|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-481 |
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: 760.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 7 IKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEEL 86
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 87 ARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIA 166
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 167 IALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKR 246
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 247 VQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPV 326
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 327 IREENQKRTLTYIEKGVEEGAKLTVDGRET---GISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIA 403
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 404 NKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHANGKDSVDFYTHKKVVTARY 481
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-481 |
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: 582.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 1 MTKvRKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLI 80
Cdd:COG1012 1 MTT-PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 81 QHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPC 160
Cdd:COG1012 80 ERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 161 WMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKT 239
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 240 GSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDD 319
Cdd:COG1012 240 AAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 320 GVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEA 399
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 400 VKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHanGKDSVDFYTHKKVVTA 479
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVTI 477
|
..
gi 502749847 480 RY 481
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
15-477 |
0e+00 |
|
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: 549.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 15 WVASKTEKYEnVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLEN 94
Cdd:pfam00171 1 WVDSESETIE-VINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 95 GKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASiATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFI 174
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 175 LKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGA 253
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 254 KNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQK 333
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 334 RTLTYIEKGVEEGAKLTVDGREtGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGAC 413
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEA-GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502749847 414 IFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGtlHANGKDSVDFYTHKKVV 477
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFG--REGGPYGLEEYTEVKTV 459
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
7-481 |
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: 540.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 7 IKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEEL 86
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 87 ARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIA 166
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 167 IALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKR 246
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 247 VQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVtVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPV 326
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 327 IREENQKRTLTYIEKGVEEGAKLTVDGRE---TGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIA 403
Cdd:TIGR01722 320 ITPQAKDRVASLIAGGAAEGAEVLLDGRGykvDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 404 NKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHANGKDSVDFYTHKKVVTARY 481
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
47-479 |
6.16e-166 |
|
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: 475.54 E-value: 6.16e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 47 DEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDS 126
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 127 LASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVY 206
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 207 G-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCM 285
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 286 ACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGHFVG 365
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 366 PTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMA 445
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420 430
....*....|....*....|....*....|....
gi 502749847 446 FFPFSGWKSSFYGtlHANGKDSVDFYTHKKVVTA 479
Cdd:cd07078 401 SAPFGGVKQSGIG--REGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
8-477 |
1.11e-150 |
|
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: 438.22 E-value: 1.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 8 KNYVNGEWVASKTEKYenVINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEEL 86
Cdd:cd07097 2 RNYIDGEWVAGGDGEE--NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 87 ARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIA 166
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 167 IALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLK 245
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 246 RVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGP 325
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 326 VIREENQKRTLTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIAN 404
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGeRLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502749847 405 KSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLgvpaPMA----FFPFSGWKSSFYGtLHANGKDSVDFYTHKKVV 477
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNL----PTAgvdyHVPFGGRKGSSYG-PREQGEAALEFYTTIKTV 471
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-481 |
1.16e-149 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 440.34 E-value: 1.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 6 KIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEE 85
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 86 LARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPI 165
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 166 AIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLK 245
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 246 RVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVtVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGP 325
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 326 VIREENQKRTLTYIEKGVEEGAKLTVDGRET---GISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKI 402
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 403 ANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHANGKDSVDFYTHKKVVTARY 481
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQ 590
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
9-482 |
3.01e-145 |
|
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: 424.45 E-value: 3.01e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 9 NYVNGEWVASKTEKYENVINPATG-EILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAI 167
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 168 ALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKR 246
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 247 VQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPV 326
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 327 IREENQKRTLTYIEKGVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIA 403
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGErltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 404 NKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHAnGKDSVDFYTHKKVVTARYS 482
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGHREA-GTTALDAFTEWKAVYVDYS 478
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
9-482 |
4.64e-138 |
|
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: 406.18 E-value: 4.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 9 NYVNGEWVASKTEKYENvINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:cd07086 1 GVIGGEWVGSGGETFTS-RNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASiatdvEAANY-----RYPVGVVGGIAPFNFPMMVPCWMF 163
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPS-----ERPGHrlmeqWNPLGVVGVITAFNFPVAVPGWNA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 164 PIAIALGNSFILKPSERTPLLMEKLVELFTEA----GLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKT 239
Cdd:cd07086 155 AIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 240 GSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDD 319
Cdd:cd07086 235 VARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 320 GVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQE 398
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGkRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 399 AVKIANKSEFANGACIFTNNAKAIRYFREK--IDAGMLGVNLGVPAPMAFFPFSGWKSSfyGTLHANGKDSVDFYTHKKV 476
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIGGAFGGEKET--GGGRESGSDAWKQYMRRST 472
|
....*.
gi 502749847 477 VTARYS 482
Cdd:cd07086 473 CTINYS 478
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
26-478 |
1.95e-130 |
|
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: 385.63 E-value: 1.95e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPM-MV-----PcwmfpiAIALGNSFILKPSE 179
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAaMItrkiaP------ALAAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 180 RTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGIL-ENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQ-ALTGaknH- 256
Cdd:cd07103 155 ETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALcASPRVRKISFTGSTAVGKLLMAQAADTVKRVSlELGG---Na 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 257 -TIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRT 335
Cdd:cd07103 232 pFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 336 LTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIF 415
Cdd:cd07103 312 EALVEDAVAKGAKVLTGGKRLG-LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502749847 416 TNNAKAIRYFREKIDAGMLGVNLGVPA-PMAffPFSGWKSSFYGtlHANGKDSVDFYTHKKVVT 478
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLISdAEA--PFGGVKESGLG--REGGKEGLEEYLETKYVS 450
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-479 |
3.91e-124 |
|
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: 366.55 E-value: 3.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 55 KAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDV 134
Cdd:cd06534 5 AAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 135 EAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-N 213
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVgA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 214 GILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVE 293
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 294 EGIADEFLEALRiaarnvkignglddgvflgpvireenqkrtltyiekgveegakltvdgretgiskghfvgpTILEEVT 373
Cdd:cd06534 245 ESIYDEFVEKLV-------------------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 374 TDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWK 453
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVK 343
|
410 420
....*....|....*....|....*.
gi 502749847 454 SSFYGTLHanGKDSVDFYTHKKVVTA 479
Cdd:cd06534 344 NSGIGREG--GPYGLEEYTRTKTVVI 367
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-458 |
1.61e-121 |
|
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: 363.94 E-value: 1.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEARGEVQRGIENVEFAAGAPTlMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAI 167
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLAT-KETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 168 ALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKR 246
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 247 VQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPV 326
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 327 IREENQKRTLTYIEKGVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIA 403
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 502749847 404 NKSEFANGACIFTNN-AKAIRYFReKIDAGMLGVN-LGVPAPMAffPFSGWKSSFYG 458
Cdd:cd07119 400 NDTPYGLAGAVWTKDiARANRVAR-RLRAGTVWINdYHPYFAEA--PWGGYKQSGIG 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
10-481 |
4.39e-117 |
|
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: 353.84 E-value: 4.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVasKTEKYENVINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:cd07124 36 VIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNLSEARGEVQRGIENVEFAA-------GAPTLMMGDslasiatdvEAANYRY-PVGVVGGIAPFNFPMMVPC 160
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAremlrlrGFPVEMVPG---------EDNRYVYrPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 161 WMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYK- 238
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYEr 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 239 -----TGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKI 313
Cdd:cd07124 265 aakvqPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 314 GNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRV 393
Cdd:cd07124 345 GDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 394 KNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPM-AFFPFSGWKSSFYGTlHANGKDSVDFYT 472
Cdd:cd07124 425 KDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALvGRQPFGGFKMSGTGS-KAGGPDYLLQFM 503
|
....*....
gi 502749847 473 HKKVVTARY 481
Cdd:cd07124 504 QPKTVTENF 512
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
26-477 |
1.16e-116 |
|
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: 350.70 E-value: 1.16e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARG 103
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 104 EVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPL 183
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 184 LMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLND 262
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 263 ADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKG 342
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 343 VEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN- 418
Cdd:cd07114 321 REEGARVLTGGErpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDl 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 419 AKAIRyFREKIDAGMLGVNL-GVPAPMAffPFSGWKSSFYGtlHANGKDSVDFYTHKKVV 477
Cdd:cd07114 401 ARAHR-VARAIEAGTVWVNTyRALSPSS--PFGGFKDSGIG--RENGIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-478 |
1.37e-116 |
|
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: 350.33 E-value: 1.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEAR-GE 104
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSLAsiaTDVEAANY--RYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTP 182
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYP---QDGGALNYvlRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 183 LLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGIL-ENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLN 261
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALvAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 262 DADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEK 341
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 342 GVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN 418
Cdd:cd07093 318 ARAEGATILTGGGrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502749847 419 -AKAIRyFREKIDAGMLGVNlgvpapmAFF------PFSGWKSSfyGTLHANGKDSVDFYTHKKVVT 478
Cdd:cd07093 398 lGRAHR-VARRLEAGTVWVN-------CWLvrdlrtPFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
10-478 |
1.09e-115 |
|
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: 348.81 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVP--RRARILFSFQQLLIQHKEELA 87
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDprERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSE-ARGEVQRGIENVEFAAGAPTLMMGDSlasIATDVEAANY--RYPVGVVGGIAPFNFPMMVPCWMFP 164
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKT---IPIDGNFLAYtrREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 165 IAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYVYKTGSA- 242
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 243 NLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVF 322
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 323 LGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKI 402
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG-SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 403 ANKSEFANGACIFTNN-AKAIRYFReKIDAGMLGVN-LGVPAPMAffPFSGWKSSFYGtlHANGKDSVDFYTHKKVVT 478
Cdd:cd07091 403 ANDTEYGLAAGVFTKDiNKALRVSR-ALKAGTVWVNtYNVFDAAV--PFGGFKQSGFG--RELGEEGLEEYTQVKAVT 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
10-477 |
1.24e-112 |
|
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: 340.78 E-value: 1.24e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARL 89
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 90 ITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASiatDVEAAN---YRYPVGVVGGIAPFNFPM-MVPCWMFPi 165
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPS---DRPNENifiFKVPIGVVAGILPWNFPFfLIARKLAP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 166 AIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANL 244
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 245 KRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLG 324
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 325 PVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIAN 404
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502749847 405 KSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFpFSGWKSSfyGTLHANGKDSVDFYTHKKVV 477
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGF-HAGWKKS--GLGGADGKHGLEEYLQTKVV 466
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-477 |
4.25e-112 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 340.51 E-value: 4.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 11 VNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLI 90
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 91 TLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALG 170
Cdd:PLN02278 109 TLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 171 NSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQA 249
Cdd:PLN02278 189 CTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGdAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 250 LTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIRE 329
Cdd:PLN02278 269 ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 330 ENQKRTLTYIEKGVEEGAKLTVDGRETGIsKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFA 409
Cdd:PLN02278 349 AAVQKVESHVQDAVSKGAKVLLGGKRHSL-GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAG 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 410 NGACIFTNNAKAIRYFREKIDAGMLGVNLG-VPAPMAffPFSGWKSSfyGTLHANGKDSVDFYTHKKVV 477
Cdd:PLN02278 428 LAAYIFTRDLQRAWRVSEALEYGIVGVNEGlISTEVA--PFGGVKQS--GLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-480 |
1.29e-110 |
|
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: 335.70 E-value: 1.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 8 KNYVNGEWVASKTEKYEnVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQ-VAVPRRARILFSFQQLLIQHKEEL 86
Cdd:cd07082 3 KYLINGEWKESSGKTIE-VYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 87 ARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIAT----DVEAANYRYPVGVVGGIAPFNFPMMVP-CW 161
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFpgtkGKIAQVRREPLGVVLAIGPFNYPLNLTvSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 162 MFPIAIAlGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTG 240
Cdd:cd07082 162 LIPALIM-GNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 241 SanLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDG 320
Cdd:cd07082 241 P--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 321 VFLGPVIREENQKRTLTYIEKGVEEGAK-LTVDGRETgiskGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEA 399
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATvLNGGGREG----GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 400 VKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLhanG-KDSVDFYTHKKVVT 478
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQ---GiGDALRSMTRRKGIV 471
|
..
gi 502749847 479 AR 480
Cdd:cd07082 472 IN 473
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
26-477 |
3.16e-110 |
|
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: 334.27 E-value: 3.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAPTLMMGDSLaSIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLM 185
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHV-PLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 186 EKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADL 265
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 266 EDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEE 345
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 346 GAKLTVDGR----ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKa 421
Cdd:cd07090 320 GAKVLCGGErvvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ- 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 422 iRYFR--EKIDAGMLGVNLGVPAPmAFFPFSGWKSSFYGtlHANGKDSVDFYTHKKVV 477
Cdd:cd07090 399 -RAHRviAQLQAGTCWINTYNISP-VEVPFGGYKQSGFG--RENGTAALEHYTQLKTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-477 |
8.63e-110 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 332.87 E-value: 8.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARG-E 104
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSlasIATDVEAANY--RYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTP 182
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEV---IPVRGPFLNYtvREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 183 LLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLN 261
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 262 DADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEK 341
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 342 GVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKA 421
Cdd:cd07115 318 GREEGARLLTGGKRPG-ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 502749847 422 IRYFREKIDAGMLGVN-LGVPAPMAffPFSGWKSSFYGTLHanGKDSVDFYTHKKVV 477
Cdd:cd07115 397 AHRVAAALKAGTVWINtYNRFDPGS--PFGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-477 |
2.48e-109 |
|
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: 331.87 E-value: 2.48e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARg 103
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 104 evqrgieNVEFAAGAPTLM--------MGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFIL 175
Cdd:cd07112 85 -------AVDVPSAANTFRwyaeaidkVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 176 KPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGIL--ENDkIKAVSFVGSKPVGEYVYK-TGSANLKRVQALTG 252
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALglHMD-VDALAFTGSTEVGRRFLEySGQSNLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 253 AKNHTIVLNDA-DLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREEN 331
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 332 QKRTLTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFAN 410
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGkRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502749847 411 GACIFTNN-AKAIRYFREkIDAGMLGVNlGVPAPMAFFPFSGWKSSFYG---TLHAngkdsVDFYTHKKVV 477
Cdd:cd07112 397 AASVWTSDlSRAHRVARR-LRAGTVWVN-CFDEGDITTPFGGFKQSGNGrdkSLHA-----LDKYTELKTT 460
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-455 |
3.77e-109 |
|
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: 331.77 E-value: 3.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 9 NYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNLSEARG-EVQRGIENVEFAAgaptlmmgDSLASIATDVEAANY---RYPVGVVGGIAPFNFPM-MVPCWMF 163
Cdd:cd07138 81 AITLEMGAPITLARAaQVGLGIGHLRAAA--------DALKDFEFEERRGNSlvvREPIGVCGLITPWNWPLnQIVLKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 164 PiAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSA 242
Cdd:cd07138 153 P-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 243 NLKRV-QALTGaKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGV 321
Cdd:cd07138 232 TVKRVaLELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 322 FLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRE--TGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEA 399
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 502749847 400 VKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAffPFSGWKSS 455
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS 444
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
10-481 |
1.93e-108 |
|
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: 330.17 E-value: 1.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFE-KWSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNLSEARG-EVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANY-----RYPVGVVGGIAPFNFPMMVPCWM 162
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYtaftrREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 163 FPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSA 242
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 243 NLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVF 322
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 323 LGPVIREENQKRTLTYIEKGVEEGAKLtVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKI 402
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEI-VRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 403 ANKSEFANGACIFTNN-AKAIRYFrEKIDAGMLGVNLGV---PApmafFPFSGWKSSfyGTLHANGKDSVDFYTHKKVVT 478
Cdd:cd07113 402 INDTPFGLTASVWTNNlSKALRYI-PRIEAGTVWVNMHTfldPA----VPFGGMKQS--GIGREFGSAFIDDYTELKSVM 474
|
...
gi 502749847 479 ARY 481
Cdd:cd07113 475 IRY 477
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
26-458 |
6.45e-108 |
|
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: 328.02 E-value: 6.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAPTLMMGDSLASIAT----DVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERT 181
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPFDASpggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 182 PLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTgsANLKRVQALTGAKNHTIVL 260
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGsGETVGDALVTDPRVRMISFTGSPAVGEAIARK--AGLKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 261 NDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIE 340
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 341 KGVEEGAKLTVDGRETgiskGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAK 420
Cdd:cd07149 321 EAVEGGARLLTGGKRD----GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQ 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 502749847 421 AIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYG 458
Cdd:cd07149 397 KALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-478 |
4.14e-106 |
|
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: 323.52 E-value: 4.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLL 184
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 185 MEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDA 263
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 264 DLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGV 343
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 344 EEGAKLTVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-AKAI 422
Cdd:cd07118 322 AEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDiDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 423 RYFReKIDAGMLGVNL---GVPApmafFPFSGWKSSFYGtlHANGKDSVDFYTHKKVVT 478
Cdd:cd07118 402 TVAR-RIRAGTVWVNTfldGSPE----LPFGGFKQSGIG--RELGRYGVEEYTELKTVH 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
45-478 |
5.11e-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: 5.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 45 ELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMG 124
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 125 DSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTP----LLmekLVELFTEAGLPNG 200
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtggLL---IAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 201 VFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGS 279
Cdd:cd07104 158 VLNVVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 280 AGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGREtgis 359
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 360 KGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-AKAIRyFREKIDAGMLGVNL 438
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlERAMA-FAERLETGMVHIND 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502749847 439 GVPAPMAFFPFSGWKSSFYGTLhaNGKDSVDFYTHKKVVT 478
Cdd:cd07104 393 QTVNDEPHVPFGGVKASGGGRF--GGPASLEEFTEWQWIT 430
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
28-478 |
1.05e-104 |
|
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: 319.66 E-value: 1.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 28 NPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQR 107
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 108 GIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEK 187
Cdd:cd07150 85 TPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 188 LVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLE 266
Cdd:cd07150 165 IAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 267 DTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEG 346
Cdd:cd07150 245 YAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 347 AKLTVDGREtgisKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFR 426
Cdd:cd07150 325 AKLLTGGKY----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 502749847 427 EKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGtlHANGKDSVDFYTHKKVVT 478
Cdd:cd07150 401 ERLESGMVHINDPTILDEAHVPFGGVKASGFG--REGGEWSMEEFTELKWIT 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-477 |
1.83e-104 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 320.29 E-value: 1.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 1 MTKVRKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLI 80
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 81 QHKEELARLITLENGKNLSEAR-GEVQRGIENVEFAAG-APTLMmGDSLASIATDVeAANYRYPVGVVGGIAPFNFPMMV 158
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGlAPALE-GEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 159 PCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYK 238
Cdd:PRK13252 159 ACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 239 TGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLD 318
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 319 DGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKN 395
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGErltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 396 LQEAVKIANKSEFANGACIFTNN-AKAIRYFrEKIDAGMLGVNL--GVPAPMaffPFSGWKSSFYGtlHANGKDSVDFYT 472
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADlSRAHRVI-HQLEAGICWINTwgESPAEM---PVGGYKQSGIG--RENGIATLEHYT 472
|
....*
gi 502749847 473 HKKVV 477
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-455 |
1.49e-103 |
|
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: 316.98 E-value: 1.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07145 3 VRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAPTLMMGDSLASIATDVE----AANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERT 181
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 182 PLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVL 260
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 261 NDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIE 340
Cdd:cd07145 243 KDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 341 KGVEEGAKLTVDGRETGiskGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAK 420
Cdd:cd07145 323 DAVEKGGKILYGGKRDE---GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
410 420 430
....*....|....*....|....*....|....*
gi 502749847 421 AIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSS 455
Cdd:cd07145 400 RALKVARELEAGGVVINDSTRFRWDNLPFGGFKKS 434
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
26-477 |
1.70e-103 |
|
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: 316.39 E-value: 1.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGienVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLM 185
Cdd:cd07106 81 GGA---VAWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 186 EKLVELFTEAgLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADL 265
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 266 EDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEE 345
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 346 GAKLtVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-AKAIRY 424
Cdd:cd07106 317 GAKV-LAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDlERAEAV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 502749847 425 FReKIDAGMLGVN-LGVPAPMAffPFSGWKSSFYGtlHANGKDSVDFYTHKKVV 477
Cdd:cd07106 396 AR-RLEAGTVWINtHGALDPDA--PFGGHKQSGIG--VEFGIEGLKEYTQTQVI 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-478 |
3.01e-102 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 313.52 E-value: 3.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAG---------APTLMMGDSlasiatDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILK 176
Cdd:cd07110 81 DDVAGCFEYYADlaeqldakaERAVPLPSE------DFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 177 PSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDK-IKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKN 255
Cdd:cd07110 155 PSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 256 HTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRT 335
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 336 LTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACI 414
Cdd:cd07110 315 LSFIARGKEEGARLLCGGrRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 415 FTNNAKAIRYFREKIDAGMLGVNlgvpAPMAFFPFSGW----KSSFYGTLHANGKDSvdfYTHKKVVT 478
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWIN----CSQPCFPQAPWggykRSGIGRELGEWGLDN---YLEVKQIT 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
10-477 |
6.38e-102 |
|
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: 313.96 E-value: 6.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK-WSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNL-SEARGEVQRGIENVEFAAGAPTLMMGDSlasIATDVEAANY--RYPVGVVGGIAPFNFPMMVPCWMFPI 165
Cdd:cd07144 91 IEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKT---IPTSPNKLAYtlHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 166 AIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANL 244
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 245 KRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAAR-NVKIGNGLDDGVFL 323
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 324 GPVIREENQKRTLTYIEKGVEEGAKLTVDG--RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVK 401
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 402 IANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN------LGVpapmaffPFSGWKSSfyGTLHANGKDSVDFYTHKK 475
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINssndsdVGV-------PFGGFKMS--GIGRELGEYGLETYTQTK 478
|
..
gi 502749847 476 VV 477
Cdd:cd07144 479 AV 480
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
13-478 |
5.06e-100 |
|
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: 308.08 E-value: 5.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 13 GEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITL 92
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 93 ENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNS 172
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 173 FILKPSERTP----LLmekLVELFTEAGLPNGVFNVVYGA-HDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRV 247
Cdd:cd07151 161 VVLKPASDTPitggLL---LAKIFEEAGLPKGVLNVVVGAgSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 248 QALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVI 327
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 328 REENQKRTLTYIEKGVEEGAKLTVDGRETgiskGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSE 407
Cdd:cd07151 318 NESQVDGLLDKIEQAVEEGATLLVGGEAE----GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502749847 408 FANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLhaNGKDSVDFYTHKKVVT 478
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRF--NGEWALEEFTTDKWIS 462
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
26-458 |
1.54e-99 |
|
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: 306.67 E-value: 1.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAA------GAPTLMMGDSLASiaTDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSE 179
Cdd:cd07094 83 DRAIDTLRLAAeeaeriRGEEIPLDATQGS--DNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 180 RTPLLMEKLVELFTEAGLPNGVFNVVYGA-HDVVNGILENDKIKAVSFVGSKPVGEYVykTGSANLKRVQALTGAKNHTI 258
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 259 VLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTY 338
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 339 IEKGVEEGAKLTVDGREtgisKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN 418
Cdd:cd07094 319 VEEAVEAGARLLCGGER----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502749847 419 AKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYG 458
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-480 |
2.60e-99 |
|
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: 306.97 E-value: 2.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 3 KVRKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK---WSQVAVPRRARILFSFQQLL 79
Cdd:cd07141 3 EIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 80 IQHKEELARLITLENGKNLSEAR-GEVQRGIENVEFAAGAPTLMMGDSlasIATDVEAANY-RY-PVGVVGGIAPFNFPM 156
Cdd:cd07141 83 ERDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKT---IPMDGDFFTYtRHePVGVCGQIIPWNFPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 157 MVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEY 235
Cdd:cd07141 160 LMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 236 VYK-TGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIG 314
Cdd:cd07141 240 IQQaAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 315 NGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVK 394
Cdd:cd07141 320 NPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 395 NLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-LGVPAPMAffPFSGWKSSFYGtlHANGKDSVDFYTH 473
Cdd:cd07141 399 TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNcYNVVSPQA--PFGGYKMSGNG--RELGEYGLQEYTE 474
|
....*..
gi 502749847 474 KKVVTAR 480
Cdd:cd07141 475 VKTVTIK 481
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
10-481 |
4.38e-98 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 304.94 E-value: 4.38e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVasKTEKYENVINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:PRK03137 40 IIGGERI--TTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNLSEARGEVQRGIENVEF--------AAGAPTLMMGDslasiatdvEAANYRY-PVGVVGGIAPFNFPMMVP 159
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYyarqmlklADGKPVESRPG---------EHNRYFYiPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 160 CWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVY- 237
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYe 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 238 -----KTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVK 312
Cdd:PRK03137 269 raakvQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 313 IGNGLDDGvFLGPVIREENQKRTLTYIEKGVEEGAKLTvdGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIR 392
Cdd:PRK03137 349 VGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGRLVL--GGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 393 VKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPM-AFFPFSGWKSSfyGT-LHANGKDSVDF 470
Cdd:PRK03137 426 AKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIvGYHPFGGFNMS--GTdSKAGGPDYLLL 503
|
490
....*....|.
gi 502749847 471 YTHKKVVTARY 481
Cdd:PRK03137 504 FLQAKTVSEMF 514
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
26-477 |
5.60e-98 |
|
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: 302.62 E-value: 5.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWS-QVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARG- 103
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 104 EVQRGIENVEFAA------------GAPTLMMGDSLASIAtdveaanyRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGN 171
Cdd:cd07089 81 QVDGPIGHLRYFAdladsfpwefdlPVPALRGGPGRRVVR--------REPVGVVAAITPWNFPFFLNLAKLAPALAAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 172 SFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYVYKTGSANLKRVQAL 250
Cdd:cd07089 153 TVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 251 TGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREE 330
Cdd:cd07089 233 LGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 331 NQKRTLTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFA 409
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGgRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 410 NGACIFTNN-AKAIRYFReKIDAGMLGVNLGVpAPMAFFPFSGWKSSFYGtlHANGKDSVDFYTHKKVV 477
Cdd:cd07089 393 LSGGVWSADvDRAYRVAR-RIRTGSVGINGGG-GYGPDAPFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
10-455 |
8.64e-98 |
|
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: 302.57 E-value: 8.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEAR-GEVQRGIENVEFAAGA----------PTLMMGDSLASiatdveaanyRYPVGVVGGIAPFNFPM 156
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALardfpfeerrPGSGGGHVLVR----------REPVGVVAAIVPWNAPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 157 MVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYV 236
Cdd:cd07139 152 FLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 237 YKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNG 316
Cdd:cd07139 232 AAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 317 LDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKN 395
Cdd:cd07139 312 LDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGgRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDD 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502749847 396 LQEAVKIANKSEFANGACIFTNN-AKAIRYFReKIDAGMLGVNLGVPAPMAffPFSGWKSS 455
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADvERGLAVAR-RIRTGTVGVNGFRLDFGA--PFGGFKQS 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
26-479 |
9.78e-98 |
|
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: 301.85 E-value: 9.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEK-WSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSLAsIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLL 184
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 185 MEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDA 263
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 264 DLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDgVFLGPVIREENQKRTLTYIEKGV 343
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 344 EEGAKLTVDGR--ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-AK 420
Cdd:cd07109 319 ARGARIVAGGRiaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDgDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 421 AIRyFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGtlHANGKDSVDFYTHKKVVTA 479
Cdd:cd07109 399 ALR-VARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHG--REKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-475 |
5.97e-96 |
|
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: 298.10 E-value: 5.97e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 8 KNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEARG-EVQRGIENVEFAAGAPTLMMGdSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIA 166
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEG-SLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 167 IALGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYGA-HDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLK 245
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 246 RVQALTGAKNHTIVLNDADLEDtvTNVISAAFGSA-------GERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLD 318
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMDAD--DDFDDKAEEGQlgfafnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 319 DGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKN 395
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 396 LQEAVKIANKSEFANGACIFTNNA-KAIRYFREkIDAGMLGVNLGVPAPmAFFPFSGWKSSfyGTLHANGKDSVDFYTHK 474
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDInRALRVARG-IQTGRVWVNCYHQYP-AHAPFGGYKKS--GIGRETHKMMLDHYQQT 473
|
.
gi 502749847 475 K 475
Cdd:cd07559 474 K 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
10-477 |
8.31e-96 |
|
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: 297.90 E-value: 8.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFE-KWS-QVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKN-LSEARGEVQRGIENVEFAAGAPTLMMGDSlasIATDVEAANY--RYPVGVVGGIAPFNFPMMVPCWMFP 164
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQV---IETDIKKLTYtrHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 165 IAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGS-A 242
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 243 NLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVF 322
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 323 LGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKI 402
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHG-NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502749847 403 ANKSEFANGACIFTNN-AKAIRyFREKIDAGMLGVN-LGVPAPMAffPFSGWKSSFYGtlHANGKDSVDFYTHKKVV 477
Cdd:cd07143 406 ANDSTYGLAAAVFTNNiNNAIR-VANALKAGTVWVNcYNLLHHQV--PFGGYKQSGIG--RELGEYALENYTQIKAV 477
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
26-459 |
1.45e-95 |
|
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: 296.46 E-value: 1.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAPTLMMGDSLAsIATDVEAANY-----RYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSER 180
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGEVLP-LDISARGEGRqglvrRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 181 TPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGeYVYKtGSANLKRVQALTGAKNHTIVL 260
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVG-WDLK-ARAGKKKVVLELGGNAAVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 261 NDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIE 340
Cdd:cd07147 240 SDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 341 KGVEEGAKLTVDGREtgisKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-A 419
Cdd:cd07147 320 EAVDAGAKLLTGGKR----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDlE 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 502749847 420 KAIRYFREkIDAGmlGVNLG-VPA----PMaffPFSGWKSSFYGT 459
Cdd:cd07147 396 KALRAWDE-LEVG--GVVINdVPTfrvdHM---PYGGVKDSGIGR 434
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-477 |
6.05e-95 |
|
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: 295.56 E-value: 6.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 4 VRKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQ 81
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 82 HKEELARLITLENGKNLSEAR-GEVQRGIENVEFAAGAPTLMMGDSLASIATdVEAANYRYPVGVVGGIAPFNFPMMVPC 160
Cdd:cd07142 81 HADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 161 WMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNG-ILENDKIKAVSFVGSKPVGEYVYKT 239
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 240 GSA-NLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLD 318
Cdd:cd07142 240 AAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 319 DGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQE 398
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG-SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 399 AVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-LGVPAPMAffPFSGWKSSfyGTLHANGKDSVDFYTHKKVV 477
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI--PFGGYKMS--GIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
46-458 |
2.54e-94 |
|
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: 292.44 E-value: 2.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 46 LDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEF-AAGAPTLMMG 124
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 125 DSLASIATDveaANYRY-PVGVVGGIAPFNFPM------MVPcwmfpiAIALGNSFILKPSERTPLLMEKLVELFTEAGL 197
Cdd:cd07100 81 EPIETDAGK---AYVRYePLGVVLGIMPWNFPFwqvfrfAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 198 PNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAF 277
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 278 GSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVdGRETG 357
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL-GGKRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 358 ISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN 437
Cdd:cd07100 311 DGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420
....*....|....*....|.
gi 502749847 438 lGVPAPMAFFPFSGWKSSFYG 458
Cdd:cd07100 391 -GMVKSDPRLPFGGVKRSGYG 410
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
26-459 |
9.46e-93 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 288.84 E-value: 9.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEAR-GE 104
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLL 184
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 185 MEKLVELFTEaGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDA 263
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 264 DLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKgV 343
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER-A 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 344 EEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-AKAI 422
Cdd:cd07092 319 PAHARVLTGGRRAE-GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDvGRAM 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 502749847 423 RYFREkIDAGMLGVN--LGVPAPMaffPFSGWKSSFYGT 459
Cdd:cd07092 398 RLSAR-LDFGTVWVNthIPLAAEM---PHGGFKQSGYGK 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
27-479 |
6.39e-92 |
|
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: 286.81 E-value: 6.39e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQ 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 107 RGIENVEFAAG-APTLMmGD---SLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTP 182
Cdd:cd07099 81 LALEAIDWAARnAPRVL-APrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 183 LLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEN--DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVL 260
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAgvDKV---AFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 261 NDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIrEENQKRTL-TYI 339
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMT-TARQLDIVrRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 340 EKGVEEGAKLTVDGRETGIsKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNA 419
Cdd:cd07099 316 DDAVAKGAKALTGGARSNG-GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502749847 420 KAIRYFREKIDAGMLGVN-----LGVPApmafFPFSGWKSSFYGTLHanGKDSVDFYTHKKVVTA 479
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdvlltAGIPA----LPFGGVKDSGGGRRH--GAEGLREFCRPKAIAR 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
47-478 |
4.21e-91 |
|
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: 284.08 E-value: 4.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 47 DEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDS 126
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 127 LASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVY 206
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 207 ----GAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGE 282
Cdd:cd07105 163 hspeDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 283 RCMACAVVTVEEGIADEFLEALRIAARNVKignglDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGH 362
Cdd:cd07105 243 ICMSTERIIVHESIADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 363 FVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN-AKAIRyFREKIDAGMLGVNLGVP 441
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlARALA-VAKRIESGAVHINGMTV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 502749847 442 APMAFFPFSGWKSSFYGTLhaNGKDSVDFYTHKKVVT 478
Cdd:cd07105 397 HDEPTLPHGGVKSSGYGRF--NGKWGIDEFTETKWIT 431
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
10-475 |
7.66e-91 |
|
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: 284.73 E-value: 7.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARL 89
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 90 ITLENGKNLSEARG-EVQRGIENVEFAAGApTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIA 168
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGV-IRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 169 LGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRV 247
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 248 QALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVI 327
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 328 REENQKRTLTYIEKGVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIAN 404
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGGHrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502749847 405 KSEFANGACIFTNN-AKAIRYFREkIDAGMLGVNLGVPAPmAFFPFSGWKSSFYGtlHANGKDSVDFYTHKK 475
Cdd:cd07117 402 DSEYGLGGGVFTKDiNRALRVARA-VETGRVWVNTYNQIP-AGAPFGGYKKSGIG--RETHKSMLDAYTQMK 469
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
10-481 |
3.43e-90 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 283.93 E-value: 3.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK-----WSQVAVPRRARILFSFQQLLIQHKE 84
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 85 ELARLITLENGKNLSEARGEvqrgIENV----EFAAG-APTLmmgDSLASIATDVEAANY-----RYPVGVVGGIAPFNF 154
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWD----MDDVagcfEYYADlAEAL---DAKQKAPVSLPMETFkgyvlKEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 155 PMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDK-IKAVSFVGSKPVG 233
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPgVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 234 EYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKI 313
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 314 GNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDG-RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIR 392
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGkRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 393 VKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPApMAFFPFSGWKSSFYGtlHANGKDSVDFYT 472
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFG--RELGEWGLENYL 480
|
....*....
gi 502749847 473 HKKVVTaRY 481
Cdd:PLN02467 481 SVKQVT-KY 488
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
26-481 |
6.04e-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: 281.96 E-value: 6.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAPTLMMGDslaSIATDVEAANY--RYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPL 183
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE---TIPVGGRNLHYtlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 184 LMEKLVELFTEAgLPNGVFNVVYGAHDVVNGIL-ENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLND 262
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALvRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 263 ADLEDTVTN-VISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEK 341
Cdd:cd07107 237 ADPEAAADAaVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 342 GVEEGAKL-TVDGRETG--ISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN 418
Cdd:cd07107 317 AKREGARLvTGGGRPEGpaLEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 419 -AKAIRYFREkIDAGMLGVN------LGVpapmaffPFSGWKSSFYGTLHanGKDSVDFYTHKKVVTARY 481
Cdd:cd07107 397 iSQAHRTARR-VEAGYVWINgssrhfLGA-------PFGGVKNSGIGREE--CLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
10-439 |
2.09e-89 |
|
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: 281.02 E-value: 2.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKyeNVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARL 89
Cdd:cd07130 2 VYDGEWGGGGGVV--TSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 90 ITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASiatdvEAANYR-----YPVGVVGGIAPFNFPMMVPCWMFP 164
Cdd:cd07130 80 VSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPS-----ERPGHRmmeqwNPLGVVGVITAFNFPVAVWGWNAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 165 IAIALGNSFILKPSERTPLL---MEKLV-ELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTG 240
Cdd:cd07130 155 IALVCGNVVVWKPSPTTPLTaiaVTKIVaRVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 241 SANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDG 320
Cdd:cd07130 235 AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 321 VFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISkGHFVGPTILeEVTTDMTIWKEEIFAPVLSVIRVKNLQEAV 400
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP-GNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 502749847 401 KIANksEFANG--ACIFTNNAKAIRYFREKI--DAGMLGVNLG 439
Cdd:cd07130 393 AWNN--EVPQGlsSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG 433
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-455 |
3.21e-89 |
|
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: 279.90 E-value: 3.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQ 106
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 107 RGIENVEFAAG-APtlmmgDSLASIATDVEAANYRY----PVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERT 181
Cdd:cd07102 81 GMLERARYMISiAE-----EALADIRVPEKDGFERYirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 182 PLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLN 261
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 262 DADLEDTVTNVISAAFGSAGERCmaCAV--VTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYI 339
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSC--CSIerIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 340 EKGVEEGAKLTVDGRETGISKGH--FVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTN 417
Cdd:cd07102 314 ADAIAKGARALIDGALFPEDKAGgaYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 502749847 418 NAKAIRYFREKIDAGMLGVNLGV---PApmafFPFSGWKSS 455
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDyldPA----LAWTGVKDS 430
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-458 |
4.75e-89 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 280.26 E-value: 4.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 8 KNYVNGEWVASKTEKyENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:PRK13473 4 KLLINGELVAGEGEK-QPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEARG-EVQRGIENVEFAAGAPTLMMGDSlasiatdveAANY---------RYPVGVVGGIAPFNFPMM 157
Cdd:PRK13473 83 RLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKA---------AGEYleghtsmirRDPVGVVASIAPWNYPLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 158 VPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYV 236
Cdd:PRK13473 154 MAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 237 YKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNG 316
Cdd:PRK13473 233 LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 317 LDDGVFLGPVIREENQKRTLTYIEKGVEEG-AKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKN 395
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPD-GKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502749847 396 LQEAVKIANKSEFANGACIFTNN-AKAIRYFREkIDAGMLGVNLGVP--APMaffPFSGWKSSFYG 458
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDvGRAHRVSAR-LQYGCTWVNTHFMlvSEM---PHGGQKQSGYG 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
26-478 |
5.47e-89 |
|
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: 279.63 E-value: 5.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNL-SEARGE 104
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSLaSIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLL 184
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETL-PFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 185 MEKLVELFTEAgLPNGVFNVVYGAHDVVNGIL-ENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDA 263
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALvDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 264 DLEDTVTNVISAA-FGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKG 342
Cdd:cd07108 239 DLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 343 VEE-GAKLTVDG---RETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN 418
Cdd:cd07108 319 LSTsGATVLRGGplpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 419 AKAIRYFREKIDAGMLGVNLGVpAPMAFFPFSGWKSSFYGTlHANGKDSVDFYTHKKVVT 478
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGR-EASLEGMLEHFTQKKTVN 456
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
32-478 |
1.84e-88 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 277.64 E-value: 1.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 32 GEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIEN 111
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 112 VEFAAGAPTLMMGDSLASIATDVEAANyRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPL---LMekL 188
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSAPGRLSLAR-RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVsggVV--I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 189 VELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDT 268
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 269 VTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAK 348
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 349 LTVDGRetgiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNN---AKAIryf 425
Cdd:cd07152 318 LEAGGT----YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDvgrAMAL--- 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 502749847 426 REKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHAnGKDSVDFYTHKKVVT 478
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEPHNPFGGMGASGNGSRFG-GPANWEEFTQWQWVT 442
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
26-478 |
2.83e-87 |
|
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: 275.01 E-value: 2.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEIsekAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALAL---AASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QRGIENVEFAAGAptlMMGDSLASIATDVEAA-------NYRYPVGVVGGIAPFNFPM-MVPCWMFPiAIALGNSFILKP 177
Cdd:cd07146 80 GRAADVLRFAAAE---ALRDDGESFSCDLTANgkarkifTLREPLGVVLAITPFNHPLnQVAHKIAP-AIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 178 SERTPLLMEKLVELFTEAGLPNGVFNVVYGA-HDVVNGILENDKIKAVSFVGSKPVGEYVykTGSANLKRVQALTGAKNH 256
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 257 TIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTL 336
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 337 TYIEKGVEEGAKLTVDGREtgisKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFT 416
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQR----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502749847 417 NNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSfyGTLHANG-KDSVDFYTHKKVVT 478
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSELSPFGGVKDS--GLGGKEGvREAMKEMTNVKTYS 450
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-481 |
2.86e-86 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 274.01 E-value: 2.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 1 MTKVRKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFE--KWSQVAVPRRARILFSFQQL 78
Cdd:PLN02766 15 VPEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 79 LIQHKEELARLITLENGKNLSEARG-EVQRGIENVEFAAGAPTLMMGDSLaSIATDVEAANYRYPVGVVGGIAPFNFPMM 157
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 158 VPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYV 236
Cdd:PLN02766 174 MFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHmDVDKVSFTGSTEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 237 YKTGSA-NLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGN 315
Cdd:PLN02766 254 MQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 316 GLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKN 395
Cdd:PLN02766 334 PFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 396 LQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNlgvpAPMAF---FPFSGWKSSFYGtlHANGKDSVDFYT 472
Cdd:PLN02766 413 VEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN----CYFAFdpdCPFGGYKMSGFG--RDQGMDALDKYL 486
|
490
....*....|
gi 502749847 473 H-KKVVTARY 481
Cdd:PLN02766 487 QvKSVVTPLY 496
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
10-462 |
5.23e-86 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 272.93 E-value: 5.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEA-RGEVQRGIENVEFAAGAPTLMMGDsLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIA 166
Cdd:PRK09847 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGE-VATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 167 IALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYK-TGSANL 244
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 245 KRVQALTGAKNHTIVLNDA-DLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFL 323
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 324 GPVIREENQKRTLTYIEKGVEEGaKLTVDGRETGISKghFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIA 403
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA--AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502749847 404 NKSEFANGACIFTNN-AKAIRYFReKIDAGMLGVNLGVPAPMAfFPFSGWKSSFYG---TLHA 462
Cdd:PRK09847 419 NDSQYGLGAAVWTRDlSRAHRMSR-RLKAGSVFVNNYNDGDMT-VPFGGYKQSGNGrdkSLHA 479
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
10-458 |
1.17e-85 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 271.78 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARL 89
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 90 ITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIAL 169
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 170 GNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQ 248
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 249 ALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIR 328
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 329 EENQKRTLTYIEKGVEEGAKLTVDGRETGISkGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEF 408
Cdd:PRK11241 334 EKAVAKVEEHIADALEKGARVVCGGKAHELG-GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEF 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 502749847 409 ANGACIFTNNAKaiRYFR--EKIDAGMLGVNLGVPApMAFFPFSGWKSSFYG 458
Cdd:PRK11241 413 GLAAYFYARDLS--RVFRvgEALEYGIVGINTGIIS-NEVAPFGGIKASGLG 461
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
10-481 |
3.41e-85 |
|
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: 270.52 E-value: 3.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEA-RGEVQRGIENVEFAAGAPTLMMGdslASIATDVEAANY------RYPVGVVGGIAPFNFPMMVPC 160
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQG---KTIPINQARPNRnltltkREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 161 WMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVYKT 239
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 240 -GSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLD 318
Cdd:cd07140 246 cAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 319 DGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKN--L 396
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD-RPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 397 QEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAfFPFSGWKSSFYGTlhANGKDSVDFYTHKKV 476
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFGK--DLGEEALNEYLKTKT 481
|
....*
gi 502749847 477 VTARY 481
Cdd:cd07140 482 VTIEY 486
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-478 |
1.46e-84 |
|
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: 268.06 E-value: 1.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQvAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGDSLasiatDVEAANY----RYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSER 180
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMI-----EPEPGSFslvlREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 181 TPLLMEKLVELFTEA-GLPNGVFNVVYGA-HDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTI 258
Cdd:cd07120 156 TAQINAAIIRILAEIpSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 259 VLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTY 338
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 339 IEKGVEEGAKLTVDGR--ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFT 416
Cdd:cd07120 316 VERAIAAGAEVVLRGGpvTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502749847 417 NN-AKAIRYFReKIDAGMLGVNLGVpAPMAFFPFSGWKSSFYGTLHanGKDSVDFYTHKKVVT 478
Cdd:cd07120 396 RDlARAMRVAR-AIRAGTVWINDWN-KLFAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-458 |
1.58e-81 |
|
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: 260.79 E-value: 1.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 5 RKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKE 84
Cdd:cd07111 20 RSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 85 ELARLITLENGKNLSEAR-GEVQRGIENVEFAAGAPTLMmgdslasiatDVEAANYRyPVGVVGGIAPFNFPMMVPCWMF 163
Cdd:cd07111 100 LFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLL----------DTELAGWK-PVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 164 PIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSAN 243
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 244 LKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFL 323
Cdd:cd07111 249 GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 324 GPVIREENQKRTLTYIEKGVEEGAkltvDGRETGI---SKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAV 400
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGA----DVFQPGAdlpSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAV 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502749847 401 KIANKSEFANGACIFTNNAKAIRYFREKIDAGML---GVNLGVPAPmaffPFSGWKSSFYG 458
Cdd:cd07111 405 ALANNTPYGLAASVWSENLSLALEVALSLKAGVVwinGHNLFDAAA----GFGGYRESGFG 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
27-478 |
4.24e-78 |
|
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: 251.07 E-value: 4.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQ 106
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 107 RGIENVEF-AAGAPTLM----MGDSLASIATDVEaanYRYPVGVVGGIAPFNFPM------MVPcwmfpiAIALGNSFIL 175
Cdd:cd07101 81 DVAIVARYyARRAERLLkprrRRGAIPVLTRTTV---NRRPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 176 KPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEnDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKN 255
Cdd:cd07101 152 KPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV-DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 256 HTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRT 335
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 336 LTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIF 415
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 416 TNNAKAIRYFREKIDAGMLGVNLG-------VPAPMAffpfsGWKSSfyGTLHANGKDSVDFYTHKKVVT 478
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEGyaaawasIDAPMG-----GMKDS--GLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-455 |
2.58e-76 |
|
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: 245.64 E-value: 2.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 45 ELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMG 124
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 125 DSLASIAtDVEAANYRYPVGVVGGIAPFNFPMMVP-CWMFPIAIAlGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFN 203
Cdd:cd07095 81 ERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPnGHIVPALLA-GNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 204 VVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQAL-TGAKNHTIVLNDADLEDTVTNVISAAFGSAGE 282
Cdd:cd07095 159 LVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALeMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 283 RCMACAVVTVEEG-IADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGReTGISKG 361
Cdd:cd07095 239 RCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME-RLVAGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 362 HFVGPTILeEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNL--- 438
Cdd:cd07095 318 AFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRptt 396
|
410
....*....|....*..
gi 502749847 439 GVPAPMaffPFSGWKSS 455
Cdd:cd07095 397 GASSTA---PFGGVGLS 410
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
2-481 |
1.22e-75 |
|
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: 246.34 E-value: 1.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 2 TKVRKIKNYVNGEWVASKTEKYenVINP-ATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLI 80
Cdd:cd07083 14 EFGRAYPLVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 81 QHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDS--LASIATDVEAANYRyPVGVVGGIAPFNFPMMV 158
Cdd:cd07083 92 RRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAveVVPYPGEDNESFYV-GLGAGVVISPWNFPVAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 159 PCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKPVGEYVY 237
Cdd:cd07083 171 FTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 238 KTGSANL------KRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNV 311
Cdd:cd07083 251 EAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 312 KIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGIskGHFVGPTILEEVTTDMTIWKEEIFAPVLSVI 391
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 392 RVK--NLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLG-VPAPMAFFPFSGWKSSfyGT-LHANGKDS 467
Cdd:cd07083 409 RYKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKiTGALVGVQPFGGFKLS--GTnAKTGGPHY 486
|
490
....*....|....
gi 502749847 468 VDFYTHKKVVTARY 481
Cdd:cd07083 487 LRRFLEMKAVAERF 500
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-479 |
1.24e-75 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 247.03 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 3 KVRKIKNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEK--WSQVAVPRRARILFSFQQLLI 80
Cdd:PLN02466 54 QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 81 QHKEELARLITLENGKNLSEARG-EVQRGIENVEFAAGAPTLMMG-----DSLASIATDVEaanyryPVGVVGGIAPFNF 154
Cdd:PLN02466 134 KHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGltvpaDGPHHVQTLHE------PIGVAGQIIPWNF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 155 PMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG----AHDVVNGILENDKIkavSFVGSK 230
Cdd:PLN02466 208 PLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfgptAGAALASHMDVDKL---AFTGST 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 231 PVGEYVYKTGS-ANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAAR 309
Cdd:PLN02466 285 DTGKIVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARAL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 310 NVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLS 389
Cdd:PLN02466 365 KRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG-SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQS 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 390 VIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLgVPAPMAFFPFSGWKSSFYGtlHANGKDSVD 469
Cdd:PLN02466 444 ILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG--REKGIYSLN 520
|
490
....*....|.
gi 502749847 470 FYTH-KKVVTA 479
Cdd:PLN02466 521 NYLQvKAVVTP 531
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
26-461 |
1.94e-75 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 246.33 E-value: 1.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEV 105
Cdd:PRK09407 36 VTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 106 QrGIENVE--FAAGAPTLMMGD---SLASIATDveAANYRYPVGVVGGIAPFNFPM------MVPcwmfpiAIALGNSFI 174
Cdd:PRK09407 116 L-DVALTAryYARRAPKLLAPRrraGALPVLTK--TTELRQPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 175 LKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNG-ILENdkIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGA 253
Cdd:PRK09407 187 LKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTaLVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 254 KNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQK 333
Cdd:PRK09407 265 KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 334 RTLTYIEKGVEEGAKLTVDGR---ETGiskGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFAN 410
Cdd:PRK09407 345 TVSAHVDDAVAKGATVLAGGKarpDLG---PLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGL 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 411 GACIFTNNAKAIRYFREKIDAGMLGVNLG-------VPAPMAffpfsGWKSSFYGTLH 461
Cdd:PRK09407 422 NASVWTGDTARGRAIAARIRAGTVNVNEGyaaawgsVDAPMG-----GMKDSGLGRRH 474
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-458 |
8.58e-75 |
|
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: 244.41 E-value: 8.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 4 VRKIKNYVNGEWVAS--------KTEKYENVINPATGE-ILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFS 74
Cdd:cd07125 20 ADALKAFDEKEWEAIpiingeetETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 75 FQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEF-AAGAPTLMMGDSLasIATDVEAANYRY-PVGVVGGIAPF 152
Cdd:cd07125 100 AADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYyAAQARELFSDPEL--PGPTGELNGLELhGRGVFVCISPW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 153 NFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSKP 231
Cdd:cd07125 178 NFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 232 VGEYVYKTGSAN---LKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAA 308
Cdd:cd07125 258 TAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 309 RNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEG---AKLTVDGretgiSKGHFVGPTILEEVttdmTIW--KEEI 383
Cdd:cd07125 338 ASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAwliAPAPLDD-----GNGYFVAPGIIEIV----GIFdlTTEV 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 384 FAPVLSVIRVK--NLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLG-VPAPMAFFPFSGWKSSFYG 458
Cdd:cd07125 409 FGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNiTGAIVGRQPFGGWGLSGTG 486
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-458 |
2.34e-73 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 238.99 E-value: 2.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQ 106
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 107 RGIENVE-FAAGAPTLmmgdsLASIATDVEAAN----YRyPVGVVGGIAPFNFPMmvpcWMF-----PIAIAlGNSFILK 176
Cdd:PRK13968 92 KSANLCDwYAEHGPAM-----LKAEPTLVENQQavieYR-PLGTILAIMPWNFPL----WQVmrgavPILLA-GNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 177 PSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNH 256
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 257 TIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTL 336
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 337 TYIEKGVEEGAKLTVDGrETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFT 416
Cdd:PRK13968 321 HQVEATLAEGARLLLGG-EKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 502749847 417 NNAKAIRYFREKIDAGMLGVNlGVPAPMAFFPFSGWKSSFYG 458
Cdd:PRK13968 400 TDETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-458 |
1.01e-72 |
|
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: 237.58 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 28 NPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEAR-GEVQ 106
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 107 RGIENVEF--AAGAPTLMMGDSLASIATDVEAANYRY-PVGVVGGIAPFNFPmmvpcwmF-----PIAIAL--GNSFILK 176
Cdd:cd07098 82 VTCEKIRWtlKHGEKALRPESRPGGLLMFYKRARVEYePLGVVGAIVSWNYP-------FhnllgPIIAALfaGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 177 PSERTPLLMEKLVELFTEA----GLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTG 252
Cdd:cd07098 155 VSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 253 AKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQ 332
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 333 KRTLTYIEKGVEEGAKLTVDGR---ETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFA 409
Cdd:cd07098 315 DRLEELVADAVEKGARLLAGGKrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502749847 410 NGACIFTNNAKAIRYFREKIDAGMLGVN-LGVPAPMAFFPFSGWKSSFYG 458
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINdFGVNYYVQQLPFGGVKGSGFG 444
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
9-481 |
8.24e-70 |
|
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: 230.42 E-value: 8.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 9 NYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELAR 88
Cdd:cd07116 3 NFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 89 LITLENGKNLSEARG-EVQRGIENVEFAAGAPTLMMGdSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAI 167
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEG-SISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 168 ALGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYGAHDVVNGIL-ENDKIKAVSFVGSKPVGEYVYKTGSANLKR 246
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLaSSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 247 VQALTGAKNHTI----VLN--DADLEDTVTNVISAAFGSaGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDG 320
Cdd:cd07116 241 VTLELGGKSPNIffadVMDadDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 321 VFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRET---GISKGHFVGPTILEEvTTDMTIWKEEIFAPVLSVIRVKNLQ 397
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 398 EAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPmAFFPFSGWKSSfyGTLHANGKDSVDFYTHKKVV 477
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQS--GIGRENHKMMLDHYQQTKNL 475
|
....
gi 502749847 478 TARY 481
Cdd:cd07116 476 LVSY 479
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
10-437 |
2.31e-65 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 218.67 E-value: 2.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYENvINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARL 89
Cdd:PRK09457 4 WINGDWIAGQGEAFES-RNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 90 ITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRyPVGVVGGIAPFNFP------MMVPcwmf 163
Cdd:PRK09457 83 IARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPghlpngHIVP---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 164 piAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSAN 243
Cdd:PRK09457 158 --ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 244 LKRVQAL-TGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGI-ADEFLEALRIAARNVKIGNGLDDGV 321
Cdd:PRK09457 236 PEKILALeMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEPQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 322 -FLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGhFVGPTILeEVTTDMTIWKEEIFAPVLSVIRVKNLQEAV 400
Cdd:PRK09457 316 pFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTG-LLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAI 393
|
410 420 430
....*....|....*....|....*....|....*..
gi 502749847 401 KIANKSEFANGACIFTNNAKAIRYFREKIDAGMlgVN 437
Cdd:PRK09457 394 RLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VN 428
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-481 |
1.49e-64 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 217.39 E-value: 1.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKteKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARL 89
Cdd:PLN02315 24 YVGGEWRANG--PLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 90 ITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIAL 169
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 170 GNSFILKPSERTPLL---MEKLV-ELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLK 245
Cdd:PLN02315 182 GNCVVWKGAPTTPLItiaMTKLVaEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 246 RVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGP 325
Cdd:PLN02315 262 KCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 326 VIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILeEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANK 405
Cdd:PLN02315 342 LHTPESKKNFEKGIEIIKSQGGKILTGGSAIE-SEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 406 SEFANGACIFTNNAKAIryFR----EKIDAGMLGVNLGVPAPMAFFPFSGWKSSfyGTLHANGKDSVDFYTHKKVVTARY 481
Cdd:PLN02315 420 VPQGLSSSIFTRNPETI--FKwigpLGSDCGIVNVNIPTNGAEIGGAFGGEKAT--GGGREAGSDSWKQYMRRSTCTINY 495
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-458 |
1.83e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 215.76 E-value: 1.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 27 INPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQ 106
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 107 RGIENVEFAAGAPTLMMGDSLASiATDVEA--ANYRY-PVGVVGGIAPFNFPMmvpcW--MFPIAIAL--GNSFILKPSE 179
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADEPAD-AAAVGAsrAYVRYqPLGVVLAVMPWNFPL----WqvVRFAAPALmaGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 180 RTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIV 259
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 260 LNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYI 339
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 340 EKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNA 419
Cdd:PRK09406 321 DDAVAAGATILCGGKRPD-GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 502749847 420 KAIRYFREKIDAGMLGVNlGVPAPMAFFPFSGWKSSFYG 458
Cdd:PRK09406 400 AEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRSGYG 437
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-481 |
1.52e-63 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 211.90 E-value: 1.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 72 LFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAP 151
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 152 FNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKAVSFVGSK 230
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 231 PVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARN 310
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 311 VKIGNGLD-DGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLS 389
Cdd:PRK10090 241 VQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE-GKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 390 VIRVKNLQEAVKIANKSEFANGACIFTNN-AKAIRYFREkIDAGMLGVNLGVPAPMAFFpFSGWKSSFYGTlhANGKDSV 468
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNlNVAMKAIKG-LKFGETYINRENFEAMQGF-HAGWRKSGIGG--ADGKHGL 395
|
410
....*....|...
gi 502749847 469 DFYTHKKVVTARY 481
Cdd:PRK10090 396 HEYLQTQVVYLQS 408
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-459 |
1.60e-57 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 198.06 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 8 KNYVNGEWVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELA 87
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEARGEVQRGIENVEFAA-------GAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPC 160
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 161 WMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGIL-ENDKIKAVSFVGskpvGEyvykT 239
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLtMHPGVNCISFTG----GD----T 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 240 GSANLKR-----VQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIG 314
Cdd:PLN00412 249 GIAISKKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 315 NGLDDGVfLGPVIREENQKRTLTYIEKGVEEGAKLTVDGREtgisKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVK 394
Cdd:PLN00412 329 PPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFCQEWKR----EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 395 NLQEAVKIANKSEFANGACIFTNNA-KAIRyFREKIDAGMLGVNlGVPA--PmAFFPFSGWKSSFYGT 459
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDInKAIL-ISDAMETGTVQIN-SAPArgP-DHFPFQGLKDSGIGS 468
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-451 |
1.48e-53 |
|
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: 187.81 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 24 ENVINPAT-GEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEAR 102
Cdd:TIGR01238 53 QPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 103 GEVQRGIENVEFAAGAptlmmgdslasiATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTP 182
Cdd:TIGR01238 133 AEVREAVDFCRYYAKQ------------VRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 183 LLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYVYKTGS---ANLKRVQALTGAKNHTI 258
Cdd:TIGR01238 201 LIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDpRIAGVAFTGSTEVAQLINQTLAqreDAPVPLIAETGGQNAMI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 259 VLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTY 338
Cdd:TIGR01238 281 VDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 339 IEKGVEEGAKLTVDGRETGIS--KGHFVGPTILEevTTDMTIWKEEIFAPVLSVIRVK--NLQEAVKIANKSEFANGACI 414
Cdd:TIGR01238 361 IEHMSQTQKKIAQLTLDDSRAcqHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGV 438
|
410 420 430
....*....|....*....|....*....|....*...
gi 502749847 415 FTNNAKAIRYFREKIDAGMLGVNLG-VPAPMAFFPFSG 451
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVNRNqVGAVVGVQPFGG 476
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
26-459 |
8.92e-53 |
|
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: 184.54 E-value: 8.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQ-VAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGAPTLMMGdslASIATDVEAAN-------YRYPVGVVGGIAPFNFPM------MVPcwmfpiAIALGN 171
Cdd:cd07148 83 VTRAIDGVELAADELGQLGG---REIPMGLTPASagriaftTREPIGVVVAISAFNHPLnlivhqVAP------AIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 172 SFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVyKTGSANLKRVQALT 251
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWML-RSKLAPGTRCALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 252 GAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREEN 331
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 332 QKRTLTYIEKGVEEGAKLTVDGRETGISkghFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANG 411
Cdd:cd07148 313 VDRVEEWVNEAVAAGARLLCGGKRLSDT---TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 502749847 412 ACIFTNNAKAIRYFREKIDAGMLGVNlgvpAPMAF----FPFSGWKSSFYGT 459
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVN----DHTAFrvdwMPFAGRRQSGYGT 437
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-394 |
1.52e-51 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 188.54 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQrgiENVEF----AAGAPTLMMGDSLAsiatdveaanyryPVGVVGGIAPFNFPMMVpcwmF--PIAIAL--GNSFILK 176
Cdd:PRK11905 651 VR---EAVDFlryyAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAI----FtgQIAAALvaGNTVLAK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 177 PSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYVYKTGSANLKRVQAL---TG 252
Cdd:PRK11905 711 PAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADpRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaeTG 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 253 AKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQ 332
Cdd:PRK11905 791 GQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQ 870
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502749847 333 KRTLTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEevTTDMTIWKEEIFAPVLSVIRVK 394
Cdd:PRK11905 871 ANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFK 930
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
26-392 |
3.53e-50 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 184.37 E-value: 3.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:COG4230 574 VRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VqRgiENVEF----AAGAPTLMMGDSLasiatdveaanyRYPVGVVGGIAPfnfpmmvpcWMFPIAI-------AL--GN 171
Cdd:COG4230 654 V-R--EAVDFcryyAAQARRLFAAPTV------------LRGRGVFVCISP---------WNFPLAIftgqvaaALaaGN 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 172 SFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDK-IKAVSFVGSKPVGEYVYKTGSANLKRVQAL 250
Cdd:COG4230 710 TVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPrIAGVAFTGSTETARLINRTLAARDGPIVPL 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 251 ---TGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVI 327
Cdd:COG4230 790 iaeTGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI 869
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502749847 328 REENQKRTLTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEevTTDMTIWKEEIFAPVLSVIR 392
Cdd:COG4230 870 DAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVR 932
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
5-395 |
8.64e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 183.09 E-value: 8.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 5 RKIKNYVNGEWVAS-----KTEKYEnVINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQL 78
Cdd:PRK11904 541 AAIAAFLEKQWQAGpiingEGEARP-VVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 79 LIQHKEELARLITLENGKNLSEARGEVQrgiENVEF----AA------GAPTLMMGdslasiATDVEAANYRYPVGVVGG 148
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVR---EAVDFcryyAAqarrlfGAPEKLPG------PTGESNELRLHGRGVFVC 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 149 IAPFNFPMMVpcwmF--PIAIAL--GNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVV-NGILENDKIKA 223
Cdd:PRK11904 691 ISPWNFPLAI----FlgQVAAALaaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAG 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 224 VSFVGSkpvgeyvykTGSANLKRvQAL-------------TGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVV 290
Cdd:PRK11904 767 VAFTGS---------TETARIIN-RTLaardgpivpliaeTGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVL 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 291 TVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEG---AKLTVDgreTGISKGHFVGPT 367
Cdd:PRK11904 837 FVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP---AGTENGHFVAPT 913
|
410 420
....*....|....*....|....*...
gi 502749847 368 ILEevTTDMTIWKEEIFAPVLSVIRVKN 395
Cdd:PRK11904 914 AFE--IDSISQLEREVFGPILHVIRYKA 939
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
26-394 |
3.71e-44 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 166.69 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 26 VINPA-TGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGE 104
Cdd:PRK11809 663 VINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 105 VQRGIENVEFAAGaptlmmgdslaSIATDVEAANYRyPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLL 184
Cdd:PRK11809 743 VREAVDFLRYYAG-----------QVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 185 MEKLVELFTEAGLPNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYVYKTGSANLKR------VQALTGAKNHT 257
Cdd:PRK11809 811 AAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADaRVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAM 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 258 IVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLT 337
Cdd:PRK11809 891 IVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIER 970
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 338 YIEKGVEEGAKLTVDGRE--TGISKGHFVGPTILEEVTTDMTiwKEEIFAPVLSVIRVK 394
Cdd:PRK11809 971 HIQAMRAKGRPVFQAAREnsEDWQSGTFVPPTLIELDSFDEL--KREVFGPVLHVVRYN 1027
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
142-477 |
1.46e-43 |
|
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: 159.31 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 142 PVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYGAHDVVNGILEN--D 219
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQkfD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 220 KIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADE 299
Cdd:cd07135 187 KI---FYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 300 FLEALRIAArNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKgveEGAKLTVDGRETGISKghFVGPTILEEVTTDMTIW 379
Cdd:cd07135 264 FVEELKKVL-DEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEMDEATR--FIPPTIVSDVSWDDSLM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 380 KEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-----LGVPApmafFPFSGWKS 454
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtlihVGVDN----APFGGVGD 413
|
330 340
....*....|....*....|...
gi 502749847 455 SFYGTLHanGKDSVDFYTHKKVV 477
Cdd:cd07135 414 SGYGAYH--GKYGFDTFTHERTV 434
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
68-477 |
2.52e-43 |
|
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: 158.46 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 68 RARILFSFQQLLIQHKEELARLITLENGKNLSEAR-GEVQRGIENVEFA------------AGAPTLMMGDSlASIatdv 134
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHAlkhlkkwmkprrVSVPLLLQPAK-AYV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 135 eaanYRYPVGVVGGIAPFNFPM------MVPcwmfpiAIALGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYGA 208
Cdd:cd07087 97 ----IPEPLGVVLIIGPWNYPLqlalapLIG------AIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 209 HDVVNGILEN--DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMA 286
Cdd:cd07087 166 VEVATALLAEpfDHI---FFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 287 CAVVTVEEGIADEFLEALRiAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGveegaKLTVDGrETGISKgHFVGP 366
Cdd:cd07087 243 PDYVLVHESIKDELIEELK-KAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEE-RYIAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 367 TILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-----LGVP 441
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvllhAAIP 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 502749847 442 ApmafFPFSGWKSSFYGTLHanGKDSVDFYTHKKVV 477
Cdd:cd07087 395 N----LPFGGVGNSGMGAYH--GKAGFDTFSHLKSV 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
10-437 |
1.38e-40 |
|
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: 152.74 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 10 YVNGEWVASKTEKYenVINPAT-GEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLI-QHKEELA 87
Cdd:cd07123 36 VIGGKEVRTGNTGK--QVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 88 RLITLENGKNLSEArgEVQRGIE-------NVEFAAgapTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFpmmvpc 160
Cdd:cd07123 114 AATMLGQGKNVWQA--EIDAACElidflrfNVKYAE---ELYAQQPLSSPAGVWNRLEYRPLEGFVYAVSPFNF------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 161 wmfpIAIA---------LGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYG-AHDVVNGILENDKIKAVSFVGSK 230
Cdd:cd07123 183 ----TAIGgnlagapalMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGdGPVVGDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 231 PVGEYVYKTGSANLK------RVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEAL 304
Cdd:cd07123 259 PTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 305 RIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEevTTD--MTIWKEE 382
Cdd:cd07123 339 LEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIE--TTDpkHKLMTEE 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502749847 383 IFAPVLSViRV---KNLQEAVKIANK-SEFA-NGAcIFTNNAKAIRYFREKI--DAGMLGVN 437
Cdd:cd07123 417 IFGPVLTV-YVypdSDFEETLELVDTtSPYAlTGA-IFAQDRKAIREATDALrnAAGNFYIN 476
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
65-486 |
1.81e-39 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 149.02 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 65 VPRRARILFSFQQLLIQHKEELARLITLENGKNLSEA--------RGEVQRGIENV-EFAAGAPTLMmgdSLASIATDVE 135
Cdd:PTZ00381 28 LEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLLKHLdEYLKPEKVDT---VGVFGPGKSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 136 AAnyRYPVGVVGGIAPFNFPM---MVPCWMfpiAIALGNSFILKPSERTPLLMEKLVELFTEAgLPNGVFNVVYGAHDVV 212
Cdd:PTZ00381 105 II--PEPLGVVLVIGAWNYPLnltLIPLAG---AIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 213 NGILEnDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTV 292
Cdd:PTZ00381 179 TELLK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 293 EEGIADEFLEALRiAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEkgvEEGAKLTVDGrETGISKgHFVGPTILEEV 372
Cdd:PTZ00381 258 HRSIKDKFIEALK-EAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGG-EVDIEN-KYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 373 TTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-----LGVPApmafF 447
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcvfhLLNPN----L 407
|
410 420 430
....*....|....*....|....*....|....*....
gi 502749847 448 PFSGWKSSFYGTLHanGKDSVDFYTHKKVVTARYSLKGY 486
Cdd:PTZ00381 408 PFGGVGNSGMGAYH--GKYGFDTFSHPKPVLNKSTGNSF 444
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
55-461 |
2.59e-39 |
|
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: 147.37 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 55 KAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEAR-GEVQRGIENVEFA------------AGAPTL 121
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEILPVLSEINHAikhlkkwmkpkrVRTPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 122 MMGDSlasiatdveaANYRY-PVGVVGGIAPFNFPMMVPcwMFPI--AIALGNSFILKPSERTPLLMEKLVELFTEAGLP 198
Cdd:cd07134 89 LFGTK----------SKIRYePKGVCLIISPWNYPFNLA--FGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 199 NGVFnVVYGAHDVVNGILEN--DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAA 276
Cdd:cd07134 157 DEVA-VFEGDAEVAQALLELpfDHI---FFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 277 FGSAGERCMACAVVTVEEGIADEFLEALRIA-ARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEGAKLTVDGRE 355
Cdd:cd07134 233 FLNAGQTCIAPDYVFVHESVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 356 TgiSKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLG 435
Cdd:cd07134 313 D--AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVV 390
|
410 420 430
....*....|....*....|....*....|
gi 502749847 436 VNLGVpapMAFF----PFSGWKSSFYGTLH 461
Cdd:cd07134 391 VNDVV---LHFLnpnlPFGGVNNSGIGSYH 417
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
139-480 |
1.96e-37 |
|
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: 142.64 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 139 YRYPVGVVGGIAPFNFPMMVPcwMFPI--AIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVfNVVYGAHDVVNGIL 216
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPFQLA--LAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV-AVVEGGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 217 EN--DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEE 294
Cdd:cd07136 174 DQkfDYI---FFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 295 GIADEFLEALRIAARNVKIGNGLDDGVFlGPVIREENQKRTLTYIEKG-VEEGAKLTVDGRetgiskghFVGPTILEEVT 373
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNGkIVFGGNTDRETL--------YIEPTILDNVT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 374 TDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-----LGVPapmaFFP 448
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimhLANP----YLP 397
|
330 340 350
....*....|....*....|....*....|..
gi 502749847 449 FSGWKSSFYGTLHanGKDSVDFYTHKKVVTAR 480
Cdd:cd07136 398 FGGVGNSGMGSYH--GKYSFDTFSHKKSILKK 427
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
139-480 |
6.17e-35 |
|
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: 135.43 E-value: 6.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 139 YRYPVGVVGGIAPFNFPMMVPcwMFPI--AIALGNSFILKPSERTPLlMEKLVELFTEAGLPNGVFNVVYGAHDVVNGIL 216
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQLT--LVPLvgAIAAGNCVVIKPSEVSPA-TAKLLAELIPKYLDKECYPVVLGGVEETTELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 217 EN--DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEE 294
Cdd:cd07132 174 KQrfDYI---FYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 295 GIADEFLEALRIAARNVkIGNGLDDGVFLGPVIREENQKRTLTYIEKGveegaKLTVDGRETGISKghFVGPTILEEVTT 374
Cdd:cd07132 251 EVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGG-----KVAIGGQTDEKER--YIAPTVLTDVKP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 375 DMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGV-PAPMAFFPFSGWK 453
Cdd:cd07132 323 SDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImHYTLDSLPFGGVG 402
|
330 340
....*....|....*....|....*..
gi 502749847 454 SSFYGTLHanGKDSVDFYTHKKVVTAR 480
Cdd:cd07132 403 NSGMGAYH--GKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
142-477 |
1.22e-34 |
|
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: 134.46 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 142 PVGVVGGIAPFNFPMMVPcwMFPI--AIALGNSFILKPSERTPL---LMEKLVELFteagLPNGVFNVVYGAHDVVNGIL 216
Cdd:cd07137 101 PLGVVLVISAWNFPFLLS--LEPVigAIAAGNAVVLKPSELAPAtsaLLAKLIPEY----LDTKAIKVIEGGVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 217 EN--DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGS-AGERCMACAVVTVE 293
Cdd:cd07137 175 EQkwDKI---FFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 294 EGIADEFLEALRIAARNVKIGNGLDDGVfLGPVIREENQKRtLTYIEKGVEEGAKLTVDGRETgiSKGHFVGPTILEEVT 373
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQR-LSRLLDDPSVADKIVHGGERD--EKNLYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 374 TDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-----LGVPApmafFP 448
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtvvqYAIDT----LP 403
|
330 340
....*....|....*....|....*....
gi 502749847 449 FSGWKSSFYGTLHanGKDSVDFYTHKKVV 477
Cdd:cd07137 404 FGGVGESGFGAYH--GKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
142-437 |
5.45e-31 |
|
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: 124.13 E-value: 5.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 142 PVGVVGGIAPFNFPMMVPcwMFPI--AIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVfNVVYGAHDVVngilend 219
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLA--LGPLiaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTGGADVA------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 220 kiKAVS--------FVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVT 291
Cdd:cd07133 171 --AAFSslpfdhllFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 292 VEEGIADEFLEALR--IAARNVKIGNGLDdgvfLGPVIREENQKRTLTYIEKGVEEGAKL-TVDGRETGISKGHFVGPTI 368
Cdd:cd07133 249 VPEDKLEEFVAAAKaaVAKMYPTLADNPD----YTSIINERHYARLQGLLEDARAKGARViELNPAGEDFAATRKLPPTL 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 369 LEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN 437
Cdd:cd07133 325 VLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
49-399 |
1.72e-28 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 117.34 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 49 AAEISEKAfekWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEA----RGEVQ-RGIENVEFAAGAPTlMM 123
Cdd:cd07084 7 AADISTKA---ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenicGDQVQlRARAFVIYSYRIPH-EP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 124 GDSLaSIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAG-LPNGVF 202
Cdd:cd07084 83 GNHL-GQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 203 NVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYktgsANLK--RVQALTGAKNHTIVLNDADLEDTVT-NVISAAFGS 279
Cdd:cd07084 162 TLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLA----LDAKqaRIYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 280 AGERCMACAVVTVEEGIADE-FLEALRIAARNVKIGNGLddgvfLGPVIREENQKRTltyIEKGVEEGAKLTVDGRET-G 357
Cdd:cd07084 238 SGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLL-----LGPVQTFTTLAMI---AHMENLLGSVLLFSGKELkN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502749847 358 ISKGHFVGPTI-------LEEVTTDMTIWKEEIFAPVLSVIRVKNLQEA 399
Cdd:cd07084 310 HSIPSIYGACVasalfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLA 358
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
151-480 |
5.95e-24 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 104.42 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 151 PFNFPMMVPCWMFPI---------AIALGNSFILKPSERTPL---LMEKLVELFteagLPNGVFNVVYGAHDVVNGILEN 218
Cdd:PLN02203 108 PLGVVLIFSSWNFPIglslepligAIAAGNAVVLKPSELAPAtsaFLAANIPKY----LDSKAVKVIEGGPAVGEQLLQH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 219 --DKIkavSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIV---LNDADLEDTVTNVISAAFGS-AGERCMACAVVTV 292
Cdd:PLN02203 184 kwDKI---FFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 293 EEGIADEFLEALRIAARNVKIGNGLDDGvFLGPVIREENQKRTLTYIEKGVEEGAKL---TVDgretgiSKGHFVGPTIL 369
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVhggSID------EKKLFIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 370 EEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMA-FFP 448
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACdSLP 413
|
330 340 350
....*....|....*....|....*....|..
gi 502749847 449 FSGWKSSFYGTLHanGKDSVDFYTHKKVVTAR 480
Cdd:PLN02203 414 FGGVGESGFGRYH--GKYSFDTFSHEKAVLRR 443
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
142-480 |
7.04e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 104.36 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 142 PVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTP---LLMEKLVELFteagLPNGVFNVVYGAHDVVNGILEN 218
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPassALLAKLLEQY----LDSSAVRVVEGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 219 dKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFG-SAGERCMACAVVTVEEGIA 297
Cdd:PLN02174 188 -KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 298 DEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEEgaKLTVDGRETgiSKGHFVGPTILEEVTTDMT 377
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSD--KIVYGGEKD--RENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 378 IWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVN-LGVPAPMAFFPFSGWKSSF 456
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGESG 422
|
330 340
....*....|....*....|....
gi 502749847 457 YGTLHanGKDSVDFYTHKKVVTAR 480
Cdd:PLN02174 423 MGAYH--GKFSFDAFSHKKAVLYR 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
9-398 |
2.15e-21 |
|
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: 96.80 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 9 NYVNGEWVASKteKYENVINPATGEILCQVPISTRAELDEAAEiSEKAFEK---WSQVAVPRR----ARILFSFQQLLIQ 81
Cdd:cd07126 1 NLVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVD-SLRQCPKsglHNPLKNPERyllyGDVSHRVAHELRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 82 HKEE--LARLITLENGKNLSEARGEV---QRGIENveFAAGAPTLMM------GDSLASiatdvEAANYRYPVGVVGGIA 150
Cdd:cd07126 78 PEVEdfFARLIQRVAPKSDAQALGEVvvtRKFLEN--FAGDQVRFLArsfnvpGDHQGQ-----QSSGYRWPYGPVAIIT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 151 PFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSK 230
Cdd:cd07126 151 PFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 231 PVGEYVYKTGSANLKRVQALTGAKnhtIVLNDADLEDTVTNVISA-AFGSAGERCMACAVVTVEEGIADE-FLEALRIAA 308
Cdd:cd07126 231 KVAERLALELHGKVKLEDAGFDWK---ILGPDVSDVDYVAWQCDQdAYACSGQKCSAQSILFAHENWVQAgILDKLKALA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 309 RNVKIGNglddgVFLGPVIREENQkRTLTYIEKGVE-EGAKLTVDGRE-TGISKGHFVG---PTI----LEEVTTDMT-- 377
Cdd:cd07126 308 EQRKLED-----LTIGPVLTWTTE-RILDHVDKLLAiPGAKVLFGGKPlTNHSIPSIYGayePTAvfvpLEEIAIEENfe 381
|
410 420
....*....|....*....|.
gi 502749847 378 IWKEEIFAPVLSVIRVKNLQE 398
Cdd:cd07126 382 LVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
7-425 |
9.56e-21 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 95.03 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 7 IKNYVNGEWVASKTEKYEnVINPATGEILCQVP---ISTRAELDEAAEISEKAFEKWSqvaVPRRARILFSFQQLLIQHK 83
Cdd:cd07128 1 LQSYVAGQWHAGTGDGRT-LHDAVTGEVVARVSsegLDFAAAVAYAREKGGPALRALT---FHERAAMLKALAKYLMERK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 84 EELARlITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEaanyryPVGVVG------------GIA- 150
Cdd:cd07128 77 EDLYA-LSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVE------PLSKDGtfvgqhiltprrGVAv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 151 ---PFNFPmmvpCW--MFPIAIAL--GNSFILKPSERTPLLMEKLVELFTEAG-LPNGVFNVVYG-AHDVVNGILENDki 221
Cdd:cd07128 150 hinAFNFP----VWgmLEKFAPALlaGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGsVGDLLDHLGEQD-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 222 kAVSFVGSKPVGeyvyktgsANLKRVQALTGAKNHTIV----LNDADLEDTVT-----------NVISAAFGSAGERCMA 286
Cdd:cd07128 224 -VVAFTGSAATA--------AKLRAHPNIVARSIRFNAeadsLNAAILGPDATpgtpefdlfvkEVAREMTVKAGQKCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 287 CAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKGVEE-----GAKLTVDGRETGISKG 361
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEaevvfGGPDRFEVVGADAEKG 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502749847 362 HFVGPTILEEVTTDMT--IWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYF 425
Cdd:cd07128 375 AFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-423 |
3.08e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 81.29 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 1 MTKvrKIKNYVNGEWVASKTEKYEnVINPATGEILCQVpiSTRAeLDEAAEIsekAFEKWSQVAVPR------RARILFS 74
Cdd:PRK11903 1 MTE--LLANYVAGRWQAGSGAGTP-LFDPVTGEELVRV--SATG-LDLAAAF---AFAREQGGAALRaltyaqRAALLAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 75 FQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAgaptlMMGDSL--ASIATDVEAANY----RYPV----- 143
Cdd:PRK11903 72 IVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYA-----KLGAALgdARLLRDGEAVQLgkdpAFQGqhvlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 144 ---GVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAG-LPNGVFNVVYG-AHDVVNGILEN 218
Cdd:PRK11903 147 ptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGsSAGLLDHLQPF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 219 DkikAVSFVGSKPVGEYVYKTGS--ANLKRVQALTGAKNHTIVLNDADLEdtvtnviSAAFG------------SAGERC 284
Cdd:PRK11903 227 D---VVSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-------SEAFDlfvkevvremtvKSGQKC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 285 MACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLTYIEKgVEEGAKLTVDGRETGI-----S 359
Cdd:PRK11903 297 TAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFALvdadpA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749847 360 KGHFVGPTILeeVTTD----MTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIR 423
Cdd:PRK11903 376 VAACVGPTLL--GASDpdaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLA 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
46-407 |
4.13e-13 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 71.03 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 46 LDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGknLSEAR--GEVQRGIENVE-FAA----GA 118
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARlqGELGRTTGQLRlFADlvreGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 119 PTLMMGDSLASIATDVEAAN---YRYPVGVVGGIAPFNFPMMvpcwmFPI-------AIALGNSFILKP-------SERT 181
Cdd:cd07129 79 WLDARIDPADPDRQPLPRPDlrrMLVPLGPVAVFGASNFPLA-----FSVaggdtasALAAGCPVVVKAhpahpgtSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 182 PLLMEKLVElftEAGLPNGVFNVVYGA-HDVVNGILENDKIKAVSFVGSKPVGEYVYKTGSAnlkR-----VQALTGAKN 255
Cdd:cd07129 154 ARAIRAALR---ATGLPAGVFSLLQGGgREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAA---RpepipFYAELGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 256 HTIVLNDADLEDTVTnvISAAF-GS----AGERCMACAVVTVEEGIA-DEFLEALRIAARNVkignglDDGVFLGPVIRE 329
Cdd:cd07129 228 PVFILPGALAERGEA--IAQGFvGSltlgAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAA------PAQTMLTPGIAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 330 enqkrtlTYiEKGVEE-----GAKLTVDGRETGisKGHFVGPTILEEVTTDMT---IWKEEIFAPVLSVIRVKNLQEAVK 401
Cdd:cd07129 300 -------AY-RQGVEAlaaapGVRVLAGGAAAE--GGNQAAPTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLA 369
|
....*.
gi 502749847 402 IANKSE 407
Cdd:cd07129 370 VAEALE 375
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
46-459 |
8.79e-13 |
|
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: 69.99 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 46 LDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSE---ARGEVQ-RGIENVEFAAGAPTL 121
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkvIKNHFAaEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 122 MMGDSLASIATDVEaanyryPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGlpngv 201
Cdd:cd07081 81 LTGDENGGTLIIAE------PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAA----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 202 fnVVYGAHDVVNGILENDKIKAVSFVGSKPV--------GEYVYKTGSANLKRVQALtGAKNHTIVLND-ADLEDTVTNV 272
Cdd:cd07081 150 --VAAGAPENLIGWIDNPSIELAQRLMKFPGiglllatgGPAVVKAAYSSGKPAIGV-GAGNTPVVIDEtADIKRAVQSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 273 ISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDgvfLGPVI-REENQKRTLTYIEKG-VEEGAKLT 350
Cdd:cd07081 227 VKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQ---VQPVIlKNGDVNRDIVGQDAYkIAAAAGLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 351 VDgRETGISkghFVGPTILEEVTTDMTiwkeEIFAPVLSVIRVKNLQEAVKIANKSEFANG----ACIFTNNAKA---IR 423
Cdd:cd07081 304 VP-QETRIL---IGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAKALALKLEGGcghtSAMYSDNIKAienMN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502749847 424 YFREKIDAGMLGVNlgVPAPMA----FFPFSGWKSSFYGT 459
Cdd:cd07081 376 QFANAMKTSRFVKN--GPCSQGglgdLYNFRGWPSMTLGC 413
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
44-418 |
6.57e-11 |
|
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: 64.18 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 44 AELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENG---------KNlsEARGEVQRGIENVEf 114
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedkiaKN--HLAAEKTPGTEDLT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 115 aagaPTLMMGDSLASIatdVEAAnyryPVGVVGGIAPF---------NFPMMvpcwmfpiaIALGNSFILKPSERTPLLM 185
Cdd:cd07121 81 ----TTAWSGDNGLTL---VEYA----PFGVIGAITPStnptetiinNSISM---------LAAGNAVVFNPHPGAKKVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 186 EKLVELFTEA-----GLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGsanlKRVQAlTGAKNHTIVL 260
Cdd:cd07121 141 AYAVELINKAiaeagGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG----KKAIG-AGAGNPPVVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 261 ND-ADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLEALRiaarnvkignglDDGVFLgpVIREENQKRTLTYI 339
Cdd:cd07121 216 DEtADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQ------------RNGAYV--LNDEQAEQLLEVVL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 340 EKGVEEGAKLTVDGR-------ETGISkghfVGPT---ILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFA 409
Cdd:cd07121 282 LTNKGATPNKKWVGKdaskilkAAGIE----VPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHG 357
|
410
....*....|.
gi 502749847 410 N--GACIFTNN 418
Cdd:cd07121 358 NrhTAIIHSKN 368
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
142-464 |
2.35e-09 |
|
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: 59.16 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 142 PVGVVGGIAPFNFPMMVPCWMFpIAIALGNSFILKPSERTPlLMEKLVELFTEAGLPNGVFN--VVYGAH---DVVNGIL 216
Cdd:cd07077 100 PIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHGPKilVLYVPHpsdELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 217 ENDKIKAVSFVGSKPVGEYVYKtgSANLKRVQALtGAKNHTIVLNDADLEDTVTNVI--SAAFGSAGerCMACAVVTVEE 294
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVK--HSPHIPVIGF-GAGNSPVVVDETADEERASGSVhdSKFFDQNA--CASEQNLYVVD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 295 GIADEFLEalriaarnvkignglddgvflgpvireenqkrtlTYIEKGVEEGAKLTvdgRETGISKGHfVGPTILEEVTT 374
Cdd:cd07077 253 DVLDPLYE----------------------------------EFKLKLVVEGLKVP---QETKPLSKE-TTPSFDDEALE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 375 DMTiwkeeifaPVLSVIRVKNLQEAVKIANKSEFANG----ACIFTNNAKAIRYFREKIDAGMLGVNLGVPA-PMAFFPF 449
Cdd:cd07077 295 SMT--------PLECQFRVLDVISAVENAWMIIESGGgphtRCVYTHKINKVDDFVQYIDTASFYPNESSKKgRGAFAGK 366
|
330
....*....|....*
gi 502749847 450 SGWKSSFYGTLHANG 464
Cdd:cd07077 367 GVERIVTSGMNNIFG 381
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
44-407 |
2.72e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.06 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 44 AELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENG---------KNlsEARGEVQRGIENVEf 114
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedkiaKN--VAAAEKTPGVEDLT- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 115 aagaPTLMMGDS-LasiaTDVEAAnyryPVGVVGGIAPFNFP---------MMvpcwmfpiaIALGNSFILKPSERTPLL 184
Cdd:PRK15398 113 ----TEALTGDNgL----TLIEYA----PFGVIGAVTPSTNPtetiinnaiSM---------LAAGNSVVFSPHPGAKKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 185 MEKLVELFTEA-----GLPNGVFNVVYGAHDVVNGILENDKIKAVSFVGSKPVGEYVYKTGsanlKRVQAlTGAKNHTIV 259
Cdd:PRK15398 172 SLRAIELLNEAivaagGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSG----KKAIG-AGAGNPPVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 260 LND-ADLEDTVTNVI-SAAFGSaGERCMACAVVTVEEGIADEFLEALRiaarnvkignglDDGVFLgpVIREENQKRTLT 337
Cdd:PRK15398 247 VDEtADIEKAARDIVkGASFDN-NLPCIAEKEVIVVDSVADELMRLME------------KNGAVL--LTAEQAEKLQKV 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502749847 338 YIEKGVEEGAKL-----TVDGRETGISkGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSE 407
Cdd:PRK15398 312 VLKNGGTVNKKWvgkdaAKILEAAGIN-VPKDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLE 385
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
43-459 |
2.74e-06 |
|
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: 49.78 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 43 RAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEA-----RGEVQRGIENVEFAAG 117
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfqaggPHAQDRGLEAVAYAWR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 118 AptlmmgdslasIATDVEAANYRYPVGVVGGIA--------PFNFPMMVPCWMFPI---------AIALGNSFILKPSER 180
Cdd:cd07127 163 E-----------MSRIPPTAEWEKPQGKHDPLAmektftvvPRGVALVIGCSTFPTwngypglfaSLATGNPVIVKPHPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 181 TPLLMEKLV----ELFTEAGL-PNGVFNVVYGAHDVVNGILEND-KIKAVSFVGSKPVGEYVYKTgsANLKRVQALTGAK 254
Cdd:cd07127 232 AILPLAITVqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRpEVRIIDFTGSNAFGDWLEAN--ARQAQVYTEKAGV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 255 NHTIVLNDADLEDTVTNVisaAFGSA---GERCMACAVVTV-EEGIA--------DEFLEALrIAARNVKIGNGLDDGVF 322
Cdd:cd07127 310 NTVVVDSTDDLKAMLRNL---AFSLSlysGQMCTTPQNIYVpRDGIQtddgrksfDEVAADL-AAAIDGLLADPARAAAL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749847 323 LGPVIREEnqkrTLTYIEKGvEEGAKLTVDGREtgISKGHFVG-----PTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQ 397
Cdd:cd07127 386 LGAIQSPD----TLARIAEA-RQLGEVLLASEA--VAHPEFPDarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTD 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502749847 398 EAVKIANKSEFANGAC---IFTNNAKAIRYFRE-KIDAGM-LGVNL--GVpapmaFFPFSGWKSSFYGT 459
Cdd:cd07127 459 HSIELARESVREHGAMtvgVYSTDPEVVERVQEaALDAGVaLSINLtgGV-----FVNQSAAFSDFHGT 522
|
|
| |
