|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-531 |
0e+00 |
|
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: 809.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEI 148
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITWLLSEGERWLKPESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHAS 228
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 229 WSGCFYFRIIQAALAAVGAPENLVDVITGFAETGEALVSSV--DKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFI 306
Cdd:cd07098 161 WSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPviDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 307 ICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSL 386
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 387 VNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVF 466
Cdd:cd07098 321 VADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 467 SGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVEDR 531
Cdd:cd07098 401 GKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-529 |
2.62e-162 |
|
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: 468.61 E-value: 2.62e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 89 EERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTmVDASLGEIMTTCEKITWLLSEGERWLKP 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 169 ESRSsgrAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAP 248
Cdd:cd07078 80 VIPS---PDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----GLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 249 ENLVDVITGFA-ETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTL 325
Cdd:cd07078 153 PGVLNVVTGDGdEVGAALASHprVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 326 QSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGH 405
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 406 LGEDAvdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVA 485
Cdd:cd07078 313 GGKGY---FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 42563558 486 AINDFASNyMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVE 529
Cdd:cd07078 390 WINDYSVG-AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
71-528 |
7.75e-162 |
|
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: 468.24 E-value: 7.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEIMT 150
Cdd:cd07099 3 PATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-GLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITWLLSEGERWLKPESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWS 230
Cdd:cd07099 82 ALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 231 GCFyfriIQAALAAVGAPENLVDVITGFAETGEALVSS-VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICE 309
Cdd:cd07099 162 GEL----LAEAWAAAGPPQGVLQVVTGDGATGAALIDAgVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 310 DADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVND 389
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 390 ALDKGAEIAVRGSFGHLGEdavdQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGS 469
Cdd:cd07099 318 AVAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 470 KHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
62-527 |
3.91e-143 |
|
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: 420.78 E-value: 3.91e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMV 141
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DAsLGEIMTTCEKITWLLSEGERwLKPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVI 221
Cdd:pfam00171 85 EA-RGEVDRAIDVLRYYAGLARR-LDGETLPSDPGRLAYTRRE---PLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 222 KVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLE 298
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEA----GLPAGVLNVVTGSgAEVGEALVEHpdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 299 LGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQE 378
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 379 HSEHLQSLVNDALDKGAEIAVRGSFGhlgeDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSR 458
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAG----LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 459 YALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCqSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAD-GLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
62-531 |
1.57e-142 |
|
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: 419.92 E-value: 1.57e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMV 141
Cdd:COG1012 19 SGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DAsLGEIMTTCEKITWLLSEGERwLKPESRSSGRAmlHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVI 221
Cdd:COG1012 99 EA-RGEVDRAADFLRYYAGEARR-LYGETIPSDAP--GTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 222 KVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLE 298
Cdd:COG1012 175 KPAEQTPLSALLLAELLEEA----GLPAGVLNVVTGDgSEVGAALVAHpdVDKISFTGSTAVGRRIAAAAAENLKRVTLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 299 LGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQE 378
Cdd:COG1012 251 LGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 379 HSEHLQSLVNDALDKGAEIAVRgsfGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSR 458
Cdd:COG1012 331 QLERVLAYIEDAVAEGAELLTG---GRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563558 459 YALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQsLPFGGVKDSGFGRFAGIEGLRACCLVKSVVEDR 531
Cdd:COG1012 408 YGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
95-529 |
7.27e-125 |
|
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: 370.79 E-value: 7.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 95 SRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVdASLGEIMTTCEKITWLLSEGERWLKPESRSsg 174
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPELPS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 175 rAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDV 254
Cdd:cd06534 80 -PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA----GLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 255 ITGFA-ETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQN 331
Cdd:cd06534 155 VPGGGdEVGAALLSHprVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 332 CAGAERFYVHKDIYTAFIGQVTkivksvsagppltgrydmgaiclqehsehlqslvndaldkgaeiavrgsfghlgedav 411
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV---------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 412 dqyfppTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFA 491
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|....*...
gi 42563558 492 SNYMcQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVE 529
Cdd:cd06534 331 IGVG-PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
71-527 |
5.69e-111 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 338.25 E-value: 5.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEIMT 150
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITWLLSEGERW---LKPESRSSGRAMLHKvsrvefHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGIVIKVS 224
Cdd:cd07103 83 AASFLEWFAEEARRIygrTIPSPAPGKRILVIK------QPVGVVAAITPWNFPAAMItrkIAPALAA---GCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 225 EHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGG 301
Cdd:cd07103 154 EETPLSALALAELAEEA----GLPAGVLNVVTGSpAEIGEALCASprVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 302 KDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSE 381
Cdd:cd07103 230 NAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 382 HLQSLVNDALDKGAEIAVRGSFGHLGedavDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYAL 461
Cdd:cd07103 310 KVEALVEDAVAKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563558 462 GCAVFSGSKHRAKQIASQIQCGVAAINDFA-SNymcQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07103 386 AAYVFTRDLARAWRVAEALEAGMVGINTGLiSD---AEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-518 |
9.99e-105 |
|
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: 322.34 E-value: 9.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 70 EPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRqflRILLKY---IIEHQELICEVSSRDTGKTMVDAsLG 146
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERA---AVFLRFhdlVLERRDELLDLIQLETGKARRHA-FE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 147 EIMTTCEKITWLLSEGERWLKPESRSSGRAMLHKvSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEH 226
Cdd:cd07101 78 EVLDVAIVARYYARRAERLLKPRRRRGAIPVLTR-TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 227 ASWSGCFYFRIIQAAlaavGAPENLVDVITG-FAETGEALVSSVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAF 305
Cdd:cd07101 157 TALTALWAVELLIEA----GLPRDLWQVVTGpGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 306 IICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQS 385
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 386 LVNDALDKGAEIAVRGS----FGHLgedavdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYAL 461
Cdd:cd07101 313 HVDDAVAKGATVLAGGRarpdLGPY-------FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 42563558 462 GCAVFSGSKHRAKQIASQIQCGVAAIND-FASNYMCQSLPFGGVKDSGFGRFAGIEGL 518
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNEgYAAAWASIDAPMGGMKDSGLGRRHGAEGL 443
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-528 |
3.98e-104 |
|
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: 320.65 E-value: 3.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKT--WAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTM--VDASLG 146
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIreTRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 147 EIMTT-------CEKItwllsEGErwLKPESRSSgraMLHKVSRVefhPLGVIGAIVPWNYPfhnIFN------PMLAAv 213
Cdd:cd07114 84 YLAEWyryyaglADKI-----EGA--VIPVDKGD---YLNFTRRE---PLGVVAAITPWNSP---LLLlakklaPALAA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 214 fsGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAE 290
Cdd:cd07114 147 --GNTVVLKPSEHTPASTLELAKLAEEA----GFPPGVVNVVTGFgPETGEALVEHplVAKIAFTGGTETGRHIARAAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 291 TLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYD 370
Cdd:cd07114 221 NLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 371 MGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEV 450
Cdd:cd07114 301 MGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 451 IKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDF-ASNYMcqsLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07114 381 IALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYrALSPS---SPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
71-527 |
7.10e-104 |
|
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: 319.96 E-value: 7.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTmVDASLGEIMT 150
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP-IAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITWLLSEGERWLKPeSRSSGRAMLHKvsRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWS 230
Cdd:cd07102 82 MLERARYMISIAEEALAD-IRVPEKDGFER--YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 231 GCFyfriIQAALAAVGAPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIIC 308
Cdd:cd07102 159 GER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADprIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 309 EDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVN 388
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 389 DALDKGAEIAVRGSFGHLGeDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSG 468
Cdd:cd07102 315 DAIAKGARALIDGALFPED-KAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 469 SKHRAKQIASQIQCGVAAINdfASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07102 394 DIARAEALGEQLETGTVFMN--RCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
71-527 |
1.62e-101 |
|
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: 313.70 E-value: 1.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlGEIMT 150
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEVGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TcekITWLLSEGERWLKPESRS---SGRAMLHKVsrvefhPLGVIGAIVPWNYPFhnifnpMLA------AVFSGNGIVI 221
Cdd:cd07106 83 A---VAWLRYTASLDLPDEVIEdddTRRVELRRK------PLGVVAAIVPWNFPL------LLAawkiapALLAGNTVVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 222 KVSEHASWSGCFYFRIIQAALaavgaPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLEL 299
Cdd:cd07106 148 KPSPFTPLCTLKLGELAQEVL-----PPGVLNVVSGGDELGPALTSHpdIRKISFTGSTATGKKVMASAAKTLKRVTLEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 300 GGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEH 379
Cdd:cd07106 223 GGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 380 SEHLQSLVNDALDKGAEIAVRGSFghlgeDAVDQYF-PPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSR 458
Cdd:cd07106 303 YDKVKELVEDAKAKGAKVLAGGEP-----LDGPGYFiPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSE 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 459 YALGCAVFSGSKHRAKQIASQIQCGVAAINDFASnyMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07106 378 YGLGASVWSSDLERAEAVARRLEAGTVWINTHGA--LDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
62-535 |
1.72e-100 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 313.74 E-value: 1.72e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRrqfLRILLKY---IIEHQELICEVSSRDTGK 138
Cdd:PRK09407 30 AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRER---AAVLLRFhdlVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 139 TMVDAsLGEIMTTCEKITWLLSEGERWLKPESRSSGRAMLHKVsRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNG 218
Cdd:PRK09407 107 ARRHA-FEEVLDVALTARYYARRAPKLLAPRRRAGALPVLTKT-TELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 219 IVIKVSEHASWSgcfyfriiqaALAAV------GAPENLVDVITG-FAETGEALVSSVDKMIFVGSTAVGKMIMRNAAET 291
Cdd:PRK09407 185 VVLKPDSQTPLT----------ALAAVellyeaGLPRDLWQVVTGpGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDM 371
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 372 GAICLQEHSEHLQSLVNDALDKGAEIaVRGsfGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVI 451
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATV-LAG--GKARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 452 KLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIND-FASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVED 530
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgYAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491
|
....*
gi 42563558 531 RFWPL 535
Cdd:PRK09407 492 RVLPL 496
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
88-528 |
2.78e-98 |
|
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: 304.77 E-value: 2.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 88 VEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEImttcEKITWLLS----EGE 163
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEV----EKCAWICRyyaeNAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 164 RWLKPESRSSGramlHKVSRVEFHPLGVIGAIVPWNYPFHNIFN---PMLAAvfsGNGIVIKvseHAS-WSGCFyfRIIQ 239
Cdd:cd07100 76 AFLADEPIETD----AGKAYVRYEPLGVVLGIMPWNFPFWQVFRfaaPNLMA---GNTVLLK---HASnVPGCA--LAIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 240 AALAAVGAPENLVDVITGFAETGEALVSsvDKMI----FVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSH 315
Cdd:cd07100 144 ELFREAGFPEGVFQNLLIDSDQVEAIIA--DPRVrgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 316 VAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGA 395
Cdd:cd07100 222 AVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 396 EIavrgsfgHLGEDAVDQ---YFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHR 472
Cdd:cd07100 302 TL-------LLGGKRPDGpgaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLER 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 42563558 473 AKQIASQIQCGVAAINDF-ASNymcQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07100 375 AERVARRLEAGMVFINGMvKSD---PRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
106-529 |
5.90e-97 |
|
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: 301.33 E-value: 5.90e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 106 SFKLRRQFLRILLKYIIEHQELICEVSSRDTG-KTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSSGRAMLHKVSRV 184
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVGLLFLPAKAEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 185 EFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLVDVITGFAETGEA 264
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-----DEDEVAVVTGGADVAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 265 lVSSV--DKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHK 342
Cdd:cd07133 173 -FSSLpfDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 343 DIYTAFIGQVTKIVKSVSagPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAvrgSFGHLGEDAVD-QYFPPTVLI 421
Cdd:cd07133 252 DKLEEFVAAAKAAVAKMY--PTLADNPDYTSIINERHYARLQGLLEDARAKGARVI---ELNPAGEDFAAtRKLPPTLVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 422 NVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPF 501
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPF 406
|
410 420
....*....|....*....|....*...
gi 42563558 502 GGVKDSGFGRFAGIEGLRACCLVKSVVE 529
Cdd:cd07133 407 GGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-514 |
6.22e-96 |
|
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: 298.68 E-value: 6.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 87 EVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlGEIMTTcEKITW------LLS 160
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAA-IAILReaaglpRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 161 EGErwLKPeSRSSGramlhKVSRVEFHPLGVIGAIVPWNYPFH---NIFNPMLAAvfsGNGIVIKVSEHASWSGCFYF-R 236
Cdd:cd07104 79 EGE--ILP-SDVPG-----KESMVRRVPLGVVGVISPFNFPLIlamRSVAPALAL---GNAVVLKPDSRTPVTGGLLIaE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 237 IIQAAlaavGAPENLVDVITG-FAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADV 313
Cdd:cd07104 148 IFEEA----GLPKGVLNVVPGgGSEIGDALVEHprVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 314 SHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDK 393
Cdd:cd07104 224 DLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 394 GAEIAVrgsfghlGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRA 473
Cdd:cd07104 304 GARLLT-------GGTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERA 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 42563558 474 KQIASQIQCGVAAINDFASNYMCQSlPFGGVKDSGFGRFAG 514
Cdd:cd07104 377 MAFAERLETGMVHINDQTVNDEPHV-PFGGVKASGGGRFGG 416
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
71-528 |
1.02e-95 |
|
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: 299.16 E-value: 1.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQS-SFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTM-------VD 142
Cdd:cd07089 4 PATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtaramqVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 143 ASLGEIMTTCEKITWLLSEGERwlkPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIK 222
Cdd:cd07089 84 GPIGHLRYFADLADSFPWEFDL---PVPALRGGPGRRVVRRE---PVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 223 VSEHASWSGCFYFRIIqaalAAVGAPENLVDVITG-FAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLEL 299
Cdd:cd07089 158 PAPDTPLSALLLGEII----AETDLPAGVVNVVTGsDNAVGEALTTDprVDMVSFTGSTAVGRRIMAQAAATLKRVLLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 300 GGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEH 379
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 380 SEHLQSLVNDALDKGAEIAVRGsfGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRY 459
Cdd:cd07089 314 RDRVEGYIARGRDEGARLVTGG--GRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDY 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 460 ALGCAVFSGSKHRAKQIASQIQCGVAAINDFAsnYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07089 392 GLSGGVWSADVDRAYRVARRIRTGSVGINGGG--GYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
61-518 |
4.24e-94 |
|
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: 295.33 E-value: 4.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 61 QSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTM 140
Cdd:cd07088 10 SSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 141 VDASlGEIMTTCEKITWLLS-----EGErwLKPESRSSGRAMLHKVsrvefhPLGVIGAIVPWNYPFHNIFNPMLAAVFS 215
Cdd:cd07088 90 SLAR-VEVEFTADYIDYMAEwarriEGE--IIPSDRPNENIFIFKV------PIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 216 GNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITG-FAETGEALVSSVD-KMI-FVGSTAVGKMIMRNAAETL 292
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKvGMIsLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 293 TPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMG 372
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 373 AICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEdavDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIK 452
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42563558 453 LANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMcQSLpFGGVKDSGFGRFAGIEGL 518
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAM-QGF-HAGWKKSGLGGADGKHGL 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
69-527 |
1.25e-93 |
|
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: 293.70 E-value: 1.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEI 148
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKI-----TWLLSEGERWlkpesrSSGRAMLHKVSRvefHPLGVIGAIVPWNYPFhnifnpMLA------AVFSGN 217
Cdd:cd07093 82 PRAAANFrffadYILQLDGESY------PQDGGALNYVLR---QPVGVAGLITPWNLPL------MLLtwkiapALAFGN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 218 GIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSSVD-KMI-FVGSTAVGKMIMRNAAETLTP 294
Cdd:cd07093 147 TVVLKPSEWTPLTAWLLAELANEA----GLPPGVVNVVHGFgPEAGAALVAHPDvDLIsFTGETATGRTIMRAAAPNLKP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 295 VTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAI 374
Cdd:cd07093 223 VSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 375 CLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLA 454
Cdd:cd07093 303 ISKEHLEKVLGYVELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 455 NDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasnyMCQSL--PFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07093 383 NDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCW----LVRDLrtPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
62-527 |
1.03e-91 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 289.69 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKT-WAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTM 140
Cdd:cd07144 21 DGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 141 VDASLGEIMTTCEKITWLLSEGERwLKPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFH----NIFnPMLAAvfsG 216
Cdd:cd07144 101 HSNALGDLDEIIAVIRYYAGWADK-IQGKTIPTSPNKLAYTLHE---PYGVCGQIIPWNYPLAmaawKLA-PALAA---G 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 217 NGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLT 293
Cdd:cd07144 173 NTVVIKPAENTPLSLLYFANLVKEA----GFPPGVVNIIPGYgAVAGSALAEHpdVDKIAFTGSTATGRLVMKAAAQNLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 294 PVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSA-GPPLTGRYDMG 372
Cdd:cd07144 249 AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKvGSPFDDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 373 AICLQEHSEHLQSLVNDALDKGAEIaVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIK 452
Cdd:cd07144 329 PQVSKTQYDRVLSYIEKGKKEGAKL-VYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 453 LANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINdfASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWIN--SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
61-528 |
3.51e-90 |
|
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: 285.26 E-value: 3.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 61 QSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKT--WAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGK 138
Cdd:cd07091 16 VSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 139 TMVDASLGEIMTT----------CEKITwllseGErwlKPESRSSGRAMLHKVsrvefhPLGVIGAIVPWNYP---FHNI 205
Cdd:cd07091 96 PLEESAKGDVALSikclryyagwADKIQ-----GK---TIPIDGNFLAYTRRE------PIGVCGQIIPWNFPllmLAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 206 FNPMLAAvfsGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAVGK 282
Cdd:cd07091 162 LAPALAA---GNTVVLKPAEQTPLSALYLAELIKEA----GFPPGVVNIVPGFGPTaGAAISSHmdVDKIAFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 283 MIMRNAAET-LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSA 361
Cdd:cd07091 235 TIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 362 GPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGS-FGHLGedavdqYF-PPTVLINVNHNMKIMKEEAFGPIM 439
Cdd:cd07091 315 GDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGErHGSKG------YFiQPTVFTDVKDDMKIAKEEIFGPVV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 440 PIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGRFAGIEGLR 519
Cdd:cd07091 389 TILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTY--NVFDAAVPFGGFKQSGFGRELGEEGLE 466
|
....*....
gi 42563558 520 ACCLVKSVV 528
Cdd:cd07091 467 EYTQVKAVT 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
69-527 |
1.11e-89 |
|
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: 283.43 E-value: 1.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLgEI 148
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV-DI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITW---LLS--EGERWLKPESRSSgramlhkVSRVEfhPLGVIGAIVPWNYPFHNIF---NPMLAAvfsGNGIV 220
Cdd:cd07090 81 DSSADCLEYyagLAPtlSGEHVPLPGGSFA-------YTRRE--PLGVCAGIGAWNYPIQIASwksAPALAC---GNAMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 221 IKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTLE 298
Cdd:cd07090 149 YKPSPFTPLTALLLAEILTEA----GLPDGVFNVVQGGGETGQLLCEhpDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 299 LGGKDAFIICEDADVshvaQVAVRGTLQ----SSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAI 374
Cdd:cd07090 225 LGGKSPLIIFDDADL----ENAVNGAMManflSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 375 CLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLgEDAVD--QYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIK 452
Cdd:cd07090 301 ISEEHLEKVLGYIESAKQEGAKVLCGGERVVP-EDGLEngFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIR 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 453 LANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07090 380 RANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTY--NISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
89-529 |
1.88e-89 |
|
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: 281.72 E-value: 1.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 89 EERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKP 168
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 169 ESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaP 248
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYF-----D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 249 ENLVDVITGFAETGEALVS-SVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQS 327
Cdd:cd07087 156 PEAVAVVEGGVEVATALLAePFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 328 SGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRyDMGAICLQEHSEHLQSLVNDAldkgaEIAVRGSFghlg 407
Cdd:cd07087 236 AGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDG-----KVVIGGQV---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 408 eDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAI 487
Cdd:cd07087 306 -DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 42563558 488 NDFASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVE 529
Cdd:cd07087 385 NDVLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
64-511 |
5.34e-89 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 283.12 E-value: 5.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 64 KKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDA 143
Cdd:PLN02278 40 KTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 144 sLGEIMTTCEKITWLLSEGERW---LKPESRSSGRAMLHKvsrvefHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIV 220
Cdd:PLN02278 120 -IGEVAYGASFLEYFAEEAKRVygdIIPSPFPDRRLLVLK------QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 221 IKVSEHASWSgcfyfriiqaALAA------VGAPENLVDVITGFA-ETGEALVSS--VDKMIFVGSTAVGKMIMRNAAET 291
Cdd:PLN02278 193 VKPSELTPLT----------ALAAaelalqAGIPPGVLNVVMGDApEIGDALLASpkVRKITFTGSTAVGKKLMAGAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LTPVTLELGGKDAFIICEDADVshvaQVAVRGTLQS----SGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTG 367
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADL----DVAVKGALASkfrnSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 368 RYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEdavdQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTD 447
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG----TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563558 448 EEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNymCQSLPFGGVKDSGFGR 511
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLIS--TEVAPFGGVKQSGLGR 476
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
69-528 |
1.72e-88 |
|
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: 280.27 E-value: 1.72e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWA-QSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlGE 147
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-AD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 148 IM----------TTCEKItwllsEGErwlkpeSRSSGRAMLHKVSRVefhPLGVIGAIVPWNYP---FHNIFNPMLAAvf 214
Cdd:cd07109 81 VEaaaryfeyygGAADKL-----HGE------TIPLGPGYFVYTVRE---PHGVTGHIIPWNYPlqiTGRSVAPALAA-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 215 sGNGIVIKVSEHASWSGCfyfRIIQAALAAvGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAET 291
Cdd:cd07109 145 -GNAVVVKPAEDAPLTAL---RLAELAEEA-GLPAGALNVVTGLgAEAGAALVAHpgVDHISFTGSVETGIAVMRAAAEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLtGRYDM 371
Cdd:cd07109 220 VVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 372 GAICLQEHSEHLQSLVNDALDKGAEIAVRgsfGHLGEDAVDQ--YFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEE 449
Cdd:cd07109 299 GPLISAKQLDRVEGFVARARARGARIVAG---GRIAEGAPAGgyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 450 VIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIND-FASNYMcqSLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07109 376 AIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNyGAGGGI--ELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
94-520 |
3.36e-88 |
|
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: 278.73 E-value: 3.36e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 94 LSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSS 173
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 174 GRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLVD 253
Cdd:cd07134 86 PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAF-----DEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 254 VITGFAETGEALVS-SVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNC 332
Cdd:cd07134 161 VFEGDAEVAQALLElPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 333 AGAERFYVHKDIYTAFIGQV-TKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFghlgeDAV 411
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLkAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF-----DAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 412 DQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFA 491
Cdd:cd07134 316 QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVV 395
|
410 420
....*....|....*....|....*....
gi 42563558 492 SNYMCQSLPFGGVKDSGFGRFAGIEGLRA 520
Cdd:cd07134 396 LHFLNPNLPFGGVNNSGIGSYHGVYGFKA 424
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
64-527 |
4.33e-88 |
|
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: 279.49 E-value: 4.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 64 KKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKA--QKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMV 141
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DASLGEIMTTCEKITWLlSEGERWLKPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNG 218
Cdd:cd07112 82 DALAVDVPSAANTFRWY-AEAIDKVYGEVAPTGPDALALITRE---PLGVVGAVVPWNFPLLMAawkIAPALAA---GNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 219 IVIKVSEHASWSGcfyFRIIQAALAAvGAPENLVDVITGFAET-GEALV--SSVDKMIFVGSTAVGKMIMRNAAET-LTP 294
Cdd:cd07112 155 VVLKPAEQSPLTA---LRLAELALEA-GLPAGVLNVVPGFGHTaGEALGlhMDVDALAFTGSTEVGRRFLEYSGQSnLKR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 295 VTLELGGKDAFIICEDA-DVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGA 373
Cdd:cd07112 231 VWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 374 ICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHlgEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKL 453
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRVL--TETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVAL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563558 454 ANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMcqSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07112 389 ANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDI--TTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
51-528 |
3.50e-87 |
|
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: 277.08 E-value: 3.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 51 IYIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICE 130
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 131 VSSRDTG-------KTMVDASLGEIMTTCEkitwlLSEGERWlkpESRSSGramlhkvSRVEFHPLGVIGAIVPWNYPFH 203
Cdd:cd07138 81 AITLEMGapitlarAAQVGLGIGHLRAAAD-----ALKDFEF---EERRGN-------SLVVREPIGVCGLITPWNWPLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 204 NIFNPMLAAVFSGNGIVIKVSEHASWSGcfyfRIIQAALAAVGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAV 280
Cdd:cd07138 146 QIVLKVAPALAAGCTVVLKPSEVAPLSA----IILAEILDEAGLPAGVFNLVNGDGPVvGEALSAHpdVDMVSFTGSTRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 281 GKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVS 360
Cdd:cd07138 222 GKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 361 AGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVrGsfghlGEDAVDQ-----YFPPTVLINVNHNMKIMKEEAF 435
Cdd:cd07138 302 VGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVA-G-----GPGRPEGlergyFVKPTVFADVTPDMTIAREEIF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 436 GPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYmcqSLPFGGVKDSGFGRFAGI 515
Cdd:cd07138 376 GPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGR 452
|
490
....*....|...
gi 42563558 516 EGLRACCLVKSVV 528
Cdd:cd07138 453 YGLEEFLEVKSIQ 465
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-520 |
4.17e-87 |
|
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: 276.52 E-value: 4.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEI 148
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITWLLSEGERwLKPESRSSGRAmlHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHAS 228
Cdd:cd07150 83 TFTPELLRAAAGECRR-VRGETLPSDSP--GTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 229 WSGCFYFRIIQAAlaavGAPENLVDVITG-FAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAF 305
Cdd:cd07150 160 VIGLKIAEIMEEA----GLPKGVFNVVTGgGAEVGDELVDDprVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 306 IICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQS 385
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 386 LVNDALDKGAEIAVRGsfGHLGedavdQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAV 465
Cdd:cd07150 316 QVEDAVAKGAKLLTGG--KYDG-----NFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAI 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 466 FSGSKHRAKQIASQIQCGVAAINDfASNYMCQSLPFGGVKDSGFGRFAGIEGLRA 520
Cdd:cd07150 389 LTNDLQRAFKLAERLESGMVHIND-PTILDEAHVPFGGVKASGFGREGGEWSMEE 442
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
69-519 |
3.59e-86 |
|
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: 274.23 E-value: 3.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDaSLGEI 148
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-SRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEkITWLLSEGERWLKPES-RSSGRAMLHKvsRVEF---HPLGVIGAIVPWNYPF----HNIfNPMLAAvfsGNGIV 220
Cdd:cd07145 83 ERTIR-LFKLAAEEAKVLRGETiPVDAYEYNER--RIAFtvrEPIGVVGAITPFNFPAnlfaHKI-APAIAV---GNSVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 221 IKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTL 297
Cdd:cd07145 156 VKPSSNTPLTAIELAKILEEA----GLPPGVINVVTGYGSEvGDEIVTNpkVNMISFTGSTAVGLLIASKAGGTGKKVAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 298 ELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQ 377
Cdd:cd07145 232 ELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 378 EHSEHLQSLVNDALDKGAEIAVRGSfghlGEDAvdQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDS 457
Cdd:cd07145 312 EAVERMENLVNDAVEKGGKILYGGK----RDEG--SFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANST 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563558 458 RYALGCAVFSGSKHRAKQIASQIQCGVAAINDfASNYMCQSLPFGGVKDSGFGRfagiEGLR 519
Cdd:cd07145 386 EYGLQASVFTNDINRALKVARELEAGGVVIND-STRFRWDNLPFGGFKKSGIGR----EGVR 442
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-529 |
3.74e-85 |
|
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: 271.53 E-value: 3.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAS--LGEI 148
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITwLLSEGERWLKPES---RSSGRAmlhkvSRVEFHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGIVIK 222
Cdd:cd07110 84 AGCFEYYA-DLAEQLDAKAERAvplPSEDFK-----ARVRREPVGVVGLITPWNFPLLMAawkVAPALAA---GCTVVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 223 VSEHASWSGCFYFRIIqaalAAVGAPENLVDVITGFA-ETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTLEL 299
Cdd:cd07110 155 PSELTSLTELELAEIA----AEAGLPPGVLNVVTGTGdEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 300 GGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEH 379
Cdd:cd07110 231 GGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 380 SEHLQSLVNDALDKGAEIaVRGsfGHLGEDAVDQYF-PPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSR 458
Cdd:cd07110 311 YEKVLSFIARGKEEGARL-LCG--GRRPAHLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563558 459 YALGCAVFSGSKHRAKQIASQIQCGVAAINdfASN-YMCQsLPFGGVKDSGFGRFAGIEGLRACCLVKSVVE 529
Cdd:cd07110 388 YGLAAAVISRDAERCDRVAEALEAGIVWIN--CSQpCFPQ-APWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
71-527 |
2.37e-84 |
|
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: 269.63 E-value: 2.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVdASLGEIMT 150
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITW---LLSEgerwLKPESRSSGRAMLHkVSRVEfhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHA 227
Cdd:cd07107 83 AAALLDYfagLVTE----LKGETIPVGGRNLH-YTLRE--PYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 228 SWSGCFYFRIIQAALaavgaPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDA 304
Cdd:cd07107 156 PLSALRLAELAREVL-----PPGVFNILPGDgATAGAALVRHpdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 305 FIICEDADVSHVAQVAVRG-TLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHL 383
Cdd:cd07107 231 LIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 384 QSLVNDALDKGAEIAVRGSF--GHLGEDAVdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYAL 461
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRpeGPALEGGF--YVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42563558 462 GCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMcqSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07107 389 TAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
71-527 |
4.73e-84 |
|
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: 268.54 E-value: 4.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMT 150
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 T----------CEKItwllsEGErwLKPesrSSGRAMLHKVSRvefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIV 220
Cdd:cd07115 84 AadtfryyagwADKI-----EGE--VIP---VRGPFLNYTVRE----PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 221 IKVSEHASWSGcfyFRIIQAAlAAVGAPENLVDVITGFAE-TGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTL 297
Cdd:cd07115 150 LKPAELTPLSA---LRIAELM-AEAGFPAGVLNVVTGFGEvAGAALVEhpDVDKITFTGSTAVGRKIMQGAAGNLKRVSL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 298 ELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQ 377
Cdd:cd07115 226 ELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 378 EHSEHLQSLVNDALDKGAEIAVRGSfghlGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDS 457
Cdd:cd07115 306 AQFDRVLDYVDVGREEGARLLTGGK----RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGT 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 458 RYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07115 382 EYGLAAGVWTRDLGRAHRVAAALKAGTVWINTY--NRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
51-528 |
5.31e-83 |
|
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: 266.36 E-value: 5.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 51 IYIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKA--QKTWAQSSFKLRRQFLRILLKYIIEHQELI 128
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 129 CEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSS---GRAMLHKVsrvefhPLGVIGAIVPWNYPFHNI 205
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGsggGHVLVRRE------PVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 206 FN---PMLAAvfsGNGIVIKVSEHASWSGCfyfrIIQAALAAVGAPENLVDVITGFAETGEALVS--SVDKMIFVGSTAV 280
Cdd:cd07139 155 ALkiaPALAA---GCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRhpGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 281 GKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVS 360
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 361 AGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSfghlGEDAVDQ--YFPPTVLINVNHNMKIMKEEAFGPI 438
Cdd:cd07139 308 VGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGG----RPAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 439 MPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasnYMCQSLPFGGVKDSGFGRFAGIEGL 518
Cdd:cd07139 384 LSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF---RLDFGAPFGGFKQSGIGREGGPEGL 460
|
490
....*....|
gi 42563558 519 RACCLVKSVV 528
Cdd:cd07139 461 DAYLETKSIY 470
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-527 |
2.55e-82 |
|
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: 263.28 E-value: 2.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 87 EVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTM------VDASLGEIMTTCEKITWLLS 160
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAawagfnVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 161 EgerwLKPESRSSGRAMLHKvsrvefHPLGVIGAIVPWNYPFH----NIFNPmLAAvfsGNGIVIKVSEHASwsGCFYFr 236
Cdd:cd07105 81 G----SIPSDKPGTLAMVVK------EPVGVVLGIAPWNAPVIlgtrAIAYP-LAA---GNTVVLKASELSP--RTHWL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 237 IIQAALAAvGAPENLVDVITGFAETG----EALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICED 310
Cdd:cd07105 144 IGRVFHEA-GLPKGVLNVVTHSPEDApevvEALIAHpaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLED 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 311 ADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGR-YDMGAIclqehsEHLQSLVND 389
Cdd:cd07105 223 ADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLGSlVSAAAA------DRVKELVDD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 390 ALDKGAEIaVRGSFGHLGEDAVdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGS 469
Cdd:cd07105 297 ALSKGAKL-VVGGLADESPSGT--SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRD 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563558 470 KHRAKQIASQIQCGVAAIN-----DFAsnymcqSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07105 374 LARALAVAKRIESGAVHINgmtvhDEP------TLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
52-520 |
2.96e-82 |
|
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: 264.59 E-value: 2.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 52 YIPPRGRSQQSDKKVQCYEPA-TMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICE 130
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 131 VSSRDTGKTMVDAsLGEIMTTCEKITWLLSEGERwLKPESRSSgrAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPML 210
Cdd:cd07131 82 LVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRR-LFGETVPS--ELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 211 AAVFSGNGIVIKVSEHASWSGcfyFRIIQAaLAAVGAPENLVDVITGFAE-TGEALV--SSVDKMIFVGSTAVGKMIMRN 287
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACA---LKLVEL-FAEAGLPPGVVNVVHGRGEeVGEALVehPDVDVVSFTGSTEVGERIGET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 288 AAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTG 367
Cdd:cd07131 234 CARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 368 RYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTD 447
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563558 448 EEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQsLPFGGVKDSGFG-RFAGIEGLRA 520
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVH-LPFGGVKKSGNGhREAGTTALDA 466
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
70-518 |
7.07e-82 |
|
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: 263.07 E-value: 7.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 70 EPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIM 149
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 150 TTCEKITW---LLSEgerwLKPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEH 226
Cdd:cd07108 83 VLADLFRYfggLAGE----LKGETLPFGPDVLTYTVRE---PLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 227 ASWSGCFYFRIIQAALaavgaPENLVDVITGF-AETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKD 303
Cdd:cd07108 156 APLAVLLLAEILAQVL-----PAGVLNVITGYgEECGAALVDhpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 304 AFIICEDADVSHVAQVAVRGT-LQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEH 382
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 383 LQSLVNDALD-KGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYAL 461
Cdd:cd07108 311 VCGYIDLGLStSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 42563558 462 GCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSlpFGGVKDSGFGRFAGIEGL 518
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQS--YGGFKQSGLGREASLEGM 445
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
62-511 |
9.54e-82 |
|
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: 263.44 E-value: 9.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMV 141
Cdd:cd07559 14 KGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DASLGEIMttcekitwLLSEGERWLKP--ESRSSGRAMLHK--VSRVEFHPLGVIGAIVPWNYPFHNI---FNPMLAAvf 214
Cdd:cd07559 94 ETLAADIP--------LAIDHFRYFAGviRAQEGSLSEIDEdtLSYHFHEPLGVVGQIIPWNFPLLMAawkLAPALAA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 215 sGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAET 291
Cdd:cd07559 164 -GNTVVLKPASQTPLSILVLMELIGDLL-----PKGVVNVVTGFgSEAGKPLASHprIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LTPVTLELGGKDAFIICEDADVSHV-----AQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLT 366
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAMDADDdfddkAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 367 GRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFST 446
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 447 DEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGR 511
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCY--HQYPAHAPFGGYKKSGIGR 460
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
62-528 |
1.58e-81 |
|
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: 262.51 E-value: 1.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQ-SSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTM 140
Cdd:cd07082 14 SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 141 VDAsLGEIMTTCEKITWLLSEGER----WLKPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSG 216
Cdd:cd07082 94 KDA-LKEVDRTIDYIRDTIEELKRldgdSLPGDWFPGTKGKIAQVRRE---PLGVVLAIGPFNYPLNLTVSKLIPALIMG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 217 NGIVIKVSEHASWSGCFYFRiiqaALAAVGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAetLT 293
Cdd:cd07082 170 NTVVFKPATQGVLLGIPLAE----AFHDAGFPKGVVNVVTGRgREIGDPLVTHgrIDVISFTGSTEVGNRLKKQHP--MK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 294 PVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGA 373
Cdd:cd07082 244 RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 374 ICLQEHSEHLQSLVNDALDKGAEIAVRGsfGHLGEDavdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKL 453
Cdd:cd07082 324 LIDPKSADFVEGLIDDAVAKGATVLNGG--GREGGN----LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 454 ANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDfasnyMCQ----SLPFGGVKDSGFGRfAGI-EGLRACCLVKSVV 528
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-----KCQrgpdHFPFLGRKDSGIGT-QGIgDALRSMTRRKGIV 471
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
62-511 |
3.64e-81 |
|
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: 262.01 E-value: 3.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMV 141
Cdd:cd07117 14 SGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DASLGEIMTTCEKITWLLSEgerwLKPESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNG 218
Cdd:cd07117 94 ETRAVDIPLAADHFRYFAGV----IRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAawkLAPALAA---GNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 219 IVIKVSEHASWSGCFYFRIIQAALaavgaPENLVDVITGF-AETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPV 295
Cdd:cd07117 167 VVIKPSSTTSLSLLELAKIIQDVL-----PKGVVNIVTGKgSKSGEYLLNhpGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 296 TLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAIC 375
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 376 LQEHSEHLQSLVNDALDKGAEIAVRGsfGHLGEDAVDQ--YFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKL 453
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGG--HRLTENGLDKgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 42563558 454 ANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGR 511
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTY--NQIPAGAPFGGYKKSGIGR 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
58-514 |
6.39e-81 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 260.70 E-value: 6.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 58 RSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTG 137
Cdd:cd07151 4 RDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 138 KTMVDASL---GEIMTTCEKITWLLSEGERWLkpESRSSGramlhKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVF 214
Cdd:cd07151 84 STRIKANIewgAAMAITREAATFPLRMEGRIL--PSDVPG-----KENRVYREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 215 SGNGIVIKVSEHASWSGCFYF-RIIQAAlaavGAPENLVDVITG-FAETGEALVSS-VDKMI-FVGSTAVGKMIMRNAAE 290
Cdd:cd07151 157 LGNAVVLKPASDTPITGGLLLaKIFEEA----GLPKGVLNVVVGaGSEIGDAFVEHpVPRLIsFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 291 TLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYD 370
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 371 MGAICLQEHSEHLQSLVNDALDKGAEIAVRGsfghlgeDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEV 450
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG-------EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563558 451 IKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMcQSLPFGGVKDSGFGRFAG 514
Cdd:cd07151 386 LELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDE-PHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
52-519 |
7.33e-81 |
|
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: 261.09 E-value: 7.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 52 YIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKA--QKTWAQSSFKLRRQFLRILLKYIIEHQELIC 129
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 130 EVSSRDTGKTMVDAS--LGEIMTTCEKITWLLSegerwlKPESRSSGRAMlHKVSRVEFHPLGVIGAIVPWNYPFHNI-- 205
Cdd:cd07119 81 RLETLNTGKTLRESEidIDDVANCFRYYAGLAT------KETGEVYDVPP-HVISRTVREPVGVCGLITPWNYPLLQAaw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 206 -FNPMLAAvfsGNGIVIKVSEHASWSGCFYFRIIqaalAAVGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAVG 281
Cdd:cd07119 154 kLAPALAA---GNTVVIKPSEVTPLTTIALFELI----EEAGLPAGVVNLVTGSGATvGAELAESpdVDLVSFTGGTATG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 282 KMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSA 361
Cdd:cd07119 227 RSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 362 GPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSfgHLGEDAVDQ--YFPPTVLINVNHNMKIMKEEAFGPIM 439
Cdd:cd07119 307 GNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGK--RPTGDELAKgyFVEPTIFDDVDRTMRIVQEEIFGPVL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 440 PIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGRFAGIEGLR 519
Cdd:cd07119 385 TVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDY--HPYFAEAPWGGYKQSGIGRELGPTGLE 462
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
71-529 |
6.29e-80 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 259.28 E-value: 6.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKA-----QKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTmVDASL 145
Cdd:PLN02467 30 PATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP-LDEAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 146 GEI--MTTCEKITWLLSEGerwLKPESRSS-GRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGI 219
Cdd:PLN02467 109 WDMddVAGCFEYYADLAEA---LDAKQKAPvSLPMETFKGYVLKEPLGVVGLITPWNYPLLMAtwkVAPALAA---GCTA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 220 VIKVSEHASWSgCFYFriiqAALAA-VGAPENLVDVITGF-AETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPV 295
Cdd:PLN02467 183 VLKPSELASVT-CLEL----ADICReVGLPPGVLNVVTGLgTEAGAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 296 TLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAIC 375
Cdd:PLN02467 258 SLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 376 LQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLAN 455
Cdd:PLN02467 338 SEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGF--FIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563558 456 DSRYALGCAVFSGSKHRAKQIASQIQCGVAAINdFASNYMCQsLPFGGVKDSGFGRFAGIEGLRACCLVKSVVE 529
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERVSEAFQAGIVWIN-CSQPCFCQ-APWGGIKRSGFGRELGEWGLENYLSVKQVTK 487
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
69-519 |
2.11e-78 |
|
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: 254.06 E-value: 2.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSfklRRQFLRILLK---YIIEHQELICEVSSRDTGKTMVDAsL 145
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLP---AYERAEILERaaqLLEERREEFARTIALEAGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 146 GEIMTTCEKITwLLSEGERWLKPES-------RSSGR-AMLHKVsrvefhPLGVIGAIVPWNYPF----HNIfNPMLAAv 213
Cdd:cd07149 80 KEVDRAIETLR-LSAEEAKRLAGETipfdaspGGEGRiGFTIRE------PIGVVAAITPFNFPLnlvaHKV-GPAIAA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 214 fsGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVSSVD-KMI-FVGSTAVGKMIMRNAAe 290
Cdd:cd07149 151 --GNAVVLKPASQTPLSALKLAELLLEA----GLPKGALNVVTGSGETvGDALVTDPRvRMIsFTGSPAVGEAIARKAG- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 291 tLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYD 370
Cdd:cd07149 224 -LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 371 MGAICLQEHSEHLQSLVNDALDKGAEIAVrgsfGHLGEDAVdqyFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEV 450
Cdd:cd07149 303 VGPMISEAEAERIEEWVEEAVEGGARLLT----GGKRDGAI---LEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 451 IKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDfASNYMCQSLPFGGVKDSGFGRfagiEGLR 519
Cdd:cd07149 376 IAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTGR----EGPR 439
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
97-514 |
2.98e-78 |
|
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: 253.20 E-value: 2.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 97 KAQKTWAQS----SFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRS 172
Cdd:cd07136 5 EKQRAFFKTgatkDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRVK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 173 SGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLV 252
Cdd:cd07136 85 TPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETF-----DEEYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 253 DVITGFAETGEALVSS-VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQN 331
Cdd:cd07136 160 AVVEGGVEENQELLDQkFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 332 CAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRyDMGAICLQEHSEHLQSLVNDaldkgaEIAVRGsfghlGE-DA 410
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDN------GKIVFG-----GNtDR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 411 VDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIND- 489
Cdd:cd07136 308 ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDt 387
|
410 420
....*....|....*....|....*...
gi 42563558 490 ---FASNYMcqslPFGGVKDSGFGRFAG 514
Cdd:cd07136 388 imhLANPYL----PFGGVGNSGMGSYHG 411
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
69-527 |
1.13e-76 |
|
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: 249.17 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEI 148
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITWLlSEGERWLkpESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGIVIKVSE 225
Cdd:cd07092 82 PGAVDNFRFF-AGAARTL--EGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAawkIAPALAA---GNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 226 HASWSGcfyfrIIQAALAAVGAPENLVDVITGFAE-TGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGK 302
Cdd:cd07092 156 TTPLTT-----LLLAELAAEVLPPGVVNVVCGGGAsAGDALVAhpRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 303 DAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEH 382
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 383 LQSLVnDALDKGAEIAVRGSFGhlgeDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALG 462
Cdd:cd07092 311 VAGFV-ERAPAHARVLTGGRRA----EGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563558 463 CAVFSGSKHRAKQIASQIQCGVAAIND---FASNymcqsLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07092 386 SSVWTRDVGRAMRLSARLDFGTVWVNThipLAAE-----MPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
62-528 |
3.20e-76 |
|
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: 249.19 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQK---TWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGK 138
Cdd:cd07141 20 SGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 139 TMVDASLGEIMTTCEKITWLLSEGERWLKPESRSSGRAMLHkvSRVEfhPLGVIGAIVPWNYPFHNI---FNPMLAAvfs 215
Cdd:cd07141 100 PFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTY--TRHE--PVGVCGQIIPWNFPLLMAawkLAPALAC--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 216 GNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVSS---VDKMIFVGSTAVGKMIMRNAAET- 291
Cdd:cd07141 173 GNTVVLKPAEQTPLTALYLASLIKEA----GFPPGVVNVVPGYGPTAGAAISShpdIDKVAFTGSTEVGKLIQQAAGKSn 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDM 371
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 372 GAICLQEHSEHLQSLVNDALDKGAEIAVRGS-FGHLGedavdqYF-PPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEE 449
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGGKrHGDKG------YFiQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 450 VIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFaSNYMCQSlPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07141 403 VIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCY-NVVSPQA-PFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
84-514 |
4.53e-76 |
|
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: 247.59 E-value: 4.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDA--SLGEIMTTCEKITWLLSE 161
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAgfEVGAAIGELHEAAGLPTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 162 GERWLKPesrsSGRAMLHKVSRVefhPLGVIGAIVPWNYPFH---NIFNPMLAAvfsGNGIVIKVSEHASWSGCFyfrII 238
Cdd:cd07152 91 PQGEILP----SAPGRLSLARRV---PLGVVGVISPFNFPLIlamRSVAPALAL---GNAVVLKPDPRTPVSGGV---VI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 239 QAALAAVGAPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHV 316
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDpnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 317 AQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAE 396
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 397 IAVRGSFGHLgedavdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQI 476
Cdd:cd07152 318 LEAGGTYDGL-------FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 42563558 477 ASQIQCGVAAINDFASNYMCQSlPFGGVKDSGFG-RFAG 514
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEPHN-PFGGMGASGNGsRFGG 428
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
43-527 |
8.29e-76 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 248.21 E-value: 8.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 43 KDTEENSFIYIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKA-QKTWAQSSFKLRRQFLRILLKYI 121
Cdd:cd07143 1 GKYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 122 IEHQ-ELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSegerWlkpESRSSGRAMLHKVSRVEF---HPLGVIGAIVP 197
Cdd:cd07143 81 MERNlDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGG----W---ADKIHGQVIETDIKKLTYtrhEPIGVCGQIIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 198 WNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVS--SVDKMIF 274
Cdd:cd07143 154 WNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVVSGYGRTcGNAISShmDIDKVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 275 VGSTAVGKMIMRNAAET-LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVT 353
Cdd:cd07143 230 TGSTLVGRKVMEAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 354 KIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGS-FGHLGedavdqYF-PPTVLINVNHNMKIMK 431
Cdd:cd07143 310 EKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKrHGNEG------YFiEPTIFTDVTEDMKIVK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 432 EEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGR 511
Cdd:cd07143 384 EEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCY--NLLHHQVPFGGYKQSGIGR 461
|
490
....*....|....*.
gi 42563558 512 FAGIEGLRACCLVKSV 527
Cdd:cd07143 462 ELGEYALENYTQIKAV 477
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
93-528 |
7.58e-75 |
|
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: 244.58 E-value: 7.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 93 TLSRKAQKTWAQSSFKLRRQFLRILLK---YIIEHQELICEVSSRDTGKTMVDAsLGEIMTTCEKITWLLSEGERwLKPE 169
Cdd:cd07146 22 ALREALALAASYRSTLTRYQRSAILNKaaaLLEARREEFARLITLESGLCLKDT-RYEVGRAADVLRFAAAEALR-DDGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 170 SRSSGRAMLHKVSRVEFH--PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSgCFYFRIIqaaLAAVGA 247
Cdd:cd07146 100 SFSCDLTANGKARKIFTLrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLS-AIYLADL---LYEAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 248 PENLVDVITG-FAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTpvTLELGGKDAFIICEDADVSHVAQVAVRGT 324
Cdd:cd07146 176 PPDMLSVVTGePGEIGDELITHpdVDLVTFTGGVAVGKAIAATAGYKRQ--LLELGGNDPLIVMDDADLERAATLAVAGS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 325 LQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAvrgsFG 404
Cdd:cd07146 254 YANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVL----LG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 405 HLGEDAVdqyFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGV 484
Cdd:cd07146 330 NQRQGAL---YAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGT 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 42563558 485 AAINDfASNYMCQSLPFGGVKDSGFGRFAGI-EGLRACCLVKSVV 528
Cdd:cd07146 407 VNVNE-VPGFRSELSPFGGVKDSGLGGKEGVrEAMKEMTNVKTYS 450
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-527 |
8.07e-75 |
|
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: 244.55 E-value: 8.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKT--WAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTmVDASLGEI 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKP-ISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITWLLSEGeRWLKPESRSS-GRAMLHKVSRvefHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHA 227
Cdd:cd07118 83 EGAADLWRYAASLA-RTLHGDSYNNlGDDMLGLVLR---EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 228 SWSGcfyFRIIQAALAAvGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDA 304
Cdd:cd07118 159 SGTT---LMLAELLIEA-GLPAGVVNIVTGYgATVGQAMTEHpdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 305 FIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQ 384
Cdd:cd07118 235 QIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 385 SLVNDALDKGAEIAVRGsfGHLGEdAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCA 464
Cdd:cd07118 315 DYVDAGRAEGATLLLGG--ERLAS-AAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563558 465 VFSGSKHRAKQIASQIQCGVAAINDFASNYmcQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
84-520 |
9.16e-75 |
|
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: 244.05 E-value: 9.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGE 163
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 164 RWLKPESRSSGRA--MLHKvSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAA 241
Cdd:cd07135 83 KWAKDEKVKDGPLafMFGK-PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 242 LaavgaPENLVDVITG-FAETGEALVSSVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVA 320
Cdd:cd07135 162 L-----DPDAFQVVQGgVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 321 VRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPlTGRYDMGAICLQEHSEHLQSLVNDAldKGaEIAVR 400
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTT--KG-KVVIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 401 GSFghlgeDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQI 480
Cdd:cd07135 313 GEM-----DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRT 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 42563558 481 QCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAGIEGLRA 520
Cdd:cd07135 388 RSGGVVINDTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDT 427
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
87-528 |
1.03e-74 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 245.10 E-value: 1.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 87 EVEERVTLSRKA--QKTWAQSSFKLRRqflRILLKY---IIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSE 161
Cdd:cd07142 42 DVDRAVKAARKAfdEGPWPRMTGYERS---RILLRFadlLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 162 GERWLKPESRSSGRAMLHKVSRvefhPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGIVIKVSEHASWSGCFYfrii 238
Cdd:cd07142 119 ADKIHGMTLPADGPHHVYTLHE----PIGVVGQIIPWNFPLLMFawkVGPALAC---GNTIVLKPAEQTPLSALLA---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 239 qAALAA-VGAPENLVDVITGFAETGEALVSS---VDKMIFVGSTAVGKMIMRNAAET-LTPVTLELGGKDAFIICEDADV 313
Cdd:cd07142 188 -AKLAAeAGLPDGVLNIVTGFGPTAGAAIAShmdVDKVAFTGSTEVGKIIMQLAAKSnLKPVTLELGGKSPFIVCEDADV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 314 SHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDK 393
Cdd:cd07142 267 DKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 394 GAEIAVRGsfGHLGEDAVdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRA 473
Cdd:cd07142 347 GATLITGG--DRIGSKGY--YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTA 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 474 KQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:cd07142 423 NTLSRALKAGTVWVNCY--DVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
96-539 |
1.20e-74 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 245.32 E-value: 1.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 96 RKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSSGR 175
Cdd:PTZ00381 17 KESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 176 AMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLVDVI 255
Cdd:PTZ00381 97 VFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 256 TGFAE-TGEALVSSVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAG 334
Cdd:PTZ00381 172 EGGVEvTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 335 AERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRyDMGAICLQEHSEHLQSLVNDaldKGAEIAVRGSFghlgeDAVDQY 414
Cdd:PTZ00381 252 PDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSE-DYSRIVNEFHTKRLAELIKD---HGGKVVYGGEV-----DIENKY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 415 FPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNY 494
Cdd:PTZ00381 323 VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 495 MCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVED----------RFWPLIKTK 539
Cdd:PTZ00381 403 LNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKstgnsfdlslRYPPYTSFK 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
69-518 |
3.30e-74 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 243.02 E-value: 3.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQK--TWAQSSfKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlG 146
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEAR-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 147 EIMTTCEKItwllsegeRWLKPESRS-SGRAML---HKVSRVEFHPLGVIGAIVPWNYP---FHNIFNPMLAAvfsGNGI 219
Cdd:cd07120 80 EISGAISEL--------RYYAGLARTeAGRMIEpepGSFSLVLREPMGVAGIIVPWNSPvvlLVRSLAPALAA---GCTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 220 VIKVsehASWSGCFYFRIIQAALAAVGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVT 296
Cdd:cd07120 149 VVKP---AGQTAQINAAIIRILAEIPSLPAGVVNLFTESgSEGAAHLVASpdVDVISFTGSTATGRAIMAAAAPTLKRLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 297 LELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICL 376
Cdd:cd07120 226 LELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLID 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 377 QEHSEHLQSLVNDALDKGAEIAVRGsfGHLGED-AVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLAN 455
Cdd:cd07120 306 RANVDRVDRMVERAIAAGAEVVLRG--GPVTEGlAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALAN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563558 456 DSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYmcQSLPFGGVKDSGFGRFAGIEGL 518
Cdd:cd07120 384 DTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLF--AEAEEGGYRQSGLGRLHGVAAL 444
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
64-520 |
7.70e-73 |
|
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: 240.16 E-value: 7.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 64 KKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDA 143
Cdd:cd07086 13 ETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 144 sLGEI---MTTCEkitWLLSEGeRWLK----PESRSSGRAMlhkvsrvEF-HPLGVIGAIVPWNYPFhNIF--NPMLAAV 213
Cdd:cd07086 93 -LGEVqemIDICD---YAVGLS-RMLYgltiPSERPGHRLM-------EQwNPLGVVGVITAFNFPV-AVPgwNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 214 fSGNGIVIKVSEHASWSGCFYFRIIQAALAAVGAPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAET 291
Cdd:cd07086 160 -CGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDprVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LTPVTLELGGKDAFIICEDADVShvaqVAVRGTLQSS----GQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTG 367
Cdd:cd07086 239 FGRVLLELGGNNAIIVMDDADLD----LAVRAVLFAAvgtaGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 368 RYDMGAIclqeHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQ--YFPPTVLINVNHNMKIMKEEAFGPIMPIMQFS 445
Cdd:cd07086 315 GTLVGPL----INQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPgnYVEPTIVTGVTDDARIVQEETFAPILYVIKFD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563558 446 TDEEVIKLANDSRYALGCAVFSGSKHRAKQI--ASQIQCGVAAINDFASNYMCQsLPFGGVKDSGFGRFAGIEGLRA 520
Cdd:cd07086 391 SLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESGSDAWKQ 466
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
69-527 |
4.39e-72 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 237.89 E-value: 4.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 69 YEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEI 148
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 149 MTTCEKITWLlSEGERWLkpESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFhnifnpMLA------AVFSGNGIVIK 222
Cdd:PRK13473 102 PAIVDVFRFF-AGAARCL--EGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPL------MMAawklapALAAGNTVVLK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 223 VSEHASWSgCFYFriiqAALAAVGAPENLVDVITGF-AETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTLEL 299
Cdd:PRK13473 173 PSEITPLT-ALKL----AELAADILPPGVLNVVTGRgATVGDALVGhpKVRMVSLTGSIATGKHVLSAAADSVKRTHLEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 300 GGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEH 379
Cdd:PRK13473 248 GGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 380 SEHLQSLVNDALDKG-AEIAVRGSfghlgedAVDQ---YFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLAN 455
Cdd:PRK13473 328 RDRVAGFVERAKALGhIRVVTGGE-------APDGkgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563558 456 DSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDfasNYMCQS-LPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:PRK13473 401 DSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMLVSeMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
71-519 |
6.59e-71 |
|
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: 234.25 E-value: 6.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEIMT 150
Cdd:cd07094 6 PYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITWLLSEGERwLKPESRSSGRAMLHKVSRVEF--HPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHAS 228
Cdd:cd07094 85 AIDTLRLAAEEAER-IRGEEIPLDATQGSDNRLAWTirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 229 WSGCFYFRIIQAAlaavGAPENLVDVITG-FAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAetLTPVTLELGGKDAF 305
Cdd:cd07094 164 LSALELAKILVEA----GVPEGVLQVVTGeREVLGDAFAADerVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 306 IICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQS 385
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 386 LVNDALDKGAEIAVRGSFghlgEDAVdqyFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAV 465
Cdd:cd07094 318 WVEEAVEAGARLLCGGER----DGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 42563558 466 FSGSKHRAKQIASQIQCGVAAINDfASNYMCQSLPFGGVKDSGFGRfagiEGLR 519
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVND-SSAFRTDWMPFGGVKESGVGR----EGVP 439
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
52-527 |
2.05e-70 |
|
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: 233.87 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 52 YIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQflRILLKY---IIEHQELI 128
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERG--RILLRLadlIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 129 CEVSSRDTGKTMvdaSLGEIMTTCEKITWLLS--------EGERwLKPESRSSGRAMLHKVSRVEfhPLGVIGAIVPWNY 200
Cdd:cd07113 81 AQLETLCSGKSI---HLSRAFEVGQSANFLRYfagwatkiNGET-LAPSIPSMQGERYTAFTRRE--PVGVVAGIVPWNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 201 PFHNIFNPMLAAVFSGNGIVIKVSEHASWSgcfYFRIIQAALAAvGAPENLVDVITGFAETGEALVSS--VDKMIFVGST 278
Cdd:cd07113 155 SVMIAVWKIGAALATGCTIVIKPSEFTPLT---LLRVAELAKEA-GIPDGVLNVVNGKGAVGAQLISHpdVAKVSFTGSV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 279 AVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKS 358
Cdd:cd07113 231 ATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 359 VSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIaVRGSFGHLGEdavDQYFPPTVLINVNHNMKIMKEEAFGPI 438
Cdd:cd07113 311 FQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEI-VRGGEALAGE---GYFVQPTLVLARSADSRLMREETFGPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 439 MPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINdfASNYMCQSLPFGGVKDSGFGRFAGIEGL 518
Cdd:cd07113 387 VSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN--MHTFLDPAVPFGGMKQSGIGREFGSAFI 464
|
....*....
gi 42563558 519 RACCLVKSV 527
Cdd:cd07113 465 DDYTELKSV 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
114-518 |
1.01e-69 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 230.01 E-value: 1.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 114 LRILLKYIIEHQELICEVSSRDTGKTMVDASLgEIMTTCEKITWLLS-----EGErwLKPESRSSGRAMLHKvsrvefHP 188
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEwarryEGE--IIQSDRPGENILLFK------RA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 189 LGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASwSGCFYFRIIqaaLAAVGAPENLVDVITGFAET-GEALVS 267
Cdd:PRK10090 72 LGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTP-NNAIAFAKI---VDEIGLPKGVFNLVLGRGETvGQELAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 268 S--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVshvaQVAVRGTLQS----SGQNCAGAERFYVH 341
Cdd:PRK10090 148 NpkVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADL----DLAVKAIVDSrvinSGQVCNCAERVYVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 342 KDIYTAFIGQVTKIVKSVSAGPPLTGR-YDMGAICLQEHSEHLQSLVNDALDKGAEIAvrgsfghLGEDAVDQ---YFPP 417
Cdd:PRK10090 224 KGIYDQFVNRLGEAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVA-------LGGKAVEGkgyYYPP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 418 TVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINdfASNYMCQ 497
Cdd:PRK10090 297 TLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN--RENFEAM 374
|
410 420
....*....|....*....|.
gi 42563558 498 SLPFGGVKDSGFGRFAGIEGL 518
Cdd:PRK10090 375 QGFHAGWRKSGIGGADGKHGL 395
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
71-527 |
3.33e-69 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 230.92 E-value: 3.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRqflRILLK---YIIEHQELICEVSSRDTGKTMVDASLGE 147
Cdd:PRK13252 29 PATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERS---RILRRavdILRERNDELAALETLDTGKPIQETSVVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 148 IMTTCEKITWLLS-----EGERW-LKPESRSSGRamlhkvsRVefhPLGVIGAIVPWNYPFHnIF----NPMLAAvfsGN 217
Cdd:PRK13252 106 IVTGADVLEYYAGlapalEGEQIpLRGGSFVYTR-------RE---PLGVCAGIGAWNYPIQ-IAcwksAPALAA---GN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 218 GIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPV 295
Cdd:PRK13252 172 AMIFKPSEVTPLTALKLAEIYTEA----GLPDGVFNVVQGDGRVGAWLTEHpdIAKVSFTGGVPTGKKVMAAAAASLKEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 296 TLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAIC 375
Cdd:PRK13252 248 TMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 376 LQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLAN 455
Cdd:PRK13252 328 SFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARAN 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563558 456 DSRYALGCAVFSGSKHRAKQIASQIQCGVAAINdfASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:PRK13252 408 DTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
64-518 |
6.49e-69 |
|
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: 229.97 E-value: 6.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 64 KKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDA 143
Cdd:cd07111 37 KSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRES 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 144 SLGEIMTTCEKITWllsegerwlkpesrSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGIV 220
Cdd:cd07111 117 RDCDIPLVARHFYH--------------HAGWAQLLDTELAGWKPVGVVGQIVPWNFPLLMLawkICPALAM---GNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 221 IKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVS--SVDKMIFVGSTAVGKMIMRNAAETLTPVTLE 298
Cdd:cd07111 180 LKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNGSFGSALANhpGVDKVAFTGSTEVGRALRRATAGTGKKLSLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 299 LGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQE 378
Cdd:cd07111 256 LGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 379 HSEHLQSLVNDALDKGAEI----AVRGSFGHlgedavdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLA 454
Cdd:cd07111 336 QLKRIRELVEEGRAEGADVfqpgADLPSKGP--------FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563558 455 NDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINdfASNYMCQSLPFGGVKDSGFGRFAGIEGL 518
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWIN--GHNLFDAAAGFGGYRESGFGREGGKEGL 469
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
188-528 |
9.08e-69 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 230.09 E-value: 9.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVS 267
Cdd:PLN02766 158 PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLA----GVPDGVINVVTGFGPTAGAAIA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 268 S---VDKMIFVGSTAVGKMIMRNAAET-LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKD 343
Cdd:PLN02766 234 ShmdVDKVSFTGSTEVGRKIMQAAATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 344 IYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRG-SFGHLGedavdQYFPPTVLIN 422
Cdd:PLN02766 314 IYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGkPCGDKG-----YYIEPTIFTD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 423 VNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIN-DFASNYMCqslPF 501
Cdd:PLN02766 389 VTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNcYFAFDPDC---PF 465
|
330 340
....*....|....*....|....*..
gi 42563558 502 GGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:PLN02766 466 GGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
106-526 |
3.69e-67 |
|
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: 224.02 E-value: 3.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 106 SFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESrsSGRAMLHKVSRVE 185
Cdd:cd07132 18 PLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEP--VKKNLATLLDDVY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 186 FH--PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLVDVITGFA-ETG 262
Cdd:cd07132 96 IYkePLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYL-----DKECYPVVLGGVeETT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 263 EALVSSVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAErfYV-- 340
Cdd:cd07132 171 ELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD--YVlc 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 341 HKDIYTAFIGQVTKIVKSVSAGPPLTGRyDMGAICLQEHSEHLQSLVndaldKGAEIAVRGSFghlgeDAVDQYFPPTVL 420
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL-----SGGKVAIGGQT-----DEKERYIAPTVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 421 INVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLP 500
Cdd:cd07132 318 TDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLP 397
|
410 420 430
....*....|....*....|....*....|.
gi 42563558 501 FGGVKDSGFGRFAGIEGL-----RACCLVKS 526
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFdtfshKRSCLVKS 428
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
52-511 |
1.33e-64 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 218.62 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 52 YIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEV 131
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 132 SSRDTGKTMVDASlGEIMTTCEKITWLLSEGERWLK---PESRSSGRAMLHKvsrvefHPLGVIGAIVPWNYPFHNIFNP 208
Cdd:PRK11241 94 MTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGdtiPGHQADKRLIVIK------QPIGVTAAITPWNFPAAMITRK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 209 MLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFA-ETGEALVSS--VDKMIFVGSTAVGKMIM 285
Cdd:PRK11241 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRA----GIPAGVFNVVTGSAgAVGGELTSNplVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 286 RNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPL 365
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 366 TGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGedavDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFS 445
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563558 446 TDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIND-FASNymcQSLPFGGVKDSGFGR 511
Cdd:PRK11241 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTgIISN---EVAPFGGIKASGLGR 462
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
77-510 |
3.05e-64 |
|
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: 217.12 E-value: 3.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 77 LGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEIMTTCEKIT 156
Cdd:cd07097 28 VGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA-RGEVTRAGQIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 157 WLLSEGERwLKPESRSSGRA-MLHKVSRVefhPLGVIGAIVPWNYPFhNI----FNPMLAAvfsGNGIVIKVSEHASWSG 231
Cdd:cd07097 107 YYAGEALR-LSGETLPSTRPgVEVETTRE---PLGVVGLITPWNFPI-AIpawkIAPALAY---GNTVVFKPAELTPASA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 232 cfyFRIIQAaLAAVGAPENLVDVITGF-AETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIIC 308
Cdd:cd07097 179 ---WALVEI-LEEAGLPAGVFNLVMGSgSEVGQALVEHpdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 309 EDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVN 388
Cdd:cd07097 255 DDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 389 DALDKGAEIAV------RGSFGHlgedavdqYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALG 462
Cdd:cd07097 335 IARSEGAKLVYggerlkRPDEGY--------YLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLS 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 42563558 463 CAVFSGSKHRAKQIASQIQCGVAAINdFASNYMCQSLPFGGVKDSGFG 510
Cdd:cd07097 407 AGIVTTSLKHATHFKRRVEAGVVMVN-LPTAGVDYHVPFGGRKGSSYG 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
26-528 |
8.85e-64 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 217.75 E-value: 8.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 26 PNVPSIDVDASDVLAHGKdteensFIyipprgrSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKA--QKTWA 103
Cdd:PLN02466 48 PITPPVQVSYTQLLINGQ------FV-------DAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 104 QSSFKLRRqflRILLKY---IIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSSGramLHK 180
Cdd:PLN02466 115 KMTAYERS---RILLRFadlLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADG---PHH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 181 VsRVEFHPLGVIGAIVPWNYP---FHNIFNPMLAAvfsGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITG 257
Cdd:PLN02466 189 V-QTLHEPIGVAGQIIPWNFPllmFAWKVGPALAC---GNTIVLKTAEQTPLSALYAAKLLHEA----GLPPGVLNVVSG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 258 FAETGEALVSS---VDKMIFVGSTAVGKMIMRNAAET-LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCA 333
Cdd:PLN02466 261 FGPTAGAALAShmdVDKLAFTGSTDTGKIVLELAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 334 GAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGS-FGHLGedavd 412
Cdd:PLN02466 341 AGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDrFGSKG----- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 413 QYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFas 492
Cdd:PLN02466 416 YYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCF-- 493
|
490 500 510
....*....|....*....|....*....|....*.
gi 42563558 493 NYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVV 528
Cdd:PLN02466 494 DVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
71-527 |
1.62e-63 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 214.99 E-value: 1.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlGEIMT 150
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK-AEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITWLLSEGERWLKPE---SRSSG--RAMlhkvsrVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKvse 225
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEpadAAAVGasRAY------VRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 226 HASwsgcfyfRIIQAALAavgapenLVDVIT--GFAET--GEALVSS--VDKMI---------FVGSTAVGKMIMRNAAE 290
Cdd:PRK09406 158 HAS-------NVPQTALY-------LADLFRraGFPDGcfQTLLVGSgaVEAILrdprvaaatLTGSEPAGRAVAAIAGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 291 TLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYD 370
Cdd:PRK09406 224 EIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 371 MGAICLQEHSEHLQSLVNDALDKGAEIAVRGSfghlGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEV 450
Cdd:PRK09406 304 VGPLATEQGRDEVEKQVDDAVAAGATILCGGK----RPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563558 451 IKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYmcQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:PRK09406 380 IEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSY--PELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
71-531 |
2.18e-63 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 214.73 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlGEIMT 150
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 151 TCEKITWLLSEGERWLKPESRssgrAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKvseHA-SW 229
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK---HApNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 230 SGCFyfRIIQAALAAVGAPENLVDVITGFAETGEALVSsvDKMI----FVGSTAVGKMIMRNAAETLTPVTLELGGKDAF 305
Cdd:PRK13968 166 MGCA--QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN--DSRIaavtVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 306 IICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQS 385
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 386 LVNDALDKGAEIAvrgsfghLGEDAVD---QYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALG 462
Cdd:PRK13968 322 QVEATLAEGARLL-------LGGEKIAgagNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLS 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 463 CAVFSGSKHRAKQIASQIQCGVAAINDF-ASNymcQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVEDR 531
Cdd:PRK13968 395 ATIFTTDETQARQMAARLECGGVFINGYcASD---ARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDR 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
84-519 |
4.67e-61 |
|
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: 208.25 E-value: 4.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASlGEIMTTCEKITWLLSEGE 163
Cdd:cd07147 19 GPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEVARAIDTFRIAAEEAT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 164 RW------LKPESRSSGR-AMLHKVsrvefhPLGVIGAIVPWNYPF----HNIfNPMLAAvfsGNGIVIKVSEHASWSGC 232
Cdd:cd07147 98 RIygevlpLDISARGEGRqGLVRRF------PIGPVSAITPFNFPLnlvaHKV-APAIAA---GCPFVLKPASRTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 233 fyfrIIQAALAAVGAPENLVDVITGFAETGEALVSsvDKMI----FVGSTAVGKMIMRNAAETltPVTLELGGKDAFIIC 308
Cdd:cd07147 168 ----ILGEVLAETGLPKGAFSVLPCSRDDADLLVT--DERIkllsFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 309 EDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVN 388
Cdd:cd07147 240 SDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 389 DALDKGAEIAVRGSF-GHLgedavdqyFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFS 467
Cdd:cd07147 320 EAVDAGAKLLTGGKRdGAL--------LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 42563558 468 GSKHRAKQIASQIQCGVAAINDFASnYMCQSLPFGGVKDSGFGRfagiEGLR 519
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVINDVPT-FRVDHMPYGGVKDSGIGR----EGVR 438
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
88-514 |
5.90e-59 |
|
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: 202.26 E-value: 5.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 88 VEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLK 167
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 168 PESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALAAvga 247
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 248 peNLVDVITGFAETGEALVSSV-DKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQ 326
Cdd:cd07137 158 --KAIKVIEGGVPETTALLEQKwDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 327 S-SGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRyDMGAICLQEHSEHLQSLVNDAldkgaeiAVRGSFGH 405
Cdd:cd07137 236 CnNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDP-------SVADKIVH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 406 LGE-DAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGV 484
Cdd:cd07137 308 GGErDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGG 387
|
410 420 430
....*....|....*....|....*....|
gi 42563558 485 AAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07137 388 VTFNDTVVQYAIDTLPFGGVGESGFGAYHG 417
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
185-511 |
3.49e-58 |
|
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: 201.14 E-value: 3.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 185 EFH-PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALaavgaPENLVDVITGF-AETG 262
Cdd:cd07116 132 HFHePLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLL-----PPGVVNVVNGFgLEAG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 263 EALVSS--VDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQV--AVRGTLQ---SSGQNCAGA 335
Cdd:cd07116 207 KPLASSkrIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDADDAFFdkALEGFVMfalNQGEVCTCP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 336 ERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYF 415
Cdd:cd07116 287 SRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 416 PPTVlINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASnYM 495
Cdd:cd07116 367 VPTT-FKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHL-YP 444
|
330
....*....|....*.
gi 42563558 496 CQSlPFGGVKDSGFGR 511
Cdd:cd07116 445 AHA-AFGGYKQSGIGR 459
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
57-514 |
1.60e-57 |
|
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: 200.14 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 57 GRSQQSDKKVQCYEPA-TMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRrqfLRILLKY--IIEHQEL-ICEVS 132
Cdd:cd07124 39 GKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEER---ARLLLRAaaLLRRRRFeLAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 133 SRDTGKTMVDAsLGEImttCEKITWLLSEGERWLK-PESRSSGRAMLHKVSRVEfhPLGVIGAIVPWNYPFhNIFNPM-L 210
Cdd:cd07124 116 VLEVGKNWAEA-DADV---AEAIDFLEYYAREMLRlRGFPVEMVPGEDNRYVYR--PLGVGAVISPWNFPL-AILAGMtT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 211 AAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVSSVD-KMI-FVGSTAVGKMIMRN 287
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEA----GLPPGVVNFLPGPGEEvGDYLVEHPDvRFIaFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 288 AAET------LTPVTLELGGKDAFIICEDADVshvaQVAVRGTLQS----SGQNCAGAERFYVHKDIYTAFIGQVTKIVK 357
Cdd:cd07124 265 AAKVqpgqkwLKRVIAEMGGKNAIIVDEDADL----DEAAEGIVRSafgfQGQKCSACSRVIVHESVYDEFLERLVERTK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 358 SVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDAldKGAEIAVRGsfGHLGEDAVDQYF-PPTVLINVNHNMKIMKEEAFG 436
Cdd:cd07124 341 ALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIG--KSEGRLLLG--GEVLELAAEGYFvQPTIFADVPPDHRLAQEEIFG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563558 437 PIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07124 417 PVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAG 494
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
70-511 |
2.35e-57 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 199.35 E-value: 2.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 70 EPATMKYLGYFPALSPTEVEERVTLSRKA--QKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGE 147
Cdd:PRK09847 41 DPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 148 IMTTCEKITWLlSEGERWLKPESRSSGRAMLHKVSRvefHPLGVIGAIVPWNYPFHNI---FNPMLAAvfsGNGIVIKVS 224
Cdd:PRK09847 121 IPGAARAIRWY-AEAIDKVYGEVATTSSHELAMIVR---EPVGVIAAIVPWNFPLLLTcwkLGPALAA---GNSVILKPS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 225 EHASWSGCFYFRIIQAAlaavGAPENLVDVITGFA-ETGEALV--SSVDKMIFVGSTAVGKMIMRNAAET-LTPVTLELG 300
Cdd:PRK09847 194 EKSPLSAIRLAGLAKEA----GLPDGVLNVVTGFGhEAGQALSrhNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 301 GKDAFIICEDA-DVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEH 379
Cdd:PRK09847 270 GKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAH 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 380 SEHLQSLVNDALDKGaEIAVRGSfghlgEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRY 459
Cdd:PRK09847 350 ADSVHSFIREGESKG-QLLLDGR-----NAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQY 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 42563558 460 ALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMcqSLPFGGVKDSGFGR 511
Cdd:PRK09847 424 GLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNGR 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-511 |
4.62e-55 |
|
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: 191.72 E-value: 4.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 87 EVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEIMTTCEKITW-LLSEGERw 165
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDIsIKAYHER- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 166 lKPESRssgRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaav 245
Cdd:cd07095 79 -TGERA---TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 246 GAPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRNAAETltP---VTLELGGKDAFIICEDADVSHVAQVA 320
Cdd:cd07095 151 GLPPGVLNLVQGGRETGEALAAHegIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 321 VRGTLQSSGQNCAGAERFYVHKDIYT-AFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAV 399
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 400 RGSFGhlgeDAVDQYFPPTvLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQ 479
Cdd:cd07095 309 AMERL----VAGTAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLAR 383
|
410 420 430
....*....|....*....|....*....|....*
gi 42563558 480 IQCGVAAIN---DFASNymcqSLPFGGVKDSGFGR 511
Cdd:cd07095 384 IRAGIVNWNrptTGASS----TAPFGGVGLSGNHR 414
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
61-519 |
7.13e-55 |
|
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: 192.35 E-value: 7.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 61 QSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFkLRRQflRILLKY---IIEHQELICEVSSRDTG 137
Cdd:cd07085 13 KTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPV-LKRQ--QVMFKFrqlLEENLDELARLITLEHG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 138 KTMVDAsLGEIMTTCE------KITWLLSeGErwlkpESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFH--NIFNPM 209
Cdd:cd07085 90 KTLADA-RGDVLRGLEvvefacSIPHLLK-GE-----YLENVARGIDTYSYRQ---PLGVVAGITPFNFPAMipLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 210 laAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVSSVD-KMI-FVGSTAVGKMIMRN 287
Cdd:cd07085 160 --AIACGNTFVLKPSERVPGAAMRLAELLQEA----GLPDGVLNVVHGGKEAVNALLDHPDiKAVsFVGSTPVGEYIYER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 288 AAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTG 367
Cdd:cd07085 234 AAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 368 RYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSfghlgEDAVDQY-----FPPTVLINVNHNMKIMKEEAFGPIMPIM 442
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGR-----GVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 443 QFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIN--------DFasnymcqslPFGGVKDSGFG--RF 512
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvplaFF---------SFGGWKGSFFGdlHF 459
|
....*..
gi 42563558 513 AGIEGLR 519
Cdd:cd07085 460 YGKDGVR 466
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
71-527 |
3.58e-54 |
|
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: 190.78 E-value: 3.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 71 PATMKYLGYFPALSPTEVEERVTLSRKA--QKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTG-------KTMV 141
Cdd:cd07140 28 PTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGavytlalKTHV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DASlgeIMTT------CEKItwllsEGERWLKPESRSSgramlHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFS 215
Cdd:cd07140 108 GMS---IQTFryfagwCDKI-----QGKTIPINQARPN-----RNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 216 GNGIVIKVSEHASWSGCFYfriiqAALAA-VGAPENLVDVITGFAE-TGEALVSSVD--KMIFVGSTAVGKMIMRNAAET 291
Cdd:cd07140 175 GNTVVLKPAQVTPLTALKF-----AELTVkAGFPKGVINILPGSGSlVGQRLSDHPDvrKLGFTGSTPIGKHIMKSCAVS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 -LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYD 370
Cdd:cd07140 250 nLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 371 MGAiclQEHSEHLQSLV---NDALDKGAEIAVRGSfghlgedAVDQ---YFPPTVLINVNHNMKIMKEEAFGPIMPIMQF 444
Cdd:cd07140 330 HGP---QNHKAHLDKLVeycERGVKEGATLVYGGK-------QVDRpgfFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 445 STD--EEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFasNYMCQSLPFGGVKDSGFGRFAGIEGLRACC 522
Cdd:cd07140 400 DDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTY--NKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
....*
gi 42563558 523 LVKSV 527
Cdd:cd07140 478 KTKTV 482
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
88-514 |
5.92e-54 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 189.94 E-value: 5.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 88 VEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLK 167
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 168 PESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALAAvga 247
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 248 peNLVDVITGFAETGEALVSSV-DKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIIcEDADVSHVAQVAVRGTLQ 326
Cdd:PLN02203 165 --KAVKVIEGGPAVGEQLLQHKwDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-DSLSSSRDTKVAVNRIVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 327 S-----SGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYdMGAICLQEHSEHLQSLVNDALdkgaeiaVRG 401
Cdd:PLN02203 242 GkwgscAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPR-------VAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 402 SFGHLGE-DAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQI 480
Cdd:PLN02203 314 SIVHGGSiDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSET 393
|
410 420 430
....*....|....*....|....*....|....
gi 42563558 481 QCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:PLN02203 394 SSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHG 427
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
58-528 |
5.19e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 176.87 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 58 RSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTG 137
Cdd:PLN00412 25 RTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 138 KTMVDA------SLGEIMTTCEKITWLLSEGERWLKPESRSSGRAMLHKVSRVefhPLGVIGAIVPWNYPFHNIFNPMLA 211
Cdd:PLN00412 105 KPAKDAvtevvrSGDLISYTAEEGVRILGEGKFLVSDSFPGNERNKYCLTSKI---PLGVVLAIPPFNYPVNLAVSKIAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 212 AVFSGNGIVIKVSEHASWSGcfyFRIIQAALAAvGAPENLVDVITGF-AETGEALVS--SVDKMIFVGSTAvGKMIMRNA 288
Cdd:PLN00412 182 ALIAGNAVVLKPPTQGAVAA---LHMVHCFHLA-GFPKGLISCVTGKgSEIGDFLTMhpGVNCISFTGGDT-GIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 289 AetLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPlTGR 368
Cdd:PLN00412 257 G--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 369 YDMGAICLQEHSEHLQSLVNDALDKGAEIavrgsfgHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDE 448
Cdd:PLN00412 334 CDITPVVSESSANFIEGLVMDAKEKGATF-------CQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 449 EVIKLANDSRYAL-GCaVFSGSKHRAKQIASQIQCGVAAINDfASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSV 527
Cdd:PLN00412 407 EGIHHCNASNFGLqGC-VFTRDINKAILISDAMETGTVQINS-APARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKST 484
|
.
gi 42563558 528 V 528
Cdd:PLN00412 485 V 485
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
57-508 |
2.80e-46 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 169.73 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 57 GRSQQSDKKVQCYEPA-TMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRqflRILLK---YIIEHQELICEVS 132
Cdd:PRK03137 43 GERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRA---RILLRaaaIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 133 SRDTGKTMVDASlGEimtTCEKITWL---------LSEGerwlKPESRSSGramlhKVSRVEFHPLGVIGAIVPWNYPFh 203
Cdd:PRK03137 120 VKEAGKPWAEAD-AD---TAEAIDFLeyyarqmlkLADG----KPVESRPG-----EHNRYFYIPLGVGVVISPWNFPF- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 204 NIFNPM-LAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGF-AETGEALVSSVD-KMI-FVGSTA 279
Cdd:PRK03137 186 AIMAGMtLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEA----GLPAGVVNFVPGSgSEVGDYLVDHPKtRFItFTGSRE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 280 VGKMIMRNAAET------LTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVT 353
Cdd:PRK03137 262 VGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 354 KIVKSVSAGPPlTGRYDMGAICLQEHSEHLQSLVndalDKGAEIAvRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEE 433
Cdd:PRK03137 342 ELTKELTVGNP-EDNAYMGPVINQASFDKIMSYI----EIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563558 434 AFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSG 508
Cdd:PRK03137 416 IFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
57-514 |
6.87e-45 |
|
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: 165.07 E-value: 6.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 57 GRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDT 136
Cdd:cd07130 5 GEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 137 GKTMVDAsLGEI---MTTCEKITWLlsegerwlkpeSRS----------SGRAMLHKvsrveFHPLGVIGAIVPWNYPFh 203
Cdd:cd07130 85 GKILPEG-LGEVqemIDICDFAVGL-----------SRQlygltipserPGHRMMEQ-----WNPLGVVGVITAFNFPV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 204 NIF--NPMLAAVfSGNGIVIKVSEHASWSGCFYFRIIQAALAAVGAPENLVDVITGFAETGEALVSS--VDKMIFVGSTA 279
Cdd:cd07130 147 AVWgwNAAIALV-CGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDprVPLVSFTGSTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 280 VGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSV 359
Cdd:cd07130 226 VGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 360 SAGPPLtgryDMGAICLQEHSEHLQSLVNDALDK----GAEIavrgsfgHLGEDAVDQ---YFPPTVlINVNHNMKIMKE 432
Cdd:cd07130 306 RIGDPL----DDGTLVGPLHTKAAVDNYLAAIEEaksqGGTV-------LFGGKVIDGpgnYVEPTI-VEGLSDAPIVKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 433 EAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQI--QCGVAAINdfasnymcqsLP---------F 501
Cdd:cd07130 374 ETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVN----------IGtsgaeiggaF 443
|
490
....*....|...
gi 42563558 502 GGVKDSGFGRFAG 514
Cdd:cd07130 444 GGEKETGGGRESG 456
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
135-514 |
8.67e-43 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 159.44 E-value: 8.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 135 DTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVF 214
Cdd:PLN02174 59 DLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 215 SGNGIVIKVSEHASWSGCFYFRIIQAALAAvgapeNLVDVITG-FAETGEALVSSVDKMIFVGSTAVGKMIMRNAAETLT 293
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQYLDS-----SAVRVVEGaVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 294 PVTLELGGKDAFIICEDADVSHVAQVAVRGTLQ-SSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRyDMG 372
Cdd:PLN02174 214 PVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 373 AICLQEHSEHLQSLVNDAldkgaEIAVRGSFGhlGE-DAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVI 451
Cdd:PLN02174 293 RIVNSTHFDRLSKLLDEK-----EVSDKIVYG--GEkDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESF 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563558 452 KLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:PLN02174 366 DVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHG 428
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
62-514 |
4.83e-42 |
|
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: 157.74 E-value: 4.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 62 SDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMV 141
Cdd:cd07083 31 KERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 142 DAS--LGEIMTTCE--KITWLLSEGERWLKPESRSSGRAMLHKvsrvefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGN 217
Cdd:cd07083 111 EAIddVAEAIDFIRyyARAALRLRYPAVEVVPYPGEDNESFYV-------GLGAGVVISPWNFPVAIFTGMIVAPVAVGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 218 GIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAVGKMIMRNAAE---- 290
Cdd:cd07083 184 TVIAKPAEDAVVVGYKVFEIFHEA----GFPPGVVQFLPGVGEEvGAYLTEHerIRGINFTGSLETGKKIYEAAARlapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 291 --TLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGR 368
Cdd:cd07083 260 qtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 369 YDMGAICLQEHSEHLQSLVNDALDKGAEIAvrgsfGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDE 448
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEGQLVL-----GGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDD 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563558 449 --EVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07083 415 faEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
84-514 |
1.29e-40 |
|
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: 153.89 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRRqflRILLKY--IIEHQ--ELICeVSSRDTGKTMVDAsLGEIMttcEKITWLL 159
Cdd:cd07125 67 DAEDVDAALAIAAAAFAGWSATPVEERA---EILEKAadLLEANrgELIA-LAAAEAGKTLADA-DAEVR---EAIDFCR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 160 SEGERWLKPESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFhNIF-NPMLAAVFSGNGIVIKVSEHASWSGCfyfRII 238
Cdd:cd07125 139 YYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPL-AIFtGQIAAALAAGNTVIAKPAEQTPLIAA---RAV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 239 QAALAAvGAPENLVDVITGF-AETGEALVS--SVDKMIFVGSTAVGKMIMRNAAE---TLTPVTLELGGKDAFIICEDAD 312
Cdd:cd07125 215 ELLHEA-GVPRDVLQLVPGDgEEIGEALVAhpRIDGVIFTGSTETAKLINRALAErdgPILPLIAETGGKNAMIVDSTAL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 313 VSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNdaLD 392
Cdd:cd07125 294 PEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE--LM 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 393 KGAEiavrgsfGHLGEDAVDQ----YFPPTVLINVNHNmkIMKEEAFGPIMPIMQFSTD--EEVIKLANDSRYALGCAVF 466
Cdd:cd07125 372 RGEA-------WLIAPAPLDDgngyFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIH 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 42563558 467 SGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07125 443 SRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAG 490
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
84-508 |
3.05e-38 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 146.64 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRrqfLRILLKY---IIEHQELICEVSSRDTGK------TMVDASLGEIMTTcek 154
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEER---QAIVERFaalLEENKEELAEVIARETGKplweaaTEVTAMINKIAIS--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 155 itwLLSEGERwlKPESRSS---GRAML-HKvsrvefhPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWS 230
Cdd:PRK09457 109 ---IQAYHER--TGEKRSEmadGAAVLrHR-------PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 231 GCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVSS--VDKMIFVGSTAVGKMIMRN-AAETLTPVTLELGGKDAFII 307
Cdd:PRK09457 177 AELTVKLWQQA----GLPAGVLNLVQGGRETGKALAAHpdIDGLLFTGSANTGYLLHRQfAGQPEKILALEMGGNNPLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 308 CEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYT-AFIGQVTKIVKSVSAGPPltgryD------MGAICLQEHS 380
Cdd:PRK09457 253 DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGRW-----DaepqpfMGAVISEQAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 381 EHLQSLVNDALDKGAEIAVRGSfgHLGEDAVdqyFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYA 460
Cdd:PRK09457 328 QGLVAAQAQLLALGGKSLLEMT--QLQAGTG---LLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 42563558 461 LGCAVFSGSKHRAKQIASQIQCGVA----AINDFASnymcqSLPFGGVKDSG 508
Cdd:PRK09457 403 LSAGLLSDDREDYDQFLLEIRAGIVnwnkPLTGASS-----AAPFGGVGASG 449
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
188-510 |
2.29e-31 |
|
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: 126.76 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAETGEALVS 267
Cdd:cd07148 124 PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEA----GLPEGWCQAVPCENAVAEKLVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 268 S--VDKMIFVGSTAVGKMIMRNAAETlTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIY 345
Cdd:cd07148 200 DprVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 346 TAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSfgHLGedavDQYFPPTVLINVNH 425
Cdd:cd07148 279 DDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGK--RLS----DTTYAPTVLLDPPR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 426 NMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIND---FASNYMcqslPFG 502
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDhtaFRVDWM----PFA 428
|
....*...
gi 42563558 503 GVKDSGFG 510
Cdd:cd07148 429 GRRQSGYG 436
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
77-508 |
1.58e-29 |
|
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: 122.31 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 77 LGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQ-FLRI--LL--KYiiehqelicevssRDT---------GKTMVD 142
Cdd:cd07123 60 LATYHYADAALVEKAIEAALEARKEWARMPFEDRAAiFLKAadLLsgKY-------------RYElnaatmlgqGKNVWQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 143 AslgEIMTTCEKITWL------LSEGERWlKPESRSSGramlhKVSRVEFHPL-GVIGAIVPWNypFHNI-FNPMLAAVF 214
Cdd:cd07123 127 A---EIDAACELIDFLrfnvkyAEELYAQ-QPLSSPAG-----VWNRLEYRPLeGFVYAVSPFN--FTAIgGNLAGAPAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 215 SGNGIVIKVSEHASWSGCFYFRIIQAAlaavGAPENLVDVITGFAET-GEALVSSVD--KMIFVGSTAVGKMIMRNAAET 291
Cdd:cd07123 196 MGNVVLWKPSDTAVLSNYLVYKILEEA----GLPPGVINFVPGDGPVvGDTVLASPHlaGLHFTGSTPTFKSLWKQIGEN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 292 LT-----P-VTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPL 365
Cdd:cd07123 272 LDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 366 TGRYDMGAICLQEHSEHLQSLVNDA-LDKGAEIAVRGSfghlGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQF 444
Cdd:cd07123 352 DFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGK----CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVY 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 445 STD--EEVIKLAND-SRYALGCAVFSGSKhRAKQIASQI---QCGVAAINDFASNYMCQSLPFGGVKDSG 508
Cdd:cd07123 428 PDSdfEETLELVDTtSPYALTGAIFAQDR-KAIREATDAlrnAAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
57-514 |
1.77e-29 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 121.86 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 57 GRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDT 136
Cdd:PLN02315 27 GEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 137 GKTMVDA--SLGEIMTTCEKITWLLSEGERWLKPESRSSgramlHKVSRVeFHPLGVIGAIVPWNYPFHNI-FNPMLAAV 213
Cdd:PLN02315 107 GKILAEGigEVQEIIDMCDFAVGLSRQLNGSIIPSERPN-----HMMMEV-WNPLGIVGVITAFNFPCAVLgWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 214 fSGNGIVIKVSEHASWSGCFYFRIIQAALAAVGAPENLVDVITGFAETGEALvsSVDKMI----FVGSTAVGKMIMRNAA 289
Cdd:PLN02315 181 -CGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAI--AKDTRIplvsFTGSSKVGLMVQQTVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 290 ETLTPVTLELGGKDAFIICEDADVshvaQVAVRGTL----QSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPL 365
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADI----QLAVRSVLfaavGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 366 tgryDMGAICLQEHSEHLQslvnDALDKGAE-IAVRGSFGHLGEDAVD---QYFPPTVlINVNHNMKIMKEEAFGPIMPI 441
Cdd:PLN02315 334 ----EKGTLLGPLHTPESK----KNFEKGIEiIKSQGGKILTGGSAIEsegNFVQPTI-VEISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563558 442 MQFSTDEEVIKLANDSRYALGCAVFSgskHRAKQIASQI-----QCGVAAINdFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFT---RNPETIFKWIgplgsDCGIVNVN-IPTNGAEIGGAFGGEKATGGGREAG 478
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
46-488 |
5.02e-28 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 118.31 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 46 EENSFIYIPPR-----GRS---QQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRqflRIL 117
Cdd:PLN02419 103 EQSTQPQMPPRvpnliGGSfveSQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQ---RVM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 118 LKYiiehQELICEVSSR-------DTGKTMVDaSLGEIMTTCEKItwllsegERWLKPESRSSGRAMLHKVSRVEFH--- 187
Cdd:PLN02419 180 LKF----QELIRKNMDKlamnittEQGKTLKD-SHGDIFRGLEVV-------EHACGMATLQMGEYLPNVSNGVDTYsir 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 -PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGcfyfrIIQAALA-AVGAPENLVDVITGFAETGEAL 265
Cdd:PLN02419 248 ePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGAS-----VILAELAmEAGLPDGVLNIVHGTNDTVNAI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 266 VSSVD--KMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERfyvhkd 343
Cdd:PLN02419 323 CDDEDirAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALST------ 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 344 iyTAFIGQVT----KIVKSVSAGPPLTGR---YDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFP 416
Cdd:PLN02419 397 --VVFVGDAKswedKLVERAKALKVTCGSepdADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIG 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563558 417 PTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIN 488
Cdd:PLN02419 475 PTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
77-514 |
4.26e-27 |
|
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: 114.62 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 77 LGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAslgeIMTTCEKIT 156
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA----IAEVREAVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 157 WLlsegerwlkpesRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFR 236
Cdd:TIGR01238 141 FC------------RYYAKQVRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 237 IIQAAlaavGAPENLVDVITGFAET-GEALVS--SVDKMIFVGSTAVGKMIMRNAAETL---TPVTLELGGKDAFIICED 310
Cdd:TIGR01238 209 LMQEA----GFPAGTIQLLPGRGADvGAALTSdpRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDST 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 311 ADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDA 390
Cdd:TIGR01238 285 ALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHM 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 391 LDKGAEI--AVRgsfghlgEDAVD----QYFPPTvLINVNhNMKIMKEEAFGPIMPIMQFSTDE--EVIKLANDSRYALG 462
Cdd:TIGR01238 365 SQTQKKIaqLTL-------DDSRAcqhgTFVAPT-LFELD-DIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLT 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 42563558 463 CAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:TIGR01238 436 MGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
84-514 |
7.68e-19 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 90.69 E-value: 7.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDAsLGEIMttcEKITWL---LS 160
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA-IAEVR---EAVDFLryyAA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 161 EGERWLKPESRSsgramlhkvsrvefhPLGVIGAIVPWNYPFhNIFNPMLAAVF-SGNGIVIKVSEHASwsgcfyfrIIq 239
Cdd:PRK11905 664 QARRLLNGPGHK---------------PLGPVVCISPWNFPL-AIFTGQIAAALvAGNTVLAKPAEQTP--------LI- 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 240 AALA-----AVGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAVGKMIMRNAAETLT-PVTL--ELGGKDAFIIc 308
Cdd:PRK11905 719 AARAvrllhEAGVPKDALQLLPGDGRTvGAALVADprIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIV- 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 309 edaDVSHVAQVAVRGTL----QSSGQNCAgAER-FYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHL 383
Cdd:PRK11905 798 ---DSSALPEQVVADVIasafDSAGQRCS-ALRvLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANI 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 384 QSLVNDALDKG--------AEIAVRGSFghlgedavdqyFPPTvLINVNhNMKIMKEEAFGPIMPIMQFSTDE--EVIKL 453
Cdd:PRK11905 874 EAHIEAMRAAGrlvhqlplPAETEKGTF-----------VAPT-LIEID-SISDLEREVFGPVLHVVRFKADEldRVIDD 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563558 454 ANDSRYALGCAVFSGSKHRAKQIASQIQCG--------VAAIndfasnymCQSLPFGGVKDSGFGRFAG 514
Cdd:PRK11905 941 INATGYGLTFGLHSRIDETIAHVTSRIRAGniyvnrniIGAV--------VGVQPFGGEGLSGTGPKAG 1001
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
186-488 |
4.20e-18 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 88.33 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 186 FHPLGVIGAIVPWNYPFhNIF-NPMLAAVFSGNGIVIKVSEHASWSGcfyFRIIQAALAAvGAPENLVDVITGF-AETGE 263
Cdd:PRK11904 682 LHGRGVFVCISPWNFPL-AIFlGQVAAALAAGNTVIAKPAEQTPLIA---AEAVKLLHEA-GIPKDVLQLLPGDgATVGA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 264 ALVSS--VDKMIFVGSTAVGKMIMRN-AAETLTPVTL--ELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERF 338
Cdd:PRK11904 757 ALTADprIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVL 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 339 YVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAIC-------LQEHSEHlqslvndaLDKGAEIAVRGSFGHLGEDAv 411
Cdd:PRK11904 837 FVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIdaeakanLDAHIER--------MKREARLLAQLPLPAGTENG- 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 412 dQYFPPTVL-INvnhNMKIMKEEAFGPIMPIMQFSTDE--EVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAIN 488
Cdd:PRK11904 908 -HFVAPTAFeID---SISQLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
182-520 |
2.38e-17 |
|
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: 84.60 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 182 SRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALAavgAPENLVDVITGFAET 261
Cdd:cd07084 94 SHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPEDVTLINGDGKT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 262 GEALVS--SVDKMIFVGSTAVGKMIMRNAAEtlTPVTLELGGKDAFIICEDAD-VSHVAQVAVRGTLQSSGQNCAGAERF 338
Cdd:cd07084 171 MQALLLhpNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSML 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 339 YVHKDIY-TAFIGQV-----TKIVKSVSAGPPLTGRYDMGAICLQEHsehlqsLVNDALDKGAEIAVRGSFGHLGEDAVD 412
Cdd:cd07084 249 FVPENWSkTPLVEKLkallaRRKLEDLLLGPVQTFTTLAMIAHMENL------LGSVLLFSGKELKNHSIPSIYGACVAS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 413 QYFPPTVLINVNHnmKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRY--ALGCAVFSGSKHRAKQI--ASQIQCGVAAIN 488
Cdd:cd07084 323 ALFVPIDEILKTY--ELVTEEIFGPFAIVVEYKKDQLALVLELLERMhgSLTAAIYSNDPIFLQELigNLWVAGRTYAIL 400
|
330 340 350
....*....|....*....|....*....|..
gi 42563558 489 DFASNYMCQSLPFGGVKDSGFGrfAGIEGLRA 520
Cdd:cd07084 401 RGRTGVAPNQNHGGGPAADPRG--AGIGGPEA 430
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
84-483 |
5.86e-16 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 81.52 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 84 SPTEVEERVTLSRKAQKTWAQSSFKLRRQflrILLKY--IIEHQ--ELI--CevsSRDTGKTMVDAsLGEImttCEKITW 157
Cdd:COG4230 591 TAADVEAALAAAQAAFPAWSATPVEERAA---ILERAadLLEAHraELMalL---VREAGKTLPDA-IAEV---REAVDF 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 158 LlsegeRWLkpesrsSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFhNIF-NPMLAAVFSGNGIVIKVSEHASWSGCFYFR 236
Cdd:COG4230 661 C-----RYY------AAQARRLFAAPTVLRGRGVFVCISPWNFPL-AIFtGQVAAALAAGNTVLAKPAEQTPLIAARAVR 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 237 IIQAAlaavGAPENLVDVITGFAET-GEALVSS--VDKMIFVGSTAVGKMIMRNAAETLTP-VTL--ELGGKDAFIiced 310
Cdd:COG4230 729 LLHEA----GVPADVLQLLPGDGETvGAALVADprIAGVAFTGSTETARLINRTLAARDGPiVPLiaETGGQNAMI---- 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 311 ADVS----HVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTafigQVTKIVKS----VSAGPPLTGRYDMGAIC------- 375
Cdd:COG4230 801 VDSSalpeQVVDDVLASAFDSAGQRCSALRVLCVQEDIAD----RVLEMLKGamaeLRVGDPADLSTDVGPVIdaearan 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 376 LQEHSEHLQSlvndaldKGAEIAVrgsfGHLGEDAVD-QYFPPTvLINVNhNMKIMKEEAFGPIMPIMQFSTDE--EVIK 452
Cdd:COG4230 877 LEAHIERMRA-------EGRLVHQ----LPLPEECANgTFVAPT-LIEID-SISDLEREVFGPVLHVVRYKADEldKVID 943
|
410 420 430
....*....|....*....|....*....|.
gi 42563558 453 LANDSRYALGCAVFSGSKHRAKQIASQIQCG 483
Cdd:COG4230 944 AINATGYGLTLGVHSRIDETIDRVAARARVG 974
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
188-514 |
3.29e-11 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 66.54 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 PLGVIGAIVPWNYPFhNIFNPMLAAVF-SGNGIVIKVSEHASwsgcfyfrIIQAA----LAAVGAPENLVDVITGFAET- 261
Cdd:PRK11809 768 PLGPVVCISPWNFPL-AIFTGQVAAALaAGNSVLAKPAEQTP--------LIAAQavriLLEAGVPAGVVQLLPGRGETv 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 262 GEALVSS--VDKMIFVGSTAVGKMIMRNAAETL------TPVTLELGGKDAFIIcedaDVSHVAQVAVRGTLQSS----G 329
Cdd:PRK11809 839 GAALVADarVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIV----DSSALTEQVVADVLASAfdsaG 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 330 QNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPltGRY--DMGAICLQEHSE----HLQSL------VNDALDKGAEI 397
Cdd:PRK11809 915 QRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNP--DRLstDIGPVIDAEAKAnierHIQAMrakgrpVFQAARENSED 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 398 AVRGSFghlgedavdqyFPPTvLINVNhNMKIMKEEAFGPIMPIMQFSTDE--EVIKLANDSRYALGCAVFSGSKHRAKQ 475
Cdd:PRK11809 993 WQSGTF-----------VPPT-LIELD-SFDELKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQ 1059
|
330 340 350
....*....|....*....|....*....|....*....
gi 42563558 476 IASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAG 514
Cdd:PRK11809 1060 VTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1098
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
86-286 |
3.78e-10 |
|
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: 61.87 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 86 TEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKitwllSEGERW 165
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEK-----TPGTED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 166 LKPESRSSGRAMlhkvSRVEFHPLGVIGAIVPWNYPFHNIFN---PMLAAvfsGNGIVIKVSEHASWSGCFYFRIIQAAL 242
Cdd:cd07121 79 LTTTAWSGDNGL----TLVEYAPFGVIGAITPSTNPTETIINnsiSMLAA---GNAVVFNPHPGAKKVSAYAVELINKAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 42563558 243 AAVGAPENLVDVI-TGFAETGEALVSSVD-KMIFV-GSTAVGKMIMR 286
Cdd:cd07121 152 AEAGGPDNLVVTVeEPTIETTNELMAHPDiNLLVVtGGPAVVKAALS 198
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
188-449 |
7.23e-10 |
|
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: 61.36 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIiqaaLAAVGAPENLVDVITGFAETGEALVS 267
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRL----LHLCGMPATDVDLIHSDGPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 268 SVD-KMI-FVGSTAVGKmimRNAAETLTPVTLELGGKDAFIICED-ADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDI 344
Cdd:cd07126 218 EANpRMTlFTGSSKVAE---RLALELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENW 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 345 YTAfiGQVTKI--------VKSVSAGPPLTgrYDMGAIclQEHSEHLQSLvndaldKGAEIAVRGS----------FGHL 406
Cdd:cd07126 295 VQA--GILDKLkalaeqrkLEDLTIGPVLT--WTTERI--LDHVDKLLAI------PGAKVLFGGKpltnhsipsiYGAY 362
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 42563558 407 GEDAVdqyFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEE 449
Cdd:cd07126 363 EPTAV---FVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
86-286 |
1.72e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 59.92 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 86 TEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKitwllSEGERW 165
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAEK-----TPGVED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 166 LKPESRSSGRAMlhkvSRVEFHPLGVIGAIVPWNYPFHNIFN---PMLAAvfsGNGIV-------IKVSEHAswsgcfyF 235
Cdd:PRK15398 111 LTTEALTGDNGL----TLIEYAPFGVIGAVTPSTNPTETIINnaiSMLAA---GNSVVfsphpgaKKVSLRA-------I 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 42563558 236 RIIQAALAAVGAPENLVDVI-TGFAETGEALVSSVD-KMIFV-GSTAVGKMIMR 286
Cdd:PRK15398 177 ELLNEAIVAAGGPENLVVTVaEPTIETAQRLMKHPGiALLVVtGGPAVVKAAMK 230
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
88-455 |
2.31e-09 |
|
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: 59.48 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 88 VEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGktMVDASL-GEIMTTCEKITW---LLSEGE 163
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLqGELGRTTGQLRLfadLVREGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 164 rWLKP--ESRSSGRAMLHKVS-RVEFHPLGVIGAIVPWNYPFhnIFNPM-------LAAvfsGNGIVIKVseHASWSGC- 232
Cdd:cd07129 79 -WLDAriDPADPDRQPLPRPDlRRMLVPLGPVAVFGASNFPL--AFSVAggdtasaLAA---GCPVVVKA--HPAHPGTs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 233 -FYFRIIQAALAAVGAPENLVDVITGF-AETGEALVSsvDKMI----FVGSTAVGKMIMRNAAETLT--PVTLELGGKDA 304
Cdd:cd07129 151 eLVARAIRAALRATGLPAGVFSLLQGGgREVGVALVK--HPAIkavgFTGSRRGGRALFDAAAARPEpiPFYAELGSVNP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 305 FIICEDA---DVSHVAQVAVRGTLQSSGQNC---------AGAErfyvhkdiYTAFIGQVTKIVKSVSAGPPLTGR---- 368
Cdd:cd07129 229 VFILPGAlaeRGEAIAQGFVGSLTLGAGQFCtnpglvlvpAGPA--------GDAFIAALAEALAAAPAQTMLTPGiaea 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 369 YDMGAICLQEHsehlqslvndaldKGAEIAVRGSFG--------HLGEDAVDQYFPPTVLInvnhnmkimkEEAFGPIMP 440
Cdd:cd07129 301 YRQGVEALAAA-------------PGVRVLAGGAAAeggnqaapTLFKVDAAAFLADPALQ----------EEVFGPASL 357
|
410
....*....|....*
gi 42563558 441 IMQFSTDEEVIKLAN 455
Cdd:cd07129 358 VVRYDDAAELLAVAE 372
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
245-480 |
4.07e-09 |
|
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: 59.21 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 245 VGAPENLVDVITGFaetgealvssvDKMIFVGSTAVGKMIMRNAA--ETLTPVTLELGGKDAFIICEDA-----DVSHVA 317
Cdd:cd07128 209 CGSVGDLLDHLGEQ-----------DVVAFTGSAATAAKLRAHPNivARSIRFNAEADSLNAAILGPDAtpgtpEFDLFV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 318 QVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVnDALDKGAEI 397
Cdd:cd07128 278 KEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEV 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 398 AVRG--SFGHLGEDAVDQYF-PPTVLINVN-------HNMkimkeEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFS 467
Cdd:cd07128 357 VFGGpdRFEVVGADAEKGAFfPPTLLLCDDpdaatavHDV-----EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVT 431
|
250
....*....|...
gi 42563558 468 GSKHRAKQIASQI 480
Cdd:cd07128 432 NDPAFARELVLGA 444
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
188-363 |
2.61e-07 |
|
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: 53.00 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 PLGVIGAIVPWNYPFHNIFNpMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALAAvGAPENLVDVI-TGFAETGEALV 266
Cdd:cd07077 100 PIGVTMHILPSTNPLSGITS-ALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA-HGPKILVLYVpHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 267 S--SVDKMIFVGSTAVGKMIMRNAAEtlTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQsSGQNCAGAERFYVHKDI 344
Cdd:cd07077 178 ShpKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFF-DQNACASEQNLYVVDDV 254
|
170 180
....*....|....*....|...
gi 42563558 345 YTA----FIGQVTKIVKSVSAGP 363
Cdd:cd07077 255 LDPlyeeFKLKLVVEGLKVPQET 277
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
88-347 |
1.97e-06 |
|
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: 50.34 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 88 VEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVD--------ASLGEIMTTC-EKITWL 158
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhfAAEYIYNVYKdEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 159 LSEGERWLkpesrssgramlhkvSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRII 238
Cdd:cd07081 81 LTGDENGG---------------TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 239 QAALAAVGAPENLVDVITGFA-ETGEALVSSVDKMIFVgstAVGKMIMRNAAETLTPVTLELG-GKDAFIICEDADVSHV 316
Cdd:cd07081 146 LQAAVAAGAPENLIGWIDNPSiELAQRLMKFPGIGLLL---ATGGPAVVKAAYSSGKPAIGVGaGNTPVVIDETADIKRA 222
|
250 260 270
....*....|....*....|....*....|.
gi 42563558 317 AQVAVRGTLQSSGQNCAGAERFYVHKDIYTA 347
Cdd:cd07081 223 VQSIVKSKTFDNGVICASEQSVIVVDSVYDE 253
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
188-349 |
3.49e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 49.41 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 188 PLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVI-------KVSEHASwsgcfyfRIIQAALAAVGAPENLVDVITGFA- 259
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFsphprakKCSIEAA-------KIMREAAVAAGAPEGLIQWIEEPSi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563558 260 ETGEALVSSVD-KMIfvgsTAVGKMIMRNAAETltpvtlelGGKDAF---------IICEDADVSHvaqvAVR------- 322
Cdd:cd07122 168 ELTQELMKHPDvDLI----LATGGPGMVKAAYS--------SGKPAIgvgpgnvpaYIDETADIKR----AVKdiilskt 231
|
170 180 190
....*....|....*....|....*....|
gi 42563558 323 ---GTLQSSGQNCAgaerfyVHKDIYTAFI 349
Cdd:cd07122 232 fdnGTICASEQSVI------VDDEIYDEVR 255
|
|
| |
