|
Name |
Accession |
Description |
Interval |
E-value |
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
1-412 |
0e+00 |
|
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 439785 Cd Length: 414 Bit Score: 766.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 1 MLGLGRAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLDAAMLDRLALTPARLDAMVEGLR 80
Cdd:COG0014 3 LEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEGLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 81 QVAALPDPVGAIRDMNFMPSGIQVGKMRVPLGVIGIIYESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQ 160
Cdd:COG0014 83 QVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 161 GLDVAGLPAEVVQVVETTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAI 240
Cdd:COG0014 163 ALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRVVENATVPVIEHGDGNCHVYVDASADLEMAVDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 241 CLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMAALYVEKGVELRGCPATCAILPAALPASEEDWSTEYLAPILSIRIVDD 320
Cdd:COG0014 243 VVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAEAGVELRGDERTRAILPDVKPATEEDWGTEYLDLILAVKVVDS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 321 MDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSE 400
Cdd:COG0014 323 LDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTY 402
|
410
....*....|..
gi 1308656401 401 KYVVFGDGHIRQ 412
Cdd:COG0014 403 KYVVRGDGQIRP 414
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
1-412 |
0e+00 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 765.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 1 MLGLGRAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLDAAMLDRLALTPARLDAMVEGLR 80
Cdd:PRK00197 6 LEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGIAEGLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 81 QVAALPDPVGAIRDMNFMPSGIQVGKMRVPLGVIGIIYESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQ 160
Cdd:PRK00197 86 QVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 161 GLDVAGLPAEVVQVVETTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAI 240
Cdd:PRK00197 166 ALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVDESADLDKALKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 241 CLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMAALYVEKGVELRGCPATCAILPAALPASEEDWSTEYLAPILSIRIVDD 320
Cdd:PRK00197 246 VLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVELRGDEAALALLPDVVPATEEDWDTEYLDLILAVKVVDS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 321 MDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSE 400
Cdd:PRK00197 326 LDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTY 405
|
410
....*....|..
gi 1308656401 401 KYVVFGDGHIRQ 412
Cdd:PRK00197 406 KYIVLGDGQIRA 417
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
4-407 |
0e+00 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 701.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 4 LGRAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLDAAMLDRLALTPARLDAMVEGLRQVA 83
Cdd:cd07079 3 LAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 84 ALPDPVGAIRDMNFMPSGIQVGKMRVPLGVIGIIYESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQGLD 163
Cdd:cd07079 83 ALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEALE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 164 VAGLPAEVVQVVETTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAICLN 243
Cdd:cd07079 163 EAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIVVN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 244 AKTHRYGVCNAMETLLVHRAVAAAFLPGMAALYVEKGVELRGCPATCAILPAALPASEEDWSTEYLAPILSIRIVDDMDA 323
Cdd:cd07079 243 AKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGVELRGDEETLAILPGAKPATEEDWGTEYLDLILAVKVVDSLDE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 324 AIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSEKYV 403
Cdd:cd07079 323 AIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYI 402
|
....
gi 1308656401 404 VFGD 407
Cdd:cd07079 403 VRGD 406
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
8-401 |
1.74e-166 |
|
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion protein delta l-pyrroline-5-carboxylate synthetase that includes a gamma-glutamyl phosphate reductase region as described by this model. Alternate name: glutamate-5-semialdehyde dehydrogenase. The prosite motif begins at residue 332 of the seed alignment although not all of the members of the family exactly obey the motif. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 161862 Cd Length: 398 Bit Score: 472.35 E-value: 1.74e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 8 ARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLDAAMLDRLALTPARLDAMVEGLRQVAALPD 87
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 88 PVGAIRDMNFMPSGIQVGKMRVPLGVIGIIYESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQGLDVAGL 167
Cdd:TIGR00407 81 PVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 168 PAEVVQVVETTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAICLNAKTH 247
Cdd:TIGR00407 161 PVGAVQLIETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 248 RYGVCNAMETLLVHRAVAAAFLPGMAALYVEKGVELRGCPATCAILPAA----LPASEEDWSTEYLAPILSIRIVDDMDA 323
Cdd:TIGR00407 241 RPSTCNAIETLLVNKAIAREFLPVLENQLLEKGVTIHADAYALKLLELGpateAIVCKTDFDKEFLSLDLSVKIVESLEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308656401 324 AIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSEK 401
Cdd:TIGR00407 321 AIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
7-410 |
8.25e-112 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 343.63 E-value: 8.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 7 AARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLDAAMLDRLALTPARLDAMVEGLRQVAALP 86
Cdd:PLN02418 302 AARESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLADME 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 87 DPVGAIRDMNFMPSGIQVGKMRVPLGVIGIIYESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQGL-DVA 165
Cdd:PLN02418 382 DPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIpKTV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 166 GlpAEVVQVVetTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAICLNAK 245
Cdd:PLN02418 462 G--GKLIGLV--TSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIVVDAK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 246 THRYGVCNAMETLLVHRAVAAAflPGMAALYVE---KGVELRGCPATCAILpaALPASEEdWSTEYLAPILSIRIVDDMD 322
Cdd:PLN02418 538 TDYPAACNAMETLLVHKDLVQN--GGLNDLLVAlrsAGVTLYGGPRASKLL--NIPEAQS-FHHEYSSLACTVEIVDDVH 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 323 AAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSEKY 402
Cdd:PLN02418 613 AAIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRW 692
|
....*...
gi 1308656401 403 VVFGDGHI 410
Cdd:PLN02418 693 ILRGNGQV 700
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
7-410 |
2.48e-105 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 326.87 E-value: 2.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 7 AARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLDAAMLDRLALTPARLDAMVEGLRQVAALP 86
Cdd:TIGR01092 294 AARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAISLRQLAAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 87 DPVGAIRDMNFMPSGIQVGKMRVPLGVIGIIYESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQGLDVAG 166
Cdd:TIGR01092 374 DPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHV 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 167 LpAEVVQVVetTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAICLNAKT 246
Cdd:TIGR01092 454 G-KKLIGLV--TSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVDMAKRIVRDAKC 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 247 HRYGVCNAMETLLVHRAVA-AAFLPGMAALYVEKGVELRGCPATCAILPAALPASEEdWSTEYLAPILSIRIVDDMDAAI 325
Cdd:TIGR01092 531 DYPAACNAMETLLVHKDLLrNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKS-FRTEYSSLACTVEIVDDVYDAI 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 326 EHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSEKYVVF 405
Cdd:TIGR01092 610 DHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLR 689
|
....*
gi 1308656401 406 GDGHI 410
Cdd:TIGR01092 690 GKGQV 694
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
7-404 |
8.00e-52 |
|
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: 178.57 E-value: 8.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 7 AARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGrENGLDAAMLDRLALTPARLDAMVEGLRQVAALp 86
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAY-IRSLIANWIAMMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 87 dpVGAIRDMnFMPSGIQVGKMRVPLGVIGIIYESR-PNVTVEAASLCLKSGNACILRGGSESIHSNRAIAAcIRQGLDVA 165
Cdd:cd07077 80 --VGHIQDV-LLPDNGETYVRAFPIGVTMHILPSTnPLSGITSALRGIATRNQCIFRPHPSAPFTNRALAL-LFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 166 GLPAEVVQVVETTDRAAVGTLISMPEyVDVIVPRGGKGLIERISRDAR-VPVIKHLDGICHVYVDDRADLVKAEAICLNA 244
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 245 KTHRYGVCNAMETLLVHRAVAAAFLPGMAALYVEKGVELrgcPATCAILPAALPASEEDWSTEYLAPILS-IRIVDDMDA 323
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKV---PQETKPLSKETTPSFDDEALESMTPLECqFRVLDVISA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 324 ---AIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEYGLGAEIGISTDKIHARG-PVGLEGLTS 399
Cdd:cd07077 312 venAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRP 391
|
....*
gi 1308656401 400 EKYVV 404
Cdd:cd07077 392 LKRLV 396
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
6-405 |
8.71e-37 |
|
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: 137.36 E-value: 8.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 6 RAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLD--AAMLDRLALTPARLDaMVEGLRQVA 83
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGevARAIDTFRYAAGLAD-KLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 84 ALPDPVGAIRdmnfmpsgiqvgkmRVPLGVIGIIYESRP--NVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQg 161
Cdd:cd06534 80 PDPGGEAYVR--------------REPLGVVGVITPWNFplLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 162 ldvAGLPAEVVQVVETTDRAAVGTLISMPEyVDVIVPRGGKGLIERISRDA---RVPVIKHLDGICHVYVDDRADLVKAE 238
Cdd:cd06534 145 ---AGLPPGVVNVVPGGGDEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAaenLKPVTLELGGKSPVIVDEDADLDAAV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 239 AICLNAKTHRYG-VCNAMETLLVHRAVAAAFLPGMAALYVEKgvelrgcpatcailPAALPASEEdwstEYLAPILSIRI 317
Cdd:cd06534 221 EGAVFGAFFNAGqICTAASRLLVHESIYDEFVEKLVTVLVDV--------------DPDMPIAQE----EIFGPVLPVIR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 318 VDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFA-DGFEYGLGAEIGISTDKiharGPVGLEG 396
Cdd:cd06534 283 FKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKNSGIGREG----GPYGLEE 358
|
....*....
gi 1308656401 397 LTSEKYVVF 405
Cdd:cd06534 359 YTRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
107-368 |
6.12e-15 |
|
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: 76.03 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 107 MRVPLGVIGII--YESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQgldvAGLPAEVVQVVeTTDRAAVG 184
Cdd:pfam00171 123 RREPLGVVGAItpWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEE----AGLPAGVLNVV-TGSGAEVG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 185 TLISMPEYVDVIVPRGGKGLIERISRDARVPVIKH---LDGICHVYVDDRADLVKAEAICLNAKTHRYG-VCNAMETLLV 260
Cdd:pfam00171 198 EALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVtleLGGKNPLIVLEDADLDAAVEAAVFGAFGNAGqVCTATSRLLV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 261 HRAVAAAFLPGMAAL------------------------------YVEKGVE-----LRGCPATCA----ILPAALPASE 301
Cdd:pfam00171 278 HESIYDEFVEKLVEAakklkvgdpldpdtdmgpliskaqlervlkYVEDAKEegaklLTGGEAGLDngyfVEPTVLANVT 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 302 ED---WSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFA 368
Cdd:pfam00171 358 PDmriAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGD 427
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-370 |
1.32e-14 |
|
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: 75.16 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 6 RAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLdlqagrENG--LDAAMLDrlaltparLDAMVEGLRQVA 83
Cdd:COG1012 50 AAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTL------ETGkpLAEARGE--------VDRAADFLRYYA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 84 ALPDPV-GAIRDMNFMPSGIQVgkMRVPLGVIGII----YesrP-NVTVEAASLCLKSGNACILRGGSESIHSNRAIAAC 157
Cdd:COG1012 116 GEARRLyGETIPSDAPGTRAYV--RREPLGVVGAItpwnF---PlALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 158 IRQgldvAGLPAEVVQVVETTDRAAVGTLISMPEyVDVIV----PRGGKGLIERISRDaRVPVIKHLDGICHVYVDDRAD 233
Cdd:COG1012 191 LEE----AGLPAGVLNVVTGDGSEVGAALVAHPD-VDKISftgsTAVGRRIAAAAAEN-LKRVTLELGGKNPAIVLDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 234 LVKAEAICLNAKTHRYG-VCNAMETLLVHRAVAAAFLPGMAAL------------------------------YVEKGVE 282
Cdd:COG1012 265 LDAAVEAAVRGAFGNAGqRCTAASRLLVHESIYDEFVERLVAAakalkvgdpldpgtdmgpliseaqlervlaYIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 283 ------------------------LRGCPATCAIlpaalpaseedWSTEYLAPILSIRIVDDMDAAIEHINDfssqhTD- 337
Cdd:COG1012 345 egaelltggrrpdgeggyfveptvLADVTPDMRI-----------AREEIFGPVLSVIPFDDEEEAIALAND-----TEy 408
|
410 420 430
....*....|....*....|....*....|....*..
gi 1308656401 338 ----AMVSEDYTRARRFIAEVDSSSVMINASTRFADG 370
Cdd:COG1012 409 glaaSVFTRDLARARRVARRLEAGMVWINDGTTGAVP 445
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
6-369 |
1.36e-14 |
|
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: 74.94 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 6 RAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQLDLQAGRENGLD--AAMLDRLALTpARLDAMVEGLRQVA 83
Cdd:cd07078 5 AAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGevARAADTFRYY-AGLARRLHGEVIPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 84 ALPDPVGAIRdmnfmpsgiqvgkmRVPLGVIGIIyeSRPNVTVEAASL----CLKSGNACILRGGSESIHSNRAIAACIR 159
Cdd:cd07078 84 PDPGELAIVR--------------REPLGVVGAI--TPWNFPLLLAAWklapALAAGNTVVLKPSELTPLTALLLAELLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 160 QgldvAGLPAEVVQVVeTTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDA---RVPVIKHLDGICHVYVDDRADLVK 236
Cdd:cd07078 148 E----AGLPPGVLNVV-TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAaenLKRVTLELGGKSPLIVFDDADLDA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 237 AEAICLNAKTHRYG-VCNAMETLLVHRAVAAAFLPGMAAL------------------------------YVEKGVE--- 282
Cdd:cd07078 223 AVKGAVFGAFGNAGqVCTAASRLLVHESIYDEFVERLVERvkalkvgnpldpdtdmgplisaaqldrvlaYIEDAKAega 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 283 -------LRGCPATCAILPAALPASEEDWS---TEYLAPILSIRIVDDMDAAIEHINDfssqhTD-----AMVSEDYTRA 347
Cdd:cd07078 303 kllcggkRLEGGKGYFVPPTVLTDVDPDMPiaqEEIFGPVLPVIPFKDEEEAIELAND-----TEyglaaGVFTRDLERA 377
|
410 420
....*....|....*....|..
gi 1308656401 348 RRFIAEVDSSSVMINASTRFAD 369
Cdd:cd07078 378 LRVAERLEAGTVWINDYSVGAE 399
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
72-365 |
8.36e-14 |
|
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: 72.61 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 72 LDAMVEGLRQVAALPD--PVGAIrdmnfmPSGIQvGK----MRVPLGVI-GIIYESRP-NVTVEAASLCLKSGNACILRG 143
Cdd:cd07105 61 VDLAAGMLREAASLITqiIGGSI------PSDKP-GTlamvVKEPVGVVlGIAPWNAPvILGTRAIAYPLAAGNTVVLKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 144 GSESIHSNRAIAACIRQgldvAGLPAEVVQVVETT-DRAA--VGTLISMPEYVDV------IVPRggkgLIERISRDARV 214
Cdd:cd07105 134 SELSPRTHWLIGRVFHE----AGLPKGVLNVVTHSpEDAPevVEALIAHPAVRKVnftgstRVGR----IIAETAAKHLK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 215 PVIKHLDGICHVYVDDRADLVKA-EAICLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMAALY----------------- 276
Cdd:cd07105 206 PVLLELGGKAPAIVLEDADLDAAaNAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAeklfagpvvlgslvsaa 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 277 ------------VEKGVEL------RGCPATCAILPAALPASEED---WSTEYLAPILSIRIVDDMDAAIEHINDFSSQH 335
Cdd:cd07105 286 aadrvkelvddaLSKGAKLvvgglaDESPSGTSMPPTILDNVTPDmdiYSEESFGPVVSIIRVKDEEEAVRIANDSEYGL 365
|
330 340 350
....*....|....*....|....*....|
gi 1308656401 336 TDAMVSEDYTRARRFIAEVDSSSVMINAST 365
Cdd:cd07105 366 SAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
98-405 |
5.56e-11 |
|
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: 63.99 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 98 MPSGIQVGK-------MRVPLGVIGII--YESRPNVTVEAASLCLKSGNACILRGgsesihSNRAIAACIRQG--LDVAG 166
Cdd:cd07094 104 IPLDATQGSdnrlawtIREPVGVVLAItpFNFPLNLVAHKLAPAIATGCPVVLKP------ASKTPLSALELAkiLVEAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 167 LPAEVVQVVeTTDRAAVGTLISMPEYVDVIVPRGGKGLIERISRDARVP-VIKHLDGICHVYVDDRADLVKAEAICLNAK 245
Cdd:cd07094 178 VPEGVLQVV-TGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKrIALELGGNAPVIVDRDADLDAAIEALAKGG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 246 THRYG-VCNAMETLLVHRAVAAAFLPGM--------------------------AALYVEKGVE----------LRGCPA 288
Cdd:cd07094 257 FYHAGqVCISVQRIYVHEELYDEFIEAFvaavkklkvgdpldedtdvgpliseeAAERVERWVEeaveagarllCGGERD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 289 TCAILPAAL---PASEEDWSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINAST 365
Cdd:cd07094 337 GALFKPTVLedvPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSS 416
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1308656401 366 RF-ADGFEYGLGAEIGISTDKIhargPVGLEGLTSEKYVVF 405
Cdd:cd07094 417 AFrTDWMPFGGVKESGVGREGV----PYAMEEMTEEKTVVI 453
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
109-362 |
2.44e-10 |
|
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: 61.74 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 109 VPLGVI-GIIYESRPNVTVEAASL-CLKSGNACILrggseSIH-----SNRAIAACIRQGLDVAGLPAEVVQVVETTDRA 181
Cdd:cd07122 94 EPVGVIaALIPSTNPTSTAIFKALiALKTRNAIIF-----SPHprakkCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 182 AVGTLISMPEyVDVIVPRGGKGLIeRISRDARVPVIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYGV-CNAMETLLV 260
Cdd:cd07122 169 LTQELMKHPD-VDLILATGGPGMV-KAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTiCASEQSVIV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 261 HRAVAAAFLPGM-----------------AALYVEKGV--------------ELRG--CPATCAILPAALPA--SEEDWS 305
Cdd:cd07122 247 DDEIYDEVRAELkrrgayflneeekekleKALFDDGGTlnpdivgksaqkiaELAGieVPEDTKVLVAEETGvgPEEPLS 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308656401 306 TEYLAPILSIRIVDDMDAAIE---HINDFSSQ-HTDAMVSEDYTRARRFIAEVDSSSVMIN 362
Cdd:cd07122 327 REKLSPVLAFYRAEDFEEALEkarELLEYGGAgHTAVIHSNDEEVIEEFALRMPVSRILVN 387
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
108-405 |
4.48e-10 |
|
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: 61.07 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 108 RVPLGVIGII--YESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAacirQGLDVAGLPAEVVQVVeTTDRAAVGT 185
Cdd:cd07149 121 REPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLA----ELLLEAGLPKGALNVV-TGSGETVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 186 LISMPEYVDVIVPRGGKGLIERISRDARV-PVIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYG-VCNAMETLLVHRA 263
Cdd:cd07149 196 ALVTDPRVRMISFTGSPAVGEAIARKAGLkKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGqVCISVQRIFVHED 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 264 VAAAFLPGMAAL------------------------------YVEKGVE-----LRGCPATCAIL-PAALPASEED---W 304
Cdd:cd07149 276 IYDEFLERFVAAtkklvvgdpldedtdvgpmiseaeaerieeWVEEAVEggarlLTGGKRDGAILePTVLTDVPPDmkvV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 305 STEYLAPILSIRIVDDMDAAIEHIND---------FSSQHTDAMvsedytrarRFIAEVDSSSVMINASTRF-ADGFEYG 374
Cdd:cd07149 356 CEEVFAPVVSLNPFDTLDEAIAMANDspyglqagvFTNDLQKAL---------KAARELEVGGVMINDSSTFrVDHMPYG 426
|
330 340 350
....*....|....*....|....*....|..
gi 1308656401 375 lgaeiGISTDKIHARGP-VGLEGLTSEKYVVF 405
Cdd:cd07149 427 -----GVKESGTGREGPrYAIEEMTEIKLVCF 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
107-380 |
5.79e-10 |
|
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: 60.66 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 107 MRVPLGVIGIIyeSRPN--VTVEA--ASLCLKSGNACILRGGSESIHSNRAIAACIRQGLDVAGLPAEVVQVVetTDRAA 182
Cdd:cd07086 130 QWNPLGVVGVI--TAFNfpVAVPGwnAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV--TGGGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 183 VGTLISMPEYVDVIVPRG----GKGLIERISRDARvPVIKHLDGICHVYVDDRADLVKA-EAICLNA-KT--HRygvCNA 254
Cdd:cd07086 206 GGELLVHDPRVPLVSFTGstevGRRVGETVARRFG-RVLLELGGNNAIIVMDDADLDLAvRAVLFAAvGTagQR---CTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 255 METLLVHRAVAAAFLPGMAALY--------------------------VEKGVE---------------LRGCPATCAIL 293
Cdd:cd07086 282 TRRLIVHESVYDEFLERLVKAYkqvrigdpldegtlvgplinqaavekYLNAIEiaksqggtvltggkrIDGGEPGNYVE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 294 PA---ALPASEEDWSTEYLAPILSIRIVDDMDAAIEHIND----FSSqhtdAMVSEDYTRARRFI--AEVDSSSVMINAS 364
Cdd:cd07086 362 PTivtGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDvpqgLSS----SIFTEDLREAFRWLgpKGSDCGIVNVNIP 437
|
330
....*....|....*.
gi 1308656401 365 TrfadgfeygLGAEIG 380
Cdd:cd07086 438 T---------SGAEIG 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
6-364 |
2.24e-08 |
|
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: 55.82 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 6 RAARTASRVIARASTNVKNSALLATAEAIDAARPALLDanqldLQAgRENG--LDAAM--LDRLALTPARLDAMVEGLRQ 81
Cdd:cd07110 26 RAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAE-----LEA-RDNGkpLDEAAwdVDDVAGCFEYYADLAEQLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 82 VAALPDPVGAirdmnfmpSGIQVGKMRVPLGVIGIIYE-SRPNVT----VEAAslcLKSGNACILRGGSESIHSNRAIAA 156
Cdd:cd07110 100 KAERAVPLPS--------EDFKARVRREPVGVVGLITPwNFPLLMaawkVAPA---LAAGCTVVLKPSELTSLTELELAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 157 CIRQgldvAGLPAEVVQVVeTTDRAAVGTLISMPEYVDVIVPRG----GKGLIERISRDARvPVIKHLDGICHVYVDDRA 232
Cdd:cd07110 169 IAAE----AGLPPGVLNVV-TGTGDEAGAPLAAHPGIDKISFTGstatGSQVMQAAAQDIK-PVSLELGGKSPIIVFDDA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 233 DLVKA-EAICLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMA----ALYV----EKGVEL-------------------- 283
Cdd:cd07110 243 DLEKAvEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLAtaaeAIRVgdplEEGVRLgplvsqaqyekvlsfiargk 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 284 -------------RGCPATCAILP---AALPASEEDWSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRA 347
Cdd:cd07110 323 eegarllcggrrpAHLEKGYFIAPtvfADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERC 402
|
410
....*....|....*..
gi 1308656401 348 RRFIAEVDSSSVMINAS 364
Cdd:cd07110 403 DRVAEALEAGIVWINCS 419
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
108-367 |
4.25e-08 |
|
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: 55.05 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 108 RVPLGVIGII--YESRPNVTVEAASLCLKSGNACILRggsesiHSNRAIAACIRQG--LDVAGLPAEVVQVVeTTDRAAV 183
Cdd:cd07145 121 REPIGVVGAItpFNFPANLFAHKIAPAIAVGNSVVVK------PSSNTPLTAIELAkiLEEAGLPPGVINVV-TGYGSEV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 184 GTLISMPEYVDVIVPRGGKGLIERISRDARVP---VIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYG-VCNAMETLL 259
Cdd:cd07145 194 GDEIVTNPKVNMISFTGSTAVGLLIASKAGGTgkkVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGqVCNAVKRIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 260 VHRAVAAAFL--------------------------PGMAALYVEKGVE---------LRGC--PATCAILPAALPASEE 302
Cdd:cd07145 274 VEEEVYDKFLkllvekvkklkvgdpldestdlgpliSPEAVERMENLVNdavekggkiLYGGkrDEGSFFPPTVLENDTP 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308656401 303 D---WSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRF 367
Cdd:cd07145 354 DmivMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRF 421
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
107-374 |
9.84e-08 |
|
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: 53.89 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 107 MRVPLGVIGII--YESRPNVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRqglDVAGLPAEVVQVVETTDRAAVG 184
Cdd:cd07120 114 LREPMGVAGIIvpWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILA---EIPSLPAGVVNLFTESGSEGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 185 TLISMPEyVDVIVPRGGKGLIERISRDArVPVIK----HLDG-ICHVYVDDrADLVKAEAICLNAKTHRYG-VCNAMETL 258
Cdd:cd07120 191 HLVASPD-VDVISFTGSTATGRAIMAAA-APTLKrlglELGGkTPCIVFDD-ADLDAALPKLERALTIFAGqFCMAGSRV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 259 LVHRAVAAAFLPGMAAL------------------------------YVEKG------VELRGCPATCAILPAAL--PAS 300
Cdd:cd07120 268 LVQRSIADEVRDRLAARlaavkvgpgldpasdmgplidranvdrvdrMVERAiaagaeVVLRGGPVTEGLAKGAFlrPTL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 301 EEDWST-------EYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFADGFEY 373
Cdd:cd07120 348 LEVDDPdadivqeEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEE 427
|
.
gi 1308656401 374 G 374
Cdd:cd07120 428 G 428
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
99-362 |
4.12e-07 |
|
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: 51.76 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 99 PSGIQVGKMRV---PLGVIGII----YesrPnvtveaASLCLK-------SGNACILRGgSEsiHSnRAIAACIRQGLDv 164
Cdd:cd07087 86 PLLLQPAKAYVipePLGVVLIIgpwnY---P------LQLALApligaiaAGNTVVLKP-SE--LA-PATSALLAKLIP- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 165 AGLPAEVVQVVETTdrAAVGTLIsMPEYVDVIV----PRGGKgLIERISRDARVPVIKHLDGICHVYVDDRADL-VKAEA 239
Cdd:cd07087 152 KYFDPEAVAVVEGG--VEVATAL-LAEPFDHIFftgsPAVGK-IVMEAAAKHLTPVTLELGGKSPCIVDKDANLeVAARR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 240 I----CLNAkthryG-VCNAMETLLVHRAVAAAFLPGM----AALY------------------VEKGVEL--------- 283
Cdd:cd07087 228 IawgkFLNA-----GqTCIAPDYVLVHESIKDELIEELkkaiKEFYgedpkespdygriinerhFDRLASLlddgkvvig 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 284 -RGCPATCAILPAALpaSEEDWST-----EYLAPILSIRIVDDMDAAIEHIND---------FssqhtdamvSEDYTRAR 348
Cdd:cd07087 303 gQVDKEERYIAPTIL--DDVSPDSplmqeEIFGPILPILTYDDLDEAIEFINSrpkplalylF---------SEDKAVQE 371
|
330
....*....|....
gi 1308656401 349 RFIAEVDSSSVMIN 362
Cdd:cd07087 372 RVLAETSSGGVCVN 385
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
107-379 |
5.46e-07 |
|
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: 51.58 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 107 MRVPLGVIGIIYESRPNVTVEAASLC--LKSGNACILRGGSESIHSNRAIAacirQGLDVAGLPAEVVQVVETTDRAAVG 184
Cdd:cd07131 132 RRQPIGVVALITPWNFPVAIPSWKIFpaLVCGNTVVFKPAEDTPACALKLV----ELFAEAGLPPGVVNVVHGRGEEVGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 185 TLISMPEyVDVIVPRGGKGLIERISR---DARVPVIKHLDGICHVYVDDRADLVKA-EAICLNA-KT--HRygvCNAMET 257
Cdd:cd07131 208 ALVEHPD-VDVVSFTGSTEVGERIGEtcaRPNKRVALEMGGKNPIIVMDDADLDLAlEGALWSAfGTtgQR---CTATSR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 258 LLVHRAVAAAFLPG-------------------MAALYVEKGVE--------LRGCPATCAILPAALPASEED------- 303
Cdd:cd07131 284 LIVHESVYDEFLKRfverakrlrvgdgldeetdMGPLINEAQLEkvlnyneiGKEEGATLLLGGERLTGGGYEkgyfvep 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 304 ------------WSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTrfadgf 371
Cdd:cd07131 364 tvftdvtpdmriAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPT------ 437
|
....*...
gi 1308656401 372 eygLGAEI 379
Cdd:cd07131 438 ---IGAEV 442
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
110-383 |
3.28e-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: 49.19 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 110 PLGVI-GIIYESRPNVTVEAASL-CLKSGNACILRGGSESIHSNRAIAACIRQGLDVAGLPAEVVQVVETTDRAAVGTLI 187
Cdd:cd07081 95 PIGVVaSITPSTNPTSTVIFKSLiSLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 188 SMPEyVDVIVPRGGKGLIERiSRDARVPVIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYGV-CNAMETLLVHRAVAA 266
Cdd:cd07081 175 KFPG-IGLLLATGGPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGViCASEQSVIVVDSVYD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 267 AFLPGMAA--LYVEKGVELRG------------------------------CPATCAIL--PAALPASEEDWSTEYLAPI 312
Cdd:cd07081 253 EVMRLFEGqgAYKLTAEELQQvqpvilkngdvnrdivgqdaykiaaaaglkVPQETRILigEVTSLAEHEPFAHEKLSPV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 313 LSIRIVDDMDAAIEH----INDFSSQHTDAMVS-EDYTRAR--RFIAEVDSSSVMINASTRFA---DGFEYGLGAEIGIS 382
Cdd:cd07081 333 LAMYRAANFADADAKalalKLEGGCGHTSAMYSdNIKAIENmnQFANAMKTSRFVKNGPCSQGglgDLYNFRGWPSMTLG 412
|
.
gi 1308656401 383 T 383
Cdd:cd07081 413 C 413
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
108-405 |
3.84e-06 |
|
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: 48.80 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 108 RVPLGVI-GIIYESRPNVTV-EAASLCLKSGNACILRGGSESIHSNRAIAACIRQgldvAGLPAEVVQVVeTTDRAAVGT 185
Cdd:cd07088 131 KVPIGVVaGILPWNFPFFLIaRKLAPALVTGNTIVIKPSEETPLNALEFAELVDE----AGLPAGVLNIV-TGRGSVVGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 186 LISMPEYVDVIVPRGGKGLIERISRDARVPVIK---HLDGICHVYVDDRADLVKAEAICLNAKTHRYG-VCNAMETLLVH 261
Cdd:cd07088 206 ALVAHPKVGMISLTGSTEAGQKIMEAAAENITKvslELGGKAPAIVMKDADLDLAVKAIVDSRIINCGqVCTCAERVYVH 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 262 RAVAAAFL----PGMAAL--------------------------YVEKGVE------LRGCPATCA----ILPAALPASE 301
Cdd:cd07088 286 EDIYDEFMeklvEKMKAVkvgdpfdaatdmgplvneaaldkveeMVERAVEagatllTGGKRPEGEkgyfYEPTVLTNVR 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 302 EDWS---TEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMIN-----ASTRFADGF-E 372
Cdd:cd07088 366 QDMEivqEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINrenfeAMQGFHAGWkK 445
|
330 340 350
....*....|....*....|....*....|...
gi 1308656401 373 YGLGAEigistDKIHargpvGLEGLTSEKYVVF 405
Cdd:cd07088 446 SGLGGA-----DGKH-----GLEEYLQTKVVYL 468
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
101-276 |
5.10e-06 |
|
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: 48.38 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 101 GIQVGKMRVPLGVIGIIYESRPNVTVEAASLC--LKSGNACILRGGSESIHSNRAIAacirQGLDVAGLPAEVVQVVETT 178
Cdd:cd07109 108 GYFVYTVREPHGVTGHIIPWNYPLQITGRSVApaLAAGNAVVVKPAEDAPLTALRLA----ELAEEAGLPAGALNVVTGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 179 DRAAVGTLISMPEyVDVIV----PRGGKgLIERISRDARVPVIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYG-VCN 253
Cdd:cd07109 184 GAEAGAALVAHPG-VDHISftgsVETGI-AVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGqTCS 261
|
170 180
....*....|....*....|...
gi 1308656401 254 AMETLLVHRAVAAAFLPGMAALY 276
Cdd:cd07109 262 AGSRLLVHRSIYDEVLERLVERF 284
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-364 |
6.34e-06 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 48.19 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 13 RVIARASTNVKNSalLATAEAIDAARP---ALLD----ANQLDLQAGRENGLDAamldrlaltparldamveglRQVAAL 85
Cdd:PLN02467 79 RAIAAKITERKSE--LAKLETLDCGKPldeAAWDmddvAGCFEYYADLAEALDA--------------------KQKAPV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 86 PDPvgairdMNFMPSGIqvgkMRVPLGVIGII----YESRPNVTVEAASLClkSGNACILRGgsesihSNRAIAACIRQG 161
Cdd:PLN02467 137 SLP------METFKGYV----LKEPLGVVGLItpwnYPLLMATWKVAPALA--AGCTAVLKP------SELASVTCLELA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 162 --LDVAGLPAEVVQVVETTDRAAVGTLISMPeYVDVIVPRG----GKGLIERISRDARvPVIKHLDGICHVYVDDRADLV 235
Cdd:PLN02467 199 diCREVGLPPGVLNVVTGLGTEAGAPLASHP-GVDKIAFTGstatGRKIMTAAAQMVK-PVSLELGGKSPIIVFDDVDLD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 236 KAEAICLnakthrYG-------VCNAMETLLVHRAVAAAFLPGMAAL------------------------------YVE 278
Cdd:PLN02467 277 KAVEWAM------FGcfwtngqICSATSRLLVHERIASEFLEKLVKWaknikisdpleegcrlgpvvsegqyekvlkFIS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 279 ----KGVELR--GC-PATCA-------ILPAALPASEEDWSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDY 344
Cdd:PLN02467 351 taksEGATILcgGKrPEHLKkgffiepTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDL 430
|
410 420
....*....|....*....|
gi 1308656401 345 TRARRFIAEVDSSSVMINAS 364
Cdd:PLN02467 431 ERCERVSEAFQAGIVWINCS 450
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
6-362 |
8.21e-06 |
|
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: 47.68 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 6 RAARTASRVIARASTNVKNSALLATAEAIDAARPALLDAnqldlqAGRENG---LDAAmldrlaltpARLDAMVEGLRQV 82
Cdd:cd07151 39 RAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEW------LIRESGstrIKAN---------IEWGAAMAITREA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 83 AALPDPV-GAIrdmnfMPSGIQvGK----MRVPLGVIGIIyesRP-----NVTVEAASLCLKSGNACILRGGSESIHSNR 152
Cdd:cd07151 104 ATFPLRMeGRI-----LPSDVP-GKenrvYREPLGVVGVI---SPwnfplHLSMRSVAPALALGNAVVLKPASDTPITGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 153 AIAACIrqgLDVAGLPAEVVQVVeTTDRAAVGTlismpEYVDVIVPRggkglieRISRDARVPVIKHLDGIC-------- 224
Cdd:cd07151 175 LLLAKI---FEEAGLPKGVLNVV-VGAGSEIGD-----AFVEHPVPR-------LISFTGSTPVGRHIGELAgrhlkkva 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 225 --------HVYVDDrADLVKA-EAICLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMAAL-------------------- 275
Cdd:cd07151 239 lelggnnpFVVLED-ADIDAAvNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERvkalpygdpsdpdtvvgpli 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 276 ----------YVEKGVE-----LRGCPATCAILP----AALPASEEDWSTEYLAPILSIRIVDDMDAAIEHINDFSSQHT 336
Cdd:cd07151 318 nesqvdglldKIEQAVEegatlLVGGEAEGNVLEptvlSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420
....*....|....*....|....*.
gi 1308656401 337 DAMVSEDYTRARRFIAEVDSSSVMIN 362
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHIN 423
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
107-366 |
1.15e-05 |
|
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: 47.18 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 107 MRVPLGVIGII----YesrP-NVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQgldvAGLPAEVVQVVeTTDRA 181
Cdd:cd07082 138 RREPLGVVLAIgpfnY---PlNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHD----AGFPKGVVNVV-TGRGR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 182 AVGTLISMPEYVDVIVPRGGKGLIERISRDA-RVPVIKHLDGICHVYVDDRADLVKA-EAICLNAKTHRYGVCNAMETLL 259
Cdd:cd07082 210 EIGDPLVTHGRIDVISFTGSTEVGNRLKKQHpMKRLVLELGGKDPAIVLPDADLELAaKEIVKGALSYSGQRCTAIKRVL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 260 VHRAVAAAFL-----------PGM---------------AALYVE--------KGVEL----RGCPATCaILPAALPASE 301
Cdd:cd07082 290 VHESVADELVellkeevaklkVGMpwdngvditplidpkSADFVEgliddavaKGATVlnggGREGGNL-IYPTLLDPVT 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 302 ED---WSTEYLAPILSIRIVDDMDAAIEHINdfSSQH-TDAMV-SEDYTRARRFIAEVDSSSVMINASTR 366
Cdd:cd07082 369 PDmrlAWEEPFGPVLPIIRVNDIEEAIELAN--KSNYgLQASIfTKDINKARKLADALEVGTVNINSKCQ 436
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
110-362 |
3.46e-05 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 45.79 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 110 PLGVIGII----YesrP-NVTVEAASLCLKSGNACILRGGSESIHSNRAIAACIRQGLDvaglpAEVVQVVETtDRAAVG 184
Cdd:PTZ00381 109 PLGVVLVIgawnY---PlNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLD-----PSYVRVIEG-GVEVTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 185 TLISMPeyVDVIV----PRGGKgLIERISRDARVPVIKHLDGICHVYVDDRADL-VKAEAI----CLNAKThrygVCNAM 255
Cdd:PTZ00381 180 ELLKEP--FDHIFftgsPRVGK-LVMQAAAENLTPCTLELGGKSPVIVDKSCNLkVAARRIawgkFLNAGQ----TCVAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 256 ETLLVHRAVAAAFLPG------------------------------MAALYVEKG--VELRG--CPATCAILPAAL--PA 299
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEAlkeaikeffgedpkksedysrivnefhtkrLAELIKDHGgkVVYGGevDIENKYVAPTIIvnPD 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308656401 300 SEEDWSTEYL-APILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMIN 362
Cdd:PTZ00381 333 LDSPLMQEEIfGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
108-368 |
5.27e-05 |
|
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: 45.29 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 108 RVPLGVIGII----YE-SRPNVTVEAAslcLKSGNACILRggsESIHSNRaIAACIRQGLDVAGLPAEVVQVVetTDRAA 182
Cdd:cd07099 117 YRPYGVVGVIspwnYPlLTPMGDIIPA---LAAGNAVVLK---PSEVTPL-VGELLAEAWAAAGPPQGVLQVV--TGDGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 183 VGT-LISmpEYVDVIV----PRGGKGLIERISRDArVPVIKHLDGICHVYVDDRADLVKA-EAICLNAKTHRYGVCNAME 256
Cdd:cd07099 188 TGAaLID--AGVDKVAftgsVATGRKVMAAAAERL-IPVVLELGGKDPMIVLADADLERAaAAAVWGAMVNAGQTCISVE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 257 TLLVHRAVAAAFL-----------PGMAALY-------------------VEKGVElRGCPATC----------AILPAA 296
Cdd:cd07099 265 RVYVHESVYDEFVarlvakaralrPGADDIGdadigpmttarqldivrrhVDDAVA-KGAKALTggarsngggpFYEPTV 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308656401 297 LPASEEDWST---EYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFA 368
Cdd:cd07099 344 LTDVPHDMDVmreETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTA 418
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
108-362 |
1.36e-04 |
|
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: 43.77 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 108 RVPLGVIGII------YESRPNVTVEAaslcLKSGNACILRggsesiHSNRA--IAACIRQGLDVAGLPAEVVQVVETTD 179
Cdd:cd07102 114 REPLGVVLIIapwnypYLTAVNAVIPA----LLAGNAVILK------HSPQTplCGERFAAAFAEAGLPEGVFQVLHLSH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 180 rAAVGTLISMPeYVDVIV----PRGGKGlIERISRDARVPVIKHLDGICHVYVDDRADLVKA-EAICLNAKTHRYGVCNA 254
Cdd:cd07102 184 -ETSAALIADP-RIDHVSftgsVAGGRA-IQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAaESLVDGAFFNSGQSCCS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 255 METLLVHRAVAAAFL-----------------------P---GMAALYVEKGVE---LRGcpATCAILPAALPASEEDws 305
Cdd:cd07102 261 IERIYVHESIYDAFVeafvavvkgyklgdpldpsttlgPvvsARAADFVRAQIAdaiAKG--ARALIDGALFPEDKAG-- 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308656401 306 TEYLA--------------------PILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMIN 362
Cdd:cd07102 337 GAYLAptvltnvdhsmrvmreetfgPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN 413
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
108-368 |
1.37e-04 |
|
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: 43.84 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 108 RVPLGVIGIIyesRP-----NVTVEAASLCLKSGNACILRGGSESIHSnrAIAAciRQGLDVAGLPAEVVQVVETTDRAA 182
Cdd:cd07101 116 RRPKGVVGVI---SPwnyplTLAVSDAIPALLAGNAVVLKPDSQTALT--ALWA--VELLIEAGLPRDLWQVVTGPGSEV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 183 VGTLISMPEYVD---------VIVPRGGKGLIerisrdarvPVIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYG-VC 252
Cdd:cd07101 189 GGAIVDNADYVMftgstatgrVVAERAGRRLI---------GCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGqLC 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 253 NAMETLLVHRAVAAAFL-------------------PGMAAL-----------YVEKGVE-----LRGCPATCAI----- 292
Cdd:cd07101 260 VSIERIYVHESVYDEFVrrfvartralrlgaaldygPDMGSLisqaqldrvtaHVDDAVAkgatvLAGGRARPDLgpyfy 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308656401 293 LPAALPASEED---WSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMINASTRFA 368
Cdd:cd07101 340 EPTVLTGVTEDmelFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAA 418
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
106-362 |
2.27e-04 |
|
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: 42.98 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 106 KMRVPLGVIG----IIYESR------------------PNVTVEAAslclksGNACILRGGSESIHSNRAIAACIRQGLD 163
Cdd:cd07134 82 RVRTPLLLFGtkskIRYEPKgvcliispwnypfnlafgPLVSAIAA------GNTAILKPSELTPHTSAVIAKIIREAFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 164 vaglPAEVVqVVETTdrAAVGT-LISMPeyVDVIV----PRGGKGLIERISRDArVPVIKHLDGICHVYVDDRADLVK-A 237
Cdd:cd07134 156 ----EDEVA-VFEGD--AEVAQaLLELP--FDHIFftgsPAVGKIVMAAAAKHL-ASVTLELGGKSPTIVDETADLKKaA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 238 EAI----CLNA-KThrygvCNAMETLLVHRAVAAAFLPGM----AALY-------------------------------V 277
Cdd:cd07134 226 KKIawgkFLNAgQT-----CIAPDYVFVHESVKDAFVEHLkaeiEKFYgkdaarkaspdlarivndrhfdrlkgllddaV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 278 EKGVELRGC----PATCAILPAAL---PASEEDWSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRF 350
Cdd:cd07134 301 AKGAKVEFGgqfdAAQRYIAPTVLtnvTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKV 380
|
330
....*....|..
gi 1308656401 351 IAEVDSSSVMIN 362
Cdd:cd07134 381 LARTSSGGVVVN 392
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
110-405 |
3.24e-04 |
|
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: 42.67 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 110 PLGVIGII----YesrP--NVTVEAASlCLKSGNACILRGGSESIHSNRAIAACIRQGLDVAGLPAEVVQVV----ETTD 179
Cdd:cd07098 120 PLGVVGAIvswnY---PfhNLLGPIIA-ALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVtclpETAE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 180 raavgTLISMPEyVDVIVPRGGKGLIERISRDAR---VPVIKHLDGICHVYVDDRADLVKAEAICLNAKTHRYGV-CNAM 255
Cdd:cd07098 196 -----ALTSHPV-IDHITFIGSPPVGKKVMAAAAeslTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQnCIGI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 256 ETLLVHRAVAAAFL-------------PGMAALY---------------------VEKGVEL---------RGCPATCAI 292
Cdd:cd07098 270 ERVIVHEKIYDKLLeiltdrvqalrqgPPLDGDVdvgamisparfdrleelvadaVEKGARLlaggkryphPEYPQGHYF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 293 LPAALPASEED---WSTEYLAPILSIRIVDDMDAAIEHINDFSSQHTDAMVSEDYTRARRFIAEVDSSSVMIN--ASTRF 367
Cdd:cd07098 350 PPTLLVDVTPDmkiAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfGVNYY 429
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1308656401 368 ADGFEYGLGAEIGistdkiHAR--GPVGLEGLTSEKYVVF 405
Cdd:cd07098 430 VQQLPFGGVKGSG------FGRfaGEEGLRGLCNPKSVTE 463
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
6-274 |
3.92e-04 |
|
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: 42.52 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 6 RAARTASRVIARASTNVKNSALLATAEAIDAARPALLDANQldlqagRENGldaamldrlaltPARLDAMVEG------L 79
Cdd:cd07104 7 AAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLI------RESG------------STRPKAAFEVgaaiaiL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 80 RQVAALP-DPVGAIrdmnfMPSGIQvGKM----RVPLGVIGIIyeSRPNV----TVEAASLCLKSGNACILRGGSES-IH 149
Cdd:cd07104 69 REAAGLPrRPEGEI-----LPSDVP-GKEsmvrRVPLGVVGVI--SPFNFplilAMRSVAPALALGNAVVLKPDSRTpVT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 150 SNRAIAacirQGLDVAGLPAEVVQVVeTTDRAAVG-TLISMPEyVDVIVPRGGKGLIERISRDArvpvIKHLDGIC---- 224
Cdd:cd07104 141 GGLLIA----EIFEEAGLPKGVLNVV-PGGGSEIGdALVEHPR-VRMISFTGSTAVGRHIGELA----GRHLKKVAlelg 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1308656401 225 ----HVYVDDrADLVKA-EAICLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMAA 274
Cdd:cd07104 211 gnnpLIVLDD-ADLDLAvSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVA 264
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
72-274 |
4.61e-03 |
|
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: 39.20 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 72 LDAMVEGLRQVAALP-DPVGAIrdmnfMPSgiQVGKM----RVPLGVIGIIyeSRPN----VTVEAASLCLKSGNACILR 142
Cdd:cd07152 74 VGAAIGELHEAAGLPtQPQGEI-----LPS--APGRLslarRVPLGVVGVI--SPFNfpliLAMRSVAPALALGNAVVLK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308656401 143 GGSESIHSNRAIAACIrqgLDVAGLPAEVVQVVeTTDRAAVGTLISMPEyVDVIVPRGGKGLIERISRDA-----RVPVi 217
Cdd:cd07152 145 PDPRTPVSGGVVIARL---FEEAGLPAGVLHVL-PGGADAGEALVEDPN-VAMISFTGSTAVGRKVGEAAgrhlkKVSL- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308656401 218 kHLDGICHVYVDDRADL-VKAEAICLNAKTHRYGVCNAMETLLVHRAVAAAFLPGMAA 274
Cdd:cd07152 219 -ELGGKNALIVLDDADLdLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAA 275
|
|
| |
