|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
5-494 |
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: 799.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 5 ISHFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDEL 84
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 85 AELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKR 244
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 245 AQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVPVGDqTAERLRARLIERINNLRVGHSLDPKADYGP 324
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGD-EADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDYIGQGVAAGAELVVDGRDRASDDltfglpegdanLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMV 404
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPG-----------YENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 405 RARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDLNQHGPAAIQFY 484
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFY 468
|
490
....*....|
gi 489498938 485 TKVKTVTSRW 494
Cdd:cd07085 469 TQTKTVTSRW 478
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-494 |
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: 602.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 1 MTT-QISHFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVND 79
Cdd:COG1012 1 MTTpEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 80 TIDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLW 159
Cdd:COG1012 81 RREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 160 KAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGA 238
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 239 AATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVPVGDqTAERLRARLIERINNLRVGHSLDP 318
Cdd:COG1012 241 AENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHES-IYDEFVERLVAAAKALKVGDPLDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 319 KADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRdrasddltfglpegDANLEGGFFIGPTLFDHVAAHMSIYTDEIFG 398
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGR--------------RPDGEGGYFVEPTVLADVTPDMRIAREEIFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 399 PVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDlnQHGP 478
Cdd:COG1012 386 PVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGR 463
|
490
....*....|....*.
gi 489498938 479 AAIQFYTKVKTVTSRW 494
Cdd:COG1012 464 EGLEEYTETKTVTIRL 479
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
5-494 |
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: 576.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 5 ISHFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDEL 84
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 85 AELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKR 244
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 245 AQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVPVGDqtAERLRARLIERINNLRVGHSLDPKADYGP 324
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA--ADEWVPEIRERAEKIRIGPGDDPGAEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDYIGQGVAAGAELVVDGRDRASDdltfGLPEGDanleggfFIGPTLFDHVAAHMSIYTDEIFGPVLCMV 404
Cdd:TIGR01722 319 LITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVD----GYEEGN-------WVGPTLLERVPPTMKAYQEEIFGPVLCVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 405 RARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDLNQHGPAAIQFY 484
Cdd:TIGR01722 388 EADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFY 467
|
490
....*....|
gi 489498938 485 TKVKTVTSRW 494
Cdd:TIGR01722 468 TRGKTVTTRW 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
18-490 |
7.22e-173 |
|
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: 495.13 E-value: 7.22e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 18 STRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLA 97
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 98 DARGDVQRGIEVIEFCLGIPHLLKGEYTEGAgPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSE 177
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 178 RDPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMI 256
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 257 VMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRD 336
Cdd:pfam00171 244 VLEDADLDAAVEAAVFGAFGNAGQVCTATSRLL-VHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 337 YIGQGVAAGAELVVDGRdrasddltfglpegdANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLP 416
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGE---------------AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489498938 417 SEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDLNqhGPAAIQFYTKVKTV 490
Cdd:pfam00171 388 NDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-508 |
1.29e-155 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 456.52 E-value: 1.29e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 1 MTTQISHFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDT 80
Cdd:PLN02419 110 MPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 81 IDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWK 160
Cdd:PLN02419 190 MDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 161 AGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAA 240
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 241 TGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVPVGDqtAERLRARLIERINNLRVGHSLDPKA 320
Cdd:PLN02419 350 KGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD--AKSWEDKLVERAKALKVTCGSEPDA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 321 DYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRAsddltfgLPegdaNLEGGFFIGPTLFDHVAAHMSIYTDEIFGPV 400
Cdd:PLN02419 428 DLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIV-------VP----GYEKGNFIGPTILSGVTPDMECYKEEIFGPV 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 401 LCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDLNQHGPAA 480
Cdd:PLN02419 497 LVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAG 576
|
490 500
....*....|....*....|....*...
gi 489498938 481 IQFYTKVKTVTSRWPSgIKDGAEFVIPT 508
Cdd:PLN02419 577 VDFFTQIKLVTQKQKD-IHSPFSLAIPI 603
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
7-490 |
2.33e-144 |
|
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: 422.81 E-value: 2.33e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTrsADVFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07097 3 NYIDGEWVAGGDG--EENRNPsDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPAL 165
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 166 ACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKR 244
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 245 AQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGP 324
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLI-VTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDYIGQGVAAGAELVVDGRDrasddltfgLPEGDanleGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMV 404
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGER---------LKRPD----EGYYLAPALFAGVTNDMRIAREEIFGPVAAVI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 405 RARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIpVPVAYHT-FGGWKRSGFGDLNQhGPAAIQF 483
Cdd:cd07097 387 RVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPT-AGVDYHVpFGGRKGSSYGPREQ-GEAALEF 464
|
....*..
gi 489498938 484 YTKVKTV 490
Cdd:cd07097 465 YTTIKTV 471
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
45-491 |
1.95e-143 |
|
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: 418.92 E-value: 1.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 45 DAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEY 124
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 125 TEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVH 204
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 205 GD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCM 283
Cdd:cd07078 161 GDgDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 284 AIS---VAVPVGDQtaerLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDdl 360
Cdd:cd07078 241 AASrllVHESIYDE----FVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 361 tfglpegdanleGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVS 440
Cdd:cd07078 315 ------------KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAE 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489498938 441 RVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07078 383 RLEAGTVWINDYSVGAEPSAPFGGVKQSGIG--REGGPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
7-491 |
6.92e-133 |
|
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: 393.64 E-value: 6.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRSADVFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPAL 165
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 166 ACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKR 244
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 245 AQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGP 324
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLI-VHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDYIGQGVAAGAELVVDGrDRASDDltfglpegdaNLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMV 404
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGG-ERLTGG----------GYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 405 RARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdLNQHGPAAIQFY 484
Cdd:cd07131 389 EVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG-HREAGTTALDAF 467
|
....*..
gi 489498938 485 TKVKTVT 491
Cdd:cd07131 468 TEWKAVY 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
24-491 |
7.47e-125 |
|
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: 372.15 E-value: 7.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDV 103
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVP 183
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 184 VRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAqCF--GGaknH--MIVM 258
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV-SLelGG---NapFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 259 PDADLDQAVDALIGAGYGSAGERCMA---ISVAVPVgdqtAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVR 335
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCanrIYVHESI----YDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 336 DYIGQGVAAGAELVVDGRDRASddltfglpegdanleGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRL 415
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGL---------------GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIAR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498938 416 PSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVP-IPVPVAyhTFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07103 378 ANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGlISDAEA--PFGGVKESGLG--REGGKEGLEEYLETKYVS 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
24-491 |
9.05e-120 |
|
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: 359.19 E-value: 9.05e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADAR-GD 102
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEF----CLGIPHLlkgeyTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSER 178
Cdd:cd07093 81 IPRAAANFRFfadyILQLDGE-----SYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 179 DPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIV 257
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 258 MPDADLDQAVDALIGAGYGSAGERCMAIS---VAVPVgdqtAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARV 334
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSrilVQRSI----YDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 335 RDYIGQGVAAGAELVVDGRdrasddltfglPEGDANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALR 414
Cdd:cd07093 312 LGYVELARAEGATILTGGG-----------RPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 415 LPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPI----PVPvayhtFGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07093 381 LANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLvrdlRTP-----FGGVKASGIG--REGGDYSLEFYTELKNV 453
|
.
gi 489498938 491 T 491
Cdd:cd07093 454 C 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-490 |
2.44e-116 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 351.88 E-value: 2.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 6 SHFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADAR-GDVQRGIEVIEFCLGIPHLLKGEYTEGAGpGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:PRK13252 88 ALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRG-GSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKR 244
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 245 AQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCM-AISVAVPVGDQtaERLRARLIERINNLRVGHSLDPKADYG 323
Cdd:PRK13252 247 VTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVFVQKSIK--AAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 324 PLVTGAALARVRDYIGQGVAAGAELVVDGRdrasddltfGLPEGdaNLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCM 403
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGGE---------RLTEG--GFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 404 VRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNV----PIPVPVayhtfGGWKRSGFGDLNqhGPA 479
Cdd:PRK13252 394 LTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgesPAEMPV-----GGYKQSGIGREN--GIA 466
|
490
....*....|.
gi 489498938 480 AIQFYTKVKTV 490
Cdd:PRK13252 467 TLEHYTQIKSV 477
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
24-490 |
1.16e-115 |
|
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: 348.91 E-value: 1.16e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDV 103
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCLGIPHLLKGEYTEGAGpGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVP 183
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 184 VRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADL 263
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 264 DQAVDALIGAGYGSAGERCM-AISVAVPVGdqTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGV 342
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSnGTRVFVQRS--IKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 343 AAGAELVVDGrDRASDdltfglpegDANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYG 422
Cdd:cd07090 318 QEGAKVLCGG-ERVVP---------EDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498938 423 NGVAIFTRDGDAARDFVSRVQVGMVGVN----VPIPVPvayhtFGGWKRSGFGDLNqhGPAAIQFYTKVKTV 490
Cdd:cd07090 388 LAAGVFTRDLQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
24-490 |
8.07e-113 |
|
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: 341.45 E-value: 8.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKG--WAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARG 101
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 102 DVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPS 181
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 182 VPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPD 260
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETgEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 261 ADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQ 340
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLL-VQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 341 GVAAGAELVVDGRDRASDDltfglpegdanLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHE 420
Cdd:cd07114 320 AREEGARVLTGGERPSGAD-----------LGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 421 YGNGVAIFTRDGDAARDFVSRVQVGMVGVNvpipvpvAYHT------FGGWKRSGFGDLNqhGPAAIQFYTKVKTV 490
Cdd:cd07114 389 YGLAAGIWTRDLARAHRVARAIEAGTVWVN-------TYRAlspsspFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-491 |
8.97e-112 |
|
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: 339.54 E-value: 8.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRsADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAE 86
Cdd:cd07086 1 GVIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 87 LLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALA 166
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 167 CGNAFVLKPSERDPSVPVRLAELFIEA----GLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATG 242
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADY 322
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-VHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 323 GPLVTGAALARVRDYIGQGVAAGAELVVDGRdRASDDltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLC 402
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGK-RIDGG------------EPGNYVEPTIVTGVTDDARIVQEETFAPILY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 403 MVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSR--VQVGMVGVNVP-----IPVPvayhtFGGWKRSGFGdlNQ 475
Cdd:cd07086 386 VIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPtsgaeIGGA-----FGGEKETGGG--RE 458
|
490
....*....|....*.
gi 489498938 476 HGPAAIQFYTKVKTVT 491
Cdd:cd07086 459 SGSDAWKQYMRRSTCT 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-490 |
1.89e-109 |
|
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: 332.87 E-value: 1.89e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 26 DPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARG-DVQ 104
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 105 RGIEVIEFCLGIPHLLKGEYTEGAGPGIDvYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPV 184
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLN-YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 185 RLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADL 263
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAgAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 264 DQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVA 343
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGS-RLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 344 AGAELVVDGRDRAsddltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGN 423
Cdd:cd07115 321 EGARLLTGGKRPG---------------ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498938 424 GVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAyHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07115 386 AAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPG-SPFGGYKQSGFG--REMGREALDEYTEVKSV 449
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-490 |
4.07e-109 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 332.69 E-value: 4.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALAC 167
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 168 GNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQ 246
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 247 CFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLV 326
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAER-VYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 327 TGAALARVRDYIGQGVAAGAELVVDGRdrasddltfglpegDANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRA 406
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGK--------------RPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 407 RDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPV-AYHTfgGWKRSGF-GDLNQHGpaaIQFY 484
Cdd:cd07088 386 SSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMqGFHA--GWKKSGLgGADGKHG---LEEY 460
|
....*.
gi 489498938 485 TKVKTV 490
Cdd:cd07088 461 LQTKVV 466
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
43-491 |
8.72e-109 |
|
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: 330.26 E-value: 8.72e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 43 DIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKG 122
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 123 EYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDP-SVPVRLAELFIEAGLPAGVFQ 201
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvTGGLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 202 VVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGE 280
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 281 RCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAELVVdgrdrasddl 360
Cdd:cd07104 241 ICMAAG-RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT---------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 361 tfglpEGDANlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVS 440
Cdd:cd07104 310 -----GGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489498938 441 RVQVGMVGVNVPipvPV---AYHTFGGWKRSGFGDLNqhGPAAIQFYTKVKTVT 491
Cdd:cd07104 382 RLETGMVHINDQ---TVndePHVPFGGVKASGGGRFG--GPASLEEFTEWQWIT 430
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
49-491 |
4.35e-107 |
|
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: 323.80 E-value: 4.35e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 49 ASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGA 128
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 129 GPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGD-K 207
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGgD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 208 EAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS- 286
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 287 --VAVPVGDQTAERLRarlierinnlrvghsldpkadygplvtgaalarvrdyigqgvaagaelvvdgrdrasddltfgl 364
Cdd:cd06534 241 llVHESIYDEFVEKLV---------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 365 pegdanleggffigpTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQV 444
Cdd:cd06534 257 ---------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRA 321
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489498938 445 GMVGVNVPIPVPVAYHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd06534 322 GTVYINDSSIGVGPEAPFGGVKNSGIG--REGGPYGLEEYTRTKTVV 366
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
8-490 |
2.09e-106 |
|
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: 326.19 E-value: 2.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA--QKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDvYSLRQPLGVVAGITPFNFPAMIPLWKAGPAL 165
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 166 ACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKR 244
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 245 AQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGP 324
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLL-VEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDYIGQGVAAGAELVVDGRDrasddltfglPEGDAnLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMV 404
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKR----------PTGDE-LAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 405 RARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvpipvpvAYH-TF-----GGWKRSGFGdlNQHGP 478
Cdd:cd07119 388 RFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN-------DYHpYFaeapwGGYKQSGIG--RELGP 458
|
490
....*....|..
gi 489498938 479 AAIQFYTKVKTV 490
Cdd:cd07119 459 TGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-490 |
3.37e-105 |
|
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: 322.24 E-value: 3.37e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA-QKG-WAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADAR 100
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAfESGvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 101 -GDVQRGIEVIEFclgIPHLLKGEYTEGAGPGIDVYSL--RQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSE 177
Cdd:cd07112 85 aVDVPSAANTFRW---YAEAIDKVYGEVAPTGPDALALitREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 178 RDPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYI--YAGaAATGKRAQCFGGAKNH 254
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFgHTAGEALGLHMDVDALAFTGSTEVGRRFleYSG-QSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 255 MIVMPDA-DLDQAVDALIGAGYGSAGERCMAIS---VAVPVgdqtAERLRARLIERINNLRVGHSLDPKADYGPLVTGAA 330
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSrllVHESI----KDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 331 LARVRDYIGQGVAAGAELvVDGRDRASDDltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYE 410
Cdd:cd07112 317 FDKVLGYIESGKAEGARL-VAGGKRVLTE------------TGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 411 EALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN----VPIPVPvayhtFGGWKRSGFG-DLNQHgpaAIQFYT 485
Cdd:cd07112 384 EAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGrDKSLH---ALDKYT 455
|
....*
gi 489498938 486 KVKTV 490
Cdd:cd07112 456 ELKTT 460
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
24-493 |
2.73e-103 |
|
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: 317.01 E-value: 2.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDV 103
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCLGIPHLLKGEyTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVP 183
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 184 VRLAELFIEAgLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDAD 262
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 263 LDQAVDALI-GAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQG 341
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRLF-VHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 342 VAAGAELVVDGrdrasddltfGLPEGDAnLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEY 421
Cdd:cd07107 318 KREGARLVTGG----------GRPEGPA-LEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEY 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 422 GNGVAIFTRDGDAARDFVSRVQVGMVGVNvpipvPVAYH----TFGGWKRSGFGdlNQHGPAAIQFYTKVKTVTSR 493
Cdd:cd07107 387 GLTAAIWTNDISQAHRTARRVEAGYVWIN-----GSSRHflgaPFGGVKNSGIG--REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-491 |
1.32e-102 |
|
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: 315.60 E-value: 1.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAE 86
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 87 LLSREHGKTLADARGD-VQRGIEVIEFCLgipHLLKG-EYTEGAGPGIDVyslRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:cd07138 81 AITLEMGAPITLARAAqVGLGIGHLRAAA---DALKDfEFEERRGNSLVV---REPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGK 243
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 244 R-AQCFGGaKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS-VAVPvgdqtAERLrARLIERI----NNLRVGHSLD 317
Cdd:cd07138 235 RvALELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTrMLVP-----RSRY-AEAEEIAaaaaEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 318 PKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRasddltfglPEGdanLEGGFFIGPTLFDHVAAHMSIYTDEIF 397
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGR---------PEG---LERGYFVKPTVFADVTPDMTIAREEIF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 398 GPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAyhTFGGWKRSGFGdlNQHG 477
Cdd:cd07138 376 GPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQSGNG--REWG 451
|
490
....*....|....
gi 489498938 478 PAAIQFYTKVKTVT 491
Cdd:cd07138 452 RYGLEEFLEVKSIQ 465
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
23-491 |
5.20e-102 |
|
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: 313.50 E-value: 5.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDA 261
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 262 DLDQAVDAligAGYGS---AGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYI 338
Cdd:cd07150 242 DLDYAVRA---AAFGAfmhQGQICMSAS-RIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 339 GQGVAAGAELVVDGRdrasddltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSE 418
Cdd:cd07150 318 EDAVAKGAKLLTGGK------------------YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELAND 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489498938 419 HEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07150 380 TEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG--REGGEWSMEEFTELKWIT 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
24-491 |
5.65e-102 |
|
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: 313.90 E-value: 5.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDV 103
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCLGIPHLLK---GEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDP 180
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDakaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 181 SVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMP 259
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLaAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 260 DADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIG 339
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATS-RLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 340 QGVAAGAELVVDGRDRasddltfglpegdANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEH 419
Cdd:cd07110 320 RGKEEGARLLCGGRRP-------------AHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDS 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498938 420 EYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVpVAYHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIG--RELGEWGLDNYLEVKQIT 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
24-491 |
1.15e-101 |
|
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: 313.02 E-value: 1.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWA-AWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEyTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGE-TIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDA 261
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 262 DLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDpKADYGPLVTGAALARVRDYIGQG 341
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGS-RLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 342 VAAGAELVVDGRdRASDdltfglpegdaNLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEY 421
Cdd:cd07109 318 RARGARIVAGGR-IAEG-----------APAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDY 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489498938 422 GNGVAIFTRDGDAARDFVSRVQVGMVGVNV-----PIPVPvayhtFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07109 386 GLVAGVWTRDGDRALRVARRLRAGQVFVNNygaggGIELP-----FGGVKKSGHG--REKGLEALYNYTQTKTVA 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
8-491 |
7.09e-100 |
|
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: 309.14 E-value: 7.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKG--WAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTL-ADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIdVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:cd07091 87 ALESLDNGKPLeESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFL-AYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATG- 242
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADY 322
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS-RIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 323 GPLVTGAALARVRDYIGQGVAAGAELVVDGrDRASDDltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLC 402
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGG-ERHGSK--------------GYFIQPTVFTDVKDDMKIAKEEIFGPVVT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 403 MVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN------VPIPvpvayhtFGGWKRSGFG-DLnq 475
Cdd:cd07091 390 ILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvfdAAVP-------FGGFKQSGFGrEL-- 460
|
490
....*....|....*.
gi 489498938 476 hGPAAIQFYTKVKTVT 491
Cdd:cd07091 461 -GEEGLEEYTQVKAVT 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-494 |
1.01e-99 |
|
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: 308.60 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKG-WAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADARG-DVQRGIEVIEFCLGIPHLLKGEYTEGAGPGID-----VYSLRQPLGVVAGITPFNFPAMIPLW 159
Cdd:cd07113 82 QLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQgerytAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 160 KAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAA 239
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 240 ATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMA---ISVAVPVGDQTAERLRARLIErinnLRVGHSL 316
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAperFYVHRSKFDELVTKLKQALSS----FQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 317 DPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDdltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEI 396
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE---------------GYFVQPTLVLARSADSRLMREET 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 397 FGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVpipvpvayHT-------FGGWKRSG 469
Cdd:cd07113 383 FGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNM--------HTfldpavpFGGMKQSG 454
|
490 500
....*....|....*....|....*
gi 489498938 470 FGdlNQHGPAAIQFYTKVKTVTSRW 494
Cdd:cd07113 455 IG--REFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
8-491 |
1.17e-99 |
|
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: 308.35 E-value: 1.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA--QKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADAR-GDVQRGIEVIEFCLGI-PHLLKGEYTEGAGPGiDVYSLRQPLGVVAGITPFNFPAMIPLWKAGP 163
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALaRDFPFEERRPGSGGG-HVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 164 ALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGK 243
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 244 RAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS-VAVPvgDQTAERLRARLIERINNLRVGHSLDPKADY 322
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTrILVP--RSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 323 GPLVTGAALARVRDYIGQGVAAGAELVVDGrdrasddltfGLPEGdanLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLC 402
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGG----------GRPAG---LDRGWFVEPTLFADVDNDMRIAQEEIFGPVLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 403 MVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAyhTFGGWKRSGFGdlNQHGPAAIQ 482
Cdd:cd07139 386 VIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA--PFGGFKQSGIG--REGGPEGLD 461
|
....*....
gi 489498938 483 FYTKVKTVT 491
Cdd:cd07139 462 AYLETKSIY 470
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-491 |
3.02e-99 |
|
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: 306.92 E-value: 3.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 11 GQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSR 90
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 91 EHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNA 170
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 171 FVLKPSERDPSVP-VRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCF 248
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAgSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 249 GGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS---VAVPVGDQTAErlraRLIERINNLRVGHSLDPKADYGPL 325
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINriiVHEDVYDEFVE----KFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 326 VTGAALARVRDYIGQGVAAGAELVVdgrdrasddltfglpEGDANlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVR 405
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLV---------------GGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 406 ARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvPIPVPVAYHT-FGGWKRSGFGDLNqhGPAAIQFY 484
Cdd:cd07151 379 ADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNDEPHVpFGGEKNSGLGRFN--GEWALEEF 455
|
....*..
gi 489498938 485 TKVKTVT 491
Cdd:cd07151 456 TTDKWIS 462
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-490 |
8.52e-98 |
|
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: 303.95 E-value: 8.52e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWaaWN---PQRRARVLMRFIELVNDTIDEL 84
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESW--WSkvtGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 85 AELLSREHGKTL-ADARGDVQRGIEVIEFCLGIPHLLKGEyTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGP 163
Cdd:cd07144 89 AAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGK-TIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 164 ALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATG 242
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVD-ALIGAGYGSaGERCMAIS---VAVPVGDQTAERLRARLIErinNLRVGHSLDP 318
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKwAAAGIMYNS-GQNCTATSriyVQESIYDKFVEKFVEHVKQ---NYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 319 KADYGPLVTGAALARVRDYIGQGVAAGAELVVDGrdrasddltFGLPEGdanLEGGFFIGPTLFDHVAAHMSIYTDEIFG 398
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGG---------EKAPEG---LGKGYFIPPTIFTDVPQDMRIVKEEIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 399 PVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVP----IPVPvayhtFGGWKRSGFGdlN 474
Cdd:cd07144 392 PVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIG--R 464
|
490
....*....|....*.
gi 489498938 475 QHGPAAIQFYTKVKTV 490
Cdd:cd07144 465 ELGEYGLETYTQTKAV 480
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
8-471 |
3.37e-97 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 302.76 E-value: 3.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFP-AMIpLWKAGPALA 166
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMI-TRKVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 167 CGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRA 245
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 246 QCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPL 325
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCAN-RILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 326 VTGAALARVRDYIGQGVAAGAELVVDGRdRASDdltfglpegdanleGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVR 405
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGK-RHSL--------------GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTR 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 406 ARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIpVPVAYHTFGGWKRSGFG 471
Cdd:PLN02278 411 FKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLG 475
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-491 |
4.28e-96 |
|
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: 298.48 E-value: 4.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 27 PNTGQIQAKVPMAGKSDIDAAVASAVEA-QKGWAAWNP-QRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQ 104
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAfDKGPWPRMSgAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 105 RGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPV 184
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 185 RLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADL 263
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 264 DQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVA 343
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 344 AGAELVVDGrDRASDdltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGN 423
Cdd:cd07118 323 EGATLLLGG-ERLAS-------------AAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498938 424 GVAIFTRDGDAARDFVSRVQVGMVGVNVPI----PVPvayhtFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07118 389 SAGVWSKDIDTALTVARRIRAGTVWVNTFLdgspELP-----FGGFKQSGIG--RELGRYGVEEYTELKTVH 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
22-471 |
2.65e-95 |
|
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: 296.57 E-value: 2.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 22 ADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARG 101
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 102 DVQRGIEVIEFCLGIPHLLKGEY-----TEGAGPGIdVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPS 176
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETipvdaYEYNERRI-AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 177 ERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHM 255
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 256 IVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVR 335
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVK-RILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 336 DYIGQGVAAGAELVVDGRDrasddltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRL 415
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKR-----------------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEI 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 416 PSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFG 471
Cdd:cd07145 382 ANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
23-491 |
6.34e-95 |
|
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: 295.50 E-value: 6.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGE------YTEGAGPGIdvYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPS 176
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEeipldaTQGSDNRLA--WTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 177 ERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIyaGAAATGKRAQCFGGAKNHM 255
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 256 IVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVR 335
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIY-VHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 336 DYIGQGVAAGAELVVDGRdrasddltfglpegdanLEGGFFiGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRL 415
Cdd:cd07094 317 RWVEEAVEAGARLLCGGE-----------------RDGALF-KPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRI 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498938 416 PSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdlnQHG-PAAIQFYTKVKTVT 491
Cdd:cd07094 379 ANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVG---REGvPYAMEEMTEEKTVV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
24-491 |
8.71e-95 |
|
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: 295.42 E-value: 8.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTL-ADARGD 102
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEyTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAELFIEAgLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAatGKRAQC---FGGaKNHMIVM 258
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA--DRLIPVsleLGG-KSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 259 PDADLDQAVDALI-GAGYGSAGERCMAIS---VAVPVGDQTAERLRARLieriNNLRVGHSLDPKADYGPLVTGAALARV 334
Cdd:cd07108 236 PDADLDDAVDGAIaGMRFTRQGQSCTAGSrlfVHEDIYDAFLEKLVAKL----SKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 335 RDYIGQGVAAGAELVVDGrdrasddltfGLPEGDANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALR 414
Cdd:cd07108 312 CGYIDLGLSTSGATVLRG----------GPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 415 LPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIpVPVAYHTFGGWKRSGFG---DLNqhgpAAIQFYTKVKTVT 491
Cdd:cd07108 382 MANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGreaSLE----GMLEHFTQKKTVN 456
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
24-491 |
1.43e-93 |
|
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: 291.96 E-value: 1.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAwnpQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDV 103
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRSTLTR---YQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCLGIPHLLKGE-----YTEGAGPGIdVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSER 178
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGEsfscdLTANGKARK-IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 179 DPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIyagAAATGKRAQCFG-GAKNHMI 256
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLElGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 257 VMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRD 336
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVK-RILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 337 YIGQGVAAGAELVVDGRDRasddltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLP 416
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ------------------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAIS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 417 SEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN-VP------IPvpvayhtFGGWKRSGFGdLNQHGPAAIQFYTKVKT 489
Cdd:cd07146 377 NSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNeVPgfrselSP-------FGGVKDSGLG-GKEGVREAMKEMTNVKT 448
|
..
gi 489498938 490 VT 491
Cdd:cd07146 449 YS 450
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
23-491 |
1.83e-93 |
|
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: 291.81 E-value: 1.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGE-YTEGAGPGID---VYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSER 178
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGEtIPFDASPGGEgriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 179 DPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAAtgKRAQCFGGAKNHMIV 257
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 258 MPDADLDQAVDALIGAGYGSAGERCmaISVA-VPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRD 336
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVC--ISVQrIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 337 YIGQGVAAGAELVVDGRdrasddltfglpegdanLEGGFFIgPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLP 416
Cdd:cd07149 318 WVEEAVEGGARLLTGGK-----------------RDGAILE-PTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 417 SEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdlnQHGPA-AIQFYTKVKTVT 491
Cdd:cd07149 380 NDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTG---REGPRyAIEEMTEIKLVC 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
28-494 |
2.39e-93 |
|
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: 293.36 E-value: 2.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 28 NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGI 107
Cdd:cd07124 55 DPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 108 EVIEFCLGIPHLLKGEYTEGAgPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLA 187
Cdd:cd07124 135 DFLEYYAREMLRLRGFPVEMV-PGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 188 ELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATG------KRAQCFGGAKNHMIVMPD 260
Cdd:cd07124 214 EILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQpgqkwlKRVIAEMGGKNAIIVDED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 261 ADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQ 340
Cdd:cd07124 294 ADLDEAAEGIVRSAFGFQGQKCSACSRVI-VHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 341 GVAAGaELVVDGrdrasddltfglpEGDANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHE 420
Cdd:cd07124 373 GKSEG-RLLLGG-------------EVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489498938 421 YGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIP-VPVAYHTFGGWKRSGFGDLNQhGPAAIQFYTKVKTVTSRW 494
Cdd:cd07124 439 YGLTGGVFSRSPEHLERARREFEVGNLYANRKITgALVGRQPFGGFKMSGTGSKAG-GPDYLLQFMQPKTVTENF 512
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
24-490 |
2.82e-93 |
|
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: 290.97 E-value: 2.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDV 103
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCLGIPhlLKGEYTEgAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVP 183
Cdd:cd07106 81 GGAVAWLRYTASLD--LPDEVIE-DDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 184 VRLAELFIEAgLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADL 263
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 264 DQAVDALIGAGYGSAGERCMAIS-VAVPvgDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGV 342
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKrLYVH--ESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 343 AAGAELVVDGRdrasddltfgLPEGDanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYG 422
Cdd:cd07106 315 AKGAKVLAGGE----------PLDGP-----GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYG 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498938 423 NGVAIFTRDGDAARDFVSRVQVGMVGVN----VPIPVPvayhtFGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07106 380 LGASVWSSDLERAEAVARRLEAGTVWINthgaLDPDAP-----FGGHKQSGIG--VEFGIEGLKEYTQTQVI 444
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
24-492 |
8.43e-93 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 290.00 E-value: 8.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD- 102
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLG----IPHLLKGEYTegagPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSER 178
Cdd:cd07092 81 LPGAVDNFRFFAGaartLEGPAAGEYL----PGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 179 DPSVPVRLAELfIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIV 257
Cdd:cd07092 157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 258 MPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDY 337
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAAC-RVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 338 IgQGVAAGAELVVDGRdrasddltfgLPEGDanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPS 417
Cdd:cd07092 315 V-ERAPAHARVLTGGR----------RAEGP-----GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELAN 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 418 EHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVpVAYHTFGGWKRSGFG-DLnqhGPAAIQFYTKVKTVTS 492
Cdd:cd07092 379 DVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPL-AAEMPHGGFKQSGYGkDL---SIYALEDYTRIKHVMV 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
24-490 |
5.15e-91 |
|
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: 285.68 E-value: 5.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAaW--NPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARG 101
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGD-WstDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 102 -DVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSL----RQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPS 176
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 177 ERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHM 255
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALtTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 256 IVMPDADLDQAVDALIGAGYGSAGERCMAIS-VAVP--VGDQTAERLRArlieRINNLRVGHSLDPKADYGPLVTGAALA 332
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTrLLVPrsRYDEVVEALAA----AFEALPVGDPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 333 RVRDYIGQGVAAGAELVVDGrdrasddltfGLPEGdanLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEA 412
Cdd:cd07089 316 RVEGYIARGRDEGARLVTGG----------GRPAG---LDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489498938 413 LRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPvAYHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07089 383 VRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYG-PDAPFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-490 |
1.77e-90 |
|
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: 284.46 E-value: 1.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGqSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNP-QRRARVLMRFIELVNDTIDELAE 86
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 87 LLSREHGKTLADARGDVQRGIEVIEFCLG-----IPHLLKGEYTEGAGPGIDVYSlRQPLGVVAGITPFNFPAMIPLWKA 161
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEelkrlDGDSLPGDWFPGTKGKIAQVR-REPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 162 GPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIyaGAAA 240
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRL--KKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 241 TGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLDPKA 320
Cdd:cd07082 241 PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 321 DYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDrasddltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPV 400
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR-----------------EGGNLIYPTLLDPVTPDMRLAWEEPFGPV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 401 LCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDLNQHgpAA 480
Cdd:cd07082 383 LPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIG--DA 460
|
490
....*....|
gi 489498938 481 IQFYTKVKTV 490
Cdd:cd07082 461 LRSMTRRKGI 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
30-491 |
8.40e-88 |
|
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: 276.87 E-value: 8.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 30 GQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEV 109
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 110 IEFCLGIPHLLKGEyTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDP-SVPVRLAE 188
Cdd:cd07152 81 LHEAAGLPTQPQGE-ILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvSGGVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 189 LFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVD 268
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 269 ALIGAGYGSAGERCMAiSVAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAEL 348
Cdd:cd07152 240 NGAWGAFLHQGQICMA-AGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 349 VVDGRDRasddltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIF 428
Cdd:cd07152 319 EAGGTYD------------------GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGII 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489498938 429 TRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGDlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07152 381 SRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGASGNGS-RFGGPANWEEFTQWQWVT 442
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
44-490 |
3.43e-87 |
|
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: 274.72 E-value: 3.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 44 IDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEF-CLGIPHLLKG 122
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 123 EYTEGAGPgiDVYSLRQPLGVVAGITPFNFPamipLWK----AGPALACGNAFVLKPSerdPSVP---VRLAELFIEAGL 195
Cdd:cd07100 81 EPIETDAG--KAYVRYEPLGVVLGIMPWNFP----FWQvfrfAAPNLMAGNTVLLKHA---SNVPgcaLAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 196 PAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQC-FGGAkNHMIVMPDADLDQAVDALIGAG 274
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLeLGGS-DPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 275 YGSAGERCMA----IsvavpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAELVV 350
Cdd:cd07100 231 LQNAGQSCIAakrfI-----VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 351 DGrdrasddltfGLPEGDanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTR 430
Cdd:cd07100 306 GG----------KRPDGP-----GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTT 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 431 DGDAARDFVSRVQVGMVGVNVP------IPvpvayhtFGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07100 371 DLERAERVARRLEAGMVFINGMvksdprLP-------FGGVKRSGYG--RELGRFGIREFVNIKTV 427
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
26-491 |
7.81e-87 |
|
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: 274.48 E-value: 7.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 26 DPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQR 105
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 106 GIEVIEF-CLGIPHLLKGEYTEG--AGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:cd07099 82 ALEAIDWaARNAPRVLAPRKVPTglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPdIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDAD 262
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 263 LDQAVDALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGV 342
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVER-VYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 343 AAGAELVVDGRDRASddltfglpegdanleGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYG 422
Cdd:cd07099 320 AKGAKALTGGARSNG---------------GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489498938 423 NGVAIFTRDGDAARDFVSRVQVGMVGVN-----VPIP-VPvayhtFGGWKRSGFGdlNQHGPAAIQFYTKVKTVT 491
Cdd:cd07099 385 LSASVFSRDLARAEAIARRLEAGAVSINdvlltAGIPaLP-----FGGVKDSGGG--RRHGAEGLREFCRPKAIA 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-494 |
1.19e-86 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 274.86 E-value: 1.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 1 MTTQIshFIDGQRTAGQSTRSaDVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDT 80
Cdd:PRK13473 1 MQTKL--LINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 81 IDELAELLSREHGKTLADARGD-VQRGIEVIEFCLGIPHLLKG----EYTEGAGPGIDvyslRQPLGVVAGITPFNFPAM 155
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGkaagEYLEGHTSMIR----RDPVGVVASIAPWNYPLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 156 IPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAgLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYI 234
Cdd:PRK13473 154 MAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 235 YAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGH 314
Cdd:PRK13473 233 LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY-AQRGIYDDLVAKLAAAVATLKVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 315 SLDPKADYGPLVTGAALARVRDYIGQGVAAG-AELVVDGRDrasddltfglPEGDanlegGFFIGPTLFDHVAAHMSIYT 393
Cdd:PRK13473 312 PDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEA----------PDGK-----GYYYEPTLLAGARQDDEIVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 394 DEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVpVAYHTFGGWKRSGFG-D 472
Cdd:PRK13473 377 REVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFML-VSEMPHGGQKQSGYGkD 455
|
490 500
....*....|....*....|..
gi 489498938 473 LNQHGpaaIQFYTKVKTVTSRW 494
Cdd:PRK13473 456 MSLYG---LEDYTVVRHVMVKH 474
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
13-494 |
3.82e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 269.83 E-value: 3.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 13 RTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREH 92
Cdd:PRK09407 25 RVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 93 GKtladARGDVQRgiEVIEFCLG-------IPHLLKGEYTEGAGPGI-DVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:PRK09407 105 GK----ARRHAFE--EVLDVALTaryyarrAPKLLAPRRRAGALPVLtKTTELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIkaVGFVGSSDIAQYIyagAAATGK 243
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVL---AEQAGR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 244 RAQCFG---GAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKA 320
Cdd:PRK09407 254 RLIGFSlelGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIE-RIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 321 DYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRAsdDLtfglpegdanleGGFFIGPTLFDHVAAHMSIYTDEIFGPV 400
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARP--DL------------GPLFYEPTVLTGVTPDMELAREETFGPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 401 LCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN---------VPIPVpvayhtfGGWKRSGFG 471
Cdd:PRK09407 399 VSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaawgsVDAPM-------GGMKDSGLG 471
|
490 500
....*....|....*....|....
gi 489498938 472 dlNQHGPAAIQFYTKVKTV-TSRW 494
Cdd:PRK09407 472 --RRHGAEGLLKYTESQTIaTQRV 493
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-490 |
8.01e-84 |
|
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: 267.44 E-value: 8.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA--QKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADAR-GDVQRGIEVIEFCLGIPHLLKGEYTEGAGPgIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATG- 242
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS---VAVPVGDQTAERLRARLIERInnlrVGHSLDPK 319
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSrtfVHESIYDEFVEKAKARALKRV----VGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 320 ADYGPLVTGAALARVRDYIGQGVAAGAELVVDGrDRASDDltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFGP 399
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGG-DRIGSK--------------GYYIQPTIFSDVKDDMKIARDEIFGP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 400 VLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN------VPIPvpvayhtFGGWKRSGFGdl 473
Cdd:cd07142 387 VQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfdASIP-------FGGYKMSGIG-- 457
|
490
....*....|....*..
gi 489498938 474 NQHGPAAIQFYTKVKTV 490
Cdd:cd07142 458 REKGIYALNNYLQVKAV 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
7-471 |
9.46e-84 |
|
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: 267.34 E-value: 9.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAE 86
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 87 LLSREHGKTLADAR-GDVQRGIEVIEFCLGIPHLLKgeyTEGAGPgidvyslrQPLGVVAGITPFNFPAMIPLWKAGPAL 165
Cdd:cd07111 104 LESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLD---TELAGW--------KPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 166 ACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRA 245
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 246 QCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPL 325
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 326 VTGAALARVRDYIGQGVAAGAELVVDGRDRASDdltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVR 405
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSK---------------GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLT 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489498938 406 ARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN--------VPipvpvayhtFGGWKRSGFG 471
Cdd:cd07111 397 FRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfdaaAG---------FGGYRESGFG 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-491 |
1.06e-83 |
|
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: 267.29 E-value: 1.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 3 TQIshFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAW---NPQRRARVLMRFIELVND 79
Cdd:cd07141 7 TKI--FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWrtmDASERGRLLNKLADLIER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 80 TIDELAELLSREHGKTLADAR-GDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIdVYSLRQPLGVVAGITPFNFPAMIPL 158
Cdd:cd07141 85 DRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFF-TYTRHEPVGVCGQIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 159 WKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAG 237
Cdd:cd07141 164 WKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 238 AAATG-KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSL 316
Cdd:cd07141 244 AGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGS-RTFVQESIYDEFVKRSVERAKKRVVGNPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 317 DPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGrDRASDDltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEI 396
Cdd:cd07141 323 DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGG-KRHGDK--------------GYFIQPTVFSDVTDDMRIAKEEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 397 FGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvpIPVPVAYHT-FGGWKRSGFGdlNQ 475
Cdd:cd07141 388 FGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQApFGGYKMSGNG--RE 463
|
490
....*....|....*.
gi 489498938 476 HGPAAIQFYTKVKTVT 491
Cdd:cd07141 464 LGEYGLQEYTEVKTVT 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
8-490 |
1.97e-83 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 266.70 E-value: 1.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWN--PQRRARVLMRFIELVNDTIDELA 85
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKvsGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKT-LADARGDVQRGIEVIEFCLGIPHLLKGEYTEgAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIE-TDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAAATG- 242
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNl 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADY 322
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGS-RIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 323 GPLVTGAALARVRDYIGQGVAAGAELVVDGrDRASDDltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLC 402
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGG-KRHGNE--------------GYFIEPTIFTDVTEDMKIVKEEIFGPVVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 403 MVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN----VPIPVPvayhtFGGWKRSGFGdlNQHGP 478
Cdd:cd07143 393 VIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELGE 465
|
490
....*....|..
gi 489498938 479 AAIQFYTKVKTV 490
Cdd:cd07143 466 YALENYTQIKAV 477
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
25-492 |
1.11e-82 |
|
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: 263.79 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 25 FDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQ 104
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 105 RGIEVIEFCL-GIPHLLKGEYTEGAGPGI-DVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:cd07101 81 DVAIVARYYArRAERLLKPRRRRGAIPVLtRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIkaVGFVGSSDIAQYIYAGAAA--TGKRAQCfgGAKNHMIVMP 259
Cdd:cd07101 161 ALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRrlIGCSLEL--GGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 260 DADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIG 339
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIE-RIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 340 QGVAAGAELVVDGRDRAsdDLtfglpegdanleGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEH 419
Cdd:cd07101 316 DAVAKGATVLAGGRARP--DL------------GPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 420 EYGNGVAIFTRDGDAARDFVSRVQVGMVGVN-------VPIPVPVayhtfGGWKRSGFGdlNQHGPAAIQFYTKVKTVTS 492
Cdd:cd07101 382 DYGLNASVWTRDGARGRRIAARLRAGTVNVNegyaaawASIDAPM-----GGMKDSGLG--RRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
25-491 |
8.07e-82 |
|
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: 261.51 E-value: 8.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 25 FDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGwAAW--NPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDE-TDWahDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEYTEgagPGIDVYS--LRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDP 180
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIE---PEPGSFSlvLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 181 SVPVRLAELFIEA-GLPAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVM 258
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLvASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 259 PDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYI 338
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGS-RVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 339 GQGVAAGAELVVDGRdrasddltfGLPEGdanLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSE 418
Cdd:cd07120 317 ERAIAAGAEVVLRGG---------PVTEG---LAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALAND 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489498938 419 HEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVpVAYHTFGGWKRSGFGDLnqHGPAAIQFYTKVKTVT 491
Cdd:cd07120 385 TDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRL--HGVAALEDFIEYKHIY 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-488 |
3.98e-81 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 260.35 E-value: 3.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARG-DVQRGIEVIEFCLGIphlLKGEytEGAGPGID----VYSLRQPLGVVAGITPFNFPAMIPLWKAG 162
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFAGV---IRAQ--EGSLSEIDedtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 163 PALACGNAFVLKPSERDPSVPVRLAELFIEAgLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAAT 241
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 242 GKRAQCFGGAKNHMIVMPDA--DLDQAVDALIGAGYGSA---GERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSL 316
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdADDDFDDKAEEGQLGFAfnqGEVCTCPSRAL-VQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 317 DPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDDLtfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEI 396
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGL-----------DKGYFYEPTLIKGGNNDMRIFQEEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 397 FGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPvAYHTFGGWKRSGFGDLNQH 476
Cdd:cd07559 386 FGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKSGIGRETHK 464
|
490
....*....|..
gi 489498938 477 GpaAIQFYTKVK 488
Cdd:cd07559 465 M--MLDHYQQTK 474
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
43-491 |
6.51e-81 |
|
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: 258.28 E-value: 6.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 43 DIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKG 122
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 123 EYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQV 202
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 203 VHGDKE----AVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSA 278
Cdd:cd07105 161 VTHSPEdapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 279 GERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDpkadyGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASD 358
Cdd:cd07105 241 GQICMSTE-RIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGGLADESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 359 DLTFglpegdanleggffIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDF 438
Cdd:cd07105 315 SGTS--------------MPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAV 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 439 VSRVQVGMVGVNVP-------IPvpvayhtFGGWKRSGFGDLNqhGPAAIQFYTKVKTVT 491
Cdd:cd07105 381 AKRIESGAVHINGMtvhdeptLP-------HGGVKSSGYGRFN--GKWGIDEFTETKWIT 431
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
8-490 |
1.66e-78 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 254.36 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA--QKGWAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADARG-DVQRGIEVIEFCLGIPHLLKGEYTEGAGPgIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPA 164
Cdd:PLN02766 104 ALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 165 LACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATG- 242
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADY 322
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASS-RVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 323 GPLVTGAALARVRDYIGQGVAAGAELvvdgrdrasddLTFGLPEGDAnlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLC 402
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATL-----------LTGGKPCGDK----GYYIEPTIFTDVTEDMKIAQDEIFGPVMS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 403 MVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvpipvpvAYHTF------GGWKRSGFGdlNQH 476
Cdd:PLN02766 407 LMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN-------CYFAFdpdcpfGGYKMSGFG--RDQ 477
|
490
....*....|....
gi 489498938 477 GPAAIQFYTKVKTV 490
Cdd:PLN02766 478 GMDALDKYLQVKSV 491
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
2-491 |
4.29e-78 |
|
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: 252.80 E-value: 4.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 2 TTQISH--FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKG--WAAWNPQRRARVLMRFIELV 77
Cdd:cd07140 1 TLKMPHqlFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 78 NDTIDELAELLSREHGK--TLAdARGDVQRGIEVIEFCLGIPHLLKGEY--TEGAGPGIDV-YSLRQPLGVVAGITPFNF 152
Cdd:cd07140 81 EEHQEELATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTipINQARPNRNLtLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 153 PAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIA 231
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 232 QYIYAGAAATG-KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNL 310
Cdd:cd07140 240 KHIMKSCAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAG-RLFVEESIHDEFVRRVVEEVKKM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 311 RVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGR--DRAsddltfglpegdanlegGFFIGPTLFDHVAAH 388
Cdd:cd07140 319 KIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKqvDRP-----------------GFFFEPTVFTDVEDH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 389 MSIYTDEIFGPVLCMVRAR--DYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAyHTFGGWK 466
Cdd:cd07140 382 MFIAKEESFGPIMIISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFK 460
|
490 500
....*....|....*....|....*.
gi 489498938 467 RSGFG-DLnqhGPAAIQFYTKVKTVT 491
Cdd:cd07140 461 QSGFGkDL---GEEALNEYLKTKTVT 483
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-491 |
6.71e-78 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 252.73 E-value: 6.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA-----QKGWAAWNPQRRARVLMRFIELVNDTID 82
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 83 ELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGID---VYSLRQPLGVVAGITPFNFPAMIPLW 159
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMEtfkGYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 160 KAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGA 238
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 239 AATGKRAQCFGGAKNHMIVMPDADLDQAVD-ALIGAgYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLD 317
Cdd:PLN02467 251 AQMVKPVSLELGGKSPIIVFDDVDLDKAVEwAMFGC-FWTNGQICSATS-RLLVHERIASEFLEKLVKWAKNIKISDPLE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 318 PKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGrdrasddltfGLPEGdanLEGGFFIGPTLFDHVAAHMSIYTDEIF 397
Cdd:PLN02467 329 EGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG----------KRPEH---LKKGFFIEPTIITDVTTSMQIWREEVF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 398 GPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVpVAYHTFGGWKRSGFG-DLNQH 476
Cdd:PLN02467 396 GPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFGrELGEW 474
|
490
....*....|....*
gi 489498938 477 GpaaIQFYTKVKTVT 491
Cdd:PLN02467 475 G---LENYLSVKQVT 486
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
23-490 |
1.47e-77 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 250.68 E-value: 1.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:NF040648 14 DVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKLITIDAGKPIKQSIIE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEyTEGAGPGIdVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:NF040648 94 VDRSIETFKLAAFYAKEIRGE-TIPSDAGL-IFTKKEPLGVVGAITPFNYPLNLAAHKIAPAIATGNSVVLHPSSKAPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAEL----FIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIyAGAAATGKRAQCFGGaKNHMIV 257
Cdd:NF040648 172 AIELAKIiekvLKKMNIPLGVFNLVTGYGEVVgDEIVKNEKVNKISFTGSVEVGESI-SKKAGMKKITLELGG-NNPLIV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 258 MPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDY 337
Cdd:NF040648 250 LKDADIEKAVESAVKGSFLNSGQVCISVG-RVIVEEEIADEFIKKLVEETKKLKVGNPLDEKTDIGPLITEEAAIRVENL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 338 IGQGVAAGAELVVDG-RDRAsddltfglpegdanleggfFIGPTLFDhVAAHMSIYTDEIFGPVLCMVRARDYEEALRLP 416
Cdd:NF040648 329 VNEAIEEGAKLLCGGnREGS-------------------LFYPTVLD-VDEDNILVKVETFGPVLPIIRVKDIDEAIEIA 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489498938 417 SEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdlnQHG-PAAIQFYTKVKTV 490
Cdd:NF040648 389 NNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKSGLG---KEGiKYAVEEMTEIKTI 460
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
9-494 |
1.75e-77 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 252.16 E-value: 1.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 9 IDGQR--TAG--QSTRSAdvfdpNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDEL 84
Cdd:PRK03137 41 IGGERitTEDkiVSINPA-----NKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 85 AELLSREHGKTLADARGDVQRGIEVIEFClgIPHLLKgeYTEGAG----PGIDVYSLRQPLGVVAGITPFNFPAMIPLWK 160
Cdd:PRK03137 116 SAWLVKEAGKPWAEADADTAEAIDFLEYY--ARQMLK--LADGKPvesrPGEHNRYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 161 AGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAA 239
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSgSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 240 ATG------KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVG 313
Cdd:PRK03137 272 KVQpgqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAI-VHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 314 HSLDPkADYGPLVTGAALARVRDYIGQGVAAGaELVVDGrdrasddltfglpEGDAnlEGGFFIGPTLFDHVAAHMSIYT 393
Cdd:PRK03137 351 NPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGG-------------EGDD--SKGYFIQPTIFADVDPKARIMQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 394 DEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGD----AARDFvsrvQVGMVGVNVPIP-VPVAYHTFGGWKRS 468
Cdd:PRK03137 414 EEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREhlekARREF----HVGNLYFNRGCTgAIVGYHPFGGFNMS 489
|
490 500
....*....|....*....|....*.
gi 489498938 469 GfGDLNQHGPAAIQFYTKVKTVTSRW 494
Cdd:PRK03137 490 G-TDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
8-490 |
2.46e-77 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 250.97 E-value: 2.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA-QKG-WAAWNPQRRARVLMRFIELVNDTIDELA 85
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfERGdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 86 ELLSREHGKTLADA-RGDVQRGIEVIEFclgIPHLLKGEYTEGAGPGIDVYSL--RQPLGVVAGITPFNFPAMIPLWKAG 162
Cdd:PRK09847 103 LLETLDTGKPIRHSlRDDIPGAARAIRW---YAEAIDKVYGEVATTSSHELAMivREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 163 PALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAAT 241
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 242 G-KRAQCFGGAKNHMIVMPDA-DLDQAVDALIGAGYGSAGERCMAiSVAVPVGDQTAERLRARLIERINNLRVGHSLDPK 319
Cdd:PRK09847 260 NmKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA-GTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 320 ADYGPLVTGAALARVRDYIGQGVAAGaELVVDGRDRasddltfGLPEgdanleggfFIGPTLFDHVAAHMSIYTDEIFGP 399
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNA-------GLAA---------AIGPTIFVDVDPNASLSREEIFGP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 400 VLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNV----PIPVPvayhtFGGWKRSGFG-DLN 474
Cdd:PRK09847 402 VLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKS 476
|
490
....*....|....*.
gi 489498938 475 QHgpaAIQFYTKVKTV 490
Cdd:PRK09847 477 LH---ALEKFTELKTI 489
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
23-471 |
2.70e-77 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 249.86 E-value: 2.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEY----TEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSER 178
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVlpldISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 179 DPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAqyiYAGAAATGKRAQCF---GGAKnhM 255
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVG---WDLKARAGKKKVVLelgGNAA--V 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 256 IVMPDADLDQAVDALIGAGYGSAGERCmaISVA-VPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARV 334
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSC--ISVQrVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 335 RDYIGQGVAAGAELVVDGRdrasddltfglpegdanLEGGFFiGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALR 414
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGK-----------------RDGALL-EPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489498938 415 LPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN-VPiPVPVAYHTFGGWKRSGFG 471
Cdd:cd07147 377 AVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVP-TFRVDHMPYGGVKDSGIG 433
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
7-492 |
1.84e-74 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 244.72 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEA--QKGWAAWNPQRRARVLMRFIELVNDTIDEL 84
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 85 AELLSREHGKTLADARG-DVQRGIEVIEFCLGIPHLLKGEYTEGAGPGiDVYSLRQPLGVVAGITPFNFPAMIPLWKAGP 163
Cdd:PLN02466 140 AALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPH-HVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 164 ALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATG 242
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFG-GAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS---VAVPVGDQTAERLRARLIERInnlrVGHSLDP 318
Cdd:PLN02466 299 LKPVTLElGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSrtfVHERVYDEFVEKAKARALKRV----VGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 319 KADYGPLVTGAALARVRDYIGQGVAAGAELVVDGrDRASDDltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFG 398
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGG-DRFGSK--------------GYYIQPTVFSNVQDDMLIAQDEIFG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 399 PVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVpIPVPVAYHTFGGWKRSGFGdlNQHGP 478
Cdd:PLN02466 440 PVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG--REKGI 516
|
490
....*....|....
gi 489498938 479 AAIQFYTKVKTVTS 492
Cdd:PLN02466 517 YSLNNYLQVKAVVT 530
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-490 |
9.60e-74 |
|
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: 241.20 E-value: 9.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARG-DVQRGIEVIEFCLGIphlLKGEytEGAGPGIDVYSL----RQPLGVVAGITPFNFPAMIPLWKAG 162
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGV---IRAE--EGSANMIDEDTLsivlREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 163 PALACGNAFVLKPSERDPSVPVRLAELFIEAgLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAAT 241
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 242 GKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKAD 321
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGS-RIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 322 YGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDDLtfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVL 401
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGL-----------DKGFFIEPTLIVNVTNDMRVAQEEIFGPVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 402 CMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPvAYHTFGGWKRSGFGDLNQHGpaAI 481
Cdd:cd07117 386 TVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIP-AGAPFGGYKKSGIGRETHKS--ML 462
|
....*....
gi 489498938 482 QFYTKVKTV 490
Cdd:cd07117 463 DAYTQMKNI 471
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-471 |
9.60e-74 |
|
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: 240.23 E-value: 9.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 27 PNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRG 106
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 107 IEVIEFCLGI-PHLLKgEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVR 185
Cdd:cd07102 83 LERARYMISIaEEALA-DIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 186 LAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQ 265
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 266 AVDALI-GAGYGSaGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAA 344
Cdd:cd07102 242 AAESLVdGAFFNS-GQSCCSIE-RIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 345 GAELVVDGRDRASDDltfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNG 424
Cdd:cd07102 320 GARALIDGALFPEDK------------AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLT 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489498938 425 VAIFTRDGDAARDFVSRVQVGMVGVNvPIPVPVAYHTFGGWKRSGFG 471
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRG 433
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-471 |
1.04e-73 |
|
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: 242.10 E-value: 1.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 2 TTQISHFIDGQRTAGQSTrsADVFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDT 80
Cdd:cd07125 30 EWEAIPIINGEETETGEG--APVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 81 IDELAELLSREHGKTLADARGDVQrgiEVIEFCLGIPHLLKGEYTEGAGPGIDVYS--LR-QPLGVVAGITPFNFPAMIP 157
Cdd:cd07125 108 RGELIALAAAEAGKTLADADAEVR---EAIDFCRYYAAQARELFSDPELPGPTGELngLElHGRGVFVCISPWNFPLAIF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 158 LWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIya 236
Cdd:cd07125 185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLI-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 237 gaaaTGKRAQCFG---------GAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVPVGDqTAERLRARLIERI 307
Cdd:cd07125 263 ----NRALAERDGpilpliaetGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEE-IAERFIEMLKGAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 308 NNLRVGHSLDPKADYGPLVTGAALARVRDYIgqgvaagaelvvdGRDRASDDLtfgLPEGDANLEGGFFIGPTLFDHVAA 387
Cdd:cd07125 338 ASLKVGDPWDLSTDVGPLIDKPAGKLLRAHT-------------ELMRGEAWL---IAPAPLDDGNGYFVAPGIIEIVGI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 388 hmSIYTDEIFGPVLCMVRAR--DYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPI--------Pvpv 457
Cdd:cd07125 402 --FDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNItgaivgrqP--- 476
|
490
....*....|....
gi 489498938 458 ayhtFGGWKRSGFG 471
Cdd:cd07125 477 ----FGGWGLSGTG 486
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
8-471 |
4.02e-73 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 239.81 E-value: 4.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALAC 167
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 168 GNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQ 246
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELtSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 247 CFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMA---ISVAVPVGDQTAERLRArlieRINNLRVGHSLDPKADYG 323
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCanrLYVQDGVYDRFAEKLQQ----AVSKLHIGDGLEKGVTIG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 324 PLVTGAALARVRDYIGQGVAAGAELVVDGRDRAsddltfglpegdanLEGGFFiGPTLFDHVAAHMSIYTDEIFGPVLCM 403
Cdd:PRK11241 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHE--------------LGGNFF-QPTILVDVPANAKVAKEETFGPLAPL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489498938 404 VRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIpVPVAYHTFGGWKRSGFG 471
Cdd:PRK11241 395 FRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLG 461
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
43-480 |
2.73e-68 |
|
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: 225.61 E-value: 2.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 43 DIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKG 122
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 123 EYTEGAGPGIDVYSLRqPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQV 202
Cdd:cd07095 81 ERATPMAQGRAVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 203 VHGDKEAVDAILHHPDIKAVGFVGSsdiaqyiyagaAATGKR-AQCFG-----------GAKNHMIVMPDADLDQAVDAL 270
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGS-----------AATGLLlHRQFAgrpgkilalemGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 271 IGAGYGSAGERCMAISVAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARvrdyigqGVAAGAELVV 350
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR-------YLLAQQDLLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 351 DGrdrasddltfGLP--EGDANLEGGFFIGPTLFDhVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIF 428
Cdd:cd07095 302 LG----------GEPllAMERLVAGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLL 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489498938 429 TRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGfgdlnQHGPAA 480
Cdd:cd07095 371 SDDEALFERFLARIRAGIVNWNRPTTGASSTAPFGGVGLSG-----NHRPSA 417
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
11-493 |
5.73e-65 |
|
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: 218.60 E-value: 5.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 11 GQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSR 90
Cdd:cd07083 24 GGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 91 EHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAG-PGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGN 169
Cdd:cd07083 104 EVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 170 AFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAA------ATG 242
Cdd:cd07083 184 TVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAArlapgqTWF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 243 KRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADY 322
Cdd:cd07083 264 KRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLI-LTQGAYEPVLERLLKRAERLSVGPPEENGTDL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 323 GPLVTGAALARVRDYIGQGVAAGaELVVDGRdrasddltfgLPEGDanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLC 402
Cdd:cd07083 343 GPVIDAEQEAKVLSYIEHGKNEG-QLVLGGK----------RLEGE-----GYFVAPTVVEEVPPKARIAQEEIFGPVLS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 403 MVR--ARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIP-VPVAYHTFGGWKRSGFGDlNQHGPA 479
Cdd:cd07083 407 VIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgALVGVQPFGGFKLSGTNA-KTGGPH 485
|
490
....*....|....
gi 489498938 480 AIQFYTKVKTVTSR 493
Cdd:cd07083 486 YLRRFLEMKAVAER 499
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
26-490 |
7.96e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 217.30 E-value: 7.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 26 DPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQR 105
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 106 GIEVIEFCLG-IPHLLKGEYTEGAGPGID-VYSLRQPLGVVAGITPFNFPamipLWK----AGPALACGNAFVLKPSERD 179
Cdd:PRK09406 87 CAKGFRYYAEhAEALLADEPADAAAVGASrAYVRYQPLGVVLAVMPWNFP----LWQvvrfAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 180 PSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMP 259
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 260 DADLDQAVDALIGAGYGSAGERCMAIS---VAVPVGDQTAERLrarlIERINNLRVGHSLDPKADYGPLVTGAALARVRD 336
Cdd:PRK09406 243 SADLDRAAETAVTARVQNNGQSCIAAKrfiVHADVYDAFAEKF----VARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 337 YIGQGVAAGAELVVDGRdrasddltfgLPEGDanlegGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLP 416
Cdd:PRK09406 319 QVDDAVAAGATILCGGK----------RPDGP-----GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498938 417 SEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN---VPIP-VPvayhtFGGWKRSGFG-DLNQHGpaaIQFYTKVKTV 490
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINgmtVSYPeLP-----FGGVKRSGYGrELSAHG---IREFCNIKTV 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
8-476 |
9.09e-63 |
|
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: 212.31 E-value: 9.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGK----TLAdarGDVQRGIEVIEFCLGIphlLKGEytEGAGPGID----VYSLRQPLGVVAGITPFNFPAMIPLW 159
Cdd:cd07116 84 ETWDNGKpvreTLA---ADIPLAIDHFRYFAGC---IRAQ--EGSISEIDentvAYHFHEPLGVVGQIIPWNFPLLMATW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 160 KAGPALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGA 238
Cdd:cd07116 156 KLAPALAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 239 AATGKRAQCFGGAKNHMIVMP------DADLDQAVDALIGAGYGSaGERCMAISVAVpVGDQTAERLRARLIERINNLRV 312
Cdd:cd07116 235 SENIIPVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFALNQ-GEVCTCPSRAL-IQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 313 GHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDDLtfglpegdanLEGGFFIGPTLFDHvaAHMSIY 392
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGL----------LGGGYYVPTTFKGG--NKMRIF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 393 TDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPvAYHTFGGWKRSGFGD 472
Cdd:cd07116 381 QEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIGR 459
|
....
gi 489498938 473 LNQH 476
Cdd:cd07116 460 ENHK 463
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
25-492 |
4.64e-62 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 210.23 E-value: 4.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 25 FDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADAR-GDV 103
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 104 QRGIEVIEFCL--GIPHLlKGEYTegAGPGIDVYSLR----QPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSE 177
Cdd:cd07098 81 LVTCEKIRWTLkhGEKAL-RPESR--PGGLLMFYKRArveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 178 RdpsvPVRLAELFIE--------AGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFG 249
Cdd:cd07098 158 Q----VAWSSGFFLSiireclaaCGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 250 GAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGA 329
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIE-RVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 330 ALARVRDYIGQGVAAGAELVVDGRdrasddlTFGLPEgdanLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDY 409
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGK-------RYPHPE----YPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 410 EEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvpiPVPVAYHT----FGGWKRSGFGDLNqhGPAAIQFYT 485
Cdd:cd07098 382 EEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN---DFGVNYYVqqlpFGGVKGSGFGRFA--GEEGLRGLC 456
|
....*..
gi 489498938 486 KVKTVTS 492
Cdd:cd07098 457 NPKSVTE 463
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
7-489 |
6.93e-62 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 210.38 E-value: 6.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 7 HFIDGQRTAGQSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAE 86
Cdd:PLN00412 18 YYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 87 LLSREHGKTLADARGDVQRGIEVIEFCL--GIPHLLKGEY-TEGAGPGIDVYSL----RQPLGVVAGITPFNFPAMIPLW 159
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFlVSDSFPGNERNKYcltsKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 160 KAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGD-KEAVDAILHHPDIKAVGFV-GSSDIAQYIYAG 237
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTgGDTGIAISKKAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 238 AAATgkraQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLD 317
Cdd:PLN00412 258 MVPL----QMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKV-VLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 318 pKADYGPLVTGAAlarvRDYIgQGvaagaeLVVDGRDRASDDLTFGLPEGdaNLeggffIGPTLFDHVAAHMSIYTDEIF 397
Cdd:PLN00412 333 -DCDITPVVSESS----ANFI-EG------LVMDAKEKGATFCQEWKREG--NL-----IWPLLLDNVRPDMRIAWEEPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 398 GPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFGdlNQHG 477
Cdd:PLN00412 394 GPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIG--SQGI 471
|
490
....*....|..
gi 489498938 478 PAAIQFYTKVKT 489
Cdd:PLN00412 472 TNSINMMTKVKS 483
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
23-471 |
5.90e-61 |
|
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: 207.44 E-value: 5.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:cd07130 15 TSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDP-- 180
Cdd:cd07130 95 VQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPlt 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 181 SVPVR--LAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSdiaqyiyagaaATGKRAQC-----FG---- 249
Cdd:cd07130 175 AIAVTkiVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGST-----------AVGRQVGQavaarFGrsll 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 250 --GAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMA---ISVAVPVGDQtaerLRARLIERINNLRVGHSLDPKADYGP 324
Cdd:cd07130 244 elGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTtrrLIVHESIYDE----VLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDYIGQGVAAGAELVVDGR--DRasddltfglpegdanleGGFFIGPTLFDhVAAHMSIYTDEIFGPVLC 402
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGKviDG-----------------PGNYVEPTIVE-GLSDAPIVKEETFAPILY 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498938 403 MVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRV--QVGMVGVNVPipvpvayhT--------FGGWKRSGFG 471
Cdd:cd07130 382 VLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG--------TsgaeiggaFGGEKETGGG 452
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
6-484 |
1.88e-58 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 200.95 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 6 SHFIDGQRTAGQSTRSADvFDPNTGQI--QAKVpmAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDE 83
Cdd:PRK09457 2 TLWINGDWIAGQGEAFES-RNPVSGEVlwQGND--ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 84 LAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVysLR-QPLGVVAGITPFNFPAMIPLWKAG 162
Cdd:PRK09457 79 LAEVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAV--LRhRPHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 163 PALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYI---YAGaa 239
Cdd:PRK09457 157 PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLhrqFAG-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 240 ATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCM-AISVAVPVGDQtAERLRARLIERINNLRVGHSL-D 317
Cdd:PRK09457 235 QPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQ-GDAFLARLVAVAKRLTVGRWDaE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 318 PKADYGPLVTGAALARVrdyigqgVAAGAELVVDGrdrASDDLTFGLPEGDANleggfFIGPTLFDhVAAHMSIYTDEIF 397
Cdd:PRK09457 314 PQPFMGAVISEQAAQGL-------VAAQAQLLALG---GKSLLEMTQLQAGTG-----LLTPGIID-VTGVAELPDEEYF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 398 GPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGfgdlnQHG 477
Cdd:PRK09457 378 GPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASG-----NHR 452
|
....*..
gi 489498938 478 PAAiqFY 484
Cdd:PRK09457 453 PSA--YY 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-471 |
1.86e-57 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 197.78 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 26 DPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQR 105
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 106 GIEVIE-FCLGIPHLLKGEYT--EGAGPGIDVyslrQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSV 182
Cdd:PRK13968 93 SANLCDwYAEHGPAMLKAEPTlvENQQAVIEY----RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 183 PVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDAD 262
Cdd:PRK13968 169 AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 263 LDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLvtgaALARVRDYIGQGV 342
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFI-IEEGIASAFTERFVAAAAALKMGDPRDEENALGPM----ARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 343 AA----GAELVVDGRDRAsddltfglpeGDANleggfFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSE 418
Cdd:PRK13968 324 EAtlaeGARLLLGGEKIA----------GAGN-----YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELAND 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489498938 419 HEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvPIPVPVAYHTFGGWKRSGFG 471
Cdd:PRK13968 389 SEFGLSATIFTTDETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
23-471 |
8.48e-57 |
|
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: 195.72 E-value: 8.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 23 DVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNP-QRRARVLMRFIELVNDTIDELAELLSREHGKTLADARG 101
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPaHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 102 DVQRGIEVIEFClgIPHLLKGEYTE------GAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKP 175
Cdd:cd07148 82 EVTRAIDGVELA--ADELGQLGGREipmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 176 SERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNhM 255
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGTRCALEHGGAAP-V 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 256 IVMPDADLDQAVDALIGAGYGSAGERCmaISVA-VPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARV 334
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQrVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 335 RDYIGQGVAAGAELVVDGRdRASDDLtfglpegdanleggffIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALR 414
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGK-RLSDTT----------------YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489498938 415 LPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIPVPVAYHTFGGWKRSGFG 471
Cdd:cd07148 380 QANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
81-477 |
5.88e-56 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 192.26 E-value: 5.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 81 IDELAELLSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWK 160
Cdd:PRK10090 12 ASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 161 AGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYAGAA 239
Cdd:PRK10090 92 MAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKIMAAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 240 ATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISvAVPVGDQTAERLRARLIERINNLRVGHSLD-P 318
Cdd:PRK10090 172 KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAE-RVYVQKGIYDQFVNRLGEAMQAVQFGNPAErN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 319 KADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRdRASDDltfglpegdanlegGFFIGPTLFDHVAAHMSIYTDEIFG 398
Cdd:PRK10090 251 DIAMGPLINAAALERVEQKVARAVEEGARVALGGK-AVEGK--------------GYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 399 PVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVP-IPVPVAYHtfGGWKRSGFGDLN-QH 476
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREnFEAMQGFH--AGWRKSGIGGADgKH 393
|
.
gi 489498938 477 G 477
Cdd:PRK10090 394 G 394
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
4-450 |
1.47e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 186.17 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 4 QISHFIDGQRTAG----QSTRSADVFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVN 78
Cdd:PRK11904 542 AIAAFLEKQWQAGpiinGEGEARPVVSPaDRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLE 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 79 DTIDELAELLSREHGKTLADARGDVQrgiEVIEFC----------LGIPHLLKGeYTegagpGIDVYSLRQPLGVVAGIT 148
Cdd:PRK11904 622 ANRAELIALCVREAGKTLQDAIAEVR---EAVDFCryyaaqarrlFGAPEKLPG-PT-----GESNELRLHGRGVFVCIS 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 149 PFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGS 227
Cdd:PRK11904 693 PWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGS 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 228 SDIAQYIYAGAAATGKRAQCF----GGAkNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARL 303
Cdd:PRK11904 773 TETARIINRTLAARDGPIVPLiaetGGQ-NAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLF-VQEDIADRVIEML 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 304 IERINNLRVGHSLDPKADYGPLVTGAALARVRDYIgqgvaagAELVVDGRDRASDDLtfglpegDANLEGGFFIGPTLFD 383
Cdd:PRK11904 851 KGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHI-------ERMKREARLLAQLPL-------PAGTENGHFVAPTAFE 916
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498938 384 hvAAHMSIYTDEIFGPVLCMVR--ARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN 450
Cdd:PRK11904 917 --IDSISQLEREVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
24-450 |
9.29e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 169.28 E-value: 9.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 24 VFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGD 102
Cdd:PRK11905 571 VLNPaDHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 103 VQrgiEVIEFC----LGIPHLLKGEYTEgagpgidvyslrqPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSER 178
Cdd:PRK11905 651 VR---EAVDFLryyaAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 179 DPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCF----GGaKN 253
Cdd:PRK11905 715 TPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALvADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaetGG-QN 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 254 HMIVMPDADLDQAVDALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALAR 333
Cdd:PRK11905 794 AMIVDSSALPEQVVADVIASAFDSAGQRCSALRV-LCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQAN 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 334 VRDYIGQGVAAGAELvvdgrdrasddltFGLPEGDAnLEGGFFIGPTLFDhvAAHMSIYTDEIFGPVLCMVRARdYEEAL 413
Cdd:PRK11905 873 IEAHIEAMRAAGRLV-------------HQLPLPAE-TEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFK-ADELD 935
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489498938 414 RLPSEHE---YGNGVAIFTRDGDAARDFVSRVQVGMVGVN 450
Cdd:PRK11905 936 RVIDDINatgYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
9-405 |
1.23e-43 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 165.88 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 9 IDGQRTAGqstRSADVFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:COG4230 562 IAGEAASG---EARPVRNPaDHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARGDVqRgiEVIEFC----------LGIPHLLkgeytegagpgidvyslrQPLGVVAGITPFNFPAMIP 157
Cdd:COG4230 639 LVREAGKTLPDAIAEV-R--EAVDFCryyaaqarrlFAAPTVL------------------RGRGVFVCISPWNFPLAIF 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 158 LWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSSDIAQYIYA 236
Cdd:COG4230 698 TGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTETARLINR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 237 GAAATGKRAQCF----GGaKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRV 312
Cdd:COG4230 778 TLAARDGPIVPLiaetGG-QNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRV-LCVQEDIADRVLEMLKGAMAELRV 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 313 GHSLDPKADYGPLVTGAALARVRDYIgQGVAAGAELVVDGRdrasddltfgLPEGDANlegGFFIGPTLF--DHVAAhms 390
Cdd:COG4230 856 GDPADLSTDVGPVIDAEARANLEAHI-ERMRAEGRLVHQLP----------LPEECAN---GTFVAPTLIeiDSISD--- 918
|
410
....*....|....*
gi 489498938 391 iYTDEIFGPVLCMVR 405
Cdd:COG4230 919 -LEREVFGPVLHVVR 932
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
32-488 |
1.30e-41 |
|
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: 155.84 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 32 IQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQrgiEVIE 111
Cdd:TIGR01238 64 IVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVR---EAVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 112 FClgiphllkGEYTEGAGPGIDVYSLRqPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFI 191
Cdd:TIGR01238 141 FC--------RYYAKQVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 192 EAGLPAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAATGKRAQCF---GGAKNHMIVMPDADLDQAV 267
Cdd:TIGR01238 212 EAGFPAGTIQLLPGRGADVGAALtSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaeTGGQNAMIVDSTALPEQVV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 268 DALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIG--QGVAAG 345
Cdd:TIGR01238 292 RDVLRSAFDSAGQRCSALRV-LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEhmSQTQKK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 346 AELVVDGRDRASddltfglpegdanlEGGFFIGPTLF--DHVAAhmsiYTDEIFGPVLCMVR--ARDYEEALRLPSEHEY 421
Cdd:TIGR01238 371 IAQLTLDDSRAC--------------QHGTFVAPTLFelDDIAE----LSEEVFGPVLHVVRykARELDQIVDQINQTGY 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489498938 422 GNGVAIFTRDGDAARDFVSRVQVGMVGVNVPI-PVPVAYHTFGGWKRSGFGDlNQHGPAAIQFYTKVK 488
Cdd:TIGR01238 433 GLTMGVHSRIETTYRWIEKHARVGNCYVNRNQvGAVVGVQPFGGQGLSGTGP-KAGGPHYLYRLTQVQ 499
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
2-472 |
5.69e-39 |
|
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: 148.50 E-value: 5.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 2 TTQISHFIDGQRTAGQSTRsaDVFDP-NTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDT 80
Cdd:cd07123 30 TVEIPLVIGGKEVRTGNTG--KQVMPhDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 81 I-DEL--AELLSRehGKTLADARGDVqrGIEVIEF-------CLGIPHLLKGEYTEGAGPGIDvYslrQPL-GVVAGITP 149
Cdd:cd07123 108 YrYELnaATMLGQ--GKNVWQAEIDA--ACELIDFlrfnvkyAEELYAQQPLSSPAGVWNRLE-Y---RPLeGFVYAVSP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 150 FNFPAMIPLWKAGPALAcGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAV-DAILHHPDIKAVGFVGSS 228
Cdd:cd07123 180 FNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 229 DIAQYIYAGAAATGKRAQCF----G--GAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVA-VPvgDQTAERLRA 301
Cdd:cd07123 259 PTFKSLWKQIGENLDRYRTYprivGetGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAyVP--ESLWPEVKE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 302 RLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAA-GAELVVDGRdraSDDLTfglpegdanlegGFFIGPT 380
Cdd:cd07123 337 RLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK---CDDSV------------GYFVEPT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 381 LFDHVAAHMSIYTDEIFGPVLCM--VRARDYEEALRLPSE-HEYGNGVAIFTRDGDA---ARDfVSRVQVGMVGVN-VPI 453
Cdd:cd07123 402 VIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTtSPYALTGAIFAQDRKAireATD-ALRNAAGNFYINdKPT 480
|
490
....*....|....*....
gi 489498938 454 PVPVAYHTFGGWKRSGFGD 472
Cdd:cd07123 481 GAVVGQQPFGGARASGTND 499
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
8-471 |
1.42e-38 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 147.29 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 8 FIDGQRTAGQSTRSAdvFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAEL 87
Cdd:PLN02315 24 YVGGEWRANGPLVSS--VNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 88 LSREHGKTLADARGDVQRGIEVIEFCLGIPHLLKGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALAC 167
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 168 GNAFVLKPSERDPSVPVRL----AELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAAATGK 243
Cdd:PLN02315 182 GNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 244 RAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAISVAVpVGDQTAERLRARLIERINNLRVGHSLDPKADYG 323
Cdd:PLN02315 262 KCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLL-LHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 324 PLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDdltfglpegdanlegGFFIGPTLFDhVAAHMSIYTDEIFGPVLCM 403
Cdd:PLN02315 341 PLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESE---------------GNFVQPTIVE-ISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 404 VRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRV--QVGMVGVNVPIPVPVAYHTFGGWKRSGFG 471
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG 474
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-471 |
1.88e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 138.18 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 39 AGKSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFclgiph 118
Cdd:PRK11809 679 ATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRY------ 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 119 llkgeYTEGAGPGIDVYSLRqPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAG 198
Cdd:PRK11809 753 -----YAGQVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAG 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 199 VFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAAatgKRAQCFG---------GAKNHMIVMPDADLDQAVD 268
Cdd:PRK11809 827 VVQLLPGRGETVGAALvADARVRGVMFTGSTEVARLLQRNLA---GRLDPQGrpipliaetGGQNAMIVDSSALTEQVVA 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 269 ALIGAGYGSAGERCMAISVaVPVGDQTAERLRARLIERINNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAEL 348
Cdd:PRK11809 904 DVLASAFDSAGQRCSALRV-LCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPV 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 349 VVDGRDRASDDLTfglpegdanlegGFFIGPTL--FDHVAAhmsiYTDEIFGPVLCMVRAR--DYEEALRLPSEHEYGNG 424
Cdd:PRK11809 983 FQAARENSEDWQS------------GTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrnQLDELIEQINASGYGLT 1046
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489498938 425 VAIFTRDGDAARDFVSRVQVGMVGVNVPI--PVpVAYHTFGGWKRSGFG 471
Cdd:PRK11809 1047 LGVHTRIDETIAQVTGSAHVGNLYVNRNMvgAV-VGVQPFGGEGLSGTG 1094
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
138-471 |
1.26e-33 |
|
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: 131.88 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 138 RQPLGVVAGITPFNFP---AMIPLwkAGpALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEAVDAIL 214
Cdd:cd07087 98 PEPLGVVLIIGPWNYPlqlALAPL--IG-AIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 215 HHP-DIkaVGFVGSSDIAQYIYAGAAATgkRAQC---FGGaKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAisvavP 290
Cdd:cd07087 174 AEPfDH--IFFTGSPAVGKIVMEAAAKH--LTPVtleLGG-KSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA-----P 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 291 ----VGDQTAERLRARLIERINNLrvgHSLDPK--ADYGPLVTGAALARVRDYIGQG-VAAGAElvVDGRDRasddltfg 363
Cdd:cd07087 244 dyvlVHESIKDELIEELKKAIKEF---YGEDPKesPDYGRIINERHFDRLASLLDDGkVVIGGQ--VDKEER-------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 364 lpegdanleggfFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQ 443
Cdd:cd07087 311 ------------YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETS 378
|
330 340 350
....*....|....*....|....*....|
gi 489498938 444 VGMVGVNVPIpVPVAYHT--FGGWKRSGFG 471
Cdd:cd07087 379 SGGVCVNDVL-LHAAIPNlpFGGVGNSGMG 407
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
46-484 |
1.15e-31 |
|
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: 126.58 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 46 AAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKT---LADARGDVQ--RGIEVIEFCLGIPHll 120
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQVqlRARAFVIYSYRIPH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 121 KGEYTEGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAG-LPAGV 199
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 200 FQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYAGAaatgKRAQCFG--GAKNHMIVMPDAD-LDQAVDALIGAGYG 276
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA----KQARIYLelAGFNWKVLGPDAQaVDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 277 SAGERCMAISVA-VPVGDQTaERLRARLIERINNLRVGHSLdpkadYGPLVTGAALARVrdyigqgVAAGAElvvDGRdr 355
Cdd:cd07084 237 CSGQKCTAQSMLfVPENWSK-TPLVEKLKALLARRKLEDLL-----LGPVQTFTTLAMI-------AHMENL---LGS-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 356 asdDLTFG---LPEGDANLEGGFFIGPTLF---DHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLP-SEHEYGNGVA-I 427
Cdd:cd07084 299 ---VLLFSgkeLKNHSIPSIYGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLElLERMHGSLTAaI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489498938 428 FTRDGDAARDFVSRVQV-GMVGVNVPIP---VPVAYHTFGGwkRSGFGDLNQHGPAAIQFY 484
Cdd:cd07084 376 YSNDPIFLQELIGNLWVaGRTYAILRGRtgvAPNQNHGGGP--AADPRGAGIGGPEAIKLV 434
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
76-490 |
6.20e-31 |
|
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: 124.64 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 76 LVNDTIDELAELLSREHGK-----TLADARGDVQRGIEVIEfclGIPHLLKGEYTEGAGPGIDVYSLR---QPLGVVAGI 147
Cdd:cd07135 39 AVKDNEEAIVEALKKDLGRppfetLLTEVSGVKNDILHMLK---NLKKWAKDEKVKDGPLAFMFGKPRirkEPLGVVLII 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 148 TPFNFPAMIPLwkaGP---ALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEAVDAILHHPDIKaVGF 224
Cdd:cd07135 116 GPWNYPVLLAL---SPlvgAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETTALLEQKFDK-IFY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 225 VGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS-VAVPvgdqtaERLRARL 303
Cdd:cd07135 191 TGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDyVLVD------PSVYDEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 304 IERIN---NLRVGHSLDPKADYGPLVTGAALARVRDYIGQgvaAGAELVVDG-RDRASddltfglpegdanleggFFIGP 379
Cdd:cd07135 265 VEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGeMDEAT-----------------RFIPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 380 TLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVN-VPIPVPVA 458
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVD 404
|
410 420 430
....*....|....*....|....*....|..
gi 489498938 459 YHTFGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07135 405 NAPFGGVGDSGYG--AYHGKYGFDTFTHERTV 434
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
139-477 |
1.56e-30 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 123.49 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 139 QPLGVVAGITPFNFP---AMIPLwkaGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFqVVHGDKEAVDAILH 215
Cdd:cd07134 99 EPKGVCLIISPWNYPfnlAFGPL---VSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGDAEVAQALLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 216 HPdIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMA---ISVAVPVG 292
Cdd:cd07134 175 LP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIApdyVFVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 293 DQTAERLRArLIERinNLRVGHSLDPKADYGPLVTGAALARVRDYIGQGVAAGAELVVDGRDRASDDltfglpegdanle 372
Cdd:cd07134 254 DAFVEHLKA-EIEK--FYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR------------- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 373 ggfFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALrlpsehEYGN------GVAIFTRDGDAARDFVSRVQVGM 446
Cdd:cd07134 318 ---YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVI------EYINakpkplALYVFSKDKANVNKVLARTSSGG 388
|
330 340 350
....*....|....*....|....*....|....*..
gi 489498938 447 VGVNVpipvpVAYH------TFGGWKRSGFGdlNQHG 477
Cdd:cd07134 389 VVVND-----VVLHflnpnlPFGGVNNSGIG--SYHG 418
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-439 |
1.18e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 113.26 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 1 MTTQISHFIDGQRTAGQSTRSAdVFDPNTGQIQAKVPMAGkSDIDAAVASAVEaQKGWA--AWNPQRRARVLMRFIELVN 78
Cdd:PRK11903 1 MTELLANYVAGRWQAGSGAGTP-LFDPVTGEELVRVSATG-LDLAAAFAFARE-QGGAAlrALTYAQRAALLAAIVKVLQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 79 DTIDELAELLSREHGKTLADARGDVQRGIEVIEF------CLGIPHLLK-GEYTE-GAGPGIDVYSLRQPL-GVVAGITP 149
Cdd:PRK11903 78 ANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYyaklgaALGDARLLRdGEAVQlGKDPAFQGQHVLVPTrGVALFINA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 150 FNFPAMiPLW-KAGPALACGNAFVLKPSERDPSVPVRLAELFIEAG-LPAGVFQVVHGDKEAVDAILHHPDIkaVGFVGS 227
Cdd:PRK11903 158 FNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDV--VSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 228 SDIAQYI--YAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYG-----SAGERCMAI-SVAVPvgDQTAERL 299
Cdd:PRK11903 235 AETAAVLrsHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVremtvKSGQKCTAIrRIFVP--EALYDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 300 RARLIERINNLRVGhslDPKAD---YGPLVTGAALARVRDYIgQGVAAGAELVVDGRdrasddltfGLPEGDANLEGGFF 376
Cdd:PRK11903 313 AEALAARLAKTTVG---NPRNDgvrMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGG---------GFALVDADPAVAAC 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489498938 377 IGPTLF--DHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFV 439
Cdd:PRK11903 380 VGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
66-471 |
1.89e-26 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 112.43 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 66 RARVLMRFIELVNDTIDELAELLSREHGKTLADAR-GDVQRGIEVIEFCLG-IPHLLKGEY--TEGA-GPGiDVYSLRQP 140
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKhLDEYLKPEKvdTVGVfGPG-KSYIIPEP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 141 LGVVAGITPFNFP---AMIPLwkAGpALACGNAFVLKPSERDPSVPVRLAELFIEAgLPAGVFQVVHGDKEAVDAILHHP 217
Cdd:PTZ00381 110 LGVVLVIGAWNYPlnlTLIPL--AG-AIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLKEP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 218 -DIkaVGFVGSSDIAQYIYAGAAAtgKRAQC---FGGaKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAIS-VAVP-- 290
Cdd:PTZ00381 186 fDH--IFFTGSPRVGKLVMQAAAE--NLTPCtleLGG-KSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDyVLVHrs 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 291 VGDQTAERLRARLIERINNlrvghslDPK--ADYGPLVTGAALARVRDYIgqgvaagaelvvdgrDRASDDLTFGlpeGD 368
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGE-------DPKksEDYSRIVNEFHTKRLAELI---------------KDHGGKVVYG---GE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 369 ANLEGGfFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVG 448
Cdd:PTZ00381 316 VDIENK-YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVV 394
|
410 420
....*....|....*....|....*
gi 489498938 449 VNVPIpVPVAYHT--FGGWKRSGFG 471
Cdd:PTZ00381 395 INDCV-FHLLNPNlpFGGVGNSGMG 418
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
139-490 |
7.48e-25 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 106.73 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 139 QPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEAVDAILHHPD 218
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 219 IKaVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGS-AGERCMAISVAVpvgdqTAE 297
Cdd:cd07137 179 DK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL-----VEE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 298 RLRARLIERINN-LRVGHSLDPK--ADYGPLVTGAALARVRDYIGQ-GVAAGaelVVDGRDRASDDLtfglpegdanleg 373
Cdd:cd07137 253 SFAPTLIDALKNtLEKFFGENPKesKDLSRIVNSHHFQRLSRLLDDpSVADK---IVHGGERDEKNL------------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 374 gfFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPI 453
Cdd:cd07137 317 --YIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV 394
|
330 340 350
....*....|....*....|....*....|....*....
gi 489498938 454 pVPVAYHT--FGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07137 395 -VQYAIDTlpFGGVGESGFG--AYHGKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
64-490 |
3.28e-23 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 101.79 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 64 QRRARvLMRFIELVNDTIDELAELLSREHGK------TLADARGDVQrgieviefclGIPHLLK-------------GEY 124
Cdd:cd07133 21 ERRDR-LDRLKALLLDNQDALAEAISADFGHrsrhetLLAEILPSIA----------GIKHARKhlkkwmkpsrrhvGLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 125 TEGAgpgiDVYSLRQPLGVVAGITPFNFP---AMIPLwkAGpALACGNAFVLKPSERDPsvpvRLAELFIEagLPAGVFq 201
Cdd:cd07133 90 FLPA----KAEVEYQPLGVVGIIVPWNYPlylALGPL--IA-ALAAGNRVMIKPSEFTP----RTSALLAE--LLAEYF- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 202 vvhgdkeavdailhHPDIKAVgFVGSSDIAQY---------IYAGAAATGK---RAQC---------FGGaKNHMIVMPD 260
Cdd:cd07133 156 --------------DEDEVAV-VTGGADVAAAfsslpfdhlLFTGSTAVGRhvmRAAAenltpvtleLGG-KSPAIIAPD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 261 ADLDQAVDALIGAGYGSAGERCMAIS-VAVPVG--DQTAERLRARLIERInnlrvGHSLDPKaDYGPLVTGAALARVRDY 337
Cdd:cd07133 220 ADLAKAAERIAFGKLLNAGQTCVAPDyVLVPEDklEEFVAAAKAAVAKMY-----PTLADNP-DYTSIINERHYARLQGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 338 IGQGVAAGAELVVdgrdrasddltfgLPEGDANLEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPS 417
Cdd:cd07133 294 LEDARAKGARVIE-------------LNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYIN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 418 EHE-----YgngvaIFTRDGDAARDFVSRVQVGMVGVNVPIpVPVAYHT--FGGWKRSGFGdlNQHGPAAIQFYTKVKTV 490
Cdd:cd07133 361 ARPrplalY-----YFGEDKAEQDRVLRRTHSGGVTINDTL-LHVAQDDlpFGGVGASGMG--AYHGKEGFLTFSHAKPV 432
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
5-439 |
1.29e-21 |
|
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: 97.73 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 5 ISHFIDGQRTAGQsTRSADVFDPNTGQIQAKVPMAGkSDIDAAVASAVE-AQKGWAAWNPQRRARVLMRFIELVNDTIDE 83
Cdd:cd07128 1 LQSYVAGQWHAGT-GDGRTLHDAVTGEVVARVSSEG-LDFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 84 LAELlSREHGKTLADARGDVQRGIEVIEFCLGI--------PHLLKGE----YTEGAGPGIDVYSLRQplGVVAGITPFN 151
Cdd:cd07128 79 LYAL-SAATGATRRDSWIDIDGGIGTLFAYASLgrrelpnaHFLVEGDveplSKDGTFVGQHILTPRR--GVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 152 FPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAG-LPAGVFQVVHGDkeaVDAILHHPDIK-AVGFVGSSD 229
Cdd:cd07128 156 FPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGDLLDHLGEQdVVAFTGSAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 230 IAQYIYAGAAATGKRAQCFGGAK--NHMIVMPDADLDQ-AVDALIGAGY----GSAGERCMAI-SVAVPVG--DQTAERL 299
Cdd:cd07128 233 TAAKLRAHPNIVARSIRFNAEADslNAAILGPDATPGTpEFDLFVKEVAremtVKAGQKCTAIrRAFVPEArvDAVIEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 300 RARLieriNNLRVGHSLDPKADYGPLVTGAALARVRDYIGQgVAAGAELVVDGRDRASddltfglpEGDANLEGGFFIGP 379
Cdd:cd07128 313 KARL----AKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFE--------VVGADAEKGAFFPP 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498938 380 TLF------DHVAAHmsiyTDEIFGPVLCMVRARDYEEALRLPSEheyGNG--VA-IFTRDGDAARDFV 439
Cdd:cd07128 380 TLLlcddpdAATAVH----DVEAFGPVATLMPYDSLAEAIELAAR---GRGslVAsVVTNDPAFARELV 441
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
135-477 |
4.11e-21 |
|
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: 95.65 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 135 YSLRQPLGVVAGITPFNFP---AMIPLwkAGpALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEAVD 211
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPfqlALAPL--IG-AIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 212 AILHHP-DikAVGFVGSSDIAQYIYAGAA-----ATGKraqcFGGaKNHMIVMPDADLDQAVDALIGAGYGSAGERCMAi 285
Cdd:cd07136 171 ELLDQKfD--YIFFTGSVRVGKIVMEAAAkhltpVTLE----LGG-KSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 286 svavP----VGDQTAERLRARLIERINNLRVGHSLDPKaDYGPLVTGAALARVRDYIGQGvaagaelvvdgrdrasdDLT 361
Cdd:cd07136 243 ----PdyvlVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----------------KIV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 362 FGlpeGDANlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHE-----YgngvaIFTRDGDAAR 436
Cdd:cd07136 301 FG---GNTD-RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEK 371
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489498938 437 DFVSRVQVGMVGVNVPIpVPVA--YHTFGGWKRSGFGdlNQHG 477
Cdd:cd07136 372 KVLENLSFGGGCINDTI-MHLAnpYLPFGGVGNSGMG--SYHG 411
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
44-415 |
5.61e-21 |
|
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: 95.30 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 44 IDAAVASAVEAQKGWAAWNPQRRArvlmRFIELVNDTIDELA-ELLSREHGKT-LADARGDVQRGIEVIEFCLGIPHLLK 121
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRA----AFLEAIADEIEALGdELVARAHAETgLPEARLQGELGRTTGQLRLFADLVRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 122 GEYTE----------GAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLwkAG----PALACGNAFVLKPSERDPSVPVRLA 187
Cdd:cd07129 77 GSWLDaridpadpdrQPLPRPDLRRMLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 188 ELFIEA----GLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSsdiaqyiYAGAAATGKRAQC-------FG--GAKN 253
Cdd:cd07129 155 RAIRAAlratGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGS-------RRGGRALFDAAAArpepipfYAelGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 254 HMIVMPDA---DLDQAVDALIGAGYGSAGERCMAISVAVPVGDQTAERLRARLIERINnlrvghsldpKADYGPLVTgaa 330
Cdd:cd07129 228 PVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAGDAFIAALAEALA----------AAPAQTMLT--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 331 lARVRDYIGQGVAA-----GAELVVDGrdrasddltfglpegdANLEGGFFIGPTLF----DHVAAHmSIYTDEIFGPVL 401
Cdd:cd07129 295 -PGIAEAYRQGVEAlaaapGVRVLAGG----------------AAAEGGNQAAPTLFkvdaAAFLAD-PALQEEVFGPAS 356
|
410
....*....|....
gi 489498938 402 CMVRARDYEEALRL 415
Cdd:cd07129 357 LVVRYDDAAELLAV 370
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
133-477 |
2.80e-18 |
|
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: 87.28 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 133 DVYSLRQPLGVVAGITPFNFP---AMIPLwkAGpALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEA 209
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYPlqlTLVPL--VG-AIAAGNCVVIKPSEVSPATAKLLAEL-IPKYLDKECYPVVLGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 210 VDAILHHpDIKAVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYGSAGERCMA---IS 286
Cdd:cd07132 169 TTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 287 VAVPVGDQTAERLRARLIERINNlrvghslDPK--ADYGPLVTGAALARVRDYI-GQGVAAGAElvVDGRDRasddltfg 363
Cdd:cd07132 248 CTPEVQEKFVEALKKTLKEFYGE-------DPKesPDYGRIINDRHFQRLKKLLsGGKVAIGGQ--TDEKER-------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 364 lpegdanleggfFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQ 443
Cdd:cd07132 311 ------------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
330 340 350
....*....|....*....|....*....|....*.
gi 489498938 444 VGMVGVNVPIpVPVAYHT--FGGWKRSGFGdlNQHG 477
Cdd:cd07132 379 SGGVCVNDTI-MHYTLDSlpFGGVGNSGMG--AYHG 411
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
139-493 |
3.49e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 87.02 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 139 QPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEAVDAILHHPD 218
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 219 IKaVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGYG-SAGERCMAisvavPVGDQTAE 297
Cdd:PLN02174 190 DK-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACIS-----PDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 298 RLRARLIERIN-NLRVGHSLDP--KADYGPLVTGAALARVRDYIGQgvaagaelvvdgrDRASDDLTFGLPEGDANLEgg 374
Cdd:PLN02174 264 EYAPKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE-------------KEVSDKIVYGGEKDRENLK-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 375 ffIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNvPIP 454
Cdd:PLN02174 329 --IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIA 405
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489498938 455 VPVAYHT--FGGWKRSGFGDLnqHGPAAIQFYTKVKTVTSR 493
Cdd:PLN02174 406 VHLALHTlpFGGVGESGMGAY--HGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
44-456 |
2.18e-16 |
|
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: 81.16 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 44 IDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARgdVQRGIEVIEfclGIPHLLKGE 123
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDK--VIKNHFAAE---YIYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 124 YTEGAGPGIDVY---SLRQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAG-- 198
Cdd:cd07081 76 KTCGVLTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGap 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 199 ---VFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQyiyaGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGAGY 275
Cdd:cd07081 156 enlIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 276 GSAGERCmAISVAVPVGDQTAERLRARLIERinnlrvghsldpkadYGPLVTGAALARVRDYIGQGVAAGAELVvdGRD- 354
Cdd:cd07081 232 FDNGVIC-ASEQSVIVVDSVYDEVMRLFEGQ---------------GAYKLTAEELQQVQPVILKNGDVNRDIV--GQDa 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 355 -RASDDLTFGLPEgdanlEGGFFIGPTLfdhVAAHMSIYTDEIFGPVLCMVRARDYEE----ALRLPSEHEYGNGVAIFT 429
Cdd:cd07081 294 yKIAAAAGLKVPQ-----ETRILIGEVT---SLAEHEPFAHEKLSPVLAMYRAANFADadakALALKLEGGCGHTSAMYS 365
|
410 420
....*....|....*....|....*..
gi 489498938 430 RDgDAARDFVSRVQVGMVGVNVPIPVP 456
Cdd:cd07081 366 DN-IKAIENMNQFANAMKTSRFVKNGP 391
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
139-493 |
3.59e-16 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 80.93 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 139 QPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELfIEAGLPAGVFQVVHGDKEAVDAILHHPD 218
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAAN-IPKYLDSKAVKVIEGGPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 219 IKaVGFVGSSDIAQYIYAGAAATGKRAQCFGGAKNHMIV---MPDADLDQAVDALIGAGYGS-AGERCMAISVaVPVGDQ 294
Cdd:PLN02203 186 DK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDY-VLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 295 TAERLRARLIERINNLRVGHSLDPKadygplvtgaALARVRDyiGQGVAAGAELVVDGRDRASddLTFGlpeGDANlEGG 374
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESK----------SMARILN--KKHFQRLSNLLKDPRVAAS--IVHG---GSID-EKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 375 FFIGPTLFDHVAAHMSIYTDEIFGPVLCMVRARDYEEALRLPSEHEYGNGVAIFTRDGDAARDFVSRVQVGMVGVNVPIp 454
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI- 404
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489498938 455 vpVAYHT----FGGWKRSGFGdlNQHGPAAIQFYTKVKTVTSR 493
Cdd:PLN02203 405 --IQYACdslpFGGVGESGFG--RYHGKYSFDTFSHEKAVLRR 443
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
44-464 |
7.85e-16 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 79.46 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 44 IDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGktladaRGDVQRGIEVIEF-CLGIPHLLKG 122
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETG------MGVVEDKVIKNHFaSEYVYNDIKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 123 EYTEG-----AGPGIDVYSlrQPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAEL----FIEA 193
Cdd:cd07122 75 MKTVGvieedEEKGIVEIA--EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 194 GLPAGVFQVV-HGDKEAVDAILHHPDIKAV------GFVGSsdiaqyiyagAAATGKRAQCfGGAKN-HMIVMPDADLDQ 265
Cdd:cd07122 153 GAPEGLIQWIeEPSIELTQELMKHPDVDLIlatggpGMVKA----------AYSSGKPAIG-VGPGNvPAYIDETADIKR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 266 AVDALIGA-----GYGSAGERcmAISVAVPVGDQTAERLRAR--------LIERINN--LRVGHSLDPKAdygplvtgaa 330
Cdd:cd07122 222 AVKDIILSktfdnGTICASEQ--SVIVDDEIYDEVRAELKRRgayflneeEKEKLEKalFDDGGTLNPDI---------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 331 larvrdyIGQGVAAGAELVvdGrdrasddltFGLPEgDANleggFFIGPtlFDHVaAHMSIYTDEIFGPVLCMVRARDYE 410
Cdd:cd07122 290 -------VGKSAQKIAELA--G---------IEVPE-DTK----VLVAE--ETGV-GPEEPLSREKLSPVLAFYRAEDFE 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489498938 411 EALRLPSE--HEYGNG--VAIFTRDGDAARDFVSRVQVGMVGVNVPipvpvayHTFGG 464
Cdd:cd07122 344 EALEKAREllEYGGAGhtAVIHSNDEEVIEEFALRMPVSRILVNTP-------SSLGG 394
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
17-232 |
3.32e-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: 77.92 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 17 QSTRSADVFDPNTGQIQAKVPMAGKSDIDAAVASAVEAQKGW---AAWNPQR---------RARVLMRFIELVndtiDEL 84
Cdd:cd07126 9 GASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhnPLKNPERyllygdvshRVAHELRKPEVE----DFF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 85 AELLSREHGKTLADARGDV---QRGIEviEFCLGIPHLLKGEYT-EGAGPGIDVYSLRQPLGVVAGITPFNFPAMIPLWK 160
Cdd:cd07126 85 ARLIQRVAPKSDAQALGEVvvtRKFLE--NFAGDQVRFLARSFNvPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498938 161 AGPALACGNAFVLKPSERDPSVPVRLAELFIEAGLPAGVFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQ 232
Cdd:cd07126 163 LMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAE 234
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
49-267 |
1.73e-13 |
|
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: 72.26 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 49 ASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTLADARGDVQRGIEVIEFCL--------GIPH-- 118
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLyknidterGITAsv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 119 -LLKGEYTEGAGpgiDVYSLRQPLGVVAGITPFNFPAMIPLwKAGPALACGNAFVLKPSERDPSVPVRLAELFIEAgLPA 197
Cdd:cd07077 81 gHIQDVLLPDNG---ETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-DAA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489498938 198 G-----VFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAQYIYagAAATGKRAQCFGGAKNHMIVMPDADLDQAV 267
Cdd:cd07077 156 HgpkilVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAV--KHSPHIPVIGFGAGNSPVVVDETADEERAS 228
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
42-423 |
6.22e-09 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 58.02 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 42 SDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGktladaRGDVQRGIE----VIEFCLGIP 117
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG------MGRVEDKIAknhlAAEKTPGTE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 118 HLLKGEYTEGAGPGIDVYSlrqPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELF----IEA 193
Cdd:cd07121 78 DLTTTAWSGDNGLTLVEYA---PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELInkaiAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 194 GLPAGVFQVVHG-DKEAVDAILHHPDIKAVGFVGSSDIAQyiyaGAAATGKRAQCFGGAKNHMIVMPDADLDQ-AVDALI 271
Cdd:cd07121 155 GGPDNLVVTVEEpTIETTNELMAHPDINLLVVTGGPAVVK----AALSSGKKAIGAGAGNPPVVVDETADIEKaARDIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 272 GAGYGS----AGE--------------RCMAISVAVPVGDQTAERLRARLierinnlrvghsldpkadygpLVTGAALAR 333
Cdd:cd07121 231 GASFDNnlpcIAEkeviavdsvadyliAAMQRNGAYVLNDEQAEQLLEVV---------------------LLTNKGATP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 334 VRDYIGQG---VAAGAELVVDGRDRasddltfglpegdanleggffigpTLFDHVAAHMSIYTDEIFGPVLCMVRARDYE 410
Cdd:cd07121 290 NKKWVGKDaskILKAAGIEVPADIR------------------------LIIVETDKDHPFVVEEQMMPILPVVRVKNFD 345
|
410
....*....|...
gi 489498938 411 EALRLPSEHEYGN 423
Cdd:cd07121 346 EAIELAVELEHGN 358
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
41-443 |
3.17e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 55.95 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 41 KSDIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGKTL-----ADARGDVQRGIEVIEFCL- 114
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFmmafqAGGPHAQDRGLEAVAYAWr 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 115 ---GIPHLLKGEYTEGAGPGIDVYSLRQP----LGVVAGITPFnfpamiPLWKAGPA----LACGNAFVLKPSERD--P- 180
Cdd:cd07127 163 emsRIPPTAEWEKPQGKHDPLAMEKTFTVvprgVALVIGCSTF------PTWNGYPGlfasLATGNPVIVKPHPAAilPl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 181 SVPVRLA-ELFIEAGL-PAGVFQVVHGDKEAVDAIL-HHPDIKAVGFVGSSDIAQYIYAGAaatgKRAQCFG--GAKNHM 255
Cdd:cd07127 237 AITVQVArEVLAEAGFdPNLVTLAADTPEEPIAQTLaTRPEVRIIDFTGSNAFGDWLEANA----RQAQVYTekAGVNTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 256 IVMPDADLDQAVDALIGAGYGSAGERCMAI-SVAVPV-GDQTAERLR------ARLIERINNLrvghSLDPK---ADYGP 324
Cdd:cd07127 313 VVDSTDDLKAMLRNLAFSLSLYSGQMCTTPqNIYVPRdGIQTDDGRKsfdevaADLAAAIDGL----LADPAraaALLGA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 325 LVTGAALARVRDyigqgVAAGAELVVDGRDRASDDLtfglpegdanlEGGFFIGPTLFDHVAAHMSIYTDEIFGPVLCMV 404
Cdd:cd07127 389 IQSPDTLARIAE-----ARQLGEVLLASEAVAHPEF-----------PDARVRTPLLLKLDASDEAAYAEERFGPIAFVV 452
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489498938 405 RARDYEEALRLPSEHEYGNG---VAIFTRDgdaaRDFVSRVQ 443
Cdd:cd07127 453 ATDSTDHSIELARESVREHGamtVGVYSTD----PEVVERVQ 490
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
43-423 |
1.04e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 54.14 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 43 DIDAAVASAVEAQKGWAAWNPQRRARVLMRFIELVNDTIDELAELLSREHGktladaRGDVQRGIE----VIEFCLGIPH 118
Cdd:PRK15398 37 SVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG------MGRVEDKIAknvaAAEKTPGVED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 119 LLKGEYTEGAGPGIDVYSlrqPLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELF----IEAG 194
Cdd:PRK15398 111 LTTEALTGDNGLTLIEYA---PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLneaiVAAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 195 LPAG-VFQVVHGDKEAVDAILHHPDIKAVGFVGSSDIAqyiyAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALI-G 272
Cdd:PRK15398 188 GPENlVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVV----KAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVkG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 273 AGYGS----AGERCMaisVAVpvgDQTAERLrarlierINNLRVGHSLdpkadygpLVTGAALARVRDY-IGQGVAAGAE 347
Cdd:PRK15398 264 ASFDNnlpcIAEKEV---IVV---DSVADEL-------MRLMEKNGAV--------LLTAEQAEKLQKVvLKNGGTVNKK 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489498938 348 LVvdGRDRASDDLTFGLpEGDANLEggFFIGPTLFDHVAAhmsiyTDEIFGPVLCMVRARDYEEALRLPSEHEYGN 423
Cdd:PRK15398 323 WV--GKDAAKILEAAGI-NVPKDTR--LLIVETDANHPFV-----VTELMMPVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
135-270 |
3.54e-07 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 52.44 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 135 YSLRQPLGVVAGITPFNFPaMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIE---AGLPAGVFQVVH---GDKE 208
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVP-LLPVMSILMGLLVKNVNLLKVSSSDPFTAAALLASFADldpTHPLADSLSVVYwdgGSTQ 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498938 209 AVDAILHHPDikAVGFVGSSDIAQYIyAGAAATGKRAQCFGGAKNHMIVMPDADLDQAVDAL 270
Cdd:pfam05893 162 LEDLIVANAD--VVIAWGGEDAINAI-RECLKPGKQWIDFGAKISFAVVDREAALDKAAERA 220
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
140-452 |
9.61e-06 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 48.26 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 140 PLGVVAGITPFNFPAMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELF----IEAGLPAGVFQVV-HGDKEAVDAIL 214
Cdd:PRK13805 108 PVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVldaaVAAGAPKDIIQWIeEPSVELTNALM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 215 HHPDIKAV------GFVGSsdiaqyiyagAAATGKRAQCFGGAKNHMIVMPDADLDQAVDALIGA-----GYGSAGERcm 283
Cdd:PRK13805 188 NHPGIALIlatggpGMVKA----------AYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSktfdnGMICASEQ-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 284 aisvAVPVGDQTAERLRARLIERinnlrvghsldpKAdYgpLVTGAALARVRDYI-------------GQGVAAGAELVv 350
Cdd:PRK13805 256 ----AVIVDDEIYDEVKEEFASH------------GA-Y--FLNKKELKKLEKFIfgkengalnadivGQSAYKIAEMA- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 351 dGrdrasddltFGLPEGD----ANLEGgffIGPtlfDHVAAHmsiytdEIFGPVLCMVRARDYEEALRLPSE----HEYG 422
Cdd:PRK13805 316 -G---------FKVPEDTkiliAEVKG---VGE---SEPLSH------EKLSPVLAMYKAKDFEDAVEKAEKlvefGGLG 373
|
330 340 350
....*....|....*....|....*....|
gi 489498938 423 NGVAIFTRDGDAARDFVSRVQVGMVGVNVP 452
Cdd:PRK13805 374 HTAVIYTNDDELIKEFGLRMKACRILVNTP 403
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
114-218 |
5.44e-04 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 42.26 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498938 114 LGIPHLLKGEYTEGAGPgidvYSLRQPLGVVAGITPFNFPaMIPLWKAGPALACGNAFVLKPSERDPSVPVRLAELFIEA 193
Cdd:cd07080 90 LGSPGILDEWVPPGRGG----YIRAQPRGLVVHIIAGNVP-LLPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADV 164
|
90 100 110
....*....|....*....|....*....|.
gi 489498938 194 GLPAGV---FQVV---HGDKEAVDAILHHPD 218
Cdd:cd07080 165 DPNHPLtdsISVVywpGGDAELEERILASAD 195
|
|
| |
