|
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: 938.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 40 VKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEI 119
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 120 ARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKR 279
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVG-EAKKWLPELVERAKNLRVNAGDQPGADLGPL 358
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 359 ITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIV 438
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205526 439 NDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 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: 891.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 40 VKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEI 119
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 120 ARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKR 279
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVERAKNLRVNAGDQPGADLGPLI 359
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 360 TPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 439
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205526 440 DNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 516
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
22-532 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 674.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 22 VNSTWY---PASSFSSSSVPTVKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSI 98
Cdd:PLN02419 93 LRSSWLstsPEQSTQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 99 LSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGV 178
Cdd:PLN02419 173 TTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 179 CAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAIS 258
Cdd:PLN02419 253 CAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 259 FVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVE 338
Cdd:PLN02419 333 FVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 339 RAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEI 418
Cdd:PLN02419 413 RAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEI 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 419 FGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFY 498
Cdd:PLN02419 493 FGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFY 572
|
490 500 510
....*....|....*....|....*....|....
gi 205526 499 GKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 532
Cdd:PLN02419 573 GKAGVDFFTQIKLVTQKQKDIHSPFS---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: 553.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 38 PTVKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLK 117
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRN 276
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 277 GKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVERAKNLRVNAGDQPGADL 355
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 356 GPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAI 435
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 436 KIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDtnFYGKQGIQFYTQLKTITSQ 515
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIR 478
|
.
gi 205526 516 W 516
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-512 |
1.21e-175 |
|
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: 502.83 E-value: 1.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 48 FVESKSDKwIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQ 127
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 128 GKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGA 286
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 287 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAK 364
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSR-LLVHEsiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 365 ERVCNLIDSGAKEGASILLDGRKikvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYG 444
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205526 445 NGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
43-513 |
1.50e-138 |
|
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: 409.04 E-value: 1.50e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIAR 121
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 122 LITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 201
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVERAKNLRVNAGDQPGADLGPLI 359
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 360 TPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 439
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 440 DNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKT 511
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKA 472
|
..
gi 205526 512 IT 513
Cdd:cd07131 473 VY 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
80-513 |
4.99e-135 |
|
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: 398.50 E-value: 4.99e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 80 EAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGET 159
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 160 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 239
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 240 G-QHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM 318
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 319 ALStAVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGrkiKVKGYENG 396
Cdd:cd07078 241 AAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 397 NFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIP 476
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 205526 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 |
1.65e-125 |
|
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: 375.82 E-value: 1.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKwiDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIAR 121
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 122 LITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 201
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKKWLPELVERAKNLRVNAGDQPGADLGPLI 359
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 360 TPQAKERVCNLIDSGAKEGASILLDGRKIkvKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 439
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERL--KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 440 DNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVP-----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKT 511
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKT 470
|
.
gi 205526 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 |
2.25e-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: 359.96 E-value: 2.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKwIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARL 122
Cdd:cd07086 2 VIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVC 202
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 203 GNTFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGK 278
Cdd:cd07086 161 GNTVVWKPSETTPltaiAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 279 RVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVERAKNLRVNAGDQPGADLGP 357
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 358 LITPQAKERVCNLIDSGAKEGASILLDGRKIkvKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKI 437
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 205526 438 VNDNPYGNGTAIFTTNGAIARKY--AHMVDVGQVGVNVP 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 |
2.28e-114 |
|
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: 346.47 E-value: 2.28e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GD 137
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVEHACSVTSLMLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 218 TMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 297 NKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 375 AKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 454
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 205526 455 AIARKYAHMVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-512 |
1.95e-111 |
|
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: 339.24 E-value: 1.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARL 122
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 201
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVERAKNLRVnaGD--QPGADLG 356
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 357 PLITPQAKERVCNLIDSGAKEGASILLDGRKIKVkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIK 436
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205526 437 IVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
61-513 |
6.06e-111 |
|
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: 337.48 E-value: 6.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 61 NPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 140
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 141 GLQVV----EHACSVTslmlGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVP 215
Cdd:cd07103 83 AASFLewfaEEARRIY----GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 216 GATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAknHG--VV 292
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 293 MPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNL 370
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 371 IDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIF 450
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205526 451 TTNGAIARKYAHMVDVGQVGVNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 513
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-472 |
1.40e-107 |
|
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: 330.04 E-value: 1.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAM 200
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 201 VCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKR 279
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGP 357
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 358 LITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKI 437
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 205526 438 VNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-512 |
3.32e-106 |
|
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: 325.25 E-value: 3.32e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV 138
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 139 FRGLQVVEHacsVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07106 81 GGAVAWLRY---TASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 219 MLLAKLLQDSgAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANK 298
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 299 ENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAK 376
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 377 EGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAI 456
Cdd:cd07106 316 KGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 205526 457 ARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 512
Cdd:cd07106 392 AEAVARRLEAGTVWIN-THGALDPDAPFGGHKQSGIGVE--FGIEGLKEYTQTQVI 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-513 |
9.48e-101 |
|
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: 311.74 E-value: 9.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIAR 121
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 122 LITLEQGktladAEGDVFRGLQVvehACSVTSLmlgETMPSITKDMDLYSY-------RLPLGVCAGIAPFNFPA-MIPL 193
Cdd:cd07138 81 AITLEMG-----APITLARAAQV---GLGIGHL---RAAADALKDFEFEERrgnslvvREPIGVCGLITPWNWPLnQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 194 WMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFER 272
Cdd:cd07138 150 KVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKkwLPELVERAK----NLRVNAG 348
Cdd:cd07138 229 AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAAaaaeAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 349 DQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKiKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLET 428
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 429 ETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPL-PmfsFTGSRSSfrGDTNFYGKQGIQFYT 507
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQS--GNGREWGRYGLEEFL 459
|
....*.
gi 205526 508 QLKTIT 513
Cdd:cd07138 460 EVKSIQ 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
84-513 |
5.20e-99 |
|
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: 303.77 E-value: 5.20e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 84 AACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSI 163
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 164 TKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QH 242
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 243 EAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 322
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 323 aVLVGEAKKwlPELVERAKnlrvnagdqpgadlgplitpqakervcnlidsgakegasilldgrkikvkgyengnfvgpT 402
Cdd:cd06534 241 -LLVHESIY--DEFVEKLV------------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 403 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMF 482
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA 337
|
410 420 430
....*....|....*....|....*....|.
gi 205526 483 SFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd06534 338 PFGGVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
59-512 |
1.02e-98 |
|
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: 306.01 E-value: 1.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG 136
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 DVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 216
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 217 ATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPD 295
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 296 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 373
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 374 GAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 453
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 205526 454 GAIARKYAHMVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
43-510 |
2.12e-98 |
|
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: 305.58 E-value: 2.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARL 122
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 123 ITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMLGETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 201
Cdd:TIGR01804 81 ETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPL 358
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSN-GTRVFVHKKikERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 359 ITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIV 438
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205526 439 NDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTynLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-512 |
4.67e-97 |
|
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: 301.92 E-value: 4.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV 138
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 139 FRGLQVVEHACSVTSLMLGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 219 MLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANK 298
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 299 ENTLNQLVGAAFGAAGQRCmALSTAVLVGEA--KKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVC-SNGTRVFVQRSikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 375 AKEGASILLDGRKIKVK-GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 453
Cdd:cd07090 317 KQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205526 454 GAIARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
37-513 |
1.62e-96 |
|
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: 301.05 E-value: 1.62e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 37 VPTvKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA--WADTSILSRQQVLLRYQQLIKE 114
Cdd:cd07091 2 QPT-GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 115 NLKEIARLITLEQGKTL-ADAEGDVfrglqvvehACSVTSL---------MLGETMPSITKDMDlYSYRLPLGVCAGIAP 184
Cdd:cd07091 81 DRDELAALESLDNGKPLeESAKGDV---------ALSIKCLryyagwadkIQGKTIPIDGNFLA-YTRREPIGVCGQIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 185 FNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSN 263
Cdd:cd07091 151 WNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 264 QAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERA 340
Cdd:cd07091 231 AVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFVQESiyDEFVEKFKARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 341 KNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFG 420
Cdd:cd07091 310 EKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 421 PVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGK 500
Cdd:cd07091 386 PVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGREL--GE 462
|
490
....*....|...
gi 205526 501 QGIQFYTQLKTIT 513
Cdd:cd07091 463 EGLEEYTQVKAVT 475
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-512 |
3.26e-96 |
|
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: 299.74 E-value: 3.26e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 61 NPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG-DVF 139
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 140 RGLQVVEHACSVTSLMLGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 219
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 220 LLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANK 298
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 299 ENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAK 376
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 377 EGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAI 456
Cdd:cd07115 321 EGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205526 457 ARKYAHMVDVGQVGVNVpipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 512
Cdd:cd07115 397 AHRVAAALKAGTVWINT--------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
39-513 |
3.55e-96 |
|
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: 301.45 E-value: 3.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 39 TVKLFIDGKFVESkSDKwIDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLK 117
Cdd:cd07124 32 EYPLVIGGKEVRT-EEK-IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFER---- 272
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERaakv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 --GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA-KKWLPELVERAKNLRVNAGD 349
Cdd:cd07124 269 qpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 350 QPGADLGPLITPQAKERVCNLIDSGAKEGaSILLDGRKIKVKgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETE 429
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 430 TLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMF-SFTGSRSSfrGDTnfyGKQG-----I 503
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMS--GTG---SKAGgpdylL 500
|
490
....*....|
gi 205526 504 QFyTQLKTIT 513
Cdd:cd07124 501 QF-MQPKTVT 509
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
58-513 |
1.31e-93 |
|
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: 292.70 E-value: 1.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 58 DIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 137
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 218 TMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 297 NkentLNQLVG-AAFGA---AGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAKERVC 368
Cdd:cd07150 242 D----LDYAVRaAAFGAfmhQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 369 NLIDSGAKEGASILldgrkikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 448
Cdd:cd07150 315 RQVEDAVAKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205526 449 IFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
42-513 |
2.16e-93 |
|
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: 292.94 E-value: 2.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEI 119
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 120 ARLITLEQGKTLA--------------DAEGDVFRGLQVVEHacsVTSLMLGETMPSitkdmdlysyRLPLGVCAGIAPF 185
Cdd:cd07139 81 ARLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEER---RPGSGGGHVLVR----------REPVGVVAAIVPW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 186 NFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQA 265
Cdd:cd07139 148 NAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 266 GEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKK--WLPELVERAKNL 343
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYdeVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 344 RVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVL 423
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 424 VVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVP-LPmfsFTGSRSSfrGDTNFYGKQG 502
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQS--GIGREGGPEG 459
|
490
....*....|.
gi 205526 503 IQFYTQLKTIT 513
Cdd:cd07139 460 LDAYLETKSIY 470
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
42-513 |
2.32e-93 |
|
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: 293.19 E-value: 2.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF-PAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGKTLAdaegdVFRGLQVvehACSVTSL---------MLGETM-PSIT----KDMDLYSYRLPLGVCAGIAPFN 186
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEV---GQSANFLryfagwatkINGETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 187 FPAMIPLWMFPMAMVCGNTFLMKPSERVPgATML-LAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQA 265
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 266 GEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCmALSTAVLVGEAKkwLPELVE----RAK 341
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSK--FDELVTklkqALS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 342 NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGP 421
Cdd:cd07113 310 SFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 422 VLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQ 501
Cdd:cd07113 386 VVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSA 462
|
490
....*....|..
gi 205526 502 GIQFYTQLKTIT 513
Cdd:cd07113 463 FIDDYTELKSVM 474
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
78-513 |
7.86e-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: 290.20 E-value: 7.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 78 EMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLG 157
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 158 ETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGTLN 236
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 237 IIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 315
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 316 RCMALSTaVLVGE--AKKWLPELVERAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGAKEGAsilldgrKIKVK 391
Cdd:cd07104 241 ICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGA-------RLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 392 GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGV 471
Cdd:cd07104 311 GTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 205526 472 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07104 391 NDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-472 |
1.00e-92 |
|
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: 291.40 E-value: 1.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESkSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADT-SILSRQQVLLRYQQLIKENLKEI 119
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 120 ARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSY----RLPLGVCAGIAPFNFP------A 189
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIaqvrREPLGVVLAIGPFNYPlnltvsK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 190 MIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEY 268
Cdd:cd07082 162 LIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 269 IFERGSRngKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVN 346
Cdd:cd07082 236 LKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHEsvADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 347 AGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGrkikvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVL 426
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPII 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 205526 427 ETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07082 387 RVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-510 |
3.88e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 290.44 E-value: 3.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARL 122
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 201
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPL 358
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 359 ITPQAKERVCNLIDSGAKEGASILLDGRKIKVKgyenGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIV 438
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205526 439 NDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-513 |
5.81e-92 |
|
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: 288.47 E-value: 5.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 60 HNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 137
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 218 TMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 297 NKENTLNqlvGAAFGA---AGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAKERVCN 369
Cdd:cd07118 242 DLDAAAD---AVVFGVyfnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 370 LIDSGAKEGASILLDGRKIkvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAI 449
Cdd:cd07118 316 YVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205526 450 FTTNGAIARKYAHMVDVGQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-513 |
5.90e-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: 288.73 E-value: 5.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 57 IDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG 136
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 DVFRGLQVVEHACSVTSLMLGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIP-----FDAspggegrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGsrnG-KRVQANMG 285
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 286 AKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKK--WLPELVERAKNLRVnaGD--QPGADLGPLITP 361
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 362 QAKERVCNLIDSGAKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDN 441
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 442 PYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPipvplpmfsftgsrSSFRGDTNFYG--------KQGIQF----YTQL 509
Cdd:cd07149 383 PYGLQAGVFTNDLQKALKAARELEVGGVMINDS--------------STFRVDHMPYGgvkesgtgREGPRYaieeMTEI 448
|
....
gi 205526 510 KTIT 513
Cdd:cd07149 449 KLVC 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-513 |
1.31e-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: 1.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWA-DTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 137
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVE-HACSVTSLMlGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 216
Cdd:cd07109 81 VEAAARYFEyYGGAADKLH-GETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 217 ATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPD 295
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 296 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLID 372
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 373 SGAKEGASILLDGRKIKVKgYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 452
Cdd:cd07109 316 RARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205526 453 NGAIARKYAHMVDVGQVGVNVPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-512 |
1.15e-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: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 38 PTvKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA-WADTSILSRQQVLLRYQQLIKENL 116
Cdd:cd07144 7 PT-GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 117 KEIARLITLEQGKTL-ADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWM 195
Cdd:cd07144 86 DLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGS 274
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 275 RNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAK-NLRVNAGDQP 351
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 352 GADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKiKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETL 431
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 432 DEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYT 507
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYT 475
|
....*
gi 205526 508 QLKTI 512
Cdd:cd07144 476 QTKAV 480
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-514 |
9.93e-89 |
|
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: 279.98 E-value: 9.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV 138
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 139 FRGlqVVEH-------ACSVTSLMLGETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPS 211
Cdd:cd07092 81 LPG--AVDNfrffagaARTLEGPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 212 ERVPGATMLLAKLLQDsGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHG 290
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 291 VVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVC 368
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 369 NLIDsGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 448
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 449 IFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 514
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-472 |
3.14e-88 |
|
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: 279.23 E-value: 3.14e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 57 IDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 DVFRGLQVVEHACSVTSLMLGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 212
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 213 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGV 291
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 292 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAKERV 367
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 368 CNLIDSGAKEGASILLDGRKIKvkgyenGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGT 447
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420
....*....|....*....|....*
gi 205526 448 AIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
41-513 |
6.35e-87 |
|
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: 276.54 E-value: 6.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF---PAWADTSILSRQQVLLRYQQLIKENLK 117
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMLGETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLW 194
Cdd:cd07141 88 YLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 195 MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYIFERG 273
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 274 SR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVNAGDQ 350
Cdd:cd07141 245 GKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 351 PGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETET 430
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 431 LDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVK 476
|
...
gi 205526 511 TIT 513
Cdd:cd07141 477 TVT 479
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
38-512 |
1.21e-86 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 275.99 E-value: 1.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 38 PTVKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLK 117
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMF 196
Cdd:PRK13252 85 ELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 197 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRN 276
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 277 GKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK--WLPELVERAKNLRVnaGD--QPG 352
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSIKaaFEARLLERVERIRI--GDpmDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 353 ADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLD 432
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 433 EAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYTQIK 475
|
..
gi 205526 511 TI 512
Cdd:PRK13252 476 SV 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-513 |
1.03e-85 |
|
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: 272.70 E-value: 1.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTL-ADAEGD 137
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVEHACSVTSLMLGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 218 TMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYgEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 297 NKENTLNQLV-GAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAKERVCNLI 371
Cdd:cd07108 239 DLDDAVDGAIaGMRFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 372 DSGAKE-GASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIF 450
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205526 451 TTNGAIARKYAHMVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 513
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
57-513 |
6.94e-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: 6.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 57 IDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG 136
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 DVFRGLQVVEHACSVTSLMLGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 212
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 213 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSrnGKRVQANMGAKNHGV 291
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 292 VMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNL 370
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 371 IDSGAKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIF 450
Cdd:cd07094 319 VEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205526 451 TTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 513
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
80-513 |
1.30e-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: 266.37 E-value: 1.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 80 EAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGET 159
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 160 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 239
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 240 GQ----HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 315
Cdd:cd07105 163 HSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 316 RCMalSTA-VLVGE--AKKWLPELVERAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRkikVKG 392
Cdd:cd07105 243 ICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGL---ADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 393 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 205526 473 VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07105 393 GMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
42-453 |
1.33e-83 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 268.73 E-value: 1.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKsDKwIDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:PRK03137 39 LIIGGERITTE-DK-IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGKTLADAEGDVFRGLQVVE-HACSVTSLMLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEyYARQMLKLADGKPVESRPGEHNRYFYI-PLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFER------ 272
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERaakvqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA-KKWLPELVERAKNLRVNAGDQP 351
Cdd:PRK03137 276 GQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVyDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 352 gADLGPLITPQAKERVCNLIDSGAKEGaSILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETL 431
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420
....*....|....*....|..
gi 205526 432 DEAIKIVNDNPYGNGTAIFTTN 453
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNN 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-512 |
6.24e-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: 6.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 40 VKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF--PAWADTSILSRQQVLLRYQQLIKENLK 117
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQGKT-LADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMF 196
Cdd:cd07143 87 YLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLT-YTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 197 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSR 275
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 276 -NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVNAGDQPG 352
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQEGiyDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 353 ADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLD 432
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 433 EAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTnfYGKQGIQFYTQ 508
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIGRE--LGEYALENYTQ 473
|
....
gi 205526 509 LKTI 512
Cdd:cd07143 474 IKAV 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-472 |
8.92e-83 |
|
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: 265.01 E-value: 8.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV 138
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 139 FRGLQVVEHACSVTSLMLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 219 MLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDAN 297
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 298 KENTLNQLV-GAAFGAAGQRCMALSTAvLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 375 AKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 454
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410
....*....|....*...
gi 205526 455 AIARKYAHMVDVGQVGVN 472
Cdd:cd07107 398 SQAHRTARRVEAGYVWIN 415
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-512 |
9.20e-83 |
|
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: 265.75 E-value: 9.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSVTSLMLGETMPSitkdmdlYSYRLPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07559 82 VAETLDNGKpiretLAADipLAIDHFRYFAGVIRAQEGSLSEIDEDTLS-------YHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFER 272
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 GSRNGKRVQANMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRCMALSTAvLVGEA--KKWLPELVERAKNLRV 345
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVCTCPSRA-LVQESiyDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 346 NAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVV 425
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 426 LETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGI 503
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyhQYPAHAP---FGGYKKSGIGRETH--KMML 467
|
....*....
gi 205526 504 QFYTQLKTI 512
Cdd:cd07559 468 DHYQQTKNI 476
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-512 |
7.69e-82 |
|
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: 262.56 E-value: 7.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWA-DTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG- 136
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 ------DVFRGlqVVEHACS--------VTSLMLGETMPSITKDmdlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVC 202
Cdd:cd07089 81 qvdgpiGHLRY--FADLADSfpwefdlpVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 203 GNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQ 281
Cdd:cd07089 151 GNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 282 ANMGAKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAVLVGEAKKwlPELVERAKN----LRVNAGDQPGA 353
Cdd:cd07089 231 LELGGKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVPRSRY--DEVVEALAAafeaLPVGDPADPGT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 354 DLGPLITPQAKERVCNLIDSGAKEGASILLDGRKikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDE 433
Cdd:cd07089 304 VMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 434 AIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTnfYGKQGIQFYTQL 509
Cdd:cd07089 382 AVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP-----FGGYKQSGLGRE--NGIEGLEEFLET 454
|
...
gi 205526 510 KTI 512
Cdd:cd07089 455 KSI 457
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-515 |
1.93e-81 |
|
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: 261.86 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 46 GKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITL 125
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 126 EQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNT 205
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 206 FLMKPSERVP--GATmLLAKLLQDSGAPDGTLNIIHGqheAVNFICD----HPDIKAISFVGSNQAGEYIFERGSRNGKR 279
Cdd:cd07151 161 VVLKPASDTPitGGL-LLAKIFEEAGLPKGVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 280 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVnaGDQ--PGADL 355
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 356 GPLITPQAKERVCNLIDSGAKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAI 435
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 436 KIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITS 514
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISV 463
|
.
gi 205526 515 Q 515
Cdd:cd07151 464 Q 464
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-513 |
6.45e-81 |
|
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: 259.85 E-value: 6.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 60 HNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVF 139
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 140 RGLQVVEHACSVTSLMLGE---TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 216
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 217 ATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPdIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 297 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 375 AKEGASILLDGRKIKVKGyengNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 454
Cdd:cd07099 319 VAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 455 AIARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 513
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
58-512 |
2.02e-80 |
|
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: 259.07 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 58 DIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADA- 134
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 135 EGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 214
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 215 PGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVV 292
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 293 MPDA-NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAKERV 367
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 368 CNLIDSGAKEGASILLDGRKIKVKGyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGT 447
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205526 448 AIFTTNGAIARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 512
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
39-476 |
2.48e-80 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 259.07 E-value: 2.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 39 TVKLFIDGKFVESKSDKWiDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKE 118
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 119 IARLITLEQGK----TLAD---AEGDVFR---GLqvvehACSVTSLMLGETMPSITkdmdlySY--RLPLGVCAGIAPFN 186
Cdd:PRK13473 81 FARLESLNCGKplhlALNDeipAIVDVFRffaGA-----ARCLEGKAAGEYLEGHT------SMirRDPVGVVASIAPWN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 187 FPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQA 265
Cdd:PRK13473 150 YPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 266 GEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNL 343
Cdd:PRK13473 229 GKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiyDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 344 RVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEG-ASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPV 422
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 205526 423 LVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIP 476
Cdd:PRK13473 384 VSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-513 |
2.07e-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: 256.12 E-value: 2.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV 138
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 139 ---------FRGL--QVVEHAcsvtslmlGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:cd07110 81 ddvagcfeyYADLaeQLDAKA--------ERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGA 286
Cdd:cd07110 153 LKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTgDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 287 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAK 364
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 365 ERVCNLIDSGAKEGASILLDGRKikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYG 444
Cdd:cd07110 312 EKVLSFIARGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 445 NGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 513
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-512 |
9.01e-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: 255.07 E-value: 9.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSVTSLMLGETMPSITKdmdlysyRLPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07117 82 MVETLDNGKpiretRAVDipLAADHFRYFAGVIRAEEGSANMIDEDTLSIVL-------REPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFER 272
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAGDQ 350
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiyDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 351 PGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETET 430
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 431 LDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQ 508
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGRETH--KSMLDAYTQ 467
|
....
gi 205526 509 LKTI 512
Cdd:cd07117 468 MKNI 471
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
66-516 |
1.15e-77 |
|
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: 251.06 E-value: 1.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 66 EVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVV 145
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 146 EHACSVTSLMLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKL 224
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 225 LQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQ 304
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 305 LVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASIL 382
Cdd:cd07152 241 GAWGAFLHQGQICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 383 LDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAH 462
Cdd:cd07152 320 AGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 205526 463 MVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 516
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
57-513 |
3.20e-76 |
|
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: 247.66 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 57 IDIHNPATNEVVGRVPQSTKAEMEAAVAAckrafpAWADTSILSRQQ---VLLRYQQLIKENLKEIARLITLEQGKTLAD 133
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAL------AASYRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 134 AEGDVFRGLQVVEHACSVTSLMLGETMPS-IT---KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 209
Cdd:cd07146 75 TRYEVGRAADVLRFAAAEALRDDGESFSCdLTangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 210 PSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIfeRGSRNGKRVQANMGAKN 288
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 289 HGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVnaGD--QPGADLGPLITPQAK 364
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 365 ERVCNLIDSGAKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYG 444
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205526 445 NGTAIFTTNGAIARKYAHMVDVGQVGVNvpiPVP---LPMFSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 513
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
41-512 |
4.43e-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: 248.18 E-value: 4.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFP--AWADTSILSRQQVLLRYQQLIKENLKE 118
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 119 IARLITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMLGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWM 195
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNF-ICDHPDIKAISFVGSNQAGEYIFERGS 274
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 275 R-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEakKWLPELVERAKN--LRVNAGD-- 349
Cdd:cd07142 242 KsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpf 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 350 QPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETE 429
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 430 TLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQL 509
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQV 471
|
...
gi 205526 510 KTI 512
Cdd:cd07142 472 KAV 474
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
79-472 |
5.86e-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: 246.22 E-value: 5.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 79 MEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQV----VEHACSvtsl 154
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWIcryyAENAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 155 MLgETMPSITKDMDLYSYRLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSG 229
Cdd:cd07100 77 FL-ADEPIETDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 230 APDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 309
Cdd:cd07100 151 FPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 310 FGAAGQRCMAlSTAVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRK 387
Cdd:cd07100 231 LQNAGQSCIA-AKRFIVHEdvYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 388 IKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVG 467
Cdd:cd07100 310 PDGPGA----FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
....*
gi 205526 468 QVGVN 472
Cdd:cd07100 386 MVFIN 390
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-499 |
8.39e-76 |
|
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: 246.39 E-value: 8.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 57 IDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG 136
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 DVFRGLQVVEHACSVTSLMLGETMPsitkdMDLYS---------YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 207
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLP-----LDISArgegrqglvRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 208 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAK 287
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 288 NHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVnaGD--QPGADLGPLITPQA 363
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKT--GDpkDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 364 KERVCNLIDSGAKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPY 443
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 205526 444 GNGTAIFTTN-GAIARKYAHMvDVGQVGVN-VPipvplpmfsftgsrsSFRGDTNFYG 499
Cdd:cd07147 384 GLQAGVFTRDlEKALRAWDEL-EVGGVVINdVP---------------TFRVDHMPYG 425
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
61-513 |
1.67e-74 |
|
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: 243.40 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 61 NPATNEVVGRVPQSTKAEMEAAVAACKRAF--PAWADTSILsRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV 138
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 139 FRGLQVVEHACSVTSLMLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 218
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVL-REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 219 MLLAKLLQD-SGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 296
Cdd:cd07120 161 AAIIRILAEiPSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 297 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 374
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSR-VLVQRsiADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 375 AKEGASILLDGRKIkVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 454
Cdd:cd07120 320 IAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 205526 455 AIARKYAHMVDVGQVGVNVPIPVpLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 513
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
42-472 |
2.27e-74 |
|
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: 243.84 E-value: 2.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIAR 121
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 122 LITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMlgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAM 200
Cdd:cd07111 104 LESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL----------DTELAGWK-PVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 201 VCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRVNAGDQPGADLGPL 358
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 359 ITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIV 438
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430
....*....|....*....|....*....|....
gi 205526 439 NDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
37-476 |
4.57e-74 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 243.49 E-value: 4.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 37 VPTVKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA-----WADTSILSRQQVLLRYQQL 111
Cdd:PLN02467 5 VPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 112 IKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRL---PLGVCAGIAPFNFP 188
Cdd:PLN02467 85 ITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVlkePLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 189 AMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNQAGE 267
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 268 YIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVERAKNLRV 345
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 346 NAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGrkIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVV 425
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 205526 426 LETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIP 476
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
37-472 |
9.87e-73 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 240.11 E-value: 9.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 37 VPTV---KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFP--AWADTSILSRQQVLLRYQQL 111
Cdd:PLN02766 15 VPEIkftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 112 IKENLKEIARLITLEQGKTLADAEG-DVFRGLQVVEHACSVTSLMLGETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAM 190
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 191 IPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYI 269
Cdd:PLN02766 174 MFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 270 FERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVN 346
Cdd:PLN02766 254 MQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 347 AGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVL 426
Cdd:PLN02766 333 DPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGY----YIEPTIFTDVTEDMKIAQDEIFGPVMSLM 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 205526 427 ETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:PLN02766 409 KFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
45-474 |
1.59e-68 |
|
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: 228.25 E-value: 1.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 45 DGKFVESKSDkwIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLIT 124
Cdd:cd07130 4 DGEWGGGGGV--VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 125 LEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGN 204
Cdd:cd07130 82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 205 TFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIfergsrnGKRV 280
Cdd:cd07130 162 VVVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQV-------GQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAK-------NHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKKwlPELVERAKNL--RVNAGD-- 349
Cdd:cd07130 235 AARFGRSllelggnNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHESIY--DEVLERLKKAykQVRIGDpl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 350 QPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKvkgyENGNFVGPTIISnVKPSMTCYKEEIFGPVLVVLETE 429
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 205526 430 TLDEAIKIVNDNPYGNGTAIFTTNGAIARKY--AHMVDVGQVGVNVP 474
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIG 433
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
60-512 |
8.67e-68 |
|
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: 225.59 E-value: 8.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 60 HNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVF 139
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 140 RGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 219
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 220 LLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE 299
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 300 NTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKE 377
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 378 GASILLDGRKIKVkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIA 457
Cdd:cd07102 320 GARALIDGALFPE-DKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 205526 458 RKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 512
Cdd:cd07102 399 EALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRGVT--LSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-510 |
1.07e-67 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 226.33 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARL 122
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 123 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 201
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 202 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 280
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM-ALSTAVLVGEAKKWLPELVERAKNLRVNAGDQPGADLGPLI 359
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 360 TPQAKERVCNLIDSGAKEGASILLDGRKIKVkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 439
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205526 440 DNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 510
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
41-512 |
2.23e-67 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 225.55 E-value: 2.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA--WADTSILSRQQVLLRYQQLIKENLKE 118
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 119 IARLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFP 197
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 198 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYIF-ERGSR 275
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 276 NGKRVQANMGAKNHGVVMPDANKentLNQLVGAA----FGAAGQRCMAlSTAVLVGE--AKKWLPELVERAKNLRVNAGD 349
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 350 QPGADLGPLITPQAKERVCNLIDSGAKEGaSILLDGRKIKVKGYengnfVGPTIISNVKPSMTCYKEEIFGPVLVVLETE 429
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 430 TLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQ 504
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALE 481
|
....*...
gi 205526 505 FYTQLKTI 512
Cdd:PRK09847 482 KFTELKTI 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
41-517 |
2.45e-67 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 226.61 E-value: 2.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFP--AWADTSILSRQQVLLRYQQLIKENLKE 118
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 119 IARLITLEQGKTLADAEG-DVFRGLQVVEHACSVTSLMLGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWM 195
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPA---DGPHHVQTLhePIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYIFERGS 274
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 275 R-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAvLVGEakKWLPELVERAKN--LRVNAGD-- 349
Cdd:PLN02466 296 KsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RVYDEFVEKAKAraLKRVVGDpf 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 350 QPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETE 429
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 430 TLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN------VPIPvplpmfsFTGSRSSFRGDTNfyGKQGI 503
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIGREK--GIYSL 519
|
490
....*....|....
gi 205526 504 QFYTQLKTITSQWK 517
Cdd:PLN02466 520 NNYLQVKAVVTPLK 533
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-514 |
7.60e-66 |
|
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: 220.64 E-value: 7.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 60 HNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVF 139
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 140 RGLQVVEH-ACSVTSLMLGE----TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 214
Cdd:cd07101 81 DVAIVARYyARRAERLLKPRrrrgAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 215 PGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVM 293
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 294 PDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLI 371
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 372 DSGAKEGASILLDGRKIKVKG---YEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 448
Cdd:cd07101 315 DDAVAKGATVLAGGRARPDLGpyfYE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205526 449 IFTTNGAIARKYAHMVDVGQVGVNVPI-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 514
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEGYaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-476 |
7.77e-66 |
|
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: 219.84 E-value: 7.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 78 EMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfrGLQVVEHACSVTSLMlg 157
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEV--AAMAGKIDISIKAYH-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 158 ETMPSITKDMD----LYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDG 233
Cdd:cd07095 77 ERTGERATPMAqgraVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 234 TLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 312
Cdd:cd07095 156 VLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 313 AGQRCMALSTAVLVG--EAKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKv 390
Cdd:cd07095 236 AGQRCTCARRLIVPDgaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 391 kgyENGNFVGPTIIsNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVG 470
Cdd:cd07095 315 ---AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
....*.
gi 205526 471 VNVPIP 476
Cdd:cd07095 391 WNRPTT 396
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
60-472 |
5.38e-64 |
|
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: 216.01 E-value: 5.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 60 HNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAegdvf 139
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 140 rglqvvehacsvtslMLGETMPSITKdMD-------------------LYSYRL------PLGVCAGIAPFNFP------ 188
Cdd:cd07098 76 ---------------SLGEILVTCEK-IRwtlkhgekalrpesrpgglLMFYKRarveyePLGVVGAIVSWNYPfhnllg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 189 AMIPlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQ 264
Cdd:cd07098 140 PIIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 265 AGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKN 342
Cdd:cd07098 214 VGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKiyDKLLEILTDRVQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 343 LRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPV 422
Cdd:cd07098 293 LRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 205526 423 LVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07098 373 MVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
110-517 |
1.85e-63 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 213.06 E-value: 1.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 110 QLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA 189
Cdd:PRK10090 6 AGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 190 -MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGE 267
Cdd:PRK10090 86 fLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 268 YIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC-MALSTAVLVGEAKKWLPELVERAKNLRV- 345
Cdd:PRK10090 165 KIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 346 NAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVV 425
Cdd:PRK10090 245 NPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 426 LETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNvpipvplpmfsftgsRSSFRGDTNFY------- 498
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---------------RENFEAMQGFHagwrksg 385
|
410 420
....*....|....*....|....
gi 205526 499 -----GKQGIQFYTQLKTITSQWK 517
Cdd:PRK10090 386 iggadGKHGLHEYLQTQVVYLQSD 409
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-515 |
3.07e-63 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 215.51 E-value: 3.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 49 VESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQG 128
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 129 KTLADAEGDVfrgLQVVehacsVTSLMLGETMPSITKD----------MDLYSYRLPLGVCAGIAPFNFPA------MIP 192
Cdd:PRK09407 106 KARRHAFEEV---LDVA-----LTARYYARRAPKLLAPrrragalpvlTKTTELRQPKGVVGVISPWNYPLtlavsdAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 193 lwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIkaISFVGSNQAGEYIFE 271
Cdd:PRK09407 178 ------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVLAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 272 RGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVERAKNLRVNAGDQ 350
Cdd:PRK09407 250 QAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESiYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 351 PGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKG---YEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLE 427
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE------PTVLTGVTPDMELAREETFGPVVSVYP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 428 TETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIpvpLPMFSFTGSRSSFRGDTNF---YGKQGIQ 504
Cdd:PRK09407 404 VADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---AAAWGSVDAPMGGMKDSGLgrrHGAEGLL 480
|
490
....*....|.
gi 205526 505 FYTQLKTITSQ 515
Cdd:PRK09407 481 KYTESQTIATQ 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
43-475 |
1.16e-61 |
|
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: 210.90 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKfvESKSDKWIDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIAR 121
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 122 LITLEQGKTLADAEGDV--------FRGLQVVEhacsvtsLMLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07125 114 LAAAEAGKTLADADAEVreaidfcrYYAAQARE-------LFSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFE- 271
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 272 RGSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVERAKNLRVNAG 348
Cdd:cd07125 266 LAERDGPILPliAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 349 DQPGADLGPLITPQAKERVCNLIDSGAKEGASIlldgrKIKVKGYENGNFVGPTIISNVKPSmtCYKEEIFGPVLVVL-- 426
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLI-----APAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrf 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 205526 427 ETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPI 475
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
42-472 |
1.51e-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: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKSDKWIdiHNP-ATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:cd07083 21 LVIGGEWVDTKERMVS--VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGKTLADAEGDVFRGLQVVE-HACSVTSLML-GETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPM 198
Cdd:cd07083 99 ATLTYEVGKNWVEAIDDVAEAIDFIRyYARAALRLRYpAVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 199 AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNG 277
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 278 ------KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKKWLPELVERAKNLRVNAGDQ 350
Cdd:cd07083 258 pgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 351 PGADLGPLITPQAKERVCNLIDSGAKEGaSILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVL--ET 428
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKD 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 205526 429 ETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07083 413 DDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
43-472 |
1.75e-56 |
|
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: 196.13 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARL 122
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 123 ITLEQGKTLADAEG-------DVFRGLQVVEHACSvtslmlgETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWM 195
Cdd:cd07116 84 ETWDNGKPVRETLAadiplaiDHFRYFAGCIRAQE-------GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 196 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYIFERGS 274
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 275 RNGKRVQANMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTAvLVGEA--KKWLPELVERAKNLRVNA 347
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA-LIQESiyDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 348 GDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKpSMTCYKEEIFGPVLVVLE 427
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 205526 428 TETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
42-444 |
1.90e-56 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 196.33 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 42 LFIDGKFVESKSDKwIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIAR 121
Cdd:PRK09457 3 LWINGDWIAGQGEA-FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 122 LITLEQGKTLADAEGDVfrGLQVVEHACSVTSLM--LGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMA 199
Cdd:PRK09457 82 VIARETGKPLWEAATEV--TAMINKIAISIQAYHerTGEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGeYIFER--GSRNG 277
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTG-YLLHRqfAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 278 KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK---WLPELVERAKNLRVNAGD-QPGA 353
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQgdaFLARLVAVAKRLTVGRWDaEPQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 354 DLGPLITPQAKERVC----NLIDSGAKegasILLDGRKIKvkgyENGNFVGPTII--SNVK--PSmtcykEEIFGPVLVV 425
Cdd:PRK09457 317 FMGAVISEQAAQGLVaaqaQLLALGGK----SLLEMTQLQ----AGTGLLTPGIIdvTGVAelPD-----EEYFGPLLQV 383
|
410
....*....|....*....
gi 205526 426 LETETLDEAIKIVNDNPYG 444
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFG 402
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
61-512 |
3.04e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 194.96 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 61 NPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVF- 139
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 140 --RGLQ-VVEHAcsvtSLMLGETmPSITKDMD----LYSYRlPLGVCAGIAPFNFPamipLWM---FPM-AMVCGNTFLM 208
Cdd:PRK09406 87 caKGFRyYAEHA----EALLADE-PADAAAVGasraYVRYQ-PLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 209 KPSERVPGATMLLAKLLQDSGAPDG---TLNIIHGQHEAvnfICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMG 285
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGcfqTLLVGSGAVEA---ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 286 AKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL---VGEAkkWLPELVERAKNLRVNAGDQPGADLGPLITPQ 362
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadVYDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 363 AKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP 442
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATT 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205526 443 YGNGTAIFTTNGAIARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTI 512
Cdd:PRK09406 388 FGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
41-516 |
3.04e-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: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPA--WADTSILSRQQVLLRYQQLIKENLKE 118
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 119 IARLITLEQGK--TLAdAEGDVFRGLQVVEHACSVTSLMLGETMP--SITKDMDL-YSYRLPLGVCAGIAPFNFPAMIPL 193
Cdd:cd07140 87 LATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIFER 272
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 -GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVERAKNLRVNAGD 349
Cdd:cd07140 246 cAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 350 QPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVV--LE 427
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIIskFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 428 TETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNV--PIPVPLPMFSFtgSRSSFRGDtnfYGKQGIQF 505
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPFGGF--KQSGFGKD---LGEEALNE 475
|
490
....*....|.
gi 205526 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 |
2.01e-55 |
|
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: 193.44 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWiDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF--PAWA-DTSIlsRQQVLLRYQQLIKENLK 117
Cdd:TIGR04284 2 RLLIDGKLVAGSAGTF-PTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSrDTAL--RVRCLRQLRDALRAHVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQG--KTL---ADAEGDVFRGLQVVEHACSVT-SLMLGETMPsitkdMDLYSYRL----PLGVCAGIAPFNF 187
Cdd:TIGR04284 79 ELRELTIAEVGapRMLtagAQLEGPVDDLGFAADLAESYAwTTDLGVASP-----MGIPTRRTlrreAVGVVGAITPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 188 PAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHEAVNFICDHPDIKAISFVGSNQA 265
Cdd:TIGR04284 154 PHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 266 GEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAVLVGEAKkwLPELVERAK- 341
Cdd:TIGR04284 234 GRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVPRAR--YDEAVAAAAa 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 342 ---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKikVKGYENGNFVGPTIISNVKPSMTCYKEEI 418
Cdd:TIGR04284 308 tmgSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTVIAGLDNNARVAREEI 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 205526 419 FGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:TIGR04284 386 FGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
61-472 |
6.40e-55 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 191.61 E-value: 6.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 61 NPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 140
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 141 GLQVVEHACSVTSLMLgETMPSITKDMD-LYSYRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKPSERV 214
Cdd:PRK13968 93 SANLCDWYAEHGPAML-KAEPTLVENQQaVIEYR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 215 PGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMP 294
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 295 DANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 373
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 374 GAKEGASILLDGRKIKVKGyengNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 453
Cdd:PRK13968 326 TLAEGARLLLGGEKIAGAG----NYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410
....*....|....*....
gi 205526 454 GAIARKYAHMVDVGQVGVN 472
Cdd:PRK13968 402 ETQARQMAARLECGGVFIN 420
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
61-474 |
7.09e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 179.26 E-value: 7.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 61 NPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 140
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 141 GLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----G 216
Cdd:PLN02315 120 IIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 217 ATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVqANMGAKNHGVVMPD 295
Cdd:PLN02315 200 MTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 296 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 373
Cdd:PLN02315 279 ADIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 374 GAKEGASILLDGRKIKvkgyENGNFVGPTIISnVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 453
Cdd:PLN02315 358 IKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
410 420
....*....|....*....|...
gi 205526 454 GAIARKY--AHMVDVGQVGVNVP 474
Cdd:PLN02315 433 PETIFKWigPLGSDCGIVNVNIP 455
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
41-503 |
4.23e-47 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 171.09 E-value: 4.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 41 KLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIA 120
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 121 RLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGE-------TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPL 193
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 194 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNqAGEYIfer 272
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGGD-TGIAI--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 gSRNGKRV--QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAVLVGE--AKKWLPELVERAKNLRVNAG 348
Cdd:PLN00412 253 -SKKAGMVplQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VVLVMEsvADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 349 DQpGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLET 428
Cdd:PLN00412 331 ED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205526 429 ETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPiPVPLP-MFSFTGSRSSfrgdtnFYGKQGI 503
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQGI 471
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
57-505 |
2.75e-44 |
|
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: 162.59 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 57 IDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAF-------PAWADTSILSRQQVLLRyqqlikENLKEIARLITLEQGK 129
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrnnwlPAHERIAILERLADLME------ERADELALLIAREGGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 130 TLADAEGDVFRGLQVVEHACSVTSLMLGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmA 199
Cdd:cd07148 75 PLVDAKVEVTRAIDGVELAADELGQLGGREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-A 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 200 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN-IIHGQHEAVNFICDhPDIKAISFVGSNQAGEYIFERGSrNGK 278
Cdd:cd07148 149 IAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLA-PGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 279 RVqanmgAKNHG-----VVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-VLVGEAKKWLPELVERAKNLRVnaGDQ-- 350
Cdd:cd07148 227 RC-----ALEHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVfVPAEIADDFAQRLAAAAEKLVV--GDPtd 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 351 PGADLGPLITPQAKERVCNLIDSGAKEGASILLDGRKIKVKGYEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLETET 430
Cdd:cd07148 300 PDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDD 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205526 431 LDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 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 |
1.28e-41 |
|
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: 156.59 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 40 VKLFIDGKfvESKSDKWIDIHNPAT-NEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLK- 117
Cdd:cd07123 33 IPLVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 118 EIARLITLEQGKTLADAEGDV-------FR----------GLQVVEHACSVTSLMlgetmpsitkdmdlySYRlPL-GVC 179
Cdd:cd07123 111 ELNAATMLGQGKNVWQAEIDAacelidfLRfnvkyaeelyAQQPLSSPAGVWNRL---------------EYR-PLeGFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 180 AGIAPFNFPAM------IPLWMfpmamvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHP 252
Cdd:cd07123 175 YAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 253 DIKAISFVGS--------NQAGEYIfeRGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTA- 323
Cdd:cd07123 248 HLAGLHFTGStptfkslwKQIGENL--DRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAy 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 324 VLVGEAKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSgAKE--GASILLDGRKIKVKGYengnFVGP 401
Cdd:cd07123 326 VPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDH-AKSdpEAEIIAGGKCDDSVGY----FVEP 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 205526 402 TIISNVKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVND-NPYGNGTAIF 450
Cdd:cd07123 401 TVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
56-472 |
3.50e-38 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 149.96 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 56 WIDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADA 134
Cdd:PRK11904 563 ARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 135 EGDVfRglqvvE-------HACSVTSLML-GETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTF 206
Cdd:PRK11904 643 IAEV-R-----EavdfcryYAAQARRLFGaPEKLPGPTGESNELRLH-GRGVFVCISPWNFPLAIFLGQVAAALAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 207 LMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIfERG--SRNGKRVQ-- 281
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARII-NRTlaARDGPIVPli 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 282 ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStaVL-VGE--AKKWLPELVERAKNLRVnaGD--QPGADLG 356
Cdd:PRK11904 795 AETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR--VLfVQEdiADRVIEMLKGAMAELKV--GDprLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 357 PLITPQAKERVCNLIDSGAKEG---ASILLDGrkikvkGYENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETL 431
Cdd:PRK11904 871 PVIDAEAKANLDAHIERMKREArllAQLPLPA------GTENGHFVAPTAFE--IDSISQLEREVFGPILHVIryKASDL 942
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 205526 432 DEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN 472
Cdd:PRK11904 943 DKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
82-472 |
2.44e-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: 2.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 82 AVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GDVFRGLQVVEHAC----------S 150
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALkhlkkwmkprR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 151 V-TSLMLGETMPSITKDmdlysyrlPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQD 227
Cdd:cd07087 83 VsVPLLLQPAKAYVIPE--------PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 228 SGAPDGtLNIIHGQHEAVNFICDHP-DIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLV 306
Cdd:cd07087 153 YFDPEA-VAVVEGGVEVATALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 307 GAAFGAAGQRCMALSTaVLVGEAKKwlPELVERAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGakegaSIL 382
Cdd:cd07087 230 WGKFLNAGQTCIAPDY-VLVHESIK--DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDG-----KVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 383 LDGRKIKVKGYengnfVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGAIA 457
Cdd:cd07087 301 IGGQVDKEERY-----IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQ 370
|
410
....*....|....*
gi 205526 458 RKYAHMVDVGQVGVN 472
Cdd:cd07087 371 ERVLAETSSGGVCVN 385
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
83-472 |
7.92e-36 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 139.78 E-value: 7.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 83 VAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLadaegdvfRGLQVVEHACSVTSL--MLGE-- 158
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHP--------FETKMTEVLLTVAEIehLLKHld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 159 --------TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqDSGA 230
Cdd:PTZ00381 85 eylkpekvDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 231 PDGTLNIIHGQHEAVNFICDHP-DIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 309
Cdd:PTZ00381 164 DPSYVRVIEGGVEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 310 FGAAGQRCMALSTaVLVGEA--KKWLPELVERAKNLrvnAGDQP--GADLGPLITPQAKERVCNLIDSgakegasillDG 385
Cdd:PTZ00381 242 FLNAGQTCVAPDY-VLVHRSikDKFIEALKEAIKEF---FGEDPkkSEDYSRIVNEFHTKRLAELIKD----------HG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 386 RKIKVKGY--ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHM 463
Cdd:PTZ00381 308 GKVVYGGEvdIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLEN 387
|
....*....
gi 205526 464 VDVGQVGVN 472
Cdd:PTZ00381 388 TSSGAVVIN 396
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
59-472 |
1.21e-35 |
|
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: 139.28 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPAT-NEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 137
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVEHACSvtslmlgetmpSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 217
Cdd:TIGR01238 135 VREAVDFCRYYAK-----------QVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 218 TMLLAKLLQDSGAPDGTLNIIHGQHEAVN-FICDHPDIKAISFVGSNQAGEYI----FERGSRNGKRVqANMGAKNHGVV 292
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 293 MPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVERA-KNLRVNAGDQPGADLGPLITPQAKERVCNLI 371
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 372 DSGAKEGASILLDGRKIKVKgYENGNFVGPTIISnvKPSMTCYKEEIFGPVL--VVLETETLDEAIKIVNDNPYGNGTAI 449
Cdd:TIGR01238 362 EHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGV 438
|
410 420
....*....|....*....|...
gi 205526 450 FTTNGAIARKYAHMVDVGQVGVN 472
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVN 461
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-444 |
3.42e-33 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 135.07 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 50 ESKSDKWIDIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQG 128
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 129 KTLADAEGDVfRglqvvE-------HACSVTSLMLGETmpsitkdmdlySYRlPLGVCAGIAPFNFP---------Amip 192
Cdd:COG4230 645 KTLPDAIAEV-R-----EavdfcryYAAQARRLFAAPT-----------VLR-GRGVFVCISPWNFPlaiftgqvaA--- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 193 lwmfpmAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAge 267
Cdd:COG4230 704 ------ALAAGNTVLAKPAEQTP----LIAaravRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTET-- 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 268 yifergsrnGKRVQANMGAKNHGVVMPDAnkEnT--LN-----------QLVG----AAFGAAGQRCMALStaVL-VGE- 328
Cdd:COG4230 772 ---------ARLINRTLAARDGPIVPLIA--E-TggQNamivdssalpeQVVDdvlaSAFDSAGQRCSALR--VLcVQEd 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 329 -AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKEGASIlldgRKIKV-KGYENGNFVGPTIISn 406
Cdd:COG4230 838 iADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLpEECANGTFVAPTLIE- 912
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 205526 407 vKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYG 444
Cdd:COG4230 913 -IDSISDLEREVFGPVLHVVryKADELDKVIDAINATGYG 951
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
58-444 |
1.32e-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: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 58 DIHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG 136
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 137 DVfRglQVVE----HACSVTSlmlgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 212
Cdd:PRK11809 742 EV-R--EAVDflryYAGQVRD------------DFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 213 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEY----IFERGSRNGKRVQ--ANMG 285
Cdd:PRK11809 806 QTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLlqrnLAGRLDPQGRPIPliAETG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 286 AKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVERAKNLRVNAGDQPGADLGPLITPQAK 364
Cdd:PRK11809 886 GQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 365 ERVCNLIDSGAKEGASILLDGRKiKVKGYENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNP 442
Cdd:PRK11809 966 ANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVryNRNQLDELIEQINASG 1042
|
..
gi 205526 443 YG 444
Cdd:PRK11809 1043 YG 1044
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
59-444 |
1.88e-32 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 132.68 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPA-TNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 137
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 V--------FRGLQVvehacsvtslmlgetmpsitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 209
Cdd:PRK11905 651 VreavdflrYYAAQA--------------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 210 PSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNQAGEYIfER--GSRNGKRVQ- 281
Cdd:PRK11905 711 PAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPl 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 282 -ANMGAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRCMALStaVL-VGE--AKKWLPELVERAKNLRVNAGDQPGA 353
Cdd:PRK11905 786 iAETGGQNAMIVDSSALPE----QVVADviasAFDSAGQRCSALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLST 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 354 DLGPLITPQAKERVCNLIDSGAKEGASIlldgRKIKV-KGYENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETET 430
Cdd:PRK11905 860 DVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADE 933
|
410
....*....|....
gi 205526 431 LDEAIKIVNDNPYG 444
Cdd:PRK11905 934 LDRVIDDINATGYG 947
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
80-472 |
1.91e-32 |
|
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: 129.27 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 80 EAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKtlADAEGDVFRGLQVVE---HAC------- 149
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK--PAAEVDLTEILPVLSeinHAIkhlkkwm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 150 -----SVTSLMLGetmpsiTKDMDLYSyrlPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLA 222
Cdd:cd07134 79 kpkrvRTPLLLFG------TKSKIRYE---PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 223 KLLQDSGAPDgTLNIIHGQHEAVNFICDHPdIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 302
Cdd:cd07134 148 KIIREAFDED-EVAVFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 303 NQLVGAAFGAAGQRCMALSTaVLVGEAKKwlPELVER-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGAKE 377
Cdd:cd07134 226 KKIAWGKFLNAGQTCIAPDY-VFVHESVK--DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 378 GASILLDGrkikvKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIA 457
Cdd:cd07134 303 GAKVEFGG-----QFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANV 377
|
410
....*....|....*
gi 205526 458 RKYAHMVDVGQVGVN 472
Cdd:cd07134 378 NKVLARTSSGGVVVN 392
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
175-512 |
6.24e-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: 118.86 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 175 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHEAVNFICDHPDI 254
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 255 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKkwLP 334
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 335 ELVERAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDsgaKEGASILLDGRKIKVKgyengNFVGPTIISNVKPSM 411
Cdd:cd07135 263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLD---TTKGKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 412 TCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT-----TNGAIARKYAHMVDVGQVGVNVPIPVpLPmfsFTG 486
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTddkseIDHILTRTRSGGVVINDTLIHVGVDN-AP---FGG 410
|
330 340
....*....|....*....|....*.
gi 205526 487 SRSSfrGDTNFYGKQGIQFYTQLKTI 512
Cdd:cd07135 411 VGDS--GYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
80-434 |
3.68e-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: 116.95 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 80 EAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKT---LADAEGDV--FRGLQVVEHACSVTSL 154
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 155 MLGEtmPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDG 233
Cdd:cd07084 82 PGNH--LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 234 TLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGA 312
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 313 AGQRCMALStAVLVGEAKKWLPeLVERAKNLRVNAGDQpGADLGPLITPQAKERVcnlidsgAKEGAsilLDGRKIKVKG 392
Cdd:cd07084 238 SGQKCTAQS-MLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAMI-------AHMEN---LLGSVLLFSG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 205526 393 YENGNFVGPTIISNVKPS---MTC---------YKEEIFGPVLVVLETETLDEA 434
Cdd:cd07084 305 KELKNHSIPSIYGACVASalfVPIdeilktyelVTEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
170-459 |
1.81e-26 |
|
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: 112.21 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 170 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNF 247
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 248 IC----DHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 323
Cdd:cd07136 172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 324 VLVGEAKK--WLPELVERAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGakegasilldgrKIKVKGY--ENGN 397
Cdd:cd07136 246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNG------------KIVFGGNtdRETL 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205526 398 FVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGAIARK 459
Cdd:cd07136 311 YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
101-512 |
1.00e-25 |
|
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: 109.81 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 101 RQQVLLRYQQLIKENLKEIARLITLEQGKTLADAegdvFRG-LQVVEHACSVTSLMLGETMPSITKDMDLYSYRL----- 174
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAES----FRDeVSVLVSSCKLAIKELKKWMAPEKVKTPLTTFPAkaeiv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 175 --PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHEAVNFIC 249
Cdd:cd07137 99 sePLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPeylDTKA----IKVIEGGVPETTALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 250 DHPDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTaVLVGE 328
Cdd:cd07137 175 EQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 329 akKWLPELVERAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgAKEGASILLDGRKIkvkgyENGNFVGPTIIS 405
Cdd:cd07137 253 --SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERD-----EKNLYIEPTILL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 406 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN-VPIPVPLPMFSF 484
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPF 404
|
410 420
....*....|....*....|....*...
gi 205526 485 TGSRSSfrGDTNFYGKQGIQFYTQLKTI 512
Cdd:cd07137 405 GGVGES--GFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
175-472 |
5.74e-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: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 175 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHE------AV 245
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 246 NFicDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVL 325
Cdd:cd07133 177 PF--DH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA-PDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 326 VGEAKkwLPELVERAKNL------RVNAGDqpgaDLGPLITPQAKERVCNLIDSGAKEGASI---------LLDGRKIkv 390
Cdd:cd07133 249 VPEDK--LEEFVAAAKAAvakmypTLADNP----DYTSIINERHYARLQGLLEDARAKGARVielnpagedFAATRKL-- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 391 kgyengnfvGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGAIARKYAHMVD 465
Cdd:cd07133 321 ---------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDRVLRRTH 386
|
....*..
gi 205526 466 VGQVGVN 472
Cdd:cd07133 387 SGGVTIN 393
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
168-453 |
6.43e-21 |
|
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: 95.37 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 168 DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEA- 244
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 245 --VNFICDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA--- 319
Cdd:cd07132 171 elLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdy 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 320 -LSTA----VLVGEAKKWLPELVeraknlrvnaGDQP--GADLGPLITPQAKERVCNLIDSGakegasilldgrKIKVKG 392
Cdd:cd07132 246 vLCTPevqeKFVEALKKTLKEFY----------GEDPkeSPDYGRIINDRHFQRLKKLLSGG------------KVAIGG 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205526 393 Y--ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN--DNP---YgngtaIFTTN 453
Cdd:cd07132 304 QtdEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINsrEKPlalY-----VFSNN 366
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
175-512 |
3.68e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 87.41 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 175 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHEAVNFICDHPDI 254
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 255 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTAVlvgEAKKWL 333
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYIL---TTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 334 PELVERAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgaKEGASILLDGRKikvKGYENGNfVGPTIISNVKPS 410
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 411 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAIARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSRS 489
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
|
330 340
....*....|....*....|...
gi 205526 490 SFRGdtNFYGKQGIQFYTQLKTI 512
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
79-472 |
1.55e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 79.00 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 79 MEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAegdvFRG-LQVVEHACSVTSLMLG 157
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEA----YRDeVGVLTKSANLALSNLK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 158 ETMPSITKDMDLYSYRL-------PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ-- 226
Cdd:PLN02203 84 KWMAPKKAKLPLVAFPAtaevvpePLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIPky 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 227 -DSGApdgtLNIIHGQHEAVNFICDHPDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT---L 302
Cdd:PLN02203 162 lDSKA----VKVIEGGPAVGEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkvaV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 303 NQLVGAAFGA-AGQRCMALSTaVLVGEakKWLPELVERAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSGAKEg 378
Cdd:PLN02203 237 NRIVGGKWGScAGQACIAIDY-VLVEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKDPRVA- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 379 ASIL----LDGRKIkvkgyengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 454
Cdd:PLN02203 313 ASIVhggsIDEKKL---------FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNE 383
|
410
....*....|....*...
gi 205526 455 AIARKYAHMVDVGQVGVN 472
Cdd:PLN02203 384 KLKRRILSETSSGSVTFN 401
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
80-439 |
1.54e-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: 72.57 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 80 EAAVAACKRAFPAWADTSILSRQQVLLRYQQLI---KENLKEIA--------RLITLEQGKT------LADA--EGDVFR 140
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIealGDELVARAhaetglpeARLQGELGRTtgqlrlFADLvrEGSWLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 141 GlqVVEHAcSVTSLMLGEtmpsitkdMDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMKPSE 212
Cdd:cd07129 82 A--RIDPA-DPDRQPLPR--------PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 213 RVPGATMLLAKL----LQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSR--NGKRVQANMG 285
Cdd:cd07129 145 AHPGTSELVARAiraaLRATGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 286 AKNHGVVMPDANKEN--TLNQ-LVGAAFGAAGQRCmaLSTAVLVGEAKKWLPELVERAKNLrvnAGDQPGadlGPLITPq 362
Cdd:cd07129 225 SVNPVFILPGALAERgeAIAQgFVGSLTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTMLTP- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 363 akeRVCNLIDSGAKE-----GASILLDGRkikvkGYENGNFVGPTIisnVKPSMTCY------KEEIFGPVLVVLETETL 431
Cdd:cd07129 296 ---GIAEAYRQGVEAlaaapGVRVLAGGA-----AAEGGNQAAPTL---FKVDAAAFladpalQEEVFGPASLVVRYDDA 364
|
....*...
gi 205526 432 DEAIKIVN 439
Cdd:cd07129 365 AELLAVAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
43-438 |
2.47e-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: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKsdKWIDIHNPATNEVVGRVPQSTKAEMEAAVAACKRAFPAWADTSILSRQQVLL------RYQQLIKENL 116
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLLygdvshRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 117 KE--IARLITLEQGKTLADAEGDVFRGLQVVEHAC--SVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIP 192
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 193 LWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFER 272
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 273 GSRNGKRVQANMGAKnhgVVMPDANKENTLN-QLVGAAFGAAGQRCMALStavLVGEAKKWLPE-LVERAKNLrvnAGDQ 350
Cdd:cd07126 240 LHGKVKLEDAGFDWK---ILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS---ILFAHENWVQAgILDKLKAL---AEQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 351 PGADL--GPLITpQAKERVCNLIDS-GAKEGASILLDGRKIKvkgyeNGNFvgPTIISNVKPS------MTCYKE----- 416
Cdd:cd07126 311 KLEDLtiGPVLT-WTTERILDHVDKlLAIPGAKVLFGGKPLT-----NHSI--PSIYGAYEPTavfvplEEIAIEenfel 382
|
410 420
....*....|....*....|....*
gi 205526 417 ---EIFGPVLVVleTETLDEAIKIV 438
Cdd:cd07126 383 vttEVFGPFQVV--TEYKDEQLPLV 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
43-461 |
8.68e-10 |
|
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: 61.13 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 43 FIDGKFVESKSDKwIDIHNPATNEVVGRVpQSTKAEMEAAVA-ACKRAFPAWADTSILSRQQVL---LRYQQLIKENLKE 118
Cdd:cd07128 4 YVAGQWHAGTGDG-RTLHDAVTGEVVARV-SSEGLDFAAAVAyAREKGGPALRALTFHERAAMLkalAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 119 IArlitLEQGKTLADAEGDVFRGLQVVEHACSVTSLmLGETMPSITKDMDLYSYR----------LPL-GVCAGIAPFNF 187
Cdd:cd07128 82 LS----AATGATRRDSWIDIDGGIGTLFAYASLGRR-ELPNAHFLVEGDVEPLSKdgtfvgqhilTPRrGVAVHINAFNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 188 PAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQheaVNFICDHPDIK-AISFVGSNQA 265
Cdd:cd07128 157 PVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQdVVAFTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 266 GEYIfeRGS----RNGKRVQANMGAKNHGVVMPDAnKENT------LNQLVGAAFGAAGQRCMALSTAVL-------VGE 328
Cdd:cd07128 234 AAKL--RAHpnivARSIRFNAEADSLNAAILGPDA-TPGTpefdlfVKEVAREMTVKAGQKCTAIRRAFVpearvdaVIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 329 AkkwlpeLVERAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSgAKEGASILL---DGRKIKVKGYENGNFVGPTI 403
Cdd:cd07128 311 A------LKARLAKVVV--GDprLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFggpDRFEVVGADAEKGAFFPPTL 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205526 404 I--SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNdnpYGNG---TAIFTTNGAIARKYA 461
Cdd:cd07128 382 LlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAA---RGRGslvASVVTNDPAFARELV 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
76-493 |
1.37e-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: 60.57 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 76 KAEMEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLI--TLEQGKTLADAEGDVF---RGLQVVEHACS 150
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVmhTTGQAFMMAFQAGGPHaqdRGLEAVAYAWR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 151 VTSLMLGETM---PSITKD---MDLYSYRLPLGVCAGIAPFNFPAmiplW-----MFPmAMVCGNTFLMKPServPGATM 219
Cdd:cd07127 163 EMSRIPPTAEwekPQGKHDplaMEKTFTVVPRGVALVIGCSTFPT----WngypgLFA-SLATGNPVIVKPH---PAAIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 220 LLA-------KLLQDSG-APD-GTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIfERGSRnGKRVQANMGAKNHG 290
Cdd:cd07127 235 PLAitvqvarEVLAEAGfDPNlVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANAR-QAQVYTEKAGVNTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 291 VVmpdankENTlNQLVGA----AFGAA---GQRCMAlSTAVLV-------GEAKKWLPEL---VERAKNLRVNAGDQPGA 353
Cdd:cd07127 313 VV------DST-DDLKAMlrnlAFSLSlysGQMCTT-PQNIYVprdgiqtDDGRKSFDEVaadLAAAIDGLLADPARAAA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 354 DLGPLITPQAKERVcnlidSGAKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDE 433
Cdd:cd07127 385 LLGAIQSPDTLARI-----AEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDH 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205526 434 AIKIVNDNPYGNGT---AIFTTNGAIARKYAHMVDvgQVGVNVPIPVPLPMF-SFTGSRSSFRG 493
Cdd:cd07127 460 SIELARESVREHGAmtvGVYSTDPEVVERVQEAAL--DAGVALSINLTGGVFvNQSAAFSDFHG 521
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
59-438 |
4.33e-08 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 55.87 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 59 IHNPATNEVVGRVpQSTKAEMEAAVA-ACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 137
Cdd:PRK11903 23 LFDPVTGEELVRV-SATGLDLAAAFAfAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 138 VFRGLQVVEHACSV------TSLMLGETMPSITKDmDLYSYR---LPL-GVCAGIAPFNFPAMiPLW-MFPMAMVCGNTF 206
Cdd:PRK11903 102 IDGGIFTLGYYAKLgaalgdARLLRDGEAVQLGKD-PAFQGQhvlVPTrGVALFINAFNFPAW-GLWeKAAPALLAGVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 207 LMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQHEAvnfICDH---PDIkaISFVGSNQAGEYIFERGS--RNGKRV 280
Cdd:PRK11903 180 IVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG---LLDHlqpFDV--VSFTGSAETAAVLRSHPAvvQRSVRV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 281 QANMGAKNHGVVMPDANKEntlnqlvGAAFGA------------AGQRCMALSTaVLVGEA--KKWLPELVERAKNLRVN 346
Cdd:PRK11903 255 NVEADSLNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQKCTAIRR-IFVPEAlyDAVAEALAARLAKTTVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 347 AGDQPGADLGPLITPQAKERVCNLIDsGAKEGASILLDGRKIKVKGYEN--GNFVGPTIISNVKP--SMTCYKEEIFGPV 422
Cdd:PRK11903 327 NPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPavAACVGPTLLGASDPdaATAVHDVEVFGPV 405
|
410
....*....|....*.
gi 205526 423 LVVLETETLDEAIKIV 438
Cdd:PRK11903 406 ATLLPYRDAAHALALA 421
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
144-338 |
4.03e-06 |
|
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: 49.14 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 144 VVEHACSVTSLMLGETmpsitkdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAK 223
Cdd:cd07077 79 SVGHIQDVLLPDNGET----------YVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 224 LLQDSGAPDGTLNII----HGQHEAVNFICDHPDIKAISFVGSNQAGEYIfeRGSRNGKRVQAnMGAKNHGVVMPDANKE 299
Cdd:cd07077 148 LFQAADAAHGPKILVlyvpHPSDELAEELLSHPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADE 224
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 205526 300 NTLNQLV--GAAF-GAAgqrCMALSTAVLVGEAKKWLPELVE 338
Cdd:cd07077 225 ERASGSVhdSKFFdQNA---CASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
79-293 |
1.27e-03 |
|
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: 41.48 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 79 MEAAVAACKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLAD-------AEGDVFRGLQVVEHACSV 151
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205526 152 TSlmlGETMPSITKDMDlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD---- 227
Cdd:cd07081 81 LT---GDENGGTLIIAE------PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaava 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205526 228 SGAPDGTLNIIHGQH-EAVNFICDHPDIKAISFVGsnqaGEYIFERGSRNGKRVQAnMGAKNHGVVM 293
Cdd:cd07081 152 AGAPENLIGWIDNPSiELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVI 213
|
|
| |
