|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-482 |
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: 806.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 4 IGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDEL 83
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 84 AEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVPVGaETANRLVEKLIPKIESLRIGPYTDDQADMGP 323
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVG-DEADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 324 LVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSL 403
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGDLNQHGTDSIKFWTKTKTVTARW 482
Cdd:cd07085 400 INANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-482 |
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: 603.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 4 IGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDEL 83
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 84 AEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVPVGAetANRLVEKLIPKIESLRIGPYTDDQADMGP 323
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA--ADEWVPEIRERAEKIRIGPGDDPGAEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 324 LVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSL 403
Cdd:TIGR01722 319 LITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIAL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGDLNQHGTDSIKFWTKTKTVTARW 482
Cdd:TIGR01722 399 INASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-482 |
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: 584.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 2 REIGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMD 81
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 82 ELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 162 PAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMN 240
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 241 GKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQAD 320
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLL-VHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 321 MGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEA 400
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 401 LSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGDlnQHGTDSIKFWTKTKTVTA 480
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTI 477
|
..
gi 930192169 481 RW 482
Cdd:COG1012 478 RL 479
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-496 |
2.02e-172 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 498.89 E-value: 2.02e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 4 IGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDEL 83
Cdd:PLN02419 114 VPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 84 AEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVPVGaeTANRLVEKLIPKIESLRIGPYTDDQADMGP 323
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVG--DAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 324 LVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSL 403
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGDLNQHGTDSIKFWTKTKTVTARWP 483
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|...
gi 930192169 484 SgIKSGAEFVMPT 496
Cdd:PLN02419 592 D-IHSPFSLAIPI 603
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
13-478 |
1.95e-167 |
|
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: 480.49 E-value: 1.95e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 13 VAGTSGRVSnVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHG 92
Cdd:pfam00171 2 VDSESETIE-VINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 93 KTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAgPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFIL 172
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 173 KPSERDPSLPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAK 251
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 252 NHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYT 331
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLL-VHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 332 RVRGLIDRGVEEGAKLLVDGRDfklqGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGN 411
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 412 GVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGDLNqhGTDSIKFWTKTKTV 478
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-478 |
1.27e-135 |
|
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: 400.09 E-value: 1.27e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 6 HFIGGKQVAGTSGRVsnVYNPA-TGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07097 3 NYIDGEWVAGGDGEE--NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 165 ACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGP 323
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLI-VTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 324 LVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSL 403
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGE--RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIpVPLAYHS-FGGWKASSFGDLNQhGTDSIKFWTKTKTV 478
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPT-AGVDYHVpFGGRKGSSYGPREQ-GEAALEFYTTIKTV 471
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
45-480 |
3.08e-134 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 395.04 E-value: 3.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 45 AAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCG-IPHLAKGEF 123
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGlARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 124 TEGAGPAiDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVN 203
Cdd:cd07078 82 PSPDPGE-LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 204 GDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCM 282
Cdd:cd07078 161 GDGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 283 AISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGrdfKLQGYEDG 362
Cdd:cd07078 241 AASR-LLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 363 YFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIP 442
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 930192169 443 VPLAYHSFGGWKASSFGdlNQHGTDSIKFWTKTKTVTA 480
Cdd:cd07078 397 GAEPSAPFGGVKQSGIG--REGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-479 |
2.87e-125 |
|
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: 373.99 E-value: 2.87e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 6 HFIGGKQVAGTSGRVSNVYNPATG-EVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 165 ACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGP 323
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLI-VHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 324 LVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSL 403
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGdLNQHGTDSIKFWTKTKTVT 479
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG-HREAGTTALDAFTEWKAVY 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-479 |
1.46e-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: 341.08 E-value: 1.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 6 HFIGGKQVAGTSGRVSNvYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAE 85
Cdd:cd07086 1 GVIGGEWVGSGGETFTS-RNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 86 MLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIA 165
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 166 CGNAFILKPSERDPSLPIRLAELMIEA----GLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNG 241
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 242 KRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADM 321
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-VHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 322 GPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEAL 401
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 402 SLPMKHEYGNGVAIYTRDGDAARDFASR---------INIGMIGINVPIPvplayhsFGGWKASSFGdlNQHGTDSIKFW 472
Cdd:cd07086 397 AINNDVPQGLSSSIFTEDLREAFRWLGPkgsdcgivnVNIPTSGAEIGGA-------FGGEKETGGG--RESGSDAWKQY 467
|
....*..
gi 930192169 473 TKTKTVT 479
Cdd:cd07086 468 MRRSTCT 474
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
23-478 |
4.42e-111 |
|
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: 336.58 E-value: 4.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVCGIPHLAKGEFTEGAGPAIdMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLP 182
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 183 IRLAELMIEAGLPAGILNVVNGDkGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGG-GETGQLLCeHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 262 MDQAVNALMGAGYGSAGERCM-AISVAVPVGaeTANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRG 340
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSnGTRVFVQRS--IKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 341 VEEGAKLLVDGRDFKLQ-GYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRD 419
Cdd:cd07090 317 KQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930192169 420 GDAARDFASRINIGMIGIN----VPIPVPlayhsFGGWKASSFGDLNqhGTDSIKFWTKTKTV 478
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
23-459 |
3.79e-109 |
|
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: 331.70 E-value: 3.79e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVCGiphLAK---GEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP 179
Cdd:cd07103 81 DYAASFLEWFAE---EARriyGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 180 SLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAqCF--GGaknH--M 254
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV-SLelGG---NapF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 255 IIMPDADMDQAVNALMGAGYGSAGERCMA---ISVAVPVgaetANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYT 331
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCVCanrIYVHESI----YDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 332 RVRGLIDRGVEEGAKLLVDGRDFKLqgyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGN 411
Cdd:cd07103 310 KVEALVEDAVAKGAKVLTGGKRLGL----GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 930192169 412 GVAIYTRDGDAARDFASRINIGMIGINVPIPvPLAYHSFGGWKASSFG 459
Cdd:cd07103 386 AAYVFTRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKESGLG 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
23-479 |
4.35e-109 |
|
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: 331.45 E-value: 4.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAK-GD 101
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 VIRGLEVCEFVCG-IPHLAkGEFTEGAGPAIDmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPS 180
Cdd:cd07093 81 IPRAAANFRFFADyILQLD-GESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 181 LPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPD 259
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 260 ADMDQAVNALMGAGYGSAGERCMAIS---VAVPVgaetANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGL 336
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSrilVQRSI----YDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 337 IDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIY 416
Cdd:cd07093 315 VELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 417 TRDGDAARDFASRINIGMIGINVPI----PVPlayhsFGGWKASSFGdlNQHGTDSIKFWTKTKTVT 479
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLvrdlRTP-----FGGVKASGIG--REGGDYSLEFYTELKNVC 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-478 |
6.14e-108 |
|
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: 329.23 E-value: 6.14e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIAC 166
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 167 GNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDkGAV--DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRA 244
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGR-GSVvgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 245 QCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPL 324
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAER-VYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 325 VTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGyedGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLP 404
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 405 MKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPL-AYHSfgGWKASSF-GDLNQHGtdsIKFWTKTKTV 478
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMqGFHA--GWKKSGLgGADGKHG---LEEYLQTKVV 466
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
25-478 |
8.39e-107 |
|
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: 325.55 E-value: 8.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 25 NPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKG-DVI 103
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 104 RGLEVCEFVCGIPHLAKGEFTEGAGPAIDmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPI 183
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLN-YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 184 RLAELMIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTG-FGEVagAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 262 MDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGV 341
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGS-RLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 342 EEGAKLLVDGRdfklQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGD 421
Cdd:cd07115 320 EEGARLLTGGK----RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930192169 422 AARDFASRINIGMIGIN----VPIPVPlayhsFGGWKASSFGdlNQHGTDSIKFWTKTKTV 478
Cdd:cd07115 396 RAHRVAAALKAGTVWINtynrFDPGSP-----FGGYKQSGFG--REMGREALDEYTEVKSV 449
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
23-479 |
7.13e-106 |
|
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: 323.13 E-value: 7.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLP 182
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 183 IRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 262 MDQAVNAlmgAGYGS---AGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLID 338
Cdd:cd07150 243 LDYAVRA---AAFGAfmhQGQICMSAS-RIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 339 RGVEEGAKLLVDgrdfklqGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTR 418
Cdd:cd07150 319 DAVAKGAKLLTG-------GKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930192169 419 DGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGdlNQHGTDSIKFWTKTKTVT 479
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG--REGGEWSMEEFTELKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
42-479 |
7.80e-105 |
|
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: 319.86 E-value: 7.80e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 42 ELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKG 121
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 122 EFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP-SLPIRLAELMIEAGLPAGILN 200
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvTGGLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 201 VVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVN-ALMGAgYGSAG 278
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSaAAFGA-FLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 279 ERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfklqg 358
Cdd:cd07104 240 QICMAAG-RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT------ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 359 yEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN 438
Cdd:cd07104 313 -YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 930192169 439 VPIPVPLAYHSFGGWKASSFGDLNqhGTDSIKFWTKTKTVT 479
Cdd:cd07104 392 DQTVNDEPHVPFGGVKASGGGRFG--GPASLEEFTEWQWIT 430
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
50-480 |
5.84e-103 |
|
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: 312.63 E-value: 5.84e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 50 AKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGP 129
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 130 AIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGD-KGA 208
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGgDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 209 VDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvav 288
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 289 pvgaetanrlveklipkieslRIgpytddqadmgpLVTKDAYTRVrglIDRGVeegakllvdgrdfklqgyedgyfvggC 368
Cdd:cd06534 240 ---------------------RL------------LVHESIYDEF---VEKLV--------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 369 LFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYH 448
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA 337
|
410 420 430
....*....|....*....|....*....|..
gi 930192169 449 SFGGWKASSFGdlNQHGTDSIKFWTKTKTVTA 480
Cdd:cd06534 338 PFGGVKNSGIG--REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
23-478 |
1.04e-102 |
|
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: 315.26 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKG 100
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 101 DVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPS 180
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 181 LPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTD-PDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPD 259
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEhPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 260 ADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDR 339
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLL-VQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 340 GVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRD 419
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930192169 420 GDAARDFASRINIGMIGINvpipvplAYHS------FGGWKASSFGDLNqhGTDSIKFWTKTKTV 478
Cdd:cd07114 400 LARAHRVARAIEAGTVWVN-------TYRAlspsspFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-478 |
2.53e-102 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 315.28 E-value: 2.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 6 HFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAE 85
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 86 MLSKEHGKTIEDAK-GDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIdMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:PRK13252 89 LETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQIACWKSAPAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 165 ACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDkGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:PRK13252 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTeHPDIAKVSFTGGVPTGKKVMAAAAASLKE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCM-AISVAVPvgAETANRLVEKLIPKIESLRIGPYTDDQADMG 322
Cdd:PRK13252 247 VTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVFVQ--KSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 323 PLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALS 402
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 403 LPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINV----PIPVPlayhsFGGWKASSFGDLNqhGTDSIKFWTKTKTV 478
Cdd:PRK13252 405 RANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgesPAEMP-----VGGYKQSGIGREN--GIATLEHYTQIKSV 477
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-468 |
1.29e-100 |
|
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: 310.78 E-value: 1.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 165 ACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 244 AQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGP 323
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLL-VEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 324 LVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSL 403
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930192169 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINvpipvplAYH------SFGGWKASSFG-DLNQHGTDS 468
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN-------DYHpyfaeaPWGGYKQSGIGrELGPTGLEE 463
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-482 |
4.20e-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: 306.68 E-value: 4.20e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 5 GHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA-QPKWAATNPQRRARVFFKFVELLNKHMDEL 83
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 84 AEMLSKEHGKTIEdakgdVIRGLEVCEFVCGIPHLAkGEFTEGAGPAIDM------------YSIRQPVGIGAGITPFNF 151
Cdd:cd07113 81 AQLETLCSGKSIH-----LSRAFEVGQSANFLRYFA-GWATKINGETLAPsipsmqgerytaFTRREPVGVVAGIVPWNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 152 PGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGdKGAVDAILT-DPDIGAVSFVGSTPIA 230
Cdd:cd07113 155 SVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLIsHPDVAKVSFTGSVATG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 231 RYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCmAISVAVPVGAETANRLVEKLIPKIESLR 310
Cdd:cd07113 234 KKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSKFDELVTKLKQALSSFQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 311 IGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLS 390
Cdd:cd07113 313 VGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLMREETFGPVVS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 391 VVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN----VPIPVPlayhsFGGWKASSFGdlNQHGT 466
Cdd:cd07113 389 FVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfLDPAVP-----FGGMKQSGIG--REFGS 461
|
490
....*....|....*.
gi 930192169 467 DSIKFWTKTKTVTARW 482
Cdd:cd07113 462 AFIDDYTELKSVMIRY 477
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
10-479 |
4.92e-95 |
|
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: 295.75 E-value: 4.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 10 GKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSK 89
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 90 EHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNA 169
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 170 FILKPSERDP-SLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCF 247
Cdd:cd07151 161 VVLKPASDTPiTGGLLLAKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 248 GGAKNHMIIMPDADMDQAVN-ALMGAgYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVT 326
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNaAVFGK-FLHQGQICMAIN-RIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLIN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 327 KDAYTRVRGLIDRGVEEGAKLLVDGRdfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMK 406
Cdd:cd07151 319 ESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 407 HEYGNGVAIYTRDGDAARDFASRINIGMIGINvPIPV---PLAyhSFGGWKASSFGDLNqhGTDSIKFWTKTKTVT 479
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVndePHV--PFGGEKNSGLGRFN--GEWALEEFTTDKWIS 462
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
6-456 |
7.47e-95 |
|
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: 295.18 E-value: 7.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 6 HFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAE 85
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 86 MLSKEHGKTIEDAKGDVIRglevcefvCGIPHLAKG-------EFTEGAGPAIdmySIRQPVGIGAGITPFNFPGMIPMW 158
Cdd:cd07138 81 AITLEMGAPITLARAAQVG--------LGIGHLRAAadalkdfEFEERRGNSL---VVREPIGVCGLITPWNWPLNQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 159 MFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDkGAV--DAILTDPDIGAVSFVGSTPIARYVYGT 236
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD-GPVvgEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 237 AAMNGKR-AQCFGGaKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAIS-VAVPVG--AETANRLVEKLipkiESLRIG 312
Cdd:cd07138 229 AADTVKRvALELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTrMLVPRSryAEAEEIAAAAA----EAYVVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 313 PYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVV 392
Cdd:cd07138 304 DPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSII 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930192169 393 RAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAyhSFGGWKAS 456
Cdd:cd07138 383 PYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS 444
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
5-479 |
1.14e-94 |
|
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: 295.27 E-value: 1.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 5 GHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDE 82
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 83 LAEMLSKEHGKTI-EDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIdMYSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:cd07091 85 LAALESLDNGKPLeESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFL-AYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 162 PAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGSTPIARYVYGTAA- 238
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPG-FGPTagAAISSHMDVDKIAFTGSTAVGRTIMEAAAk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 239 MNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQ 318
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS-RIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 319 ADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYE 398
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG----SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN--------VPipvplayhsFGGWKASSFG-DLnqhGTDSI 469
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvfdaaVP---------FGGFKQSGFGrEL---GEEGL 465
|
490
....*....|
gi 930192169 470 KFWTKTKTVT 479
Cdd:cd07091 466 EEYTQVKAVT 475
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-478 |
1.13e-93 |
|
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: 292.20 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 25 NPATGEVQATVALANVEELRAAVENAKAAQPK--WAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGL--------EVCEFVCG-IPHLAKGEFTegagpaidmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILK 173
Cdd:cd07112 88 VPSAantfrwyaEAIDKVYGeVAPTGPDALA---------LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 174 PSERDPSLPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTDPDIGAVSFVGSTPIARYVYGTAA-MNGKRAQCFGGAK 251
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFgHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 252 NHMIIMPDA-DMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAY 330
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS-RLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 331 TRVRGLIDRGVEEGAKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYG 410
Cdd:cd07112 318 DKVLGYIESGKAEGARLVAGGK--RVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYG 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930192169 411 NGVAIYTRDGDAARDFASRINIGMIGIN----VPIPVPlayhsFGGWKASSFG-DLNQHGTDSikfWTKTKTV 478
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGrDKSLHALDK---YTELKTT 460
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
7-481 |
1.39e-93 |
|
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: 292.17 E-value: 1.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVaGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNP-QRRARVFFKFVELLNKHMDELAE 85
Cdd:cd07082 5 LINGEWK-ESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 86 MLSKEHGKTIEDAKGDVIRGLE-----VCEFVCGIPHLAKGEFTEGAGPAIDMYSiRQPVGIGAGITPFNFPGMIPMWMF 160
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDyirdtIEELKRLDGDSLPGDWFPGTKGKIAQVR-REPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 161 APAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGSTPIARYVYGTAA 238
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTG-RGREigDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 239 MngKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDQ 318
Cdd:cd07082 242 M--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 319 ADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGrdfklqGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYE 398
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINvpipvplAYHS-------FGGWKASSFGDLNQHgtDSIKF 471
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN-------SKCQrgpdhfpFLGRKDSGIGTQGIG--DALRS 463
|
490
....*....|
gi 930192169 472 WTKTKTVTAR 481
Cdd:cd07082 464 MTRRKGIVIN 473
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
4-478 |
2.35e-92 |
|
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: 289.31 E-value: 2.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 4 IGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA-QPKWAATNPQRRARVFFKFVELLNKHMDE 82
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 83 LAEMLSKEHGKTIE-DAKGDVIRGLEVCEFVCGIPHLAKGEfTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:cd07144 88 LAAIEALDSGKPYHsNALGDLDEIIAVIRYYAGWADKIQGK-TIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 162 PAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 NGKRAQCFGGAKNHMIIMPDADMDQAVN-ALMGAGYGSaGERCMAISvAVPVGAETANRLVEKLIPKI-ESLRIGPYTDD 317
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKwAAAGIMYNS-GQNCTATS-RIYVQESIYDKFVEKFVEHVkQNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 318 QADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGrDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNY 397
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGG-EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 398 EEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVP----IPVPlayhsFGGWKASSFG-DLNQHGTDSikfW 472
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIGrELGEYGLET---Y 474
|
....*.
gi 930192169 473 TKTKTV 478
Cdd:cd07144 475 TQTKAV 480
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-468 |
1.77e-90 |
|
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: 285.27 E-value: 1.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 2 REIGHFIGGKQVaGTSGRVSNVyNPA-TGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHM 80
Cdd:cd07124 31 REYPLVIGGKEV-RTEEKIESR-NPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 81 DELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGeFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMF 160
Cdd:cd07124 109 FELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRG-FPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 161 APAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07124 188 TAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 ------NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGP 313
Cdd:cd07124 268 vqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVI-VHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 314 YTDDQADMGPLVTKDAYTRVRGLIDRGVEEGaKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVR 393
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 394 AQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPL-AYHSFGGWKASsfgdlnqhGTDS 468
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALvGRQPFGGFKMS--------GTGS 491
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-481 |
6.15e-90 |
|
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: 282.34 E-value: 6.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVCGIPHLAKGEfTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLP 182
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 183 IRLAELMIEAgLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 262 MDQAVNALM-GAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRG 340
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRLF-VHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 341 VEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDG 420
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 421 DAARDFASRINIGMIGIN--------VPipvplayhsFGGWKASSFGdlNQHGTDSIKFWTKTKTVTAR 481
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssrhflgAP---------FGGVKNSGIG--REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
23-480 |
1.74e-89 |
|
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: 281.04 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWA-ATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGD 101
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 VIRGLEVCEFVCGIPHLAKGEfTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSL 181
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGE-TIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 182 PIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMP 258
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlgaEAGA--ALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 259 DADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDqADMGPLVTKDAYTRVRGLID 338
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGS-RLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 339 RGVEEGAKLLVDGRdfKLQG-YEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYT 417
Cdd:cd07109 316 RARARGARIVAGGR--IAEGaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930192169 418 RDGDAARDFASRINIGMIGINV-----PIPVPlayhsFGGWKASSFGdlNQHGTDSIKFWTKTKTVTA 480
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNygaggGIELP-----FGGVKKSGHG--REKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
23-468 |
1.79e-89 |
|
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: 281.16 E-value: 1.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAK--- 99
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 100 GDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP 179
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 180 SLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMP 258
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 259 DADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLID 338
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATS-RLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 339 RGVEEGAKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTR 418
Cdd:cd07110 320 RGKEEGARLLCGGR--RPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 930192169 419 DGDAARDFASRINIGMIGINVPIPVpLAYHSFGGWKASSFG-DLNQHGTDS 468
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGrELGEWGLDN 447
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
23-459 |
2.75e-89 |
|
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: 280.77 E-value: 2.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07145 3 VRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGL--------EVCEFVCGIPHLAKGEFTEGAgpaiDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKP 174
Cdd:cd07145 83 ERTIrlfklaaeEAKVLRGETIPVDAYEYNERR----IAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 175 SERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNH 253
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 254 MIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRV 333
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVK-RILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 334 RGLIDRGVEEGAKLLVDGRDfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGV 413
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 930192169 414 AIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFG 459
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-479 |
3.87e-88 |
|
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: 277.32 E-value: 3.87e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKwaaTNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVCGIPHLAKGE-----FTEGAGPAIdMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSER 177
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGEsfscdLTANGKARK-IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 178 DPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVygtAAMNGKRAQCFG-GAKNHMI 255
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIgDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLElGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 256 IMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRG 335
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVK-RILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 336 LIDRGVEEGAKLLVDGRdfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAI 415
Cdd:cd07146 315 RVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930192169 416 YTRDGDAARDFASRINIGMIGIN-VP------IPvplayhsFGGWKASSFGdLNQHGTDSIKFWTKTKTVT 479
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNeVPgfrselSP-------FGGVKDSGLG-GKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
7-479 |
1.31e-87 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 276.76 E-value: 1.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAK-GDVIRGLEVCEFVCGIphLAKGEFTE-----GAGPAIdmySIRQPVGIGAGITPFNFPGMIPMW 158
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAAL--ARDFPFEErrpgsGGGHVL---VRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 159 MFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAA 238
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 239 MNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAIS-VAVPvgAETANRLVEKLIPKIESLRIGPYTDD 317
Cdd:cd07139 237 ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTrILVP--RSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 318 QADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNY 397
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPA--GLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 398 EEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAyhSFGGWKASSFGdlNQHGTDSIKFWTKTKT 477
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA--PFGGFKQSGIG--REGGPEGLDAYLETKS 468
|
..
gi 930192169 478 VT 479
Cdd:cd07139 469 IY 470
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-459 |
5.61e-87 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 275.80 E-value: 5.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFP-GMIPMwMFAPAIA 165
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITR-KVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 166 CGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRA 244
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 245 QCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPL 324
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCAN-RILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 325 VTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQG--YEDGYFVGgclfdhVTPEMDIYKTEIFGPVLSVVRAQNYEEALS 402
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGtfYEPTVLGD------VTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 403 LPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIpVPLAYHSFGGWKASSFG 459
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLG 475
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
23-479 |
5.66e-87 |
|
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: 274.70 E-value: 5.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEfvcgiphLAKGEFTEGAGPAIDM-----------YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFI 171
Cdd:cd07094 83 DRAIDTLR-------LAAEEAERIRGEEIPLdatqgsdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 172 LKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVygTAAMNGKRAQCFGGA 250
Cdd:cd07094 156 LKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 251 KNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAY 330
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIY-VHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 331 TRVRGLIDRGVEEGAKLLvdgrdfkLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYG 410
Cdd:cd07094 313 ERVERWVEEAVEAGARLL-------CGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYG 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930192169 411 NGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFgdlnqhGTDSIKF----WTKTKTVT 479
Cdd:cd07094 386 LQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGV------GREGVPYameeMTEEKTVV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-479 |
1.60e-86 |
|
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: 273.47 E-value: 1.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIE-DAKGD 101
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 VIRGLEVCEFVCGIPHLAKGEfTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSL 181
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 182 PIRLAELMIEAgLPAGILNVVNGDKGAVDAILTD-PDIGAVSFVGSTPIARYVYGTAAmnGKRAQC---FGGaKNHMIIM 257
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDhPDVDKVTFTGSTEVGKIIYRAAA--DRLIPVsleLGG-KSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 258 PDADMDQAVN-ALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGL 336
Cdd:cd07108 236 PDADLDDAVDgAIAGMRFTRQGQSCTAGS-RLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 337 IDRGVEE-GAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAI 415
Cdd:cd07108 315 IDLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930192169 416 YTRDGDAARDFASRINIGMIGINVPIpVPLAYHSFGGWKASSFGdlNQHGTDS-IKFWTKTKTVT 479
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLG--REASLEGmLEHFTQKKTVN 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-465 |
2.49e-86 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 273.32 E-value: 2.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGtSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:PRK13473 6 LINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRG-LEVCEFVCG----IPHLAKGEFTEGAGPAIDmysiRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:PRK13473 85 ESLNCGKPLHLALNDEIPAiVDVFRFFAGaarcLEGKAAGEYLEGHTSMIR----RDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 162 PAIACGNAFILKPSERDPSLPIRLAELMIEAgLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMN 240
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 241 GKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQAD 320
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 321 MGPLVTKDAYTRVRGLIDRGVEEG-AKLLVDGRDFKLqgyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEE 399
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG----KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930192169 400 ALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPV----PlayHsfGGWKASSFG-DLNQHG 465
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLvsemP---H--GGQKQSGYGkDMSLYG 460
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-478 |
6.71e-86 |
|
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: 271.32 E-value: 6.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVCGIP----HLAKGEftegagpaiDMYSI--RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSE 176
Cdd:cd07106 81 GGAVAWLRYTASLDlpdeVIEDDD---------TRRVElrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 177 RDPSLPIRLAELMIEAgLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMII 256
Cdd:cd07106 152 FTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 257 MPDADMDQAVNALMGAGYGSAGERCMAIS-VAVPvgAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRG 335
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKrLYVH--ESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 336 LIDRGVEEGAKLLVDGRdfKLQGyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAI 415
Cdd:cd07106 309 LVEDAKAKGAKVLAGGE--PLDG--PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 416 YTRDGDAARDFASRINIGMIGIN----VPIPVPlayhsFGGWKASSFGdlNQHGTDSIKFWTKTKTV 478
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINthgaLDPDAP-----FGGHKQSGIG--VEFGIEGLKEYTQTQVI 444
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
29-460 |
3.61e-85 |
|
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: 269.55 E-value: 3.61e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 29 GEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEV 108
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 109 CEFVCGIPHLAKGE-FTEGAGPAidMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP-SLPIRLA 186
Cdd:cd07152 81 LHEAAGLPTQPQGEiLPSAPGRL--SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvSGGVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 187 ELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAV 266
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 267 NALMGAGYGSAGERCMAiSVAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAK 346
Cdd:cd07152 239 SNGAWGAFLHQGQICMA-AGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 347 LLVDGRdfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDF 426
Cdd:cd07152 318 LEAGGT-------YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430
....*....|....*....|....*....|....
gi 930192169 427 ASRINIGMIGINVPIPVPLAYHSFGGWKASSFGD 460
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEPHNPFGGMGASGNGS 424
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
23-478 |
3.08e-84 |
|
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: 267.57 E-value: 3.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWA-ATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEdakgd 101
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVM----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 VIRGLEVCEFVCGIPHLAK------GEFTEGAGPAIDMYSI----RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFI 171
Cdd:cd07089 76 TARAMQVDGPIGHLRYFADladsfpWEFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 172 LKPSERDPSLPIRLAELMIEAGLPAGILNVVNG-DKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGA 250
Cdd:cd07089 156 LKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGsDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 251 KNHMIIMPDADMDQAVNALMGAGYGSAGERCmAISVAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAY 330
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGC-ALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 331 TRVRGLIDRGVEEGAKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYG 410
Cdd:cd07089 315 DRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930192169 411 NGVAIYTRDGDAARDFASRINIGMIGINvPIPVPLAYHSFGGWKASSFGdlNQHGTDSIKFWTKTKTV 478
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-479 |
1.38e-82 |
|
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: 263.03 E-value: 1.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGD- 101
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 VIRGLEVCEFVCG----IPHLAKGEFTEGagpaidMYSI--RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPS 175
Cdd:cd07092 81 LPGAVDNFRFFAGaartLEGPAAGEYLPG------HTSMirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 176 ERDPSLPIRLAELMIEaGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHM 254
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 255 IIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVR 334
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAAC-RVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 335 GLIDRgVEEGAKLLVDGRdfklQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVA 414
Cdd:cd07092 313 GFVER-APAHARVLTGGR----RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 415 IYTRDGDAARDFASRINIGMIGINVPIPVPlAYHSFGGWKASSFG-DLNQHGTDSikfWTKTKTVT 479
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLA-AEMPHGGFKQSGYGkDLSIYALED---YTRIKHVM 449
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
23-459 |
1.48e-81 |
|
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: 260.61 E-value: 1.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFvcgiphlAKGEFTEGAGPAIDM-----------YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFI 171
Cdd:cd07149 83 DRAIETLRL-------SAEEAKRLAGETIPFdaspggegrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 172 LKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMngKRAQCFGGA 250
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 251 KNHMIIMPDADMDQAVNALMGAGYGSAGERCmaISVA-VPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDA 329
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVC--ISVQrIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 330 YTRVRGLIDRGVEEGAKLLvdgrdfkLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEY 409
Cdd:cd07149 312 AERIEEWVEEAVEGGARLL-------TGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 930192169 410 GNGVAIYTRDGDAARDFASRINIGMIGINvPIPVPLAYH-SFGGWKASSFG 459
Cdd:cd07149 385 GLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHmPYGGVKESGTG 434
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
45-479 |
2.56e-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: 259.05 E-value: 2.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 45 AAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFT 124
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 125 EGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG 204
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 205 DK----GAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGER 280
Cdd:cd07105 164 SPedapEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 281 CMAISvAVPVGAETANRLVEKLIPKIESLRIGPytddqADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDfklQGYE 360
Cdd:cd07105 244 CMSTE-RIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA---DESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 361 DGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVP 440
Cdd:cd07105 315 SGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGM 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 930192169 441 -------IPvplayhsFGGWKASSFGDLNqhGTDSIKFWTKTKTVT 479
Cdd:cd07105 395 tvhdeptLP-------HGGVKSSGYGRFN--GKWGIDEFTETKWIT 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
26-479 |
2.73e-81 |
|
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: 259.96 E-value: 2.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 26 PATGEVQATVALANVEELRAAVENAKAAQPK--WAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVI 103
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 104 RGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPI 183
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 184 RLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADM 262
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 263 DQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVE 342
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 343 EGAKLLVDGrdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDA 422
Cdd:cd07118 323 EGATLLLGG---ERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930192169 423 ARDFASRINIGMIGINVPI----PVPlayhsFGGWKASSFG-DLNQHGTDSikfWTKTKTVT 479
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLdgspELP-----FGGFKQSGIGrELGRYGVEE---YTELKTVH 453
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
2-459 |
9.35e-79 |
|
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: 253.86 E-value: 9.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 2 REIGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMD 81
Cdd:cd07111 20 RSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 82 ELAEMLSKEHGKTIEDAKGdvirglevcefvCGIPhLAKGEFTEGAGPAIDMYSI---RQPVGIGAGITPFNFPGMIPMW 158
Cdd:cd07111 100 LFAVLESLDNGKPIRESRD------------CDIP-LVARHFYHHAGWAQLLDTElagWKPVGVVGQIVPWNFPLLMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 159 MFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAA 238
Cdd:cd07111 167 KICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 239 MNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQ 318
Cdd:cd07111 247 GTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 319 ADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYE 398
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAK 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN--------VPipvplayhsFGGWKASSFG 459
Cdd:cd07111 402 EAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfdaaAG---------FGGYRESGFG 461
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
24-480 |
7.17e-78 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 250.99 E-value: 7.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 24 YNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVI 103
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 104 RGLEVCEFVCGI-------PHLAKGEFTEGAGPAIDmysiRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSE 176
Cdd:cd07099 81 LALEAIDWAARNaprvlapRKVPTGLLMPNKKATVE----YRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 177 RDPSLPIRLAELMIEAGLPAGILNVVNGDkGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMII 256
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGD-GATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 257 MPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGL 336
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVER-VYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 337 IDRGVEEGAKLLVDGRDfklqGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIY 416
Cdd:cd07099 315 VDDAVAKGAKALTGGAR----SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 417 TRDGDAARDFASRINIGMIGIN-----VPIP-VPlayhsFGGWKASSFGdlNQHGTDSIKFWTKTKTVTA 480
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINdvlltAGIPaLP-----FGGVKDSGGG--RRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
5-459 |
3.16e-77 |
|
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: 249.95 E-value: 3.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 5 GHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKGdvirglevcefvCGIPhLAKGEF---------TEGAGPAID----MYSIRQPVGIGAGITPFNF 151
Cdd:cd07559 82 VAETLDNGKPIRETLA------------ADIP-LAIDHFryfagviraQEGSLSEIDedtlSYHFHEPLGVVGQIIPWNF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 152 PGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELmIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGSTPI 229
Cdd:cd07559 149 PLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTG-FGSEagKPLASHPRIAKLAFTGSTTV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 230 ARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADM--DQAVNALMGAGYGSA---GERCMAISVAVpVGAETANRLVEKLIP 304
Cdd:cd07559 227 GRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDadDDFDDKAEEGQLGFAfnqGEVCTCPSRAL-VQESIYDEFIERAVE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 305 KIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEI 384
Cdd:cd07559 306 RFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930192169 385 FGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPlAYHSFGGWKASSFG 459
Cdd:cd07559 386 FGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKSGIG 459
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
7-478 |
2.07e-76 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 247.21 E-value: 2.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSgrvSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:NF040648 2 FINGKWIDRED---IDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRGLEVCEfvcgiphLAKGEFTEGAGPAIDM-----YSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFK-------LAAFYAKEIRGETIPSdagliFTKKEPLGVVGAITPFNYPLNLAAHKIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 162 PAIACGNAFILKPSERDPSLPIRLAELMIEA----GLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGT 236
Cdd:NF040648 152 PAIATGNSVVLHPSSKAPLAAIELAKIIEKVlkkmNIPLGVFNLVTGYGEVVgDEIVKNEKVNKISFTGSVEVGESISKK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 237 AAMngKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTD 316
Cdd:NF040648 232 AGM--KKITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVG-RVIVEEEIADEFIKKLVEETKKLKVGNPLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 317 DQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfklqgyEDGYFVGGCLFDhVTPEMDIYKTEIFGPVLSVVRAQN 396
Cdd:NF040648 309 EKTDIGPLITEEAAIRVENLVNEAIEEGAKLLCGGN-------REGSLFYPTVLD-VDEDNILVKVETFGPVLPIIRVKD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 397 YEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFgdlnqhGTDSIKF----W 472
Cdd:NF040648 381 IDEAIEIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKSGL------GKEGIKYaveeM 454
|
....*.
gi 930192169 473 TKTKTV 478
Cdd:NF040648 455 TEIKTI 460
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
24-479 |
2.51e-76 |
|
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: 246.87 E-value: 2.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 24 YNPATGEVQATVALANVEELRAAVENAKAA--QPKWAaTNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGD 101
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAfdETDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 VIRGLEVCEFVCGiphLAKGEFTEGAGPAIDMYSI--RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP 179
Cdd:cd07120 81 ISGAISELRYYAG---LARTEAGRMIEPEPGSFSLvlREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 180 SLPIRLAELMIEA-GLPAGILNVVNGDKGAVDAIL-TDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIM 257
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLvASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 258 PDADMDQAVNALMGAGYGSAGERCMAIS---VAVPVGAETANRLVEKLipkiESLRIGPYTDDQADMGPLVTKDAYTRVR 334
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSrvlVQRSIADEVRDRLAARL----AAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 335 GLIDRGVEEGAKLLVDGRDFKlQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVA 414
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVT-EGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930192169 415 IYTRDGDAARDFASRINIGMIGINVPIPVpLAYHSFGGWKASSFGDLnqHGTDSIKFWTKTKTVT 479
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRL--HGVAALEDFIEYKHIY 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
43-478 |
4.56e-76 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 245.45 E-value: 4.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 43 LRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVirglEVCEFVC------GIP 116
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEV----EKCAWICryyaenAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 117 HLAKGEFTEGAGPAidmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPA 196
Cdd:cd07100 77 FLADEPIETDAGKA---YVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 197 GILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQC-FGGAkNHMIIMPDADMDQAVNALMGAGYG 275
Cdd:cd07100 154 GVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLeLGGS-DPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 276 SAGERCMA----IsvavpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDG 351
Cdd:cd07100 233 NAGQSCIAakrfI-----VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 352 RdfKLQGyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRIN 431
Cdd:cd07100 308 K--RPDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 930192169 432 IGMIGINVP------IPvplayhsFGGWKASSFG-DLNQHGtdsIKFWTKTKTV 478
Cdd:cd07100 384 AGMVFINGMvksdprLP-------FGGVKRSGYGrELGRFG---IREFVNIKTV 427
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-478 |
6.40e-76 |
|
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: 246.67 E-value: 6.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 4 IGHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA-QPKWAAT-NPQRRARVFFKFVELLNKHMD 81
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 82 ELAEMLSKEHGKTIEDAKG-DVIRGLEVCEFVCGIPHLAKGEFTEgAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMF 160
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIE-TDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 161 APAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 -NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQ 318
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGS-RIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 319 ADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGrdfKLQGYEdGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYE 398
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGG---KRHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN----VPIPVPlayhsFGGWKASSFGdlNQHGTDSIKFWTK 474
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELGEYALENYTQ 473
|
....
gi 930192169 475 TKTV 478
Cdd:cd07143 474 IKAV 477
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
24-438 |
7.42e-75 |
|
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: 242.92 E-value: 7.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 24 YNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDvI 103
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 104 RG-LEVCEFVCGI--------PHLAKGEFTEgagpaidmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKP 174
Cdd:cd07102 80 RGmLERARYMISIaeealadiRVPEKDGFER--------YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 175 SERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHM 254
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 255 IIMPDADMDQAVNALM-GAGYGSaGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRV 333
Cdd:cd07102 232 YVRPDADLDAAAESLVdGAFFNS-GQSCCSIE-RIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 334 RGLIDRGVEEGAKLLVDGRDFKlQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGV 413
Cdd:cd07102 310 RAQIADAIAKGARALIDGALFP-EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTA 388
|
410 420
....*....|....*....|....*
gi 930192169 414 AIYTRDGDAARDFASRINIGMIGIN 438
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMN 413
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
7-481 |
1.54e-74 |
|
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: 243.02 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPK---WAATNPQRRARVFFKFVELLNKHMDEL 83
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 84 AEMLSKEHGKTIEDAK-GDVIRGLEVCEFVCG---------IPhlAKGEFTegagpaidMYSIRQPVGIGAGITPFNFPG 153
Cdd:cd07141 90 ASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGwadkihgktIP--MDGDFF--------TYTRHEPVGVCGQIIPWNFPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 154 MIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG-DKGAVDAILTDPDIGAVSFVGSTPIARY 232
Cdd:cd07141 160 LMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 233 VYGTAA-MNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRI 311
Cdd:cd07141 240 IQQAAGkSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGS-RTFVQESIYDEFVKRSVERAKKRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 312 GPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSV 391
Cdd:cd07141 319 GNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG----DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 392 VRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPlAYHSFGGWKASSFGdlNQHGTDSIKF 471
Cdd:cd07141 395 FKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNG--RELGEYGLQE 471
|
490
....*....|
gi 930192169 472 WTKTKTVTAR 481
Cdd:cd07141 472 YTEVKTVTIK 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-478 |
2.08e-74 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 242.40 E-value: 2.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAK-GDVIRGLEVCEFVCGIPHLAKGEFTEGAGPaIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTDPDIGAVSFVGSTPIARYVYGTAA-M 239
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfgpTAGA--AIASHMDVDKVAFTGSTEVGKIIMQLAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQA 319
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGS-RTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 320 DMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfklQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEE 399
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGGD----RIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 400 ALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN------VPIPvplayhsFGGWKASSFGdlNQHGTDSIKFWT 473
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfdASIP-------FGGYKMSGIG--REKGIYALNNYL 469
|
....*
gi 930192169 474 KTKTV 478
Cdd:cd07142 470 QVKAV 474
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
7-482 |
1.84e-73 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 240.92 E-value: 1.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAgTSGRVSNVyNPA-TGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAE 85
Cdd:TIGR01237 36 VINGERVE-TENKIVSI-NPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 86 MLSKEHGKTIEDAKGDVIRGLEVCEFVC-GIPHLAKGEFTEGAGPAIDMYsIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAIDFMEYYArQMIELAKGKPVNSREGETNQY-VYTPTGVTVVISPWNFPFAIMVGMTVAPI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 165 ACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTD-PDIGAVSFVGSTPIARYVYGTAAM---- 239
Cdd:TIGR01237 193 VTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDhPKTSLITFTGSREVGTRIFERAAKvqpg 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 --NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDD 317
Cdd:TIGR01237 273 qkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAV-VHEKVYDEVVERFVEITESLKVGPPDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 318 QADMGPLVTKDAYTRVRGLIDRGVEEGaKLLVDGRDFKLQGYedgyFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNY 397
Cdd:TIGR01237 352 DVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGY----FIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 398 EEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIP-VPLAYHSFGGWKASSFgDLNQHGTDSIKFWTKTK 476
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITgAIVGYQPFGGFKMSGT-DSKAGGPDYLALFMQAK 505
|
....*.
gi 930192169 477 TVTARW 482
Cdd:TIGR01237 506 TVTEMF 511
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
8-482 |
4.26e-73 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 240.22 E-value: 4.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 8 IGGKQVAGTSGRVSnvYNPA-TGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:PRK03137 41 IGGERITTEDKIVS--INPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRGLEVCEFVC--------GIPHLAK-GEFTEgagpaidMYSIrqPVGIGAGITPFNFPGMIPM 157
Cdd:PRK03137 119 LVKEAGKPWAEADADTAEAIDFLEYYArqmlkladGKPVESRpGEHNR-------YFYI--PLGVGVVISPWNFPFAIMA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 158 WMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTD-PDIGAVSFVGSTPIARYVYGT 236
Cdd:PRK03137 190 GMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDhPKTRFITFTGSREVGLRIYER 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 237 AAMNG------KRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLR 310
Cdd:PRK03137 270 AAKVQpgqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAI-VHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 311 IGPyTDDQADMGPLVTKDAYTRVRGLIDRGVEEGaKLLVDGRdfklQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLS 390
Cdd:PRK03137 349 VGN-PEDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE----GDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 391 VVRAQNYEEALSLPMKHEYGNGVAIYTRDGD----AARDFasriNIGMIGINVPIPVPL-AYHSFGGWKASsfgdlnqhG 465
Cdd:PRK03137 423 FIKAKDFDHALEIANNTEYGLTGAVISNNREhlekARREF----HVGNLYFNRGCTGAIvGYHPFGGFNMS--------G 490
|
490 500
....*....|....*....|....
gi 930192169 466 TDS-------IKFWTKTKTVTARW 482
Cdd:PRK03137 491 TDSkaggpdyLLLFLQAKTVSEMF 514
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
13-482 |
1.05e-71 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 236.70 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 13 VAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHG 92
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 93 KTIEDAKgdvirgLEVCEFVCG-------IPHLAKGEFTEGAGPAI-DMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:PRK09407 106 KARRHAF------EEVLDVALTaryyarrAPKLLAPRRRAGALPVLtKTTELRQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 165 ACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDkGAV--DAILTDPDIgaVSFVGSTPIARYVYGTAamnGK 242
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGP-GPVvgTALVDNADY--LMFTGSTATGRVLAEQA---GR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 243 RAQCFG---GAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQA 319
Cdd:PRK09407 254 RLIGFSlelGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIE-RIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 320 DMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGR---DFKLQGYEDGYFVGgclfdhVTPEMDIYKTEIFGPVLSVVRAQN 396
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKarpDLGPLFYEPTVLTG------VTPDMELAREETFGPVVSVYPVAD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 397 YEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVplAYHSF----GGWKASSFGdlNQHGTDSIKFW 472
Cdd:PRK09407 407 VDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAA--AWGSVdapmGGMKDSGLG--RRHGAEGLLKY 482
|
490
....*....|.
gi 930192169 473 TKTKTV-TARW 482
Cdd:PRK09407 483 TESQTIaTQRV 493
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
7-478 |
1.72e-71 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 235.49 E-value: 1.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKG-DVIRGLEVCEFVCGIPHLAKGEFTEGAGPaIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PLN02766 104 ALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTDPDIGAVSFVGSTPIARYVYGTAAM- 239
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfgpTAGA--AIASHMDVDKVSFTGSTEVGRKIMQAAATs 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQA 319
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASS-RVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 320 DMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFklqgYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEE 399
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPC----GDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 400 ALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINvpipVPLAYHS---FGGWKASSFGdlNQHGTDSIKFWTKTK 476
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN----CYFAFDPdcpFGGYKMSGFG--RDQGMDALDKYLQVK 489
|
..
gi 930192169 477 TV 478
Cdd:PLN02766 490 SV 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-459 |
2.03e-71 |
|
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: 235.94 E-value: 2.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 2 REIGHFIGGKQVAGTSGRVsnVYNPATGEVQ-ATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHM 80
Cdd:cd07125 31 WEAIPIINGEETETGEGAP--VIDPADHERTiGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 81 DELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVcgiPHLAKGEFTEGAGPAIDMYS---IRQPVGIGAGITPFNFPGMIPM 157
Cdd:cd07125 109 GELIALAAAEAGKTLADADAEVREAIDFCRYY---AAQARELFSDPELPGPTGELnglELHGRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 158 WMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARyvygt 236
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAK----- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 237 aAMNGKRAQCFG---------GAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIE 307
Cdd:cd07125 261 -LINRALAERDGpilpliaetGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLY-LQEEIAERFIEMLKGAMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 308 SLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEgAKLLvdgrdFKLQ-GYEDGYFVGGCLFDHVTPemDIYKTEIFG 386
Cdd:cd07125 339 SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLI-----APAPlDDGNGYFVAPGIIEIVGI--FDLTTEVFG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 387 PVLSVVRA--QNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPI--------PvplayhsFGGWKAS 456
Cdd:cd07125 411 PILHVIRFkaEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNItgaivgrqP-------FGGWGLS 483
|
...
gi 930192169 457 SFG 459
Cdd:cd07125 484 GTG 486
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-479 |
8.47e-71 |
|
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: 233.54 E-value: 8.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDA-KGDVIRGLEVCEFVCGIPHLAKGEF--TEGAGPAIDM-YSIRQPVGIGAGITPFNFPGMIPMWMF 160
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTipINQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 161 APAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTD-PDIGAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDhPDVRKLGFTGSTPIGKHIMKSCAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 -NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQ 318
Cdd:cd07140 249 sNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAG-RLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 319 ADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQgyedGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQN-- 396
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 397 YEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAyHSFGGWKASSFG-DLnqhGTDSIKFWTKT 475
Cdd:cd07140 404 VDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFGkDL---GEEALNEYLKT 479
|
....
gi 930192169 476 KTVT 479
Cdd:cd07140 480 KTVT 483
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-459 |
2.93e-69 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 229.41 E-value: 2.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIAC 166
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 167 GNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAMNGKRAQ 245
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTsNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 246 CFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLV 325
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCAN-RLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 326 TKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGyedGYFVGGCLFDhVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPM 405
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHELGG---NFFQPTILVD-VPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 930192169 406 KHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIpVPLAYHSFGGWKASSFG 459
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLG 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
23-459 |
8.17e-69 |
|
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: 227.13 E-value: 8.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDV 102
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFvcgiphlAKGEFTEGAGPAIDMYSI-----------RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFI 171
Cdd:cd07147 83 ARAIDTFRI-------AAEEATRIYGEVLPLDISargegrqglvrRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 172 LKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAamnGKRAQCF---G 248
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARA---GKKKVVLelgG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 249 GAKnhMIIMPDADMDQAVNALMGAGYGSAGERCmaISVA-VPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTK 327
Cdd:cd07147 233 NAA--VIVDSDADLDFAAQRIIFGAFYQAGQSC--ISVQrVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 328 DAYTRVRGLIDRGVEEGAKLLVDGRdfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKH 407
Cdd:cd07147 309 SEAERVEGWVNEAVDAGAKLLTGGK-------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDS 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 408 EYGNGVAIYTRDGDAARDFASRINIGMIGIN-VPI----PVPlayhsFGGWKASSFG 459
Cdd:cd07147 382 KFGLQAGVFTRDLEKALRAWDELEVGGVVINdVPTfrvdHMP-----YGGVKDSGIG 433
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
16-484 |
9.87e-69 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 228.10 E-value: 9.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 16 TSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTI 95
Cdd:PLN00412 28 SSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 96 EDAKGDVIRGLEVCEFVC--GIPHLAKGEFT-----EGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGN 168
Cdd:PLN00412 108 KDAVTEVVRSGDLISYTAeeGVRILGEGKFLvsdsfPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 169 AFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFV-GSTPIAryVYGTAAMngKRAQ 245
Cdd:PLN00412 188 AVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTG-KGSEigDFLTMHPGVNCISFTgGDTGIA--ISKKAGM--VPLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 246 CFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDqADMGPLV 325
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKV-VLVMESVADALVEKVNAKVAKLTVGPPEDD-CDITPVV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 326 TKDAYTRVRGLIDRGVEEGAKLLVDGRdfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPM 405
Cdd:PLN00412 341 SESSANFIEGLVMDAKEKGATFCQEWK-------REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 406 KHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFGdlNQHGTDSIKFWTKTKTVTARWPS 484
Cdd:PLN00412 414 ASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIG--SQGITNSINMMTKVKSTVINLPK 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-481 |
1.73e-68 |
|
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: 227.85 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 1 MREIGHFIGGKQVaGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHM 80
Cdd:cd07083 16 GRAYPLVIGGEWV-DTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 81 DELAEMLSKEHGKTIEDAKGDVIRGLEVCEF--VCGIPHLAKGEFTEGAgPAIDMYSIRQPVGIGAGITPFNFPGMIPMW 158
Cdd:cd07083 95 RELIATLTYEVGKNWVEAIDDVAEAIDFIRYyaRAALRLRYPAVEVVPY-PGEDNESFYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 159 MFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARYVYGTA 237
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTeHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 238 AMNGKRAQCF------GGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVA-VPVGAetANRLVEKLIPKIESLR 310
Cdd:cd07083 254 ARLAPGQTWFkrlyveTGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLiLTQGA--YEPVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 311 IGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGaKLLVDGRdfKLQGyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLS 390
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGK--RLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 391 VVR--AQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPL-AYHSFGGWKASSFGDlNQHGTD 467
Cdd:cd07083 407 VIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvGVQPFGGFKLSGTNA-KTGGPH 485
|
490
....*....|....
gi 930192169 468 SIKFWTKTKTVTAR 481
Cdd:cd07083 486 YLRRFLEMKAVAER 499
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-479 |
1.59e-67 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 225.38 E-value: 1.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPK-----WAATNPQRRARVFFKFVELLNKHMD 81
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 82 ELAEMLSKEHGKTIEDAKGDvIRGLEVC-EFVCGiphLAKGEFTEGAGP------AIDMYSIRQPVGIGAGITPFNFPGM 154
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWD-MDDVAGCfEYYAD---LAEALDAKQKAPvslpmeTFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 155 IPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTDPDIGAVSFVGSTPIAR 231
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlgtEAGA--PLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 232 YVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRI 311
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATS-RLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 312 G-PYTDDqADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLS 390
Cdd:PLN02467 324 SdPLEEG-CRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 391 VVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVpLAYHSFGGWKASSFG-DLNQHGTDSi 469
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFGrELGEWGLEN- 478
|
490
....*....|
gi 930192169 470 kfWTKTKTVT 479
Cdd:PLN02467 479 --YLSVKQVT 486
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
5-459 |
3.52e-67 |
|
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: 223.49 E-value: 3.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 5 GHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKG-DVIRGLEVCEFVCGIphlAKGEftEGAGPAID--MYSI--RQPVGIGAGITPFNFPGMIPMWM 159
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFAGV---IRAE--EGSANMIDedTLSIvlREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 160 FAPAIACGNAFILKPSErdpSLPIRLAELM--IEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGSTPIARYVYG 235
Cdd:cd07117 157 LAPALAAGNTVVIKPSS---TTSLSLLELAkiIQDVLPKGVVNIVTG-KGSKsgEYLLNHPGLDKLAFTGSTEVGRDVAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 236 TAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYT 315
Cdd:cd07117 233 AAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGS-RIFVQEGIYDEFVAKLKEKFENVKVGNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 316 DDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQ 395
Cdd:cd07117 312 DPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930192169 396 NYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPlAYHSFGGWKASSFG 459
Cdd:cd07117 392 TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIP-AGAPFGGYKKSGIG 454
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-478 |
1.90e-66 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 222.08 E-value: 1.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKGDVIRGLEVC-EFVCGIPHLAKGEFTEGAGPAIDMYsIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAiRWYAEAIDKVYGEVATTSSHELAMI-VREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG-DKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAA-MNG 241
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 242 KRAQCFGGAKNHMIIMPDA-DMDQAVNALMGAGYGSAGERCMAiSVAVPVGAETANRLVEKLIPKIESLRIGPYTDDQAD 320
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA-GTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 321 MGPLVTKDAYTRVRGLIDRGVEEGaKLLVDGRDFKLQGYedgyfVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEA 400
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 401 LSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINV----PIPVPlayhsFGGWKASSFG-DLNQHGTDsiKFwTKT 475
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLHALE--KF-TEL 486
|
...
gi 930192169 476 KTV 478
Cdd:PRK09847 487 KTI 489
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
26-479 |
2.23e-66 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 220.64 E-value: 2.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 26 PATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKgdvirg 105
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 106 LEVCEFVCGIPHLAK--GEF--TEGAGPAIDMYS----IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSER 177
Cdd:cd07101 77 EEVLDVAIVARYYARraERLlkPRRRRGAIPVLTrttvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 178 DPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIgaVSFVGSTPIARYVYGTAAMN--GKRAQCfgGAKNHM 254
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRliGCSLEL--GGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 255 IIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVR 334
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIE-RIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 335 GLIDRGVEEGAKLLVDGRDFKLQGyedGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVA 414
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930192169 415 IYTRDGDAARDFASRINIGMIGIN-------VPIPVPLayhsfGGWKASSFGdlNQHGTDSIKFWTKTKTVT 479
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNegyaaawASIDAPM-----GGMKDSGLG--RRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
24-462 |
2.92e-66 |
|
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: 220.63 E-value: 2.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 24 YNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAK-GDV 102
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 103 IRGLEVCEFVcgiphLAKGEFT----EGAGPAIDMYSIR----QPVGIGAGITPFNFP---GMIPMwmfAPAIACGNAFI 171
Cdd:cd07098 81 LVTCEKIRWT-----LKHGEKAlrpeSRPGGLLMFYKRArveyEPLGVVGAIVSWNYPfhnLLGPI---IAALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 172 LKPSER---DPSLPIRLAELMIEA-GLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCF 247
Cdd:cd07098 153 VKVSEQvawSSGFFLSIIRECLAAcGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 248 GGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTK 327
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIE-RVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 328 DAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKH 407
Cdd:cd07098 312 ARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930192169 408 EYGNGVAIYTRDGDAARDFASRINIGMIGIN--------VPIPvplayhsFGGWKASSFGDLN 462
Cdd:cd07098 392 EYGLGASVFGKDIKRARRIASQLETGMVAINdfgvnyyvQQLP-------FGGVKGSGFGRFA 447
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-478 |
3.52e-64 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 217.37 E-value: 3.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 6 HFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAA--QPKWAATNPQRRARVFFKFVELLNKHMDEL 83
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 84 AEMLSKEHGKTIED-AKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAiDMYSIRQPVGIGAGITPFNFPGMIPMWMFAP 162
Cdd:PLN02466 140 AALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPADGPH-HVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 163 AIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTDPDIGAVSFVGSTPIARYVYGTAAM 239
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfgpTAGA--ALASHMDVDKLAFTGSTDTGKIVLELAAK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 -NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKliPKIESLR--IGPYTD 316
Cdd:PLN02466 297 sNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF-VHERVYDEFVEK--AKARALKrvVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 317 DQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQN 396
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 397 YEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVpIPVPLAYHSFGGWKASSFGdlNQHGTDSIKFWTKTK 476
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG--REKGIYSLNNYLQVK 526
|
..
gi 930192169 477 TV 478
Cdd:PLN02466 527 AV 528
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
15-479 |
4.93e-64 |
|
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: 215.15 E-value: 4.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 15 GTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKT 94
Cdd:cd07130 8 GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 95 IEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKP 174
Cdd:cd07130 88 LPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 175 SERDPSLPIRLAELMIEA----GLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAmngKRaqcFG-- 248
Cdd:cd07130 168 SPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA---AR---FGrs 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 249 ----GAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMaisvavpvgaeTANRL----------VEKLIPKIESLRIGPY 314
Cdd:cd07130 242 llelGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCT-----------TTRRLivhesiydevLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 315 TDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRdfKLQGyeDGYFVGGCLFDhVTPEMDIYKTEIFGPVLSVVRA 394
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGK--VIDG--PGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 395 QNYEEALslpmkhEYGNGV------AIYTRDGDAARDFasrinIGMIG-----INVPIPVPLAY--HSFGGWKASSFGdl 461
Cdd:cd07130 386 DTLEEAI------AWNNEVpqglssSIFTTDLRNAFRW-----LGPKGsdcgiVNVNIGTSGAEigGAFGGEKETGGG-- 452
|
490
....*....|....*...
gi 930192169 462 NQHGTDSIKFWTKTKTVT 479
Cdd:cd07130 453 RESGSDAWKQYMRRSTCT 470
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-464 |
1.04e-60 |
|
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: 206.53 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 5 GHFIGGKQVAGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:cd07116 2 DNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTI-EDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIdMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:cd07116 82 VAETWDNGKPVrETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTV-AYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 164 IACGNAFILKPSERDPSLPIRLAELmIEAGLPAGILNVVNGDKGAVDAIL-TDPDIGAVSFVGSTPIARYVYGTAAMNGK 242
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLaSSKRIAKVAFTGETTTGRLIMQYASENII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 243 RAQCFGGAKNHMIIMP------DADMDQAVNALMGAGYGSaGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTD 316
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFALNQ-GEVCTCPSRAL-IQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 317 DQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQGYEDGYFVGGCLFdHVTPEMDIYKTEIFGPVLSVVRAQN 396
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTF-KGGNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930192169 397 YEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPlAYHSFGGWKASSFGDLNQH 464
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIGRENHK 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-478 |
1.25e-60 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 205.74 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 25 NPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIR 104
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 105 GLEVCEFVC--GIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLP 182
Cdd:PRK09406 87 CAKGFRYYAehAEALLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 183 IRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADM 262
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 263 DQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVE 342
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFI-VHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 343 EGAKLLVDGRdfKLQGyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDA 422
Cdd:PRK09406 326 AGATILCGGK--RPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930192169 423 ARDFASRINIGMIGIN---VPIP-VPlayhsFGGWKASSFG-DLNQHGtdsIKFWTKTKTV 478
Cdd:PRK09406 402 QERFIDDLEAGQVFINgmtVSYPeLP-----FGGVKRSGYGrELSAHG---IREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
25-459 |
8.03e-59 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 201.24 E-value: 8.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 25 NPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIR 104
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 105 GLEVCEFVC--GiPHLAKGEFT--EGAGPAIDMysirQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPS 180
Cdd:PRK13968 93 SANLCDWYAehG-PAMLKAEPTlvENQQAVIEY----RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 181 LPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDA 260
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 261 DMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRG 340
Cdd:PRK13968 248 DLELAVKAAVAGRYQNTGQVCAAAKRFI-IEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 341 VEEGAKLLVDGRdfKLQGyeDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDG 420
Cdd:PRK13968 327 LAEGARLLLGGE--KIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDE 402
|
410 420 430
....*....|....*....|....*....|....*....
gi 930192169 421 DAARDFASRINIGMIGINvPIPVPLAYHSFGGWKASSFG 459
Cdd:PRK13968 403 TQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
70-465 |
9.44e-59 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 199.58 E-value: 9.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 70 FKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPF 149
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 150 NFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTDPDIGAVSFVGST 227
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLG-RGETvgQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 228 PIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISvAVPVGAETANRLVEKLIPKIE 307
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAE-RVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 308 SLRIG-PYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlqgyEDGYFVGGCLFDHVTPEMDIYKTEIFG 386
Cdd:PRK10090 240 AVQFGnPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 387 PVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVP-IPVPLAYHSfgGWKASSFGDLN-QH 464
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREnFEAMQGFHA--GWRKSGIGGADgKH 393
|
.
gi 930192169 465 G 465
Cdd:PRK10090 394 G 394
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-456 |
1.06e-57 |
|
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: 197.11 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 45 AAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGdvirglEVCEFVcgiphlAKGEFT 124
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT------EVAAMA------GKIDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 125 -----EGAGP-AIDMYSIR-----QPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAG 193
Cdd:cd07095 72 ikayhERTGErATPMAQGRavlrhRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 194 LPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMN-GKRAQCFGGAKNHMIIMPDADMDQAVNALMGA 272
Cdd:cd07095 152 LPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRpGKILALEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 273 GYGSAGERCMAIS-VAVPVGAEtANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDG 351
Cdd:cd07095 232 AFLTAGQRCTCARrLIVPDGAV-GDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 352 RDFKlqgyEDGYFVGGCLFDhVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRIN 431
Cdd:cd07095 311 ERLV----AGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*
gi 930192169 432 IGMIGINVPIPVPLAYHSFGGWKAS 456
Cdd:cd07095 386 AGIVNWNRPTTGASSTAPFGGVGLS 410
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-456 |
3.49e-49 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 175.92 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 5 GHFIGGKQVAGTSGRVSNVyNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELA 84
Cdd:PRK09457 2 TLWINGDWIAGQGEAFESR-NPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 85 EMLSKEHGKTIEDAKgdvirgLEVCEFV--CGIPHLAKGEFT-EGAGPAID-MYSIR-QPVGIGAGITPFNFPGMIPMWM 159
Cdd:PRK09457 81 EVIARETGKPLWEAA------TEVTAMInkIAISIQAYHERTgEKRSEMADgAAVLRhRPHGVVAVFGPYNFPGHLPNGH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 160 FAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAM 239
Cdd:PRK09457 155 IVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 240 N-GKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCM-AISVAVPVGAEtANRLVEKLIPKIESLRIGPYTDD 317
Cdd:PRK09457 235 QpEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQ-GDAFLARLVAVAKRLTVGRWDAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 318 -QADMGPLVTKDAytrVRGLID---RGVEEGAKLLVDGRdfklQGYEDGYFVGGCLFDhVTPEMDIYKTEIFGPVLSVVR 393
Cdd:PRK09457 314 pQPFMGAVISEQA---AQGLVAaqaQLLALGGKSLLEMT----QLQAGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVR 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930192169 394 AQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKAS 456
Cdd:PRK09457 386 YDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGAS 448
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
3-456 |
4.42e-49 |
|
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: 176.24 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 3 EIGHFIGGKQVagTSGRVSNVYNPAT-GEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLN-KHM 80
Cdd:cd07123 32 EIPLVIGGKEV--RTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 81 DEL--AEMLSKehGKTIEDAKGDVIrgLEVCEFvcgiphlakgeFTEGAGPAIDMYSIrQPVGIGAG------------- 145
Cdd:cd07123 110 YELnaATMLGQ--GKNVWQAEIDAA--CELIDF-----------LRFNVKYAEELYAQ-QPLSSPAGvwnrleyrplegf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 146 ---ITPFNFP---GMIPMwmfAPAIAcGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDI 218
Cdd:cd07123 174 vyaVSPFNFTaigGNLAG---APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 219 GAVSFVGSTPIARYVYGTAAMNGKRAQCF----G--GAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVA-VPvg 291
Cdd:cd07123 250 AGLHFTGSTPTFKSLWKQIGENLDRYRTYprivGetGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAyVP-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 292 AETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEE-GAKLLVDGRdfklqgYED--GYFVGGC 368
Cdd:cd07123 328 ESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK------CDDsvGYFVEPT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 369 LFDHVTPEMDIYKTEIFGPVLS--VVRAQNYEEALSLPMK-HEYGNGVAIYTRDGDA---ARDfASRINIGMIGIN-VPI 441
Cdd:cd07123 402 VIETTDPKHKLMTEEIFGPVLTvyVYPDSDFEETLELVDTtSPYALTGAIFAQDRKAireATD-ALRNAAGNFYINdKPT 480
|
490
....*....|....*
gi 930192169 442 PVPLAYHSFGGWKAS 456
Cdd:cd07123 481 GAVVGQQPFGGARAS 495
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
1-460 |
4.05e-48 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 173.82 E-value: 4.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 1 MREIGHFIGGKQVAGTSGRVSNVyNPATGEVQ-ATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLN-K 78
Cdd:TIGR01236 29 SLEIPLVIGGEEVYDSNERIPQV-NPHNHQAVlAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSgP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 79 HMDELAEMLSKEHGKTIEDAKGDVIrgLEVCEFvcgiphlakgeFTEGAGPAIDMYSiRQPV---------------GIG 143
Cdd:TIGR01236 108 YRYEILAATMLGQSKTVYQAEIDAV--AELIDF-----------FRFNVKYARELYA-QQPIsapgewnrteyrpleGFV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 144 AGITPFNFPGMIPMWMFAPAIAcGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTDPDIGAVS 222
Cdd:TIGR01236 174 YAISPFNFTAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVsDQVLADPDLAGIH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 223 FVGSTPIARYVYGTAAMNGKRAQCF------GGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETAN 296
Cdd:TIGR01236 253 FTGSTNTFKHLWKKVAQNLDRYHNFprivgeTGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLY-VPHSKWP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 297 RLVEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLID--RGVEEGAKLLVDGRdfklqgYED--GYFVGGCLFDH 372
Cdd:TIGR01236 332 EFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEdaKKDPEALTILYGGK------YDDsqGYFVEPTVVES 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 373 VTPEMDIYKTEIFGPVLSVVRAQN--YEEALSLPMK-HEYGNGVAIYTRDGDAAR--DFASRINIGMIGIN-VPIPVPLA 446
Cdd:TIGR01236 406 KDPDHPLMSEEIFGPVLTVYVYPDdkYKEILDLVDStSQYGLTGAVFAKDRKAILeaDKKLRFAAGNFYINdKCTGAVVG 485
|
490
....*....|....
gi 930192169 447 YHSFGGWKASSFGD 460
Cdd:TIGR01236 486 QQPFGGARMSGTND 499
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
8-438 |
4.96e-48 |
|
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: 173.17 E-value: 4.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 8 IGGKQVAgtSGRVSNVYNPATGEVQ-ATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:TIGR01238 42 IGHSYKA--DGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEgagpaidmysirQPVGIGAGITPFNFPGMIPMWMFAPAIAC 166
Cdd:TIGR01238 120 CVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV------------ESRGVFVCISPWNFPLAIFTGQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 167 GNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAMNGKRAQ 245
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTsDPRIAGVAFTGSTEVAQLINQTLAQREDAPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 246 CF---GGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMG 322
Cdd:TIGR01238 268 PLiaeTGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRV-LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 323 PLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQgYEDGYFVGGCLFDhvTPEMDIYKTEIFGPVLSVVR--AQNYEEA 400
Cdd:TIGR01238 347 PVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRykARELDQI 423
|
410 420 430
....*....|....*....|....*....|....*...
gi 930192169 401 LSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN 438
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-438 |
7.31e-47 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 175.00 E-value: 7.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 1 MREIGHFIGGKQVAG----TSGRVSNVYNPATGEVQA-TVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVEL 75
Cdd:PRK11904 540 AAAIAAFLEKQWQAGpiinGEGEARPVVSPADRRRVVgEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 76 LNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCgipHLAKGEFTEG---AGPA-IDMYSIRQPVGIGAGITPFNF 151
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYA---AQARRLFGAPeklPGPTgESNELRLHGRGVFVCISPWNF 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 152 PGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIA 230
Cdd:PRK11904 697 PLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTaDPRIAGVAFTGSTETA 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 231 RYVYGT-AAMNGKRAqCF----GGAkNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPK 305
Cdd:PRK11904 777 RIINRTlAARDGPIV-PLiaetGGQ-NAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLF-VQEDIADRVIEMLKGA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 306 IESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRgVEEGAKLLvdgrdFKLQ---GYEDGYFVGGCLFDhvTPEMDIYKT 382
Cdd:PRK11904 854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLL-----AQLPlpaGTENGHFVAPTAFE--IDSISQLER 925
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 930192169 383 EIFGPVLSVVR--AQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN 438
Cdd:PRK11904 926 EVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
23-459 |
1.38e-44 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 162.59 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAA---QPKWAAtnPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAK 99
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALfldRNNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 100 GDVIRGLEvcefvcGIpHLAKGEFTEGAGPAIDM-----------YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGN 168
Cdd:cd07148 81 VEVTRAID------GV-ELAADELGQLGGREIPMgltpasagriaFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 169 AFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFG 248
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGTRCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 249 GAKNhMIIMPDADMDQAVNALMGAGYGSAGERCmaISVA-VPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTK 327
Cdd:cd07148 234 GAAP-VIVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQrVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 328 DAYTRVRGLIDRGVEEGAKLLVDGRDFklqgyEDGYFVGGCLFDhvtPEMD--IYKTEIFGPVLSVVRAQNYEEALSLPM 405
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRL-----SDTTYAPTVLLD---PPRDakVSTQEIFGPVVCVYSYDDLDEAIAQAN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 930192169 406 KHEYGNGVAIYTRDGDAARDFASRINIGMIGINVPIPVPLAYHSFGGWKASSFG 459
Cdd:cd07148 383 SLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
23-393 |
3.33e-41 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 158.10 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPA-TGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGd 101
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIA- 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 102 virglEVCEFV--C-----GIPHLAKGeftegagpaidmySIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKP 174
Cdd:PRK11905 650 -----EVREAVdfLryyaaQARRLLNG-------------PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKP 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 175 SERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCF----GG 249
Cdd:PRK11905 712 AEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVaDPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaetGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 250 aKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTDDQADMGPLVTKDA 329
Cdd:PRK11905 792 -QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRV-LCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA 869
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 330 YTRVRGLIDRGVEEGAKLlvdgrdFKL---QGYEDGYFVGGCLFDhvTPEMDIYKTEIFGPVLSVVR 393
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLV------HQLplpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVR 928
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
2-479 |
1.87e-40 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 152.30 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 2 REIGHFIGGKQvaGTSGRVSNVYNPATGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMD 81
Cdd:PLN02315 19 RNLGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 82 ELAEMLSKEHGKTIEDAKGDVIRGLEVCEFVCGIPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:PLN02315 97 YLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNAC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 162 PAIACGNAFILKPSERDPSLPIRL----AELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVygTA 237
Cdd:PLN02315 177 IALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMV--QQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 238 AMNGKRAQCF--GGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVAVpVGAETANRLVEKLIPKIESLRIGPYT 315
Cdd:PLN02315 255 TVNARFGKCLleLSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLL-LHESIYDDVLEQLLTVYKQVKIGDPL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 316 DDQADMGPLVTKDAytrvRGLIDRGVE----EGAKLLVDGRDFKlqgyEDGYFVGGCLFDhVTPEMDIYKTEIFGPVLSV 391
Cdd:PLN02315 334 EKGTLLGPLHTPES----KKNFEKGIEiiksQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 392 VRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRI--NIGMIGINVPIPVPLAYHSFGGWKASSFGdlNQHGTDSI 469
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG--REAGSDSW 482
|
490
....*....|
gi 930192169 470 KFWTKTKTVT 479
Cdd:PLN02315 483 KQYMRRSTCT 492
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
8-393 |
5.63e-38 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 148.55 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 8 IGGKQVAGTSgrvSNVYNPATGEVQA-TVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:COG4230 562 IAGEAASGEA---RPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGdvirglEVCEFV--C---GipHLAKGEFTEGagpaidmySIRQPVGIGAGITPFNFP-----GMIp 156
Cdd:COG4230 639 LVREAGKTLPDAIA------EVREAVdfCryyA--AQARRLFAAP--------TVLRGRGVFVCISPWNFPlaiftGQV- 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 157 mwmfAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARyvyg 235
Cdd:COG4230 702 ----AAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVaDPRIAGVAFTGSTETAR---- 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 236 taAMNGKRAQCFG---------GAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKI 306
Cdd:COG4230 774 --LINRTLAARDGpivpliaetGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRV-LCVQEDIADRVLEMLKGAM 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 307 ESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLlvdgrdFKL---QGYEDGYFVGGCLF--DHVTpemDIyK 381
Cdd:COG4230 851 AELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV------HQLplpEECANGTFVAPTLIeiDSIS---DL-E 920
|
410
....*....|..
gi 930192169 382 TEIFGPVLSVVR 393
Cdd:COG4230 921 REVFGPVLHVVR 932
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
43-472 |
5.64e-33 |
|
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: 130.44 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 43 LRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKT---IEDAKGDV--IRGLEVCEFVCGIPH 117
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 118 lAKGEfTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAG-LPA 196
Cdd:cd07084 81 -EPGN-HLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 197 GILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARyvygTAAMNGKRAQCFG--GAKNHMIIMPDAD-MDQAVNALMGAG 273
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAE----KLALDAKQARIYLelAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 274 YGSAGERCMAISVAVPVGAETANRLVEKLIPKIESLrigpyTDDQADMGPLVTKDAYTRVrglIDRGVEEGAKLLVDGRD 353
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTPLVEKLKALLARR-----KLEDLLLGPVQTFTTLAMI---AHMENLLGSVLLFSGKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 354 FKLQGYEDgyFVGGCLFDHVTPEMD-------IYKTEIFGPVLSVVRAQNYEEALSLPMKhEYGNG---VAIYTRDGDAA 423
Cdd:cd07084 307 LKNHSIPS--IYGACVASALFVPIDeilktyeLVTEEIFGPFAIVVEYKKDQLALVLELL-ERMHGsltAAIYSNDPIFL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 930192169 424 RDFASRINI-GMIGINVPIP---VPLAYHSFGGwKASSFGDlNQHGTDSIKFW 472
Cdd:cd07084 384 QELIGNLWVaGRTYAILRGRtgvAPNQNHGGGP-AADPRGA-GIGGPEAIKLV 434
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
8-393 |
6.07e-32 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 130.48 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 8 IGGKQVAGTSgrvSNVYNPA-TGEVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM 86
Cdd:PRK11809 651 LEDPVAAGEM---SPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGL 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 87 LSKEHGKTIEDAKGDViRglEVCEFVCGIPHLAKGEFTEgagpaiDMYsirQPVGIGAGITPFNFPGMIPMWMFAPAIAC 166
Cdd:PRK11809 728 LVREAGKTFSNAIAEV-R--EAVDFLRYYAGQVRDDFDN------DTH---RPLGPVVCISPWNFPLAIFTGQVAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 167 GNAFILKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-DPDIGAVSFVGSTPIARYVYGTAAmngKRAQ 245
Cdd:PRK11809 796 GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVaDARVRGVMFTGSTEVARLLQRNLA---GRLD 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 246 CFG---------GAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLRIGPYTD 316
Cdd:PRK11809 873 PQGrpipliaetGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRV-LCLQDDVADRTLKMLRGAMAECRMGNPDR 951
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 317 DQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKlQGYEDGYFVGGCL--FDHVtpemDIYKTEIFGPVLSVVR 393
Cdd:PRK11809 952 LSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENS-EDWQSGTFVPPTLieLDSF----DELKREVFGPVLHVVR 1025
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
134-459 |
8.88e-27 |
|
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: 112.23 E-value: 8.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 134 YSIRQPVGIGAGITPFNFP---GMIPMwmfAPAIACGNAFILKPSERDPSLPIRLAELmIEAGLPAGILNVVNGDKGAVD 210
Cdd:cd07087 95 YVIPEPLGVVLIIGPWNYPlqlALAPL---IGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 211 AILTDP-DIgaVSFVGSTPIARYVYGTAAMNgkRAQC---FGGaKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAisv 286
Cdd:cd07087 171 ALLAEPfDH--IFFTGSPAVGKIVMEAAAKH--LTPVtleLGG-KSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 287 avP----VGAETANRLVEKLIPKIESLrIGPYTDDQADMGPLVTKDAYTRVRGLIDrgveeGAKLLVDGrdfklQGYEDG 362
Cdd:cd07087 243 --PdyvlVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGG-----QVDKEE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 363 YFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEygNGVAIY--TRDGDAARDFASRINIGMIGINVP 440
Cdd:cd07087 310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRP--KPLALYlfSEDKAVQERVLAETSSGGVCVNDV 387
|
330 340
....*....|....*....|.
gi 930192169 441 IpVPLAYHS--FGGWKASSFG 459
Cdd:cd07087 388 L-LHAAIPNlpFGGVGNSGMG 407
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-427 |
1.37e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 109.79 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 1 MREIGHFIGGKQVAGtSGRVSNVYNPATGEVQATVALANVEeLRAAVENAKA-AQPKWAATNPQRRARVFFKFVELLNKH 79
Cdd:PRK11903 2 TELLANYVAGRWQAG-SGAGTPLFDPVTGEELVRVSATGLD-LAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 80 MDELAEMLSKEHGKTIEDAKGDVIRGL-------EVCEFVCGIPHLAKGEFTE-GAGPAIDMYSIRQPV-GIGAGITPFN 150
Cdd:PRK11903 80 RDAYYDIATANSGTTRNDSAVDIDGGIftlgyyaKLGAALGDARLLRDGEAVQlGKDPAFQGQHVLVPTrGVALFINAFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 151 FPGMiPMW-MFAPAIACGNAFILKPSERDPSLPIRLAELMIEAG-LPAGILNVVNGDKGAVDAILTDPDIgaVSFVGSTP 228
Cdd:PRK11903 160 FPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDV--VSFTGSAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 229 IARYVYGTAAM--NGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYG-----SAGERCMAIS-VAVPvgAETANRLVE 300
Cdd:PRK11903 237 TAAVLRSHPAVvqRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVremtvKSGQKCTAIRrIFVP--EALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 301 KLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRgVEEGAKLLVDGRDFKLQGYED--GYFVGGCLFdhVTPEMD 378
Cdd:PRK11903 315 ALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFALVDADPavAACVGPTLL--GASDPD 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 930192169 379 ----IYKTEIFGPVLSVVRAQNYEEALSLPMKHEyGNGVA-IYTRDGDAARDFA 427
Cdd:PRK11903 392 aataVHDVEVFGPVATLLPYRDAAHALALARRGQ-GSLVAsVYSDDAAFLAAAA 444
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
146-438 |
1.27e-24 |
|
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: 106.16 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 146 ITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAElMIEAGLPAGILNVVNGDKGAVDAILTDPdIGAVSFVG 225
Cdd:cd07134 107 ISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAK-IIREAFDEDEVAVFEGDAEVAQALLELP-FDHIFFTG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 226 STPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAisvavP----VGAETANRLVEK 301
Cdd:cd07134 185 SPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA-----PdyvfVHESVKDAFVEH 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 302 LIPKIESlRIGPYTDDQA--DMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGrdfklQGYEDGYFVGGCLFDHVTPEMDI 379
Cdd:cd07134 260 LKAEIEK-FYGKDAARKAspDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-----QFDAAQRYIAPTVLTNVTPDMKI 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930192169 380 YKTEIFGPVLSVVRAQNYEEALslpmkhEYGN------GVAIYTRDGDAARDFASRINIGMIGIN 438
Cdd:cd07134 334 MQEEIFGPVLPIITYEDLDEVI------EYINakpkplALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-478 |
1.18e-22 |
|
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: 100.37 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 75 LLNKHMDELAEMLSKEHGKT--------IEDAKGDVIRGLEvcefvcGIPHLAKGEFTEGAGPAIDMYSIR---QPVGIG 143
Cdd:cd07135 39 AVKDNEEAIVEALKKDLGRPpfetllteVSGVKNDILHMLK------NLKKWAKDEKVKDGPLAFMFGKPRirkEPLGVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 144 AGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELmIEAGLPAGILNVVNGDKGAVDAILTDPdIGAVSF 223
Cdd:cd07135 113 LIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETTALLEQK-FDKIFY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 224 VGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLI 303
Cdd:cd07135 191 TGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSVYDEFVEELK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 304 pKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDrgvEEGAKLLVDG-RDfklqgyEDGYFVGGCLFDHVTPEMDIYKT 382
Cdd:cd07135 270 -KVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD---TTKGKVVIGGeMD------EATRFIPPTIVSDVSWDDSLMSE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 383 EIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN-VPIPVPLAYHSFGGWKASSFGdl 461
Cdd:cd07135 340 ELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVDNAPFGGVGDSGYG-- 417
|
410
....*....|....*..
gi 930192169 462 NQHGTDSIKFWTKTKTV 478
Cdd:cd07135 418 AYHGKYGFDTFTHERTV 434
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
7-427 |
2.54e-22 |
|
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: 100.04 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 7 FIGGKQVAGTsGRVSNVYNPATGEVQATVALANVEeLRAAVENAKA-AQPKWAATNPQRRARVFFKFVELLNKHMDELAE 85
Cdd:cd07128 4 YVAGQWHAGT-GDGRTLHDAVTGEVVARVSSEGLD-FAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 86 mLSKEHGKTIEDAKGDVIRGLEVCEFVCGiphLAKGEFTEGA----GPAIDMYS--------IRQPV-GIGAGITPFNFP 152
Cdd:cd07128 82 -LSAATGATRRDSWIDIDGGIGTLFAYAS---LGRRELPNAHflveGDVEPLSKdgtfvgqhILTPRrGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 153 --GMipMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAG-LPAGILNVVNGDKGAVDAILTDPDIgaVSFVGSTPI 229
Cdd:cd07128 158 vwGM--LEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDV--VAFTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 230 ARYVYGTAAMNGKRAQCFGGAK--NHMIIMPDADMDQAVNAL--------MGAgygSAGERCMAIS-VAVPVGAETAnrL 298
Cdd:cd07128 234 AAKLRAHPNIVARSIRFNAEADslNAAILGPDATPGTPEFDLfvkevareMTV---KAGQKCTAIRrAFVPEARVDA--V 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 299 VEKLIPKIESLRIGPYTDDQADMGPLVTKDAYTRVRGLIDRGVEEGAKLLVDGRDFKLQG--YEDGYFVGGCLFdHVTPE 376
Cdd:cd07128 309 IEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGadAEKGAFFPPTLL-LCDDP 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 930192169 377 MD---IYKTEIFGPVLSVVRAQNYEEALSLPMKheyGNG--VA-IYTRDGDAARDFA 427
Cdd:cd07128 388 DAataVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslVAsVVTNDPAFARELV 441
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
127-438 |
3.11e-22 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 99.33 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 127 AGPAiDMYSIRQPVGIGAGITPFNFP---GMIPMwmfAPAIACGNAFILKPSERDPSLPIRLAELmIEAGLPAGILNVVN 203
Cdd:PTZ00381 98 FGPG-KSYIIPEPLGVVLVIGAWNYPlnlTLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 204 GDKGAVDAILTDPdIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYGSAGERCMA 283
Cdd:PTZ00381 173 GGVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 284 IS-VAVPvgaetaNRLVEKLIPKIESLRI---GPYTDDQADMGPLVTKDAYTRVRGLIDrgvEEGAKLLVDGRDFKLQGY 359
Cdd:PTZ00381 252 PDyVLVH------RSIKDKFIEALKEAIKeffGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEVDIENKY 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 360 edgyfVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGIN 438
Cdd:PTZ00381 323 -----VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
40-478 |
7.22e-22 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 97.87 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 40 VEELRAAVENAKAAQPKWAATnpQRRArvffkFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIrGLEVCEFVCGIPHLA 119
Cdd:cd07137 5 VRELRETFRSGRTRSAEWRKS--QLKG-----LLRLVDENEDDIFAALRQDLGKPSAESFRDEV-SVLVSSCKLAIKELK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 120 KGEFTEGAGPAIDMYS-----IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELmIEAGL 194
Cdd:cd07137 77 KWMAPEKVKTPLTTFPakaeiVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 195 PAGILNVVNGDKgAVDAILTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGY 274
Cdd:cd07137 156 DTKAIKVIEGGV-PETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 275 GS-AGERCMAISVaVPVGAETANRLVEKLIPKIESLrIGPYTDDQADMGPLVTKDAYTRVRGLIDRGvEEGAKLLVDG-R 352
Cdd:cd07137 235 GCnNGQACIAPDY-VLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDP-SVADKIVHGGeR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 353 DfklqgyEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINI 432
Cdd:cd07137 312 D------EKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSS 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 930192169 433 GMIGINVPIpVPLAYHS--FGGWKASSFGdlNQHGTDSIKFWTKTKTV 478
Cdd:cd07137 386 GGVTFNDTV-VQYAIDTlpFGGVGESGFG--AYHGKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
136-402 |
4.45e-20 |
|
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: 92.55 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 136 IRQP---VGIgagITPFNFPGMIpmwMFAP---AIACGNAFILKPSERDPslpiRLAELMIE---AGLPAGILNVVNGDk 206
Cdd:cd07133 98 EYQPlgvVGI---IVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTP----RTSALLAEllaEYFDEDEVAVVTGG- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 207 gavdailtdPDIG-AVS--------FVGSTPIARYVYGTAAMN---------GKraqcfggakNHMIIMPDADMDQAVNA 268
Cdd:cd07133 167 ---------ADVAaAFSslpfdhllFTGSTAVGRHVMRAAAENltpvtlelgGK---------SPAIIAPDADLAKAAER 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 269 LMGAGYGSAGERCMAIS-VAVPVG-----AETANRLVEKLIPKIEslrigpytdDQADMGPLVTKDAYTRVRGLIDRGVE 342
Cdd:cd07133 229 IAFGKLLNAGQTCVAPDyVLVPEDkleefVAAAKAAVAKMYPTLA---------DNPDYTSIINERHYARLQGLLEDARA 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930192169 343 EGAKL---------LVDGRDFKLQgyedgyfvggcLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALS 402
Cdd:cd07133 300 KGARVielnpagedFAATRKLPPT-----------LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAID 357
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
134-481 |
1.44e-16 |
|
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: 81.78 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 134 YSIRQPVGIGAGITPFNFPGMIpmwMFAP---AIACGNAFILKPSERDPSLPIRLAElMIEAGLPAGILNVVNGDKGAVD 210
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAK-IIEETFDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 211 AILTDP-DigAVSFVGSTPIARYVYGTAAMN---------GKraqcfggakNHMIIMPDADMDQAVNALMGAGYGSAGER 280
Cdd:cd07136 171 ELLDQKfD--YIFFTGSVRVGKIVMEAAAKHltpvtlelgGK---------SPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 281 CMAisvavP----VGAETANRLVEKLIPKIESLrIGPYTDDQADMGPLVTKDAYTRVRGLIDrgveeGAKLLVDGrdfkl 356
Cdd:cd07136 240 CVA-----PdyvlVHESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLLD-----NGKIVFGG----- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 357 QGYEDGYFVGGCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEygNGVAIY--TRDGDAARDFASRINIGM 434
Cdd:cd07136 304 NTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRP--KPLALYlfSEDKKVEKKVLENLSFGG 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 930192169 435 IGINVPIpVPLA--YHSFGGWKASSFGdlNQHGTDSIKFWTKTKTVTAR 481
Cdd:cd07136 382 GCINDTI-MHLAnpYLPFGGVGNSGMG--SYHGKYSFDTFSHKKSILKK 427
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
136-481 |
4.05e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 80.86 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 136 IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMiEAGLPAGILNVVNGDKGAVDAILtD 215
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL-E 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 216 PDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADMDQAVNALMGAGYG-SAGERCMAISVAVPVgAET 294
Cdd:PLN02174 187 QKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT-KEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 295 ANRLVEKLIPKIESLrIGPYTDDQADMGPLVTKDAYTRVRGLIDRGvEEGAKLLVDGRdfklQGYEDGYFVGGCLFDhVT 374
Cdd:PLN02174 266 APKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGE----KDRENLKIAPTILLD-VP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 375 PEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMIGINvPIPVPLAYHS--FGG 452
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIAVHLALHTlpFGG 417
|
330 340
....*....|....*....|....*....
gi 930192169 453 WKASSFGDLnqHGTDSIKFWTKTKTVTAR 481
Cdd:PLN02174 418 VGESGMGAY--HGKFSFDAFSHKKAVLYR 444
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
48-440 |
5.98e-16 |
|
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: 79.57 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 48 ENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVCEfvcgiPHLAKGEFTEGA 127
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSE-----SKLYKNIDTERG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 128 GPAID-------------MYSIRQPVGIGAGITPFNFPGMIPMwMFAPAIACGNAFILKPSERDPsLPIRLAELMIEAGL 194
Cdd:cd07077 76 ITASVghiqdvllpdngeTYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 195 PAG-----ILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTAamNGKRAQCFGGAKNHMIIMPDADMDQAVN-A 268
Cdd:cd07077 154 AAHgpkilVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGsV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 269 LMGAGYGSAGerCMAisvavpvgaetanrlvEKLIpkieslrigpytddqadmgpLVTKDAYTRVRGLI-DRGVEEGAKL 347
Cdd:cd07077 232 HDSKFFDQNA--CAS----------------EQNL--------------------YVVDDVLDPLYEEFkLKLVVEGLKV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 348 lvdgrdfklqgYEDGYFvggcLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEAL--SLPMKHEYGNGV--AIYTRDGDAA 423
Cdd:cd07077 274 -----------PQETKP----LSKETTPSFDDEALESMTPLECQFRVLDVISAVenAWMIIESGGGPHtrCVYTHKINKV 338
|
410
....*....|....*..
gi 930192169 424 RDFASRINIGMIGINVP 440
Cdd:cd07077 339 DDFVQYIDTASFYPNES 355
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
43-440 |
1.44e-14 |
|
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: 75.77 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 43 LRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGKTIEDAKgdVIRGLEVCEfvcGIPHLAKGE 122
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDK--VIKNHFAAE---YIYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 123 FTEGAGPAIDMY---SIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIEAGLPAG-- 197
Cdd:cd07081 76 KTCGVLTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGap 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 198 ---ILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGtaamNGKRAQCFGGAKNHMIIMPDADMDQAVNA-LMGAG 273
Cdd:cd07081 156 enlIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYS----SGKPAIGVGAGNTPVVIDETADIKRAVQSiVKSKT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 274 YGS----AGERCMAI--SVAVPVGAETANRLVEKLIPKiESLRIGPYTDDQADMGP-LVTKDAYTrVRGLIDRGVEEGAK 346
Cdd:cd07081 232 FDNgvicASEQSVIVvdSVYDEVMRLFEGQGAYKLTAE-ELQQVQPVILKNGDVNRdIVGQDAYK-IAAAAGLKVPQETR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 347 LlvdgrdfklqgyedgyfvggcLFDHVTP--EMDIYKTEIFGPVLSVVRAQNYEEAL--SLPMKHEYGNG--VAIYTRDg 420
Cdd:cd07081 310 I---------------------LIGEVTSlaEHEPFAHEKLSPVLAMYRAANFADADakALALKLEGGCGhtSAMYSDN- 367
|
410 420
....*....|....*....|....
gi 930192169 421 DAARD----FASRINIGMIGINVP 440
Cdd:cd07081 368 IKAIEnmnqFANAMKTSRFVKNGP 391
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
40-401 |
9.25e-13 |
|
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: 69.94 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 40 VEELRAAVENAKAAQPKWaatnpqrRARVFFKFVELLNKHMDELAEMLSKEHGKT--------IEDAKGDVIRGLEvcef 111
Cdd:cd07132 4 VRRAREAFSSGKTRPLEF-------RIQQLEALLRMLEENEDEIVEALAKDLRKPkfeavlseILLVKNEIKYAIS---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 112 vcGIPHLAKGEFTEGAGPAI--DMYSIRQPVGIGAGITPFNFPGMIpmwMFAP---AIACGNAFILKPSERDPSLPIRLA 186
Cdd:cd07132 73 --NLPEWMKPEPVKKNLATLldDVYIYKEPLGVVLIIGAWNYPLQL---TLVPlvgAIAAGNCVVIKPSEVSPATAKLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 187 ELmieagLPAGILN----VVNGdkGAVDAI-LTDPDIGAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07132 148 EL-----IPKYLDKecypVVLG--GVEETTeLLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 262 MDQAVNALMGAGYGSAGERCMAISVaVPVGAETANRLVEKLIPKIESLrigpYTDD---QADMGPLVTKDAYTRVRGLId 338
Cdd:cd07132 221 IDVAARRIAWGKFINAGQTCIAPDY-VLCTPEVQEKFVEALKKTLKEF----YGEDpkeSPDYGRIINDRHFQRLKKLL- 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930192169 339 rgveEGAKLLVDGR-DFKlqgyeDGYFVGGCLFDhVTPEMDIYKTEIFGPVLSVVRAQNYEEAL 401
Cdd:cd07132 295 ----SGGKVAIGGQtDEK-----ERYIAPTVLTD-VKPSDPVMQEEIFGPILPIVTVNNLDEAI 348
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
40-481 |
3.52e-12 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 68.21 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 40 VEELRAAVENAKAAQPKWAatnpQRRARVFFKFV-ELLNKHMDELAEMLSKEHGKTIEDAKGDVIRGLEVcefvcGIPHL 118
Cdd:PLN02203 12 VAELRETYESGRTRSLEWR----KSQLKGLLRLLkDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANL-----ALSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 119 AKGEFTEGAG------PAIDMYsIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAelmieA 192
Cdd:PLN02203 83 KKWMAPKKAKlplvafPATAEV-VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 193 GLPAGIlnvvngDKGAVDAILTDPDIG---------AVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMI---IMPDA 260
Cdd:PLN02203 157 NIPKYL------DSKAVKVIEGGPAVGeqllqhkwdKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 261 DMDQAVNALMGAGYGS-AGERCMAISVaVPVGAETANRLVEKLIPKIESLrIGPYTDDQADMGPLVTKDAYTRVRGLI-D 338
Cdd:PLN02203 231 DTKVAVNRIVGGKWGScAGQACIAIDY-VLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLkD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 339 RGVeegAKLLVDGRDFKlqgyEDGYFVGGCLFdhVTPEMD--IYKTEIFGPVLSVVRAQNYEEALslpmkhEYGNG---- 412
Cdd:PLN02203 309 PRV---AASIVHGGSID----EKKLFIEPTIL--LNPPLDsdIMTEEIFGPLLPIITVKKIEDSI------AFINSkpkp 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930192169 413 VAIY--TRDGDAARDFASRINIGMIGINVPIpVPLAYHS--FGGWKASSFGdlNQHGTDSIKFWTKTKTVTAR 481
Cdd:PLN02203 374 LAIYafTNNEKLKRRILSETSSGSVTFNDAI-IQYACDSlpFGGVGESGFG--RYHGKYSFDTFSHEKAVLRR 443
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
23-403 |
2.83e-11 |
|
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: 65.59 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 23 VYNPATGEVQATVALANVEELRAAVENAKAAqPKW----AATNPQRR---ARVFFKFVELLNKHMDE--LAEMLSKEHGK 93
Cdd:cd07126 16 LLDPLNGDKFISVPDTDEDEINEFVDSLRQC-PKSglhnPLKNPERYllyGDVSHRVAHELRKPEVEdfFARLIQRVAPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 94 TIEDAKGDVIRGLEVCEFVCG--IPHLAKGEFTEGAGPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFI 171
Cdd:cd07126 95 SDAQALGEVVVTRKFLENFAGdqVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 172 LKPSERDPSLPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTDPDIGAVSFVGSTPIARYVygTAAMNGKrAQCFGGAK 251
Cdd:cd07126 175 LKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERL--ALELHGK-VKLEDAGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 252 NHMIIMPD-ADMDQAVNALMGAGYGSAGERCMAISVAVPVGAETANRLVEKLIP-----KIESLRIGPYTDdqadmgpLV 325
Cdd:cd07126 252 DWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAGILDKLKAlaeqrKLEDLTIGPVLT-------WT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 326 TKDAYTRVRGLIdrgVEEGAKLLVDGRDFKLQGYEDGY--------FVGgcLFDHVTPE-MDIYKTEIFGPVLSVVRAQN 396
Cdd:cd07126 325 TERILDHVDKLL---AIPGAKVLFGGKPLTNHSIPSIYgayeptavFVP--LEEIAIEEnFELVTTEVFGPFQVVTEYKD 399
|
....*..
gi 930192169 397 YEEALSL 403
Cdd:cd07126 400 EQLPLVL 406
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
43-403 |
2.59e-10 |
|
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: 62.56 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 43 LRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEM-----------LSKEHGKTIEDAKG--DVIRglevc 109
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARahaetglpearLQGELGRTTGQLRLfaDLVR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 110 efvcgiphlaKGEFTEGA----------GPAIDMYSIRQPVGIGAGITPFNFP-------GMipmwmFAPAIACGNAFIL 172
Cdd:cd07129 76 ----------EGSWLDARidpadpdrqpLPRPDLRRMLVPLGPVAVFGASNFPlafsvagGD-----TASALAAGCPVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 173 KPSERDPSLPIRLAELMIEA----GLPAGILNVVNGDKGAV-DAILTDPDIGAVSFVGSTPIARYVYGTAAmngKRAQ-- 245
Cdd:cd07129 141 KAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARPEpi 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 246 -CFG--GAKNHMIIMPDAdMDQAVNALMGAGYGS----AGERCMAISVAVPVGAETANRLVEKLIPKIEslrigpytddQ 318
Cdd:cd07129 218 pFYAelGSVNPVFILPGA-LAERGEAIAQGFVGSltlgAGQFCTNPGLVLVPAGPAGDAFIAALAEALA----------A 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 319 ADMGPLVTKdaytRVRGLIDRGVEE-----GAKLLVDGrdfklQGYEDGYFVGGCLFdHVT-------PEMdiyKTEIFG 386
Cdd:cd07129 287 APAQTMLTP----GIAEAYRQGVEAlaaapGVRVLAGG-----AAAEGGNQAAPTLF-KVDaaafladPAL---QEEVFG 353
|
410
....*....|....*..
gi 930192169 387 PVLSVVRAQNYEEALSL 403
Cdd:cd07129 354 PASLVVRYDDAAELLAV 370
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
43-452 |
1.16e-08 |
|
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: 57.12 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 43 LRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGktIEDAKGDVIRGLEVCEfvcGIPHLAKGE 122
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETG--MGVVEDKVIKNHFASE---YVYNDIKDM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 123 FTEGA---GPAIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELM----IEAGLP 195
Cdd:cd07122 76 KTVGVieeDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 196 AGILNVV-NGDKGAVDAILTDPDIGAVSFVGSTPIARYVYGTaamnGKRAQCfGGAKN-HMIIMPDADMDQAVNALMGA- 272
Cdd:cd07122 156 EGLIQWIeEPSIELTQELMKHPDVDLILATGGPGMVKAAYSS----GKPAIG-VGPGNvPAYIDETADIKRAVKDIILSk 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 273 ----GYGSAGERcmaisvAVPVGAETANRLVEKL-------IPKIESLRIGPY-TDDQADM-GPLVTKDAYTrvrgLIDR 339
Cdd:cd07122 231 tfdnGTICASEQ------SVIVDDEIYDEVRAELkrrgayfLNEEEKEKLEKAlFDDGGTLnPDIVGKSAQK----IAEL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 340 -GVE--EGAKLLVdgrdfklqgyedgyfvggCLFDHVTPEmDIYKTEIFGPVLSVVRAQNYEEALSLPMK--HEYGNG-- 412
Cdd:cd07122 301 aGIEvpEDTKVLV------------------AEETGVGPE-EPLSREKLSPVLAFYRAEDFEEALEKAREllEYGGAGht 361
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 930192169 413 VAIYTRDGDAARDFASRINIGMIGINVPipvplayHSFGG 452
Cdd:cd07122 362 AVIHSNDEEVIEEFALRMPVSRILVNTP-------SSLGG 394
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
15-247 |
8.75e-07 |
|
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: 51.33 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 15 GTSGRVSNVYNPATGEVQATVALANVEELRAAvenAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAE--MLSKEHG 92
Cdd:cd07127 61 GASGWVGGEVSPYGVELGVTYPQCDPDALLAA---ARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavMHTTGQA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 93 KTIEDAKG-----DviRGLEVCEF----VCGIPHLAKGEFTEGAGPAIDMYSIRQPV--GIGAGITPFNFpgmiPMW--- 158
Cdd:cd07127 138 FMMAFQAGgphaqD--RGLEAVAYawreMSRIPPTAEWEKPQGKHDPLAMEKTFTVVprGVALVIGCSTF----PTWngy 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 159 --MFApAIACGNAFILKPSERdPSLPIRLA-----ELMIEAGLPAGILNVVNGDKGA--VDAILTDPDIGAVSFVGSTPI 229
Cdd:cd07127 212 pgLFA-SLATGNPVIVKPHPA-AILPLAITvqvarEVLAEAGFDPNLVTLAADTPEEpiAQTLATRPEVRIIDFTGSNAF 289
|
250
....*....|....*...
gi 930192169 230 ARYVYGTAamngKRAQCF 247
Cdd:cd07127 290 GDWLEANA----RQAQVY 303
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
30-440 |
1.04e-06 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 51.34 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 30 EVQATVALANVEELRAAVENAKAAQPKWAATNPQRRARVFFKF-VELLNKHMdELAEMLSKEHGKTI-EDakgDVIRGLE 107
Cdd:PRK13805 1 MTKEEMAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAaLAALDARI-PLAKMAVEETGRGVvED---KVIKNHF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 108 VCEFvcgIPHLAKGEFTEG---AGPAIDMYSIRQPVGIGAGITPFN-------FPGMIpmwmfapAIACGNAFILKPSER 177
Cdd:PRK13805 77 ASEY---IYNSYKDEKTVGvieEDDEFGIIEIAEPVGVIAGITPTTnptstaiFKALI-------ALKTRNPIIFSFHPR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 178 DPSLPIRLAELM----IEAGLPAGILNVVngDKGAVD---AILTDPDIGAVSFVGSTPIARYVYGTaamnGKRAQCFGGA 250
Cdd:PRK13805 147 AQKSSIAAAKIVldaaVAAGAPKDIIQWI--EEPSVEltnALMNHPGIALILATGGPGMVKAAYSS----GKPALGVGAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 251 KNHMIIMPDADMDQAVNALMGA-----GYGSAGERCMAI--SVAVPVGAETANR----LVEKLIPKIESLRIGPytDDQA 319
Cdd:PRK13805 221 NVPAYIDKTADIKRAVNDILLSktfdnGMICASEQAVIVddEIYDEVKEEFASHgayfLNKKELKKLEKFIFGK--ENGA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 320 DMGPLVTKDAYTrvrglIDR--GVE--EGAKLLVdgrdFKLQGYEDGYfvggcLFDHvtpemdiyktEIFGPVLSVVRAQ 395
Cdd:PRK13805 299 LNADIVGQSAYK-----IAEmaGFKvpEDTKILI----AEVKGVGESE-----PLSH----------EKLSPVLAMYKAK 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 930192169 396 NYEEALSLPMK----HEYGNGVAIYTRDGDAARDFASRINIGMIGINVP 440
Cdd:PRK13805 355 DFEDAVEKAEKlvefGGLGHTAVIYTNDDELIKEFGLRMKACRILVNTP 403
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
134-269 |
5.10e-06 |
|
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: 48.59 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 134 YSIRQPVGIGAGITPFNFPGmIPMWMFAPAIACGNAFILKPSERDPSLPIRLAE--LMIEAGLP-AGILNVVNGDKGAV- 209
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAALLAsfADLDPTHPlADSLSVVYWDGGSTq 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930192169 210 --DAILTDPDigAVSFVGSTPIARYVYGTAAmNGKRAQCFGGAKNHMIIMPDADMDQAVNAL 269
Cdd:pfam05893 162 leDLIVANAD--VVIAWGGEDAINAIRECLK-PGKQWIDFGAKISFAVVDREAALDKAAERA 220
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
41-431 |
1.52e-05 |
|
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: 47.23 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 41 EELRAAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHGK-TIEDakgDVIRGLEVCEFVCGIPHLA 119
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMgRVED---KIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 120 KGEFTEGAGPAIDMYSirqPVGIGAGITPFNFPG------MIPMwmfapaIACGNAFILKPSERDPSLPIRLAELM---- 189
Cdd:cd07121 81 TTAWSGDNGLTLVEYA---PFGVIGAITPSTNPTetiinnSISM------LAAGNAVVFNPHPGAKKVSAYAVELInkai 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 190 IEAGLPAGILNVV-NGDKGAVDAILTDPDIGAVSFVGSTPIARyvygtAAMN-GKRAQCfGGAKNHMIIMPD-ADMDQ-A 265
Cdd:cd07121 152 AEAGGPDNLVVTVeEPTIETTNELMAHPDINLLVVTGGPAVVK-----AALSsGKKAIG-AGAGNPPVVVDEtADIEKaA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 266 VNALMGAGYGS----AGE--------------RCMAISVAVPVGAETANRLVEKLIPKIESLRIGPytddqadmgPLVTK 327
Cdd:cd07121 226 RDIVQGASFDNnlpcIAEkeviavdsvadyliAAMQRNGAYVLNDEQAEQLLEVVLLTNKGATPNK---------KWVGK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 328 DAYTRVRGLidrGVEEGAKLLvdgrdfklqgyedgyfvggCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKH 407
Cdd:cd07121 297 DASKILKAA---GIEVPADIR-------------------LIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVEL 354
|
410 420
....*....|....*....|....*.
gi 930192169 408 EYGN--GVAIYTRDGDAARDFASRIN 431
Cdd:cd07121 355 EHGNrhTAIIHSKNVENLTKMARAMQ 380
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
38-411 |
1.59e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 47.20 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 38 ANVEElraAVENAKAAQPKWAATNPQRRARVFFKFVELLNKHMDELAEMLSKEHG-KTIEDakgDVIRGLEVCEFVCGIP 116
Cdd:PRK15398 36 ASVDD---AVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmGRVED---KIAKNVAAAEKTPGVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 117 HLAKGEFTEGAGPAIDMYSirqPVGIGAGITPFNFPG------MIPMwmfapaIACGNA--FILKPSERDPSLPI--RLA 186
Cdd:PRK15398 110 DLTTEALTGDNGLTLIEYA---PFGVIGAVTPSTNPTetiinnAISM------LAAGNSvvFSPHPGAKKVSLRAieLLN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 187 ELMIEAGLPAGILNVV-NGDKGAVDAILTDPDIGAVSFVGSTPIARyvygtAAMN-GKRAQCfGGAKNHMIIMPD-ADMD 263
Cdd:PRK15398 181 EAIVAAGGPENLVVTVaEPTIETAQRLMKHPGIALLVVTGGPAVVK-----AAMKsGKKAIG-AGAGNPPVVVDEtADIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930192169 264 QAVNALM-GAGYGS----AGERCMaisVAVpvgAETANRLVEKLipkiesLRIGPY--TDDQAD-MGPLVTKDAYTRVRG 335
Cdd:PRK15398 255 KAARDIVkGASFDNnlpcIAEKEV---IVV---DSVADELMRLM------EKNGAVllTAEQAEkLQKVVLKNGGTVNKK 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930192169 336 LIDRgveeGAKLLVDGRDFKLQGYEDgyfvggCLFDHVTPEMDIYKTEIFGPVLSVVRAQNYEEALSLPMKHEYGN 411
Cdd:PRK15398 323 WVGK----DAAKILEAAGINVPKDTR------LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
134-191 |
5.26e-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: 5.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 930192169 134 YSIRQPVGIGAGITPFNFPGmIPMWMFAPAIACGNAFILKPSERDPSLPIRLAELMIE 191
Cdd:cd07080 107 YIRAQPRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLAD 163
|
|
| |
