|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
30-506 |
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: 936.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 30 TKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKEL 109
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 110 ARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMG 189
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 190 MVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKR 269
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 270 VQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVG-EAKNWLPELVERAKNLRVNAGDQPGADVGPL 348
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 349 ISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIV 428
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1741435968 429 NRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSFRGDTNFYGKQGIQFYTQIKTITSQW 506
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
31-506 |
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: 841.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 31 KLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGM 190
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 VCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:TIGR01722 162 ACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKNWLPELVERAKNLRVNAGDQPGADVGPLIS 350
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLIT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 351 PQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNR 430
Cdd:TIGR01722 322 PQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 431 NPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSFRGDTNFYGKQGIQFYTQIKTITSQW 506
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
28-522 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 670.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 28 PTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIK 107
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 108 ELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFP 187
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 188 MGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNG 267
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 268 KRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKNWLPELVERAKNLRVNAGDQPGADVGP 347
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 348 LISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEI 427
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 428 VNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSFRGDTNFYGKQGIQFYTQIKTITSQWK 507
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|....*
gi 1741435968 508 AEDATLkspAVTMPT 522
Cdd:PLN02419 592 DIHSPF---SLAIPI 603
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
26-506 |
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: 547.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 26 SVPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDN 105
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 106 IKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWM 185
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 186 FPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGS 264
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 265 KNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKN-WLPELVERAKNLRVNAGDQPGA 343
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDeFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 344 DVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDE 423
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 424 AIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSFRGDtnFYGKQGIQFYTQIKTIT 503
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVT 476
|
...
gi 1741435968 504 SQW 506
Cdd:COG1012 477 IRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
38-502 |
1.78e-174 |
|
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: 499.75 E-value: 1.78e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 38 FVESkTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQ 117
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 118 GKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSiTKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYL 197
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 198 LKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGA 276
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 277 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKN-WLPELVERAKNLRVNAGDQPGADVGPLISPQARD 355
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDeFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 356 RVNSLIKSGVDEGAKLLLDGRnvkvKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGN 435
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741435968 436 GTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSFRGDTNfyGKQGIQFYTQIKTI 502
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
33-503 |
1.62e-132 |
|
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: 393.25 E-value: 1.62e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEWIDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELAR 111
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 112 LITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMV 191
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 192 CGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKNWLPELVERAKNLRVNAGDQPGADVGPLI 349
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 350 SPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVN 429
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741435968 430 RNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPI---PVPLPmfsFTGSRGSFRGDTNfYGKQGIQFYTQIKTIT 503
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP---FGGVKKSGNGHRE-AGTTALDAFTEWKAVY 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
71-503 |
6.19e-130 |
|
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: 385.02 E-value: 6.19e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 71 AAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETL 150
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 151 PSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG 230
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 231 -QHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA 309
Cdd:cd07078 162 dGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 310 LStAVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGrnvKVKGYENGN 387
Cdd:cd07078 242 AS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 388 FVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPV 467
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 1741435968 468 PLPMFSFTGSRGSfrGDTNFYGKQGIQFYTQIKTIT 503
Cdd:cd07078 398 AEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
33-502 |
3.85e-123 |
|
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: 369.27 E-value: 3.85e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEwiDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELAR 111
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 112 LITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMV 191
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 192 CGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKNWLPELVERAKNLRVNAGDQPGADVGPLI 349
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 350 SPQARDRVNSLIKSGVDEGAKLLLDGRnvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVN 429
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGE--RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 430 RNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVP-----IPVPlpmfsFTGSRGSFRGdtnfYGKQG---IQFYTQIKT 501
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKT 470
|
.
gi 1741435968 502 I 502
Cdd:cd07097 471 V 471
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
51-503 |
1.11e-114 |
|
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: 346.73 E-value: 1.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 51 NPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFR 130
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 131 GLQVV----EHACSITslvlGETLPSITKDMDTYTYRLPIGVCAGIAPFNFP-AMIPLWMFPMgMVCGNTYLLKPSERVP 205
Cdd:cd07103 83 AASFLewfaEEARRIY----GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAPA-LAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 206 GCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAknHG--VV 282
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 283 MPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSL 360
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 361 IKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIF 440
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1741435968 441 TTNGATARKYSHEVDVGQIGVNVPIP--VPLPM----FSFTGSRGsfrgdtnfyGKQGIQFYTQIKTIT 503
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLIsdAEAPFggvkESGLGREG---------GKEGLEEYLETKYVS 450
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
33-502 |
4.33e-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: 338.09 E-value: 4.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARL 112
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 113 ITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFP-AMIPLWMFPmGMV 191
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 192 CGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKNWLPELVERAKNLRVnaGD--QPGADVG 346
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 347 PLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIE 426
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 427 IVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSfTGSRGSFRGDTNfyGKQGIQFYTQIKTI 502
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
33-464 |
3.25e-110 |
|
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: 336.07 E-value: 3.25e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKtSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARL 112
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 113 ITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVC 192
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 193 GNTYLLKPSERVP----GCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGK 268
Cdd:cd07086 161 GNTVVWKPSETTPltaiAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 269 RVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKNWLPELVERAKNLRVNAGDQPGADVGP 347
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 348 LISPQARDRVNSLIKSGVDEGAKLLLDGRnvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEI 427
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 1741435968 428 VNRNPYGNGTAIFTTNGATARKY--SHEVDVGQIGVNVP 464
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIP 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
49-503 |
2.70e-106 |
|
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: 325.29 E-value: 2.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAE-GD 127
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VFRGLQVVEHACSITSLVLGETLPSiTKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGC 207
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQ-DGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 208 TMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSG 364
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 365 VDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNG 444
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1741435968 445 ATARKYSHEVDVGQIGVNVPIPVPLPMfSFTGSRGSfrGDTNFYGKQGIQFYTQIKTIT 503
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
33-462 |
3.15e-101 |
|
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: 313.09 E-value: 3.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT--WSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSiTKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGM 190
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 VCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKR 269
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 270 VQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGP 347
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 348 LISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEI 427
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1741435968 428 VNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
32-503 |
7.35e-99 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 306.35 E-value: 7.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 32 LFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELAR 111
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 112 LITLEQG--KTLAdAEGDVFRGLQVVEHAcsitsLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPA-MIPLWMFPm 188
Cdd:cd07138 81 AITLEMGapITLA-RAAQVGLGIGHLRAA-----ADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLnQIVLKVAP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 189 GMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNG 267
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 268 KRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKnwLPELVERAK----NLRVNAGDQPGA 343
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAAaaaeAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 344 DVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDE 423
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 424 AIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPL-PmfsFTGSRGSfrGDTNFYGKQGIQFYTQIKTI 502
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQS--GNGREWGRYGLEEFLEVKSI 464
|
.
gi 1741435968 503 T 503
Cdd:cd07138 465 Q 465
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
49-502 |
1.08e-97 |
|
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: 302.91 E-value: 1.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDV 128
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 129 FRGLQVVEHACsitSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCT 208
Cdd:cd07106 81 GGAVAWLRYTA---SLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 209 MLLAKLLQDSgAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANK 288
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 289 ENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVD 366
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 367 EGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGAT 446
Cdd:cd07106 316 KGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 447 ARKYSHEVDVGQIGVNvPIPVPLPMFSFTGSRGSFRGDTnfYGKQGIQFYTQIKTI 502
Cdd:cd07106 392 AEAVARRLEAGTVWIN-THGALDPDAPFGGHKQSGIGVE--FGIEGLKEYTQTQVI 444
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-462 |
1.67e-97 |
|
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: 304.53 E-value: 1.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 12 KRVPLQLGRmcyssSVPttkLFIDGKFVEskTSEWIDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILT 90
Cdd:cd07124 23 ARVREELGR-----EYP---LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 91 RQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRlPIGVCA 170
Cdd:cd07124 93 RARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 171 GIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISF 249
Cdd:cd07124 172 VISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 250 VGSNQAGEYIYER------GSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKNWL 323
Cdd:cd07124 252 TGSREVGLRIYERaakvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 324 PE-LVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGaKLLLDGR--NVKVKGYengnFVGPTIISNVKPD 400
Cdd:cd07124 332 LErLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGY----FVQPTIFADVPPD 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1741435968 401 MTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07124 407 HRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN 468
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
78-503 |
1.23e-96 |
|
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: 297.22 E-value: 1.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 78 RAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDM 157
Cdd:cd06534 5 AAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 158 DTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG-QHAAVN 236
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 237 FICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLV 316
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 317 GEAKnwLPELVERAKnlrvnagdqpgadvgplispqardrvnsliksgvdegakllldgrnvkvkgyengnfvgpTIISN 396
Cdd:cd06534 244 HESI--YDEFVEKLV------------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 397 VKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTG 476
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGG 341
|
410 420
....*....|....*....|....*..
gi 1741435968 477 SRGSFRGDTNfyGKQGIQFYTQIKTIT 503
Cdd:cd06534 342 VKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
30-503 |
4.81e-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: 299.51 E-value: 4.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 30 TKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSI--LTRQQVFLRYQQLIKDNIK 107
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 108 ELARLITLEQGKTL-ADAEGDVfrglqvvehACSITSL---------VLGETLPSITKDMdTYTYRLPIGVCAGIAPFNF 177
Cdd:cd07091 84 ELAALESLDNGKPLeESAKGDV---------ALSIKCLryyagwadkIQGKTIPIDGNFL-AYTRREPIGVCGQIIPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 178 PAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAG 256
Cdd:cd07091 154 PLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAgAAISSHMDVDKIAFTGSTAVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 257 EYIYERGSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNL 333
Cdd:cd07091 234 RTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFVQESiyDEFVEKFKARAEKR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 334 RVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVL 413
Cdd:cd07091 313 VVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 414 IVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVpIPVPLPMFSFTGSRGSFRGDTNfyGKQGI 493
Cdd:cd07091 389 TILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGREL--GEEGL 465
|
490
....*....|
gi 1741435968 494 QFYTQIKTIT 503
Cdd:cd07091 466 EEYTQVKAVT 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
48-464 |
1.71e-94 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 294.62 E-value: 1.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 48 DIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGD 127
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGC 207
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 208 TMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NkentLNQLVG-AAFGA---AGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVnaGD--QPGADVGPLISPQARDRVN 358
Cdd:cd07150 242 D----LDYAVRaAAFGAfmhQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 359 SLIKSGVDEGAKLLldgrnvkVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTA 438
Cdd:cd07150 315 RQVEDAVAKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420
....*....|....*....|....*.
gi 1741435968 439 IFTTNGATARKYSHEVDVGQIGVNVP 464
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDP 413
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
49-502 |
1.33e-93 |
|
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: 292.67 E-value: 1.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDV 128
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 129 FRGLQVVEHACSITSLVLGETLPsITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCT 208
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 209 MLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANK 288
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 289 ENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVnaGD--QPGADVGPLISPQARDRVNSLIKSG 364
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSN-GTRVFVQRSikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 365 VDEGAKLLLDGRNVKVK-GYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTN 443
Cdd:cd07090 317 KQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1741435968 444 GATARKYSHEVDVGQIGVN----VPIPVPlpmfsFTGSRGSFRGDTNfyGKQGIQFYTQIKTI 502
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
49-502 |
5.07e-93 |
|
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: 290.99 E-value: 5.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT--WSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DV---------FRGLqvvehACSITslvlGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYL 197
Cdd:cd07114 81 QVrylaewyryYAGL-----ADKIE----GAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 198 LKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGA 276
Cdd:cd07114 152 LKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETgEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 277 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQAR 354
Cdd:cd07114 232 KSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 355 DRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYG 434
Cdd:cd07114 311 EKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1741435968 435 NGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPlPMFSFTGSRGSFRGDTNfyGKQGIQFYTQIKTI 502
Cdd:cd07114 391 LAAGIWTRDLARAHRVARAIEAGTVWVNTYRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
33-500 |
8.14e-93 |
|
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: 290.94 E-value: 8.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARL 112
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 113 ITLEQGKTLADAE-GDVFRGLQVVEHACSITSLVLGETLPSITKDmDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMV 191
Cdd:TIGR01804 81 ETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 192 CGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPL 348
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSN-GTRVFVHKKikERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 349 ISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIV 428
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1741435968 429 NRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNV--PIPVPLPmfsFTGSRGSFRGDTNfyGKQGIQFYTQIK 500
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTynLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
24-500 |
5.06e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 290.05 E-value: 5.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 24 SSSVPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIK 103
Cdd:PLN02278 19 NAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 104 DNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFP-AMIP 182
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 183 LWMFPmGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYE 261
Cdd:PLN02278 179 RKVGP-ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 262 RGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVNAGD 339
Cdd:PLN02278 258 GAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 340 QPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKgyenGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEAD 419
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 420 SLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIpVPLPMFSFTGSRGSFRGDTNfyGKQGIQFYTQI 499
Cdd:PLN02278 413 TEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEI 489
|
.
gi 1741435968 500 K 500
Cdd:PLN02278 490 K 490
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
71-462 |
5.59e-92 |
|
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: 287.50 E-value: 5.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 71 AAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETL 150
Cdd:cd07104 4 RAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 151 PSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCT-MLLAKLLQDSGAPDGTLNIIH 229
Cdd:cd07104 84 PSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 230 GQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM 308
Cdd:cd07104 164 GGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 309 ALSTaVLVGE--AKNWLPELVERAKNLRVnaGDQ--PGADVGPLISPQARDRVNSLIKSGVDEGAKLLldgrnvkVKGYE 384
Cdd:cd07104 244 AAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGARLL-------TGGTY 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1741435968 385 NGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
47-503 |
1.74e-91 |
|
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: 287.18 E-value: 1.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DVFRGLQVVEHACSITSLVLGETLPsitkdMD---------TYTYRLPIGVCAGIAPFNFPamiplwmfpMGMVC----- 192
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIP-----FDaspggegriGFTIREPIGVVAAITPFNFP---------LNLVAhkvgp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 193 ----GNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKng 267
Cdd:cd07149 147 aiaaGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 268 KRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVnaGD--QPGA 343
Cdd:cd07149 225 KKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDiyDEFLERFVAATKKLVV--GDplDEDT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 344 DVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNvkvkgyeNGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDE 423
Cdd:cd07149 302 DVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 424 AIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNvPIPvplpmfsftgsrgSFRGDTNFYG--------KQGIQF 495
Cdd:cd07149 375 AIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIN-DSS-------------TFRVDHMPYGgvkesgtgREGPRY 440
|
490
....*....|..
gi 1741435968 496 ----YTQIKTIT 503
Cdd:cd07149 441 aieeMTEIKLVC 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
31-462 |
1.97e-91 |
|
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: 287.55 E-value: 1.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 31 KLFIDGKFVESKtSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSET-SILTRQQVFLRYQQLIKDNIKEL 109
Cdd:cd07082 3 KYLINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 110 ARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSI----TKDMDTYTYRLPIGVCAGIAPFNFP------A 179
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgTKGKIAQVRREPLGVVLAIGPFNYPlnltvsK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 180 MIPlwmfpmGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEY 258
Cdd:cd07082 162 LIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 259 IYERGSKngKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVN 336
Cdd:cd07082 236 LKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHEsvADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 337 AGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGrnvkvkGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVL 416
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPII 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1741435968 417 EADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07082 387 RVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
47-462 |
2.25e-90 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 284.24 E-value: 2.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DVFRGLQVVEHACSITSLVLGETLPS----ITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSE 202
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 203 RVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGV 281
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 282 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVnaGD--QPGADVGPLISPQARDRV 357
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 358 NSLIKSGVDEGAKLLLDGRNvkvkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGT 437
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420
....*....|....*....|....*
gi 1741435968 438 AIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-502 |
4.84e-88 |
|
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: 278.17 E-value: 4.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 51 NPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG-DVF 129
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 130 RGLQVVEHACSITSLVLGETLPsITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTM 209
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 210 LLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANK 288
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 289 ENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVD 366
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 367 EGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGAT 446
Cdd:cd07115 321 EGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1741435968 447 ARKYSHEVDVGQIGVNV--PIPVPLPmfsFTGSRGSFRGDTNfyGKQGIQFYTQIKTI 502
Cdd:cd07115 397 AHRVAAALKAGTVWINTynRFDPGSP---FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
32-503 |
7.44e-87 |
|
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: 275.61 E-value: 7.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 32 LFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYT--TWSETSILTRQQVFLRYQQLIKDNIKEL 109
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 110 ARLITLEQGKTLAdaegdVFRGLQVVEHACSITS-LVLGETLPSIT-----KDMDTYTYRLPIGVCAGIAPFNFPAMIPL 183
Cdd:cd07139 81 ARLWTAENGMPIS-----WSRRAQGPGPAALLRYyAALARDFPFEErrpgsGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 184 WMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERG 263
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 264 SKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAK--NWLPELVERAKNLRVNAGDQP 341
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRydEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 342 GADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGrnVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSL 421
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGG--GRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 422 DEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVpipvplPMFSFTGSRGSFR--GDTNFYGKQGIQFYTQI 499
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG------FRLDFGAPFGGFKqsGIGREGGPEGLDAYLET 466
|
....
gi 1741435968 500 KTIT 503
Cdd:cd07139 467 KSIY 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
50-503 |
1.92e-86 |
|
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: 274.21 E-value: 1.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 50 HNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT--WSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGD 127
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGC 207
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 208 TMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NKENTLNqlvGAAFGA---AGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVnaGD--QPGADVGPLISPQARDRVNS 359
Cdd:cd07118 242 DLDAAAD---AVVFGVyfnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 360 LIKSGVDEGAKLLLDGrnvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAI 439
Cdd:cd07118 316 YVDAGRAEGATLLLGG---ERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 440 FTTNGATARKYSHEVDVGQIGVNVPIP--VPLPmfsFTGSRGSFRGDTNfyGKQGIQFYTQIKTIT 503
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
12-462 |
2.09e-86 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 275.66 E-value: 2.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 12 KRVPLQLGRmcyssSVPttkLFIDGKFVEskTSEWIDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILT 90
Cdd:PRK03137 27 KKVEKELGQ-----DYP---LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 91 RQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVE-HACSITSLVLGETLPSITKDMDTYTYRlPIGVC 169
Cdd:PRK03137 97 RARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEyYARQMLKLADGKPVESRPGEHNRYFYI-PLGVG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 170 AGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAIS 248
Cdd:PRK03137 176 VVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFIT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 249 FVGSNQAGEYIYER------GSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKNW 322
Cdd:PRK03137 256 FTGSREVGLRIYERaakvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 323 LPE-LVERAKNLRVNAGDQPgADVGPLISPQARDRVNSLIKSGVDEGaKLLLDGRNVKVKGYengnFVGPTIISNVKPDM 401
Cdd:PRK03137 336 VLEkVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKA 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1741435968 402 TCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:PRK03137 410 RIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
71-503 |
2.60e-86 |
|
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: 272.91 E-value: 2.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 71 AAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETL 150
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 151 PSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG 230
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 231 --QHAA--VNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQR 306
Cdd:cd07105 164 spEDAPevVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 307 CMalSTA-VLVGE--AKNWLPELVERAKNLRvnagdQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNvkvKGY 383
Cdd:cd07105 244 CM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA---DES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 384 ENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNV 463
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1741435968 464 PI----PVpLPmFSFTGSRGSFRgdtnFYGKQGIQFYTQIKTIT 503
Cdd:cd07105 394 MTvhdePT-LP-HGGVKSSGYGR----FNGKWGIDEFTETKWIT 431
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
49-503 |
3.03e-86 |
|
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: 273.34 E-value: 3.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT-WSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGD 127
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VFRGLQVVEHACSITSLVLGETLPsITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGC 207
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 208 TMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAG-DQPgaDVGPLISPQARDRVNSLIKS 363
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 364 GVDEGAKLLLDGRNVKVKgYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTN 443
Cdd:cd07109 317 ARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1741435968 444 GATARKYSHEVDVGQIGVNVPIP---VPLPmfsFTGSRGSFRGDTNfyGKQGIQFYTQIKTIT 503
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
30-502 |
4.26e-86 |
|
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: 273.90 E-value: 4.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 30 TKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAY-TTWSETSILTRQQVFLRYQQLIKDNIKE 108
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 109 LARLITLEQGKTL-ADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMdTYTYRLPIGVCAGIAPFNFPAMIPLWMFP 187
Cdd:cd07144 88 LAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 188 MGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKN 266
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 267 GKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAK-NLRVNAGDQPGA 343
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 344 DVGPLISPQARDRVNSLIKSGVDEGAKLLLDGrNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDE 423
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGG-EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 424 AIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVP----IPVPlpmfsFTGSRGSfrGDTNFYGKQGIQFYTQI 499
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYTQT 477
|
...
gi 1741435968 500 KTI 502
Cdd:cd07144 478 KAV 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
25-502 |
1.33e-84 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 270.21 E-value: 1.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 25 SSVPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKD 104
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 105 NIKELARLITLEQGKTLADAE-GDVFRGLQVVEHACSITSLVLGETLPSITKDMdTYTYRLPIGVCAGIAPFNFPAMIPL 183
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 184 WMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERG 263
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 264 SKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVnaGD-- 339
Cdd:PRK13252 241 AASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSikAAFEARLLERVERIRI--GDpm 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 340 QPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEAD 419
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 420 SLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNV--PIPVPLPmfsFTGSRGSFRGDTNfyGKQGIQFYT 497
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYT 472
|
....*
gi 1741435968 498 QIKTI 502
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
49-504 |
6.38e-84 |
|
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: 267.27 E-value: 6.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDV 128
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 129 FRGlqVVEH-------ACSITSLVLGETLPSITkdmdTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPS 201
Cdd:cd07092 81 LPG--AVDNfrffagaARTLEGPAAGEYLPGHT----SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 202 ERVPGCTMLLAKLLQDsGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHG 280
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 281 VVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVN 358
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 359 SLIkSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTA 438
Cdd:cd07092 313 GFV-ERAPAHARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 439 IFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMfSFTGSRGSfrGdtnfYGKQ----GIQFYTQIKTITS 504
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
32-503 |
7.31e-84 |
|
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: 268.16 E-value: 7.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 32 LFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAY-TTWSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLITLEQGKTLAdaegdVFRGLQVvehACSITSL---------VLGETL-PSIT----KDMDTYTYRLPIGVCAGIAPFN 176
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEV---GQSANFLryfagwatkINGETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 177 FPAMIPLWMFPMGMVCGNTYLLKPSERVPgCTML-LAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQA 255
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 256 GEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCmALSTAVLVGEAKnwLPELVE----RAK 331
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSK--FDELVTklkqALS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 332 NLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGP 411
Cdd:cd07113 310 SFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 412 VLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPlPMFSFTGSRGSFRGDTnfYGKQ 491
Cdd:cd07113 386 VVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSA 462
|
490
....*....|..
gi 1741435968 492 GIQFYTQIKTIT 503
Cdd:cd07113 463 FIDDYTELKSVM 474
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
27-503 |
9.48e-84 |
|
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: 268.06 E-value: 9.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 27 VPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAY---TTWSETSILTRQQVFLRYQQLIK 103
Cdd:cd07141 4 IKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 104 DNIKELARLITLEQGKTLADA-EGDVFRGLQVVEHACSITSLVLGETLPSITKDMdTYTYRLPIGVCAGIAPFNFPAMIP 182
Cdd:cd07141 84 RDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFF-TYTRHEPVGVCGQIIPWNFPLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 183 LWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG-QHAAVNFICDHPAIKAISFVGSNQAGEYIYE 261
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 262 RGSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVNAG 338
Cdd:cd07141 243 AAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 339 DQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEA 418
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 419 DSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPlPMFSFTGSRGSFRGDTNfyGKQGIQFYTQ 498
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTE 474
|
....*
gi 1741435968 499 IKTIT 503
Cdd:cd07141 475 VKTVT 479
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
49-502 |
5.99e-83 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 265.26 E-value: 5.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWS-ETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAegd 127
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 vfRGLQV---VEH----ACSITSLVLGETLPSiTKDMDTYTYRL----PIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTY 196
Cdd:cd07089 78 --RAMQVdgpIGHlryfADLADSFPWEFDLPV-PALRGGPGRRVvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 197 LLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMG 275
Cdd:cd07089 155 VLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 276 AKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAVLVGEAKnwLPELVERAKN----LRVNAGDQPGADVGP 347
Cdd:cd07089 235 GKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVPRSR--YDEVVEALAAafeaLPVGDPADPGTVMGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 348 LISPQARDRVNSLIKSGVDEGAKLLLDGRnvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEI 427
Cdd:cd07089 308 LISAAQRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 428 VNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNvpipvplpmfsfTGsrGSFRGDTNF-----------YGKQGIQFY 496
Cdd:cd07089 386 ANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN------------GG--GGYGPDAPFggykqsglgreNGIEGLEEF 451
|
....*.
gi 1741435968 497 TQIKTI 502
Cdd:cd07089 452 LETKSI 457
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
36-505 |
1.27e-82 |
|
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: 264.55 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 36 GKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITL 115
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 116 EQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNT 195
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 196 YLLKPSERVPGCT-MLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSN 273
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 274 MGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVnaGDQ--PGADVGPLI 349
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVVGPLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 350 SPQARDRVNSLIKSGVDEGAKLLLDGRnvkvkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVN 429
Cdd:cd07151 318 NESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741435968 430 RNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNvPIPV-PLPMFSFTGSRGSfrGDTNFYGKQGIQFYTQIKTITSQ 505
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
49-503 |
2.10e-81 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 261.14 E-value: 2.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTL-ADAEGD 127
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VFRGLQVVEHACSITSLVLGETLPsITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGC 207
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 208 TMLLAKLLQDSgAPDGTLNII--HGQHAAVNFIcDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPD 285
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVItgYGEECGAALV-DHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 286 ANKENTLNQLV-GAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVnaGD--QPGADVGPLISPQARDRVNSL 360
Cdd:cd07108 238 ADLDDAVDGAIaGMRFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 361 IKSGVDE-GAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAI 439
Cdd:cd07108 315 IDLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1741435968 440 FTTNGATARKYSHEVDVGQIGVNVPIpVPLPMFSFTGSRGSFRGDTnfYGKQG-IQFYTQIKTIT 503
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
24-502 |
3.52e-81 |
|
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: 261.31 E-value: 3.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 24 SSSVPTtKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAY-TTWS-ETSILTRQQVFLRYQQL 101
Cdd:cd07143 2 KYEQPT-GLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWGlKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 102 IKDNIKELARLITLEQGKT-LADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMdTYTYRLPIGVCAGIAPFNFPAM 180
Cdd:cd07143 81 MERNLDYLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKL-TYTRHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 181 IPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYI 259
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 260 YERGSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVN 336
Cdd:cd07143 240 MEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQEGiyDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 337 AGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVL 416
Cdd:cd07143 319 DPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 417 EADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPlPMFSFTGSRGSFRGDTnfYGKQGIQFY 496
Cdd:cd07143 395 KFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFGGYKQSGIGRE--LGEYALENY 471
|
....*.
gi 1741435968 497 TQIKTI 502
Cdd:cd07143 472 TQIKAV 477
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
71-462 |
6.32e-81 |
|
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: 258.93 E-value: 6.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 71 AAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEH-ACSITSLVLGET 149
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 150 LPsiTKDMDTYTYRLPIGVCAGIAPFNFPamipLW-MF----PMGMVcGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGT 224
Cdd:cd07100 83 IE--TDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAGFPEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 225 LNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 304
Cdd:cd07100 156 FQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 305 QRCMAlstavlvgeAKNWLPE----------LVERAKNLRVnaGD--QPGADVGPLISPQARDRVNSLIKSGVDEGAKLL 372
Cdd:cd07100 236 QSCIA---------AKRFIVHedvydeflekFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 373 LDGrnVKVKGyeNGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSH 452
Cdd:cd07100 305 LGG--KRPDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410
....*....|
gi 1741435968 453 EVDVGQIGVN 462
Cdd:cd07100 381 RLEAGMVFIN 390
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
47-503 |
1.84e-80 |
|
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: 258.52 E-value: 1.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DVFRGLQVVEHACSITSLVLGETLPS-ITKDMDT---YTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSE 202
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdATQGSDNrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 203 RVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSknGKRVQSNMGAKNHGV 281
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 282 VMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSL 360
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 361 IKSGVDEGAKLLLDGrnvkvkgYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIF 440
Cdd:cd07094 319 VEEAVEAGARLLCGG-------ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741435968 441 TTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSfrgdtnFYGKQGIQF----YTQIKTIT 503
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
49-503 |
3.56e-78 |
|
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: 252.66 E-value: 3.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDV 128
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 129 ---------FRGL--QVVEHAcsitslvlGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYL 197
Cdd:cd07110 81 ddvagcfeyYADLaeQLDAKA--------ERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 198 LKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNF-ICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGA 276
Cdd:cd07110 153 LKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 277 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQAR 354
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 355 DRVNSLIKSGVDEGAKLLLDGRnvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYG 434
Cdd:cd07110 312 EKVLSFIARGKEEGARLLCGGR--RPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1741435968 435 NGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVpLPMFSFTGSRGSFRGDTnfYGKQGIQFYTQIKTIT 503
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGRE--LGEWGLDNYLEVKQIT 455
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-462 |
4.07e-78 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 251.83 E-value: 4.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 56 EVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVV 135
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 136 EHACSITSLVLGETLPSITKDMdTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCT-MLLAKL 214
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 215 LQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQ 294
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 295 LVGAAFGAAGQRCMAlSTAVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLL 372
Cdd:cd07152 241 GAWGAFLHQGQICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 373 LDGRnvkvkgYEnGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSH 452
Cdd:cd07152 320 AGGT------YD-GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410
....*....|
gi 1741435968 453 EVDVGQIGVN 462
Cdd:cd07152 393 RLRTGMLHIN 402
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
49-462 |
1.58e-77 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 250.76 E-value: 1.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDV 128
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 129 FRGLQVVEHACSITSLVLGETLPSITKDMDtYTYRLPIGVCAGIAPFNFPAMiplwmFPMG-----MVCGNTYLLKPSER 203
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLH-YTLREPYGVVARIVAFNHPLM-----FAAAkiaapLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 204 VPGCTMLLAKLLQDSgAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVV 282
Cdd:cd07107 155 APLSALRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 283 MPDANKENTLNQLV-GAAFGAAGQRCMALSTAvLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNS 359
Cdd:cd07107 234 FPDADPEAAADAAVaGMNFTWCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 360 LIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAI 439
Cdd:cd07107 313 YIDSAKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420
....*....|....*....|...
gi 1741435968 440 FTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWIN 415
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
50-503 |
1.99e-77 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 250.60 E-value: 1.99e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 50 HNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVF 129
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 130 RGLQVVEHACSITSLVLGE---TLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPG 206
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 207 CTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAGVDK-VAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSG 364
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 365 VDEGAKLLLDGRNVKVKGyengNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNG 444
Cdd:cd07099 319 VAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 445 ATARKYSHEVDVGQIGVN-VPIPVPLPMFSFTGSRGSfrGDTNFYGKQGIQFYTQIKTIT 503
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
48-502 |
1.20e-76 |
|
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: 248.67 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 48 DIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYT--TWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADA- 124
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 125 EGDV------FRGlqvveHACSITSlVLGETLPSiTKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLL 198
Cdd:cd07112 85 AVDVpsaantFRW-----YAEAIDK-VYGEVAPT-GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 199 KPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG-QHAAVNFICDHPAIKAISFVGSNQAGEYIYER-GSKNGKRVQSNMGA 276
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYsGQSNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 277 KNHGVVMPDA-NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVnaGD--QPGADVGPLISP 351
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 352 QARDRVNSLIKSGVDEGAKLLLDGRNVKVKGyeNGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRN 431
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1741435968 432 PYGNGTAIFTTNGATARKYSHEVDVGQIGVN----VPIPVPlpmfsFTGSRGSFRGDTNfyGKQGIQFYTQIKTI 502
Cdd:cd07112 393 VYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
47-503 |
6.13e-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: 246.50 E-value: 6.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSrayttwSETSILTRQQ---VFLRYQQLIKDNIKELARLITLEQGKTLAD 123
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAA------SYRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 124 AEGDVFRGLQV----VEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLK 199
Cdd:cd07146 75 TRYEVGRAADVlrfaAAEALRDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 200 PSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIyeRGSKNGKRVQSNMGAKN 278
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIgDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 279 HGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVnaGD--QPGADVGPLISPQAR 354
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 355 DRVNSLIKSGVDEGAKLLLDGRnvkvkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYG 434
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 435 NGTAIFTTNGATARKYSHEVDVGQIGVNvpiPVP---LPMFSFTGSRGSFRGdtnfyGKQGIQ----FYTQIKTIT 503
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
29-466 |
1.11e-75 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 246.74 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 29 TTKLFIDGKFVESKTSEWiDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKE 108
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 109 LARLITLEQGK----TLAD---AEGDVFR---GLqvvehACSITSLVLGETLPSITkdmdTYTYRLPIGVCAGIAPFNFP 178
Cdd:PRK13473 81 FARLESLNCGKplhlALNDeipAIVDVFRffaGA-----ARCLEGKAAGEYLEGHT----SMIRRDPVGVVASIAPWNYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 179 AMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSgAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGE 257
Cdd:PRK13473 152 LMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 258 YIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKnwLPELVER----AKNL 333
Cdd:PRK13473 231 HVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGI--YDDLVAKlaaaVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 334 RVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEG-AKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPV 412
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1741435968 413 LIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIP 466
Cdd:PRK13473 384 VSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
47-489 |
2.07e-74 |
|
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: 242.54 E-value: 2.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DVFRGLQVVEHACSITSLVLGETLPsitkdMDTY---------TYRLPIGVCAGIAPFNFPamiplwmfpMGMVC----- 192
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLP-----LDISargegrqglVRRFPIGPVSAITPFNFP---------LNLVAhkvap 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 193 ----GNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKngK 268
Cdd:cd07147 147 aiaaGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 269 RVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVnaGD--QPGAD 344
Cdd:cd07147 225 KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKT--GDpkDDATD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 345 VGPLISPQARDRVNSLIKSGVDEGAKLLLDGRnvkvkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEA 424
Cdd:cd07147 302 VGPMISESEAERVEGWVNEAVDAGAKLLTGGK-------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEA 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 425 IEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN-VPipvplpmfsftgsrgSFRGDTNFYG 489
Cdd:cd07147 375 LAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVP---------------TFRVDHMPYG 425
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
31-502 |
3.02e-74 |
|
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: 243.02 E-value: 3.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 31 KLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLITLEQGKTLADAEG-DVfrgLQVVEHACSITSLVLGE--TLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFP 187
Cdd:cd07559 82 VAETLDNGKPIRETLAaDI---PLAIDHFRYFAGVIRAQegSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 188 MGMVCGNTYLLKPSERVPGCTMLLAKLLQDSgAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKN 266
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAgKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 267 GKRVQSNMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRCMALSTAvLVGEA--KNWLPELVERAKNLRVNAGD 339
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVCTCPSRA-LVQESiyDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 340 QPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEAD 419
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 420 SLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPlpmfsftgSRGSFRGdtnfYGKQGI------ 493
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP--------AHAPFGG----YKKSGIgrethk 464
|
490
....*....|..
gi 1741435968 494 ---QFYTQIKTI 502
Cdd:cd07559 465 mmlDHYQQTKNI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
27-502 |
5.25e-74 |
|
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: 242.40 E-value: 5.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 27 VPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYT--TWSETSILTRQQVFLRYQQLIKD 104
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 105 NIKELARLITLEQGKTLADAE-GDVFRGLQVVEHACSITSLVLGETLPSiTKDMDTYTYRLPIGVCAGIAPFNFPAMIPL 183
Cdd:cd07142 81 HADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPA-DGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 184 WMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNF-ICDHPAIKAISFVGSNQAGEYIYER 262
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 263 GSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKnwLPELVERAKN--LRVNAGD 339
Cdd:cd07142 240 AAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHESI--YDEFVEKAKAraLKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 340 --QPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLE 417
Cdd:cd07142 317 pfRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 418 ADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVpIPVPLPMFSFTGSRGSFRGDTNfyGKQGIQFYT 497
Cdd:cd07142 393 FKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYL 469
|
....*
gi 1741435968 498 QIKTI 502
Cdd:cd07142 470 QVKAV 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
31-502 |
1.87e-71 |
|
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: 235.43 E-value: 1.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 31 KLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSITSLVLGETLPSITKdmdtytyRLPIGVCAGIAPFNFPAMIPL 183
Cdd:cd07117 82 MVETLDNGKpiretRAVDipLAADHFRYFAGVIRAEEGSANMIDEDTLSIVL-------REPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 184 WMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSgAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYER 262
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 263 GSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAGDQ 340
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiyDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 341 PGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADS 420
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 421 LDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNV--PIPVPLPmfsFTGSRGSFRGDTNFygKQGIQFYTQ 498
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGRETH--KSMLDAYTQ 467
|
....
gi 1741435968 499 IKTI 502
Cdd:cd07117 468 MKNI 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
25-466 |
6.83e-71 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 235.01 E-value: 6.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 25 SSVPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT-----WSETSILTRQQVFLRYQ 99
Cdd:PLN02467 3 IPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 100 QLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRL---PIGVCAGIAPFN 176
Cdd:PLN02467 83 AKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVlkePLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 177 FPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQA 255
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 256 GEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNL 333
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 334 RVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGrnVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVL 413
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1741435968 414 IVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIP 466
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-503 |
1.87e-68 |
|
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: 227.23 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 51 NPATNEVIGRVPKATQEEMLAAVDSCSRAY--TTWSETSILtRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDV 128
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 129 FRGLQVVEHACSITSLVLGETLPSITKDMDTYTyRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCT 208
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVL-REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 209 MLLAKLLQD-SGAPDGTLNIIHGQ-HAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:cd07120 161 AAIIRILAEiPSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSG 364
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSR-VLVQRsiADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 365 VDEGAKLLLDGRNVkVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNG 444
Cdd:cd07120 320 IAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1741435968 445 ATARKYSHEVDVGQIGVNVPIPVpLPMFSFTGSRGSFRGDTNfyGKQGIQFYTQIKTIT 503
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
27-462 |
6.25e-67 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 224.31 E-value: 6.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 27 VPT---TKLFIDGKFVES---KTSEWIDihnPATNEVIGRVPKATQEEMLAAVDSCSRAYT--TWSETSILTRQQVFLRY 98
Cdd:PLN02766 15 VPEikfTKLFINGEFVDAasgKTFETRD---PRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 99 QQLIKDNIKELARLITLEQGKTLADAEG-DVFRGLQVVEHACSITSLVLGETLpSITKDMDTYTYRLPIGVCAGIAPFNF 177
Cdd:PLN02766 92 ADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 178 PAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG-QHAAVNFICDHPAIKAISFVGSNQAG 256
Cdd:PLN02766 171 PSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 257 EYIYERGSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNL 333
Cdd:PLN02766 251 RKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVQEGiyDEFVKKLVEKAKDW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 334 RVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVL 413
Cdd:PLN02766 330 VVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGY----YIEPTIFTDVTEDMKIAQDEIFGPVM 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1741435968 414 IVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:PLN02766 406 SLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
33-500 |
8.32e-67 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 223.63 E-value: 8.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARL 112
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 113 ITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFP-AMIPLWMFPmGMV 191
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 192 CGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM-ALSTAVLVGEAKNWLPELVERAKNLRVNAGDQPGADVGPLI 349
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 350 SPQARDRVNSLIKSGVDEGAKLLLDGRNVKVkgyeNGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVN 429
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1741435968 430 RNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIpVPLPMFSFTGSRGSFRGDTNfyGKQGIQFYTQIK 500
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
26-517 |
1.83e-66 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 224.30 E-value: 1.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 26 SVPTTKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT--WSETSILTRQQVFLRYQQLIK 103
Cdd:PLN02466 54 QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 104 DNIKELARLITLEQGKTL---ADAEGDVFrgLQVVEHACSITSLVLGETLPSitkDMDTYTYRL--PIGVCAGIAPFNFP 178
Cdd:PLN02466 134 KHNDELAALETWDNGKPYeqsAKAELPMF--ARLFRYYAGWADKIHGLTVPA---DGPHHVQTLhePIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 179 AMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHA-AVNFICDHPAIKAISFVGSNQAGE 257
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPtAGAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 258 YIYERGSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAvLVGEAKnwLPELVERAKN--LR 334
Cdd:PLN02466 289 IVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHERV--YDEFVEKAKAraLK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 335 VNAGD--QPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPV 412
Cdd:PLN02466 366 RVVGDpfKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 413 LIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN------VPIPvplpmfsFTGSRGSFRGDTN 486
Cdd:PLN02466 442 QSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIGREK 514
|
490 500 510
....*....|....*....|....*....|.
gi 1741435968 487 fyGKQGIQFYTQIKTITSqwkaedaTLKSPA 517
Cdd:PLN02466 515 --GIYSLNNYLQVKAVVT-------PLKNPA 536
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
50-502 |
1.36e-65 |
|
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: 219.42 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 50 HNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVF 129
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 130 RGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTM 209
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 210 LLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKE 289
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 290 NTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDE 367
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 368 GAKLLLDGrNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATA 447
Cdd:cd07102 320 GARALIDG-ALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1741435968 448 RKYSHEVDVGQIGVNvPIPVPLPMFSFTGSRGSFRGDTnfYGKQGIQFYTQIKTI 502
Cdd:cd07102 399 EALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRGVT--LSRLGYDQLTRPKSY 450
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
100-462 |
7.15e-65 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 216.14 E-value: 7.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 100 QLIKDNIKELARLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPA 179
Cdd:PRK10090 6 AGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 180 -MIPLWMFPmGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGE 257
Cdd:PRK10090 86 fLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 258 YIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC-MALSTAVLVGEAKNWLPELVERAKNLRV- 335
Cdd:PRK10090 165 KIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 336 NAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIV 415
Cdd:PRK10090 245 NPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1741435968 416 LEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
32-462 |
2.26e-63 |
|
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: 214.57 E-value: 2.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 32 LFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELAR 111
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 112 LITLEQGKTLADA-EGDVFRGLQVVEHACSITSLvLGETLPSitkdmdtytyRLPIGVCAGIAPFNFPAMIPLWMFPMGM 190
Cdd:cd07111 104 LESLDNGKPIRESrDCDIPLVARHFYHHAGWAQL-LDTELAG----------WKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 VCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRV 270
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 271 QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVNAGDQPGADVGPL 348
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 349 ISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIV 428
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430
....*....|....*....|....*....|....
gi 1741435968 429 NRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
30-502 |
6.72e-63 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 213.60 E-value: 6.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 30 TKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT--WSETSILTRQQVFLRYQQLIKDNIK 107
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 108 ELARLITLEQGKTLADA-EGDVFRGLQVVEHACSITSLVLGETLPSITKDMdTYTYRLPIGVCAGIAPFNFPAMIPLWMF 186
Cdd:PRK09847 100 ELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHEL-AMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 187 PMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHG-QHAAVNFICDHPAIKAISFVGSNQAG-EYIYERGS 264
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGkQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 265 KNGKRVQSNMGAKNHGVVMPDANKentLNQLVGAA----FGAAGQRCMAlSTAVLVGE--AKNWLPELVERAKNLRVNAG 338
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 339 DQPGADVGPLISPQARDRVNSLIKSGVDEGaKLLLDGRNVKVKGYengnfVGPTIISNVKPDMTCYKEEIFGPVLIVLEA 418
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 419 DSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNV----PIPVPlpmfsFTGSRGSFRG-DTNFYgkqGI 493
Cdd:PRK09847 409 TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---AL 480
|
....*....
gi 1741435968 494 QFYTQIKTI 502
Cdd:PRK09847 481 EKFTELKTI 489
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
35-466 |
6.42e-62 |
|
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: 210.14 E-value: 6.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 35 DGKFVESKTSewIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLIT 114
Cdd:cd07130 4 DGEWGGGGGV--VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 115 LEQGKTLADAEGDVFRGLQVVEHACSITSLVLGETLPSITKD---MDTYTyrlPIGVCAGIAPFNFPAMIPLWMFPMGMV 191
Cdd:cd07130 82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGhrmMEQWN---PLGVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 192 CGNTYLLKPSERVP----GCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNG 267
Cdd:cd07130 159 CGNVVVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 268 KRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKNWLPELVERAKNLRVnaGD--QPGA 343
Cdd:cd07130 239 GRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 344 DVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKvkgyENGNFVGPTIISnVKPDMTCYKEEIFGPVLIVLEADSLDE 423
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEE 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1741435968 424 AIEIVNRNPYGNGTAIFTTNGATARKYshevdVGQIG-----VNVPIP 466
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRW-----LGPKGsdcgiVNVNIG 433
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
68-482 |
1.18e-61 |
|
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: 208.28 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 68 EMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVfrglQVVEHACSITSLVLG 147
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEV----AAMAGKIDISIKAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 148 ETLPSITKDMDTYTYRL---PIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGT 224
Cdd:cd07095 77 ERTGERATPMAQGRAVLrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 225 LNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYER-GSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAA 303
Cdd:cd07095 157 LNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 304 GQRCMALSTAVLVG--EAKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRnvkvK 381
Cdd:cd07095 237 GQRCTCARRLIVPDgaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME----R 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 382 GYENGNFVGPTIIsnvkpDMTCYK----EEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVG 457
Cdd:cd07095 313 LVAGTAFLSPGII-----DVTDAAdvpdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420
....*....|....*....|....*...
gi 1741435968 458 QIGVNVPI---PVPLPmFSFTGSRGSFR 482
Cdd:cd07095 388 IVNWNRPTtgaSSTAP-FGGVGLSGNHR 414
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
50-504 |
2.65e-61 |
|
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: 208.31 E-value: 2.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 50 HNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAegdvf 129
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 130 rglqvvehacsitslVLGETLPSITK---------------------DMDTYTYRL---PIGVCAGIAPFNFP------A 179
Cdd:cd07098 76 ---------------SLGEILVTCEKirwtlkhgekalrpesrpgglLMFYKRARVeyePLGVVGAIVSWNYPfhnllgP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 180 MIPlwmfpmGMVCGNTYLLKPSERVPGCTM----LLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQA 255
Cdd:cd07098 141 IIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 256 GEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNL 333
Cdd:cd07098 215 GKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKiyDKLLEILTDRVQAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 334 RVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPVL 413
Cdd:cd07098 294 RQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 414 IVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN----VPIPVPLPmfsFTGSRGSfrGDTNFYG 489
Cdd:cd07098 374 VVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQQLP---FGGVKGS--GFGRFAG 448
|
490
....*....|....*
gi 1741435968 490 KQGIQFYTQIKTITS 504
Cdd:cd07098 449 EEGLRGLCNPKSVTE 463
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
33-465 |
1.15e-60 |
|
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: 208.20 E-value: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKfvESKTSEWIDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELAR 111
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 112 LITLEQGKTLADAEGDV--------FRGLQVVEhacsitsLVLGETLPSITKDMDTYTYRlPIGVCAGIAPFNFPAMIPL 183
Cdd:cd07125 114 LAAAEAGKTLADADAEVreaidfcrYYAAQARE-------LFSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 184 WMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNII------HGQHaavnfICDHPAIKAISFVGSNQAGE 257
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVpgdgeeIGEA-----LVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 258 YIYE-RGSKNGKRVQSN--MGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKNWLPELVERAKNL 333
Cdd:cd07125 261 LINRaLAERDGPILPLIaeTGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 334 RVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEG---AKLLLDGrnvkvkgyENGNFVGPTIISNVKPDmtCYKEEIFG 410
Cdd:cd07125 341 KVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAwliAPAPLDD--------GNGYFVAPGIIEIVGIF--DLTTEVFG 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1741435968 411 PVLIVL--EADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPI 465
Cdd:cd07125 411 PILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
50-504 |
1.34e-60 |
|
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: 206.39 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 50 HNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVF 129
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 130 RGLQVVEHACSITSLVL-----GETLPSITKdmdTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERV 204
Cdd:cd07101 81 DVAIVARYYARRAERLLkprrrRGAIPVLTR---TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 205 PGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNficdhPAIKA----ISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHG 280
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVG-----GAIVDnadyVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 281 VVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVN 358
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 359 SLIKSGVDEGAKLLLDGRNVKVKG---YEngnfvgPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGN 435
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLGpyfYE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1741435968 436 GTAIFTTNGATARKYSHEVDVGQIGVNVPI-----PVPLPMFSFTGSRGSFRgdtnfYGKQGIQFYTQIKTITS 504
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNEGYaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
47-505 |
6.64e-60 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 206.27 E-value: 6.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DVfrgLQVVehacsITSLVLGETLPSITKD----------MDTYTYRLPIGVCAGIAPFNFPA------MIPLWMfpmgm 190
Cdd:PRK09407 114 EV---LDVA-----LTARYYARRAPKLLAPrrragalpvlTKTTELRQPKGVVGVISPWNYPLtlavsdAIPALL----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 vCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNficdhPAIKA----ISFVGSNQAGEYIYERGskn 266
Cdd:PRK09407 181 -AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVG-----TALVDnadyLMFTGSTATGRVLAEQA--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 267 GKR---VQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKNWLPELVERAKNLRVNAGDQPG 342
Cdd:PRK09407 252 GRRligFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESiYDEFVRAFVAAVRAMRLGAGYDYS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 343 ADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKG---YEngnfvgPTIISNVKPDMTCYKEEIFGPVLIVLEAD 419
Cdd:PRK09407 332 ADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE------PTVLTGVTPDMELAREETFGPVVSVYPVA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 420 SLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPI-----PVPLPM----FSFTGSRgsfrgdtnfYGK 490
Cdd:PRK09407 406 DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYaaawgSVDAPMggmkDSGLGRR---------HGA 476
|
490
....*....|....*
gi 1741435968 491 QGIQFYTQIKTITSQ 505
Cdd:PRK09407 477 EGLLKYTESQTIATQ 491
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
51-507 |
1.74e-59 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 203.55 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 51 NPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFR 130
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 131 GLQV----VEHACSITslvlgETLPSITKDMDTYTYRLPIGVCAGIAPFNFPamipLWMFPMGMV----CGNTYLLKPSE 202
Cdd:PRK13968 93 SANLcdwyAEHGPAML-----KAEPTLVENQQAVIEYRPLGTILAIMPWNFP----LWQVMRGAVpillAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 203 RVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVV 282
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 283 MPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLI 361
Cdd:PRK13968 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 362 KSGVDEGAKLLLDGRnvKVKGyeNGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFT 441
Cdd:PRK13968 324 EATLAEGARLLLGGE--KIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1741435968 442 TNGATARKYSHEVDVGQIGVNvpipvplpMFSFTGSRGSFRG-DTNFYGKQ----GIQFYTQIKTItsqWK 507
Cdd:PRK13968 400 TDETQARQMAARLECGGVFIN--------GYCASDARVAFGGvKKSGFGRElshfGLHEFCNIQTV---WK 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
30-506 |
1.65e-57 |
|
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: 198.87 E-value: 1.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 30 TKLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTT--WSETSILTRQQVFLRYQQLIKDNIK 107
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 108 ELARLITLEQGK--TLAdAEGDVFRGLQVVEHACSITSLVLGETLP----SITKDMdTYTYRLPIGVCAGIAPFNFPAMI 181
Cdd:cd07140 86 ELATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTIPinqaRPNRNL-TLTKREPIGVCGIVIPWNYPLMM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 182 PLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIY 260
Cdd:cd07140 164 LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 261 ERGSK-NGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KNWLPELVERAKNLRVNA 337
Cdd:cd07140 244 KSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 338 GDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIV-- 415
Cdd:cd07140 323 PLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIIsk 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 416 LEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNV--PIPVPLPMFSFTGSrgSFRGDtnfYGKQGI 493
Cdd:cd07140 399 FDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPFGGFKQS--GFGKD---LGEEAL 473
|
490
....*....|...
gi 1741435968 494 QFYTQIKTITSQW 506
Cdd:cd07140 474 NEYLKTKTVTIEY 486
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
30-504 |
1.86e-57 |
|
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: 198.84 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 30 TKLFIDGKFVESKTSEWiDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAY--TTWSETSILtRQQVFLRYQQLIKDNIK 107
Cdd:TIGR04284 1 SRLLIDGKLVAGSAGTF-PTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 108 ELARLITLEQG--KTL---ADAEGDVFRGLQVVEHACSIT-SLVLGETLPSITKDMDTYTyRLPIGVCAGIAPFNFPAMI 181
Cdd:TIGR04284 79 ELRELTIAEVGapRMLtagAQLEGPVDDLGFAADLAESYAwTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 182 PLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLL-QDSGAPDGTLNII-HGQHAAVNFICDHPAIKAISFVGSNQAGEYI 259
Cdd:TIGR04284 158 NLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTATGRAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 260 YERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAVLVGEAKnwLPELVERAK----N 332
Cdd:TIGR04284 238 MADAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVPRAR--YDEAVAAAAatmgS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 333 LRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRnvKVKGYENGNFVGPTIISNVKPDMTCYKEEIFGPV 412
Cdd:TIGR04284 312 IKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGG--RPADRDRGFFVEPTVIAGLDNNARVAREEIFGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 413 LIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPI----PVPlpmfsFTGSRGSfrGDTNFY 488
Cdd:TIGR04284 390 LTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVwysaDAP-----FGGYKQS--GIGREM 462
|
490
....*....|....*.
gi 1741435968 489 GKQGIQFYTQIKTITS 504
Cdd:TIGR04284 463 GVAGFEEYLETKLIAT 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
51-502 |
1.64e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 195.34 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 51 NPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVF- 129
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 130 --RGLQ-VVEHAcsiTSLVLGEtlPSITKDM---DTYTYRLPIGVCAGIAPFNFPamipLWMF-----PMGMVcGNTYLL 198
Cdd:PRK09406 87 caKGFRyYAEHA---EALLADE--PADAAAVgasRAYVRYQPLGVVLAVMPWNFP----LWQVvrfaaPALMA-GNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 199 KPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKN 278
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 279 HGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKNWLPEL-VERAKNLRVNAGDQPGADVGPLISPQARDRV 357
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKfVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 358 NSLIKSGVDEGAKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGT 437
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1741435968 438 AIFTTNGATARKYSHEVDVGQIGVNvPIPVPLPMFSFTGSRGSfrGdtnfYGKQ----GIQFYTQIKTI 502
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
40-462 |
2.98e-55 |
|
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: 193.18 E-value: 2.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 40 ESKTSEWIDIHNP-ATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQG 118
Cdd:cd07083 27 WVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 119 KTLADAEGDVFRGLQVVEHACSITSLVLG--ETLPSITKDMDTYTYRlPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTY 196
Cdd:cd07083 107 KNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 197 LLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSKNG------KR 269
Cdd:cd07083 186 IAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 270 VQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKNWLPELVERAKNLRVNAGDQPGADVGPL 348
Cdd:cd07083 266 LYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEENGTDLGPV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 349 ISPQARDRVNSLIKSGVDEGaKLLLDGRNVKVKGYengnFVGPTIISNVKPDMTCYKEEIFGPVL--IVLEADSLDEAIE 426
Cdd:cd07083 346 IDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQEEIFGPVLsvIRYKDDDFAEALE 420
|
410 420 430
....*....|....*....|....*....|....*.
gi 1741435968 427 IVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07083 421 VANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
33-462 |
2.57e-50 |
|
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: 179.57 E-value: 2.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARL 112
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 113 ITLEQGK----TLAdaeGDVfrgLQVVEHACSITSLVLGE--TLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMF 186
Cdd:cd07116 84 ETWDNGKpvreTLA---ADI---PLAIDHFRYFAGCIRAQegSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 187 PMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSgAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEYIYERGSK 265
Cdd:cd07116 158 APALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAgKPLASSKRIAKVAFTGETTTGRLIMQYASE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 266 NGKRVQSNMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTAvLVGEA--KNWLPELVERAKNLRVNAG 338
Cdd:cd07116 237 NIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA-LIQESiyDRFMERALERVKAIKQGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 339 DQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYENGNFVGPTIISNVKpDMTCYKEEIFGPVLIVLEA 418
Cdd:cd07116 316 LDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1741435968 419 DSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
32-434 |
5.91e-49 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 175.92 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 32 LFIDGKFVESKtSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELAR 111
Cdd:PRK09457 3 LWINGDWIAGQ-GEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 112 LITLEQGKTLADAEGDVfrGLQVVEHACSITSLvlGETLPSITKDMDTYTYRL---PIGVCAGIAPFNFPAMIPLWMFPM 188
Cdd:PRK09457 82 VIARETGKPLWEAATEV--TAMINKIAISIQAY--HERTGEKRSEMADGAAVLrhrPHGVVAVFGPYNFPGHLPNGHIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 189 GMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYER-GSKNG 267
Cdd:PRK09457 158 ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQfAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 268 KRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKN---WLPELVERAKNLRVNAGD-QPGA 343
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQgdaFLARLVAVAKRLTVGRWDaEPQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 344 DVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKvkgyENGNFVGPTII--SNVK--PDmtcykEEIFGPVLIVLEAD 419
Cdd:PRK09457 317 FMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQ----AGTGLLTPGIIdvTGVAelPD-----EEYFGPLLQVVRYD 387
|
410
....*....|....*
gi 1741435968 420 SLDEAIEIVNRNPYG 434
Cdd:PRK09457 388 DFDEAIRLANNTRFG 402
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
31-520 |
3.73e-48 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 173.79 E-value: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 31 KLFIDGKFVESKTSEWIDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLITLEQGKTLADAEGDVFRGLQVVEHACSITSLVLGE-------TLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPL 183
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 184 WMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNqAGEYIyer 262
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD-TGIAI--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 263 gSKNGKRV--QSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAVLVGE--AKNWLPELVERAKNLRVNAG 338
Cdd:PLN00412 253 -SKKAGMVplQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VVLVMEsvADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 339 DQpGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRnvkvkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEA 418
Cdd:PLN00412 331 ED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK-------REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 419 DSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPiPVPLP-MFSFTGSRGSfrgdtnFYGKQGIQFYT 497
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQGITNSI 475
|
490 500
....*....|....*....|...
gi 1741435968 498 QIKTITsqwKAEDATLKSPAVTM 520
Cdd:PLN00412 476 NMMTKV---KSTVINLPKPSYTM 495
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
51-464 |
1.08e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 173.10 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 51 NPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGDVFR 130
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 131 GLQVVEHACSITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVP----G 206
Cdd:PLN02315 120 IIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 207 CTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDA 286
Cdd:PLN02315 200 MTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 287 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSG 364
Cdd:PLN02315 280 DIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEII 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 365 VDEGAKLLLDGRNVKvkgyENGNFVGPTIISnVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNG 444
Cdd:PLN02315 359 KSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNP 433
|
410 420
....*....|....*....|..
gi 1741435968 445 ATARKY--SHEVDVGQIGVNVP 464
Cdd:PLN02315 434 ETIFKWigPLGSDCGIVNVNIP 455
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
47-495 |
2.42e-43 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 159.89 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 47 IDIHNPATNEVIGRVPKATQEEMLAAVDSCSRAYTTWSE-TSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAE 125
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 126 GDVFRGLQVVEHACSITSLVLGETLPsitkdMD---------TYTYRLPIGVCAGIAPFNFPA-MIPLWMFPmGMVCGNT 195
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIP-----MGltpasagriAFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 196 YLLKPSERVPGCTMLLAKLLQDSGAPDGTLN-IIHGQHAAVNFICDhPAIKAISFVGSNQAGEYIYERGSKnGKRVqsnm 274
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GTRC---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 275 gAKNHG-----VVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-VLVGEAKNWLPELVERAKNLRVnaGDQ--PGADVG 346
Cdd:cd07148 229 -ALEHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVfVPAEIADDFAQRLAAAAEKLVV--GDPtdPDTEVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 347 PLISPQARDRVNSLIKSGVDEGAKLLLDGRNVKVKGYEngnfvgPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIE 426
Cdd:cd07148 306 PLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1741435968 427 IVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPIPVPLPMFSFTGSRGSfrGdtnfYGKQGIQF 495
Cdd:cd07148 380 QANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
32-440 |
8.35e-38 |
|
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: 145.81 E-value: 8.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 32 LFIDGKfvESKTSEWIDIHNPAT-NEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELA 110
Cdd:cd07123 35 LVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 111 RLIT-LEQGKTLADAEGDV-------FRglqvveHACSITSLVLGETLPSITKDM-DTYTYRlPI-GVCAGIAPFNFPAM 180
Cdd:cd07123 113 NAATmLGQGKNVWQAEIDAacelidfLR------FNVKYAEELYAQQPLSSPAGVwNRLEYR-PLeGFVYAVSPFNFTAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 181 ------IPLWMfpmgmvcGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSN 253
Cdd:cd07123 186 ggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 254 QAGEYIYergskngKRVQSNM-------------GAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLvgeAK 320
Cdd:cd07123 259 PTFKSLW-------KQIGENLdryrtyprivgetGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYV---PE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 321 NWLPE----LVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLI---KSgvDEGAKLLLDGRNVKVKGYengnFVGPTI 393
Cdd:cd07123 329 SLWPEvkerLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIdhaKS--DPEAEIIAGGKCDDSVGY----FVEPTV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1741435968 394 ISNVKPDMTCYKEEIFGPVLIVL--EADSLDEAIEIVNR-NPYGNGTAIF 440
Cdd:cd07123 403 IETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
49-462 |
1.55e-36 |
|
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: 141.97 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPAT-NEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGD 127
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VFRGLQVVEHACSitslvlgetlpSITKDMDTYTYRlPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGC 207
Cdd:TIGR01238 135 VREAVDFCRYYAK-----------QVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 208 TMLLAKLLQDSGAPDGTLNIIHGQHAAVN-FICDHPAIKAISFVGSNQAGEYI----YERGSKNGKRVqSNMGAKNHGVV 282
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 283 MPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKNWLPELVERA-KNLRVNAGDQPGADVGPLISPQARDRVNSLI 361
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 362 KSgVDEGAKLLLDGRNVKVKGYENGNFVGPTIISnvKPDMTCYKEEIFGPVLIVL--EADSLDEAIEIVNRNPYGNGTAI 439
Cdd:TIGR01238 362 EH-MSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGV 438
|
410 420
....*....|....*....|...
gi 1741435968 440 FTTNGATARKYSHEVDVGQIGVN 462
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVN 461
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
43-462 |
1.02e-35 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 142.26 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 43 TSEWIDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTL 121
Cdd:PRK11904 560 EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 122 ADAEGDV-----FrglqvvehaC------SITSLVLGETLPSITKDMDTYTYRlPIGVCAGIAPFNFPAMIPLWMFPMGM 190
Cdd:PRK11904 640 QDAIAEVreavdF---------CryyaaqARRLFGAPEKLPGPTGESNELRLH-GRGVFVCISPWNFPLAIFLGQVAAAL 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 VCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGS-------NQA-----GE 257
Cdd:PRK11904 710 AAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGStetariiNRTlaardGP 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 258 ---YIYERGSKNGKRVQSNmgaknhgvvmpdANKENTLNQLVGAAFGAAGQRCMALStaVLvgeaknWLPELV-ER---- 329
Cdd:PRK11904 790 ivpLIAETGGQNAMIVDST------------ALPEQVVDDVVTSAFRSAGQRCSALR--VL------FVQEDIaDRviem 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 330 ----AKNLRVnaGD--QPGADVGPLISPQARDRVNSLIKSgVDEGAKLL----LDGrnvkvkGYENGNFVGPTIISnvKP 399
Cdd:PRK11904 850 lkgaMAELKV--GDprLLSTDVGPVIDAEAKANLDAHIER-MKREARLLaqlpLPA------GTENGHFVAPTAFE--ID 918
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1741435968 400 DMTCYKEEIFGPVLIVL--EADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:PRK11904 919 SISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
159-462 |
1.98e-35 |
|
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: 137.27 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 159 TYTYRLPIGVCAGIAPFNFP---AMIPLwmfpMG-MVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGtLNIIHGQHAA 234
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPlqlALAPL----IGaIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 235 VNFIC----DHpaikaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAL 310
Cdd:cd07087 169 ATALLaepfDH-----IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 311 STaVLVgeAKNWLPELVERAKNlRVNA--GDQPG--ADVGPLISPQARDRVNSLIKSGvdegaKLLLDGRnvkvkGYENG 386
Cdd:cd07087 244 DY-VLV--HESIKDELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDG-----KVVIGGQ-----VDKEE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 387 NFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNP-----YgngtaIFTTNGATARKYSHEVDVGQIGV 461
Cdd:cd07087 310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCV 384
|
.
gi 1741435968 462 N 462
Cdd:cd07087 385 N 385
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
158-487 |
3.83e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 137.85 E-value: 3.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 158 DTYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLqDSGAPDGTLNIIHGQHAAVNF 237
Cdd:PTZ00381 102 KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 238 ICDHPaIKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVG 317
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY-VLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 318 EA--KNWLPELVERAKNLrvnAGDQP--GADVGPLISPQARDRVNSLIKsgvDEGAKLLLDGR-NVKVKgyengnFVGPT 392
Cdd:PTZ00381 259 RSikDKFIEALKEAIKEF---FGEDPkkSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEvDIENK------YVAPT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 393 IISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVNVPI----PVP 468
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhllNPN 406
|
330 340
....*....|....*....|...
gi 1741435968 469 LPmfsFTG----SRGSFRGDTNF 487
Cdd:PTZ00381 407 LP---FGGvgnsGMGAYHGKYGF 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
165-462 |
4.89e-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: 127.73 E-value: 4.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 165 PIGVCAGIAPFNFPAMipLWMFPM--GMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDgtlniihgqHAAV------- 235
Cdd:cd07134 100 PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED---------EVAVfegdaev 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 236 -----NFICDHpaikaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAL 310
Cdd:cd07134 169 aqallELPFDH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 311 STaVLVGEAKnwLPELVER-----AKNLRVNAGDQPGADVGPLISPQARDRVNSLIKSGVDEGAKLLLDGRNVkvkgyEN 385
Cdd:cd07134 244 DY-VFVHESV--KDAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AA 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1741435968 386 GNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07134 316 QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
40-462 |
3.94e-31 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 128.52 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 40 ESKTSEWIDIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQG 118
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 119 KTLADAEGDV--------FRGLQVVEHacsitslvlgetlpsitkdMDTYTYRLPIGVCAGIAPFNFPAMIplwmFpMGM 190
Cdd:COG4230 645 KTLPDAIAEVreavdfcrYYAAQARRL-------------------FAAPTVLRGRGVFVCISPWNFPLAI----F-TGQ 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 VC-----GNTYLLKPSERVPgctmLLA----KLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAgeyiy 260
Cdd:COG4230 701 VAaalaaGNTVLAKPAEQTP----LIAaravRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTET----- 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 261 ergsknGKRVQSNMGAKNHGVVMPDAnkEnT--LN-----------QLVG----AAFGAAGQRCMALStaVL-VGE--AK 320
Cdd:COG4230 772 ------ARLINRTLAARDGPIVPLIA--E-TggQNamivdssalpeQVVDdvlaSAFDSAGQRCSALR--VLcVQEdiAD 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 321 NWLPELVERAKNLRVNAGDQPGADVGPLISPQARDRVNSLIksgvdegAKLLLDGRNVKV----KGYENGNFVGPTI--I 394
Cdd:COG4230 841 RVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHI-------ERMRAEGRLVHQlplpEECANGTFVAPTLieI 913
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 395 SNVKpDMtcyKEEIFGPVLIVL--EADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:COG4230 914 DSIS-DL---EREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
49-434 |
4.42e-30 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 125.36 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 49 IHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEGD 127
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 128 VfRglQVVE----HACSITSLVLGetlpsitkdmdtyTYRLPIGVCAGIAPFNFPAMIplwmFpMGMVC-----GNTYLL 198
Cdd:PRK11905 651 V-R--EAVDflryYAAQARRLLNG-------------PGHKPLGPVVCISPWNFPLAI----F-TGQIAaalvaGNTVLA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 199 KPSERVPgctmLLA----KLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGeyiyergskngKRVQSN 273
Cdd:PRK11905 710 KPAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVA-----------RLIQRT 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 274 M--------------GAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRCMALStaVL-VGE--AKNWLPELVERAKN 332
Cdd:PRK11905 775 LakrsgppvpliaetGGQNAMIVDSSALPE----QVVADviasAFDSAGQRCSALR--VLcLQEdvADRVLTMLKGAMDE 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 333 LRVNAGDQPGADVGPLISPQARDRVNSLIksgvdegAKLLLDGRNVKV----KGYENGNFVGPTIISnVK--PDMtcyKE 406
Cdd:PRK11905 849 LRIGDPWRLSTDVGPVIDAEAQANIEAHI-------EAMRAAGRLVHQlplpAETEKGTFVAPTLIE-IDsiSDL---ER 917
|
410 420 430
....*....|....*....|....*....|
gi 1741435968 407 EIFGPVLIVL--EADSLDEAIEIVNRNPYG 434
Cdd:PRK11905 918 EVFGPVLHVVrfKADELDRVIDDINATGYG 947
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
165-441 |
1.64e-29 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 120.79 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 165 PIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQdSGAPDGTLNIIHGQHAAVNFICDHPAI 244
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 245 KaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKnwLP 324
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 325 ELVERAK---NLRVNAGDQPGADVGPLISPQARDRVNSLIKSgvdEGAKLLLDGRNVKVKgyengNFVGPTIISNVKPDM 401
Cdd:cd07135 263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1741435968 402 TCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFT 441
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
48-462 |
8.48e-29 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 121.62 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 48 DIHNPA-TNEVIGRVPKATQEEMLAAVDSCSRAYTTWSETSILTRQQVFLRYQQLIKDNIKELARLITLEQGKTLADAEG 126
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 127 DVfRglQVVE----HACSITSlvlgetlpsitkDMDTYTYRlPIGVCAGIAPFNFPAMIplwmFpMGMVC-----GNTYL 197
Cdd:PRK11809 742 EV-R--EAVDflryYAGQVRD------------DFDNDTHR-PLGPVVCISPWNFPLAI----F-TGQVAaalaaGNSVL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 198 LKPSERVPgctmLLA----KLLQDSGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGSNQAGEY----IYERGSKNGK 268
Cdd:PRK11809 801 AKPAEQTP----LIAaqavRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLlqrnLAGRLDPQGR 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 269 RVQ--SNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKNWLPELVERAKNLRVNAGDQPGADV 345
Cdd:PRK11809 877 PIPliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMGNPDRLSTDI 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 346 GPLISPQARDRVNSLIksgvdegAKLLLDGRNVKVKGYEN------GNFVGPTIISnvKPDMTCYKEEIFGPVLIVL--E 417
Cdd:PRK11809 957 GPVIDAEAKANIERHI-------QAMRAKGRPVFQAARENsedwqsGTFVPPTLIE--LDSFDELKREVFGPVLHVVryN 1027
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1741435968 418 ADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:PRK11809 1028 RNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
160-457 |
1.68e-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: 111.83 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 160 YTYRLPIGVCAGIAPFNFP---AMIPLwmfpMG-MVCGNTYLLKPSERVPGCTMLLAKLLQDSgAPDGTLNIIHGQHAAV 235
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPfqlALAPL----IGaIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 236 NFIC----DHpaikaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlS 311
Cdd:cd07136 170 QELLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-P 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 312 TAVLVGEAK--NWLPELVERAKNLRvnaGDQP--GADVGPLISPQARDRVNSLIKSGvdegaKLLLDGrnvkvKGYENGN 387
Cdd:cd07136 244 DYVLVHESVkeKFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNG-----KIVFGG-----NTDRETL 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1741435968 388 FVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNP-----YgngtaIFTTNGATARKYSHEVDVG 457
Cdd:cd07136 311 YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKKVLENLSFG 380
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
91-417 |
2.62e-26 |
|
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: 111.56 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 91 RQQVFLRYQQLIKDNIKELARLITLEQGKT---LADAEGDV--FRGLQVVEHACSITSLVLGEtlPSITKDMDTYTYRLP 165
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPHEPGNH--LGQGLKQQSHGYRWP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 166 IGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGA-PDGTLNIIHGQHAAVNFICDHPAI 244
Cdd:cd07084 101 YGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKTMQALLLHPNP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 245 KAISFVGSNQAGEYIyeRGSKNGKRVQSNMGAKNHGVVMPDAN-KENTLNQLVGAAFGAAGQRCMALStAVLVGEAKNWL 323
Cdd:cd07084 181 KMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS-MLFVPENWSKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 324 PeLVERAKNLRVNAGDQpGADVGPLISPQARDRVNSLiksGVDEGAKLLLDGRnvKVKGYENGNFVGPTIISNV----KP 399
Cdd:cd07084 258 P-LVEKLKALLARRKLE-DLLLGPVQTFTTLAMIAHM---ENLLGSVLLFSGK--ELKNHSIPSIYGACVASALfvpiDE 330
|
330 340
....*....|....*....|.
gi 1741435968 400 DMTCYK---EEIFGPVLIVLE 417
Cdd:cd07084 331 ILKTYElvtEEIFGPFAIVVE 351
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
165-462 |
2.88e-25 |
|
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: 108.34 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 165 PIGVCAGIAPFNFP---AMIPLwmfpmgmVC----GNTYLLKPSERVPGCTMLLAKLLQDSGAPDgTLNIIHG------Q 231
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL-------IAalaaGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGgadvaaA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 232 HAAVNFicDHpaikaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlS 311
Cdd:cd07133 173 FSSLPF--DH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA-P 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 312 TAVLVGEAKnwLPELVERAKNL------RVNAGDqpgaDVGPLISPQARDRVNSLIKSGVDEGAKLLldgrNVKVKGYEN 385
Cdd:cd07133 245 DYVLVPEDK--LEEFVAAAKAAvakmypTLADNP----DYTSIINERHYARLQGLLEDARAKGARVI----ELNPAGEDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 386 GN--FVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNP-----YgngtaIFTTNGATARKYSHEVDVGQ 458
Cdd:cd07133 315 AAtrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDRVLRRTHSGG 389
|
....
gi 1741435968 459 IGVN 462
Cdd:cd07133 390 VTIN 393
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
165-462 |
2.31e-22 |
|
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: 99.41 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 165 PIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQ---DSGApdgtLNIIHGQHAAVNFICDH 241
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPeylDTKA----IKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 242 PAIKaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTaVLVGEak 320
Cdd:cd07137 177 KWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEE-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 321 NWLPELVERAKN-LRVNAGDQP--GADVGPLISPQARDRVNSLIK-SGVdeGAKLLLDGRNVkvkgyENGNFVGPTIISN 396
Cdd:cd07137 253 SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDdPSV--ADKIVHGGERD-----EKNLYIEPTILLD 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 397 VKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
157-430 |
2.63e-20 |
|
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: 93.44 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 157 MDT-YTYRLPIGVCAGIAPFNFPamIPLWMFPM--GMVCGNTYLLKPSERVPGCTMLLAKLL-----QD------SGAPD 222
Cdd:cd07132 91 LDDvYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEcypvvlGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 223 GTLNIIHgqhaavNFicDHpaikaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGA 302
Cdd:cd07132 169 TTELLKQ------RF--DY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFIN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 303 AGQRCMALSTAVLVGEAKNwlpELVERAKN-LRVNAGDQP--GADVGPLISPQARDRVNSLIKSGvdegaKLLLDGRNVk 379
Cdd:cd07132 236 AGQTCIAPDYVLCTPEVQE---KFVEALKKtLKEFYGEDPkeSPDYGRIINDRHFQRLKKLLSGG-----KVAIGGQTD- 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1741435968 380 vkgyENGNFVGPTIISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNR 430
Cdd:cd07132 307 ----EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINS 353
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
165-516 |
5.06e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 86.64 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 165 PIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDgTLNIIHGQHAAVNFICDHPAI 244
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 245 KaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVVMPDANKENTLNQLVGAAFGAA-GQRCMALSTAVlvgEAKNWL 323
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNnGQACISPDYIL---TTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 324 PELVERAK-NLRVNAGDQP--GADVGPLISPQARDRVNSLIKSGvDEGAKLLLDGRnvkvKGYENGNfVGPTIISNVKPD 400
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGE----KDRENLK-IAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 401 MTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN-VPIPVPLPMFSFTGSRG 479
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
|
330 340 350
....*....|....*....|....*....|....*..
gi 1741435968 480 SFRGdtNFYGKQGIQFYTQIKTITSQWKAEDATLKSP 516
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAVLYRSLFGDSAVRYP 455
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
165-462 |
4.72e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 77.46 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 165 PIGVCAGIAPFNFPamIPLWMFPM--GMVCGNTYLLKPSERVPGCTMLLAKLLQ---DSGApdgtLNIIHGQHAAVNFIC 239
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIPkylDSKA----VKVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 240 DHPAIKaISFVGSNQAGEYIYERGSKNGKRVQSNMGAKNHGVV---MPDANKENTLNQLVGAAFGA-AGQRCMALSTaVL 315
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDY-VL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 316 VGEakNWLPELVERAKN-LRVNAGDQPG--ADVGPLISPQARDRVNSLIKSgvDEGAKLLLDGRNVKvkgyENGNFVGPT 392
Cdd:PLN02203 260 VEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD--PRVAASIVHGGSID----EKKLFIEPT 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 393 IISNVKPDMTCYKEEIFGPVLIVLEADSLDEAIEIVNRNPYGNGTAIFTTNGATARKYSHEVDVGQIGVN 462
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN 401
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
33-443 |
5.84e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 77.15 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 33 FIDGKFVESktSEWIDIHNPATNEVIGRVPKATQEEMLAAVDS---CSRA-----------YTTWSEtsiltrqqVFLRY 98
Cdd:cd07126 2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSlrqCPKSglhnplknperYLLYGD--------VSHRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 99 QQLIKDNIKE--LARLITLEQGKTLADAEGDVFRGLQVVEHAC--SITSLVLGETLPSITKDMDTYTYRLPIGVCAGIAP 174
Cdd:cd07126 72 AHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 175 FNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDGTLNIIHGQHAAVNFICDHPAIKAISFVGSNQ 254
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 255 ageyIYERGSKNGK-RVQSNMGAKNHGVVMPDANKENTLN-QLVGAAFGAAGQRCMALStavLVGEAKNWLPE-LVERAK 331
Cdd:cd07126 232 ----VAERLALELHgKVKLEDAGFDWKILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS---ILFAHENWVQAgILDKLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 332 NLrvnAGDQPGAD--VGPLIS---PQARDRVNSLIKSgvdEGAKLLLDGRNVK------VKG-YENGNFVGP--TIISNV 397
Cdd:cd07126 305 AL---AEQRKLEDltIGPVLTwttERILDHVDKLLAI---PGAKVLFGGKPLTnhsipsIYGaYEPTAVFVPleEIAIEE 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1741435968 398 KPDMTCykEEIFGPVLIVLE--ADSLDEAIEIVNRNPYgNGTAIFTTN 443
Cdd:cd07126 379 NFELVT--TEVFGPFQVVTEykDEQLPLVLEALERMHA-HLTAAVVSN 423
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
71-438 |
4.41e-13 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 71.03 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 71 AAVDSCSRAYTTWSETSILTRQQvFLRyqqLIKDNIK-----------------------ELARliTLEQGKTLADA--E 125
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAA-FLE---AIADEIEalgdelvarahaetglpearlqgELGR--TTGQLRLFADLvrE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 126 GDVFRGlqVVEHAcsitsLVLGETLPSitkdMDTYTYRLPIGVCAGIAPFNFP---------------Amiplwmfpmgm 190
Cdd:cd07129 77 GSWLDA--RIDPA-----DPDRQPLPR----PDLRRMLVPLGPVAVFGASNFPlafsvaggdtasalaA----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 191 vcGNTYLLKPSERVPGCTMLLAKL----LQDSGAPDGTLNIIHGQ-----HAAVnficDHPAIKAISFVGSNQAGEYIYE 261
Cdd:cd07129 135 --GCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGVFSLLQGGgrevgVALV----KHPAIKAVGFTGSRRGGRALFD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 262 RGSK--NGKRVQSNMGAKNHGVVMPDANKEN--TLNQ-LVGAAFGAAGQRCmaLSTAVLVGEAKNWLPELVERAKNLrvn 336
Cdd:cd07129 209 AAAArpEPIPFYAELGSVNPVFILPGALAERgeAIAQgFVGSLTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 337 AGDQPGadvGPLISPQARDRVNslikSGVDE-----GAKLLLDGRnvkvkGYENGNFVGPTIisnVKPDMTCY------K 405
Cdd:cd07129 284 LAAAPA---QTMLTPGIAEAYR----QGVEAlaaapGVRVLAGGA-----AAEGGNQAAPTL---FKVDAAAFladpalQ 348
|
410 420 430
....*....|....*....|....*....|...
gi 1741435968 406 EEIFGPVLIVLEADSLDEAIEIVNRNPyGNGTA 438
Cdd:cd07129 349 EEVFGPASLVVRYDDAAELLAVAEALE-GQLTA 380
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
167-450 |
3.92e-11 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 65.37 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 167 GVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGA-PDGTLNIIHGQhaaVNFICDHPAIK 245
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 246 -AISFVGSNQAGEYIyeRGSKN--GKRVQSNMGAK--NHGVVMPDAnKENT------LNQLVGAAFGAAGQRCMALSTAV 314
Cdd:cd07128 223 dVVAFTGSAATAAKL--RAHPNivARSIRFNAEADslNAAILGPDA-TPGTpefdlfVKEVAREMTVKAGQKCTAIRRAF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 315 L-------VGEAknwlpeLVERAKNLRVnaGD--QPGADVGPLISPQARDRVnsliKSGVD---EGAKLLL---DGRNVK 379
Cdd:cd07128 300 VpearvdaVIEA------LKARLAKVVV--GDprLEGVRMGPLVSREQREDV----RAAVAtllAEAEVVFggpDRFEVV 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1741435968 380 VKGYENGNFVGPTIISNVKPDMT--CYKEEIFGPVLIVLEADSLDEAIEIVNRnpyGNG---TAIFTTNGATARKY 450
Cdd:cd07128 368 GADAEKGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFAREL 440
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
167-430 |
1.03e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 60.87 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 167 GVCAGIAPFNFPAMiPLW-MFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGA-PDGTLNIIHGQHAAvnfICDH-PA 243
Cdd:PRK11903 150 GVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG---LLDHlQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 244 IKAISFVGSNQAGEYIYERGSKNGKRVQSNMGAK--NHGVVMPDANKEntlnqlvGAAFGA------------AGQRCMA 309
Cdd:PRK11903 226 FDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADslNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQKCTA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 310 LSTaVLVGEA--KNWLPELVERAKNLRVNAGDQPGADVGPLISpqaRDRVNSlIKSGVD---EGAKLLLDGRNVKVKGYE 384
Cdd:PRK11903 299 IRR-IFVPEAlyDAVAEALAARLAKTTVGNPRNDGVRMGPLVS---RAQLAA-VRAGLAalrAQAEVLFDGGGFALVDAD 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1741435968 385 N--GNFVGPTIISNVKPD--MTCYKEEIFGPVLIVLEADSLDEAIEIVNR 430
Cdd:PRK11903 374 PavAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALARR 423
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
144-328 |
4.51e-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: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 144 LVLGETLPSitkDMDTYTYRLPIGVCAGIAPFNFPAMIPLWMFpMGMVCGNTYLLKPSERVPGCTMLLAKLLQDSGAPDG 223
Cdd:cd07077 82 HIQDVLLPD---NGETYVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 224 TLNII----HGQHAAVNFICDHPAIKAISFVGSNQAGEYIYERGskNGKRVQSnMGAKNHGVVMPDANKENTLNQLV--G 297
Cdd:cd07077 158 PKILVlyvpHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIG-FGAGNSPVVVDETADEERASGSVhdS 234
|
170 180 190
....*....|....*....|....*....|..
gi 1741435968 298 AAF-GAAgqrCMALSTAVLVGEAKNWLPELVE 328
Cdd:cd07077 235 KFFdQNA---CASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
67-487 |
5.26e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 45.72 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 67 EEMLAAVDSCSRAYTTWSETsilTRQQVFLRYQQLIKDNIKELARLITLEQGKTLAD-------AEGDVFRGLQVVEHAC 139
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQE---MVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 140 SItslvlgetlpsITKDMD--TYTYRLPIGVCAGIAPFNFPAMIPLWMFPMGMVCGNTYLLKPSERVPGCTMLLAKLLQD 217
Cdd:cd07081 79 GV-----------LTGDENggTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 218 ----SGAPDGTLNIIHGQHAAV-NFICDHPAIKAISFVGsnqaGEYIYERGSKNGKRVQSnMGAKNHGVVMPD-ANKENT 291
Cdd:cd07081 148 aavaAGAPENLIGWIDNPSIELaQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVIDEtADIKRA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 292 LNQLVGAAFGAAGQRCMALSTAVLVGEAKNWLPELVER--AKNLRVNAGDQ------PGADVGPLISPQARDRVNSLIKS 363
Cdd:cd07081 223 VQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGqgAYKLTAEELQQvqpvilKNGDVNRDIVGQDAYKIAAAAGL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741435968 364 GVDEGAKLLldgrnvkvkgyengnFVGPTIISNVKPDMTcykeEIFGPVLIVLEADSLDEAIEI----VNRNPYGNGTAI 439
Cdd:cd07081 303 KVPQETRIL---------------IGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAKalalKLEGGCGHTSAM 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1741435968 440 FTTNG---ATARKYSHEVDVGQIGVNVPIPVplpmfSFTGSRGSFRGDTNF 487
Cdd:cd07081 364 YSDNIkaiENMNQFANAMKTSRFVKNGPCSQ-----GGLGDLYNFRGWPSM 409
|
|
| |
