 461
Cdd:cd07128 376 FFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFARELV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
43-438 |
1.40e-06 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 50.86 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 43 FIGGKFVESkSDKWIDIHNPATNEVIGRVpQATKAEMDAAIASCK-RAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAK 121
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFAReQGGAALRALTYAQRAALLAAIVKVLQANRDAYYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 122 LITLEQGKTLADAEGDVFRGLQVVEHACSV------TSLMMGETMPSITKDmDLYSYR---LPL-GVCAGIAPFNFPAMi 191
Cdd:PRK11903 86 IATANSGTTRNDSAVDIDGGIFTLGYYAKLgaalgdARLLRDGEAVQLGKD-PAFQGQhvlVPTrGVALFINAFNFPAW- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 192 PLW-MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQHEAvnfICDH---PDIkaISFVGSNKAG 266
Cdd:PRK11903 164 GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG---LLDHlqpFDV--VSFTGSAETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 267 EYIFERGS--RHGKRVQANMGAKNHGVVMPDANKEntlnqlvGAAFGA------------AGQRCMALSTaVLVGEAkkw 332
Cdd:PRK11903 239 AVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQKCTAIRR-IFVPEA--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 333 LPELVEHAKNLR---VNAGD--QPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRKIKVKGYEN--GNFVGPTIIS 405
Cdd:PRK11903 308 LYDAVAEALAARlakTTVGNprNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPavAACVGPTLLG 386
|
410 420 430
....*....|....*....|....*....|....*
gi 11095441 406 NVKPN--MTCYKEEIFGPVLVVLETETLDEAIQIV 438
Cdd:PRK11903 387 ASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
79-293 |
4.46e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 46.10 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 79 MDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLAD-------AEGDVFRGLQVVEHACSV 151
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 152 TSlmmGETMPSITKDMDlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD---- 227
Cdd:cd07081 81 LT---GDENGGTLIIAE------PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaava 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11095441 228 SGAPDGTLNIIHGQH-EAVNFICDHPDIKAISFVGsnkaGEYIFERGSRHGKRVQAnMGAKNHGVVM 293
Cdd:cd07081 152 AGAPENLIGWIDNPSiELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVI 213
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
144-338 |
4.81e-05 |
|
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: 45.68 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 144 VVEHACSVTSLMMGETmpsitkdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAK 223
Cdd:cd07077 79 SVGHIQDVLLPDNGET----------YVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095441 224 LLQDSGAPDGTLNII----HGQHEAVNFICDHPDIKAISFVGSNKAGEYIfeRGSRHGKRVQAnMGAKNHGVVMPDANKE 299
Cdd:cd07077 148 LFQAADAAHGPKILVlyvpHPSDELAEELLSHPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADE 224
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 11095441 300 NTLNQLV--GAAF-GAAgqrCMALSTAVLVGEAKKWLPELVE 338
Cdd:cd07077 225 ERASGSVhdSKFFdQNA---CASEQNLYVVDDVLDPLYEEFK 263
|
|
| |
