|
Name |
Accession |
Description |
Interval |
E-value |
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
2-418 |
0e+00 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 759.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 2 DVKQYMQQLGQQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPASLDRLELTPARIQAM 81
Cdd:PRK00197 1 DIMEYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 82 IEGLKQVAALPDPVGEITNLNYQPSGIQVGQMRVPLGVIGIIYESRPNVTVDAAALCLKSGNACILRGGSESIYSNRAIA 161
Cdd:PRK00197 81 AEGLRQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 162 AAIASGLAEAGLPQQAVQVVETTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKHLDGICHVYIDGKADID 241
Cdd:PRK00197 161 AVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVDESADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 242 KAVAIAMNAKTHRYGVCNAMETLLVAESIAATVLPILAEQYTAKNVELRGCLKTCSLIKNAVRATEEDWHTEYLAPILAI 321
Cdd:PRK00197 241 KALKIVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVELRGDEAALALLPDVVPATEEDWDTEYLDLILAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 322 KIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLH 401
Cdd:PRK00197 321 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 400
|
410
....*....|....*..
gi 998903496 402 GLTSLKFIVLGDGHIRQ 418
Cdd:PRK00197 401 ELTTYKYIVLGDGQIRA 417
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
5-418 |
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: 758.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 5 QYMQQLGQQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPASLDRLELTPARIQAMIEG 84
Cdd:COG0014 1 AYLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 85 LKQVAALPDPVGEITNLNYQPSGIQVGQMRVPLGVIGIIYESRPNVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAI 164
Cdd:COG0014 81 LRQVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 165 ASGLAEAGLPQQAVQVVETTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKHLDGICHVYIDGKADIDKAV 244
Cdd:COG0014 161 QEALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRVVENATVPVIEHGDGNCHVYVDASADLEMAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 245 AIAMNAKTHRYGVCNAMETLLVAESIAATVLPILAEQYTAKNVELRGCLKTCSLIKNAVRATEEDWHTEYLAPILAIKIV 324
Cdd:COG0014 241 DIVVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAEAGVELRGDERTRAILPDVKPATEEDWGTEYLDLILAVKVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 325 ADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLHGLT 404
Cdd:COG0014 321 DSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 400
|
410
....*....|....
gi 998903496 405 SLKFIVLGDGHIRQ 418
Cdd:COG0014 401 TYKYVVRGDGQIRP 414
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
8-413 |
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: 694.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 8 QQLGQQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPASLDRLELTPARIQAMIEGLKQ 87
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 88 VAALPDPVGEITNLNYQPSGIQVGQMRVPLGVIGIIYESRPNVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAIASG 167
Cdd:cd07079 81 VAALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 168 LAEAGLPQQAVQVVETTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIA 247
Cdd:cd07079 161 LEEAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 248 MNAKTHRYGVCNAMETLLVAESIAATVLPILAEQYTAKNVELRGCLKTCSLIKNAVRATEEDWHTEYLAPILAIKIVADI 327
Cdd:cd07079 241 VNAKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGVELRGDEETLAILPGAKPATEEDWGTEYLDLILAVKVVDSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 328 DEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLHGLTSLK 407
Cdd:cd07079 321 DEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYK 400
|
....*.
gi 998903496 408 FIVLGD 413
Cdd:cd07079 401 YIVRGD 406
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
14-407 |
1.04e-162 |
|
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: 463.10 E-value: 1.04e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPASLDRLELTPARIQAMIEGLKQVAALPD 93
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 94 PVGEITNLNYQPSGIQVGQMRVPLGVIGIIYESRPNVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAIASGLAEAGL 173
Cdd:TIGR00407 81 PVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 174 PQQAVQVVETTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTH 253
Cdd:TIGR00407 161 PVGAVQLIETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 254 RYGVCNAMETLLVAESIAATVLPILAEQYTAKNVELRGCLKTCSLIK----NAVRATEEDWHTEYLAPILAIKIVADIDE 329
Cdd:TIGR00407 241 RPSTCNAIETLLVNKAIAREFLPVLENQLLEKGVTIHADAYALKLLElgpaTEAIVCKTDFDKEFLSLDLSVKIVESLEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998903496 330 AIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLHGLTSLK 407
Cdd:TIGR00407 321 AIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
14-416 |
4.76e-107 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 331.69 E-value: 4.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPASLDRLELTPARIQAMIEGLKQVAALPD 93
Cdd:PLN02418 303 ARESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLADMED 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 94 PVGEITNLNYQPSGIQVGQMRVPLGVIGIIYESRPNVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAIASGLAEaGL 173
Cdd:PLN02418 383 PIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPK-TV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 174 PQQAVQVVetTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTH 253
Cdd:PLN02418 462 GGKLIGLV--TSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIVVDAKTD 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 254 RYGVCNAMETLLV-AESIAATVLPILAEQYTAKNVELRGCLKTCSLIkNAVRATEedWHTEYLAPILAIKIVADIDEAIA 332
Cdd:PLN02418 540 YPAACNAMETLLVhKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLL-NIPEAQS--FHHEYSSLACTVEIVDDVHAAID 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 333 HINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLHGLTSLKFIVLG 412
Cdd:PLN02418 617 HIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRG 696
|
....
gi 998903496 413 DGHI 416
Cdd:PLN02418 697 NGQV 700
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
3-416 |
2.49e-103 |
|
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: 321.86 E-value: 2.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 3 VKQYMQQLGQQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPASLDRLELTPARIQAMI 82
Cdd:TIGR01092 284 EQTGERDMAVAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 83 EGLKQVAALPDPVGEITNLNYQPSGIQVGQMRVPLGVIGIIYESRPNVTVDAAALCLKSGNACILRGGSESIYSNRAIAA 162
Cdd:TIGR01092 364 ISLRQLAAMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 163 AIASGLAEAGLpQQAVQVVetTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKHLDGICHVYIDGKADIDK 242
Cdd:TIGR01092 444 VITEAIPIHVG-KKLIGLV--TSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVDM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 243 AVAIAMNAKTHRYGVCNAMETLLVAESIAAT-VLPILAEQYTAKNVELRGCLKTCSLIKNAVRATEEdWHTEYLAPILAI 321
Cdd:TIGR01092 521 AKRIVRDAKCDYPAACNAMETLLVHKDLLRNgLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKS-FRTEYSSLACTV 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 322 KIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLH 401
Cdd:TIGR01092 600 EIVDDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVE 679
|
410
....*....|....*
gi 998903496 402 GLTSLKFIVLGDGHI 416
Cdd:TIGR01092 680 GLLTTRWLLRGKGQV 694
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
14-411 |
1.16e-47 |
|
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: 167.79 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKDLEAGKQNGMDPAsLDRLELTPARIQAMIEGLKQVAALPD 93
Cdd:cd07077 3 AKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANW-IAMMGCSESKLYKNIDTERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 94 PVGEITnlnyQPSGIQVGQMRVPLGVIGIIYESR-PNVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAIASGLAeAG 172
Cdd:cd07077 82 HIQDVL----LPDNGETYVRAFPIGVTMHILPSTnPLSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADA-AH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 173 LPQQAVQVVETTDRAAVGELITMKDyVDVIVPRGGKSLIERI-SAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAK 251
Cdd:cd07077 157 GPKILVLYVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAvKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 252 THRYGVCNAMETLLVAESiaatVLPILAEQYTAKNVELRGCLKTCSLIKNA-VRATEEDWHTEYLAPILAIKIVADIDE- 329
Cdd:cd07077 236 FFDQNACASEQNLYVVDD----VLDPLYEEFKLKLVVEGLKVPQETKPLSKeTTPSFDDEALESMTPLECQFRVLDVISa 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 330 ---AIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYGLGAEIGISTDKLHARG-PVGLHGLTS 405
Cdd:cd07077 312 venAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRP 391
|
....*.
gi 998903496 406 LKFIVL 411
Cdd:cd07077 392 LKRLVR 397
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-411 |
4.81e-38 |
|
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: 141.21 E-value: 4.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREiSKAESGRKN-NALLKIAEAIAAGSAEIASENRKDLEAGKQNGMD--PASLDRLELTpARIQAMIEGLKQVAA 90
Cdd:cd06534 3 ARAAFKA-WAALPPAERaAILRKIADLLEERREELAALETLETGKPIEEALGevARAIDTFRYA-AGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 91 LPDPVGEITnlnyqpsgiqvgqmRVPLGVIGIIYESRP--NVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAIAsgl 168
Cdd:cd06534 81 DPGGEAYVR--------------REPLGVVGVITPWNFplLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQ--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 169 aEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKSLIERI---SAEATIPVIKHLDGICHVYIDGKADIDKAVA 245
Cdd:cd06534 144 -EAGLPPGVVNVV-PGGGDEVGAALLSHPRVDKISFTGSTAVGKAImkaAAENLKPVTLELGGKSPVIVDEDADLDAAVE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 246 IAMNAKTHRYG-VCNAMETLLVAESIAatvlpilaEQYTAKnvelrgcLKTcslIKNAVRATEEDWHTEYLAPILAIKIV 324
Cdd:cd06534 222 GAVFGAFFNAGqICTAASRLLVHESIY--------DEFVEK-------LVT---VLVDVDPDMPIAQEEIFGPVLPVIRF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 325 ADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFA-DGFEYGLGAEIGISTDKlharGPVGLHGL 403
Cdd:cd06534 284 KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKNSGIGREG----GPYGLEEY 359
|
....*...
gi 998903496 404 TSLKFIVL 411
Cdd:cd06534 360 TRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
14-409 |
4.68e-21 |
|
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: 94.91 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRkdLEAGKqngmdPASLDRLEltparIQAMIEGLKQVAALPD 93
Cdd:pfam00171 38 ARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELET--LENGK-----PLAEARGE-----VDRAIDVLRYYAGLAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 94 -PVGEITNlnyQPSGIQVGQMRVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRGGSESIysnrAIAAAIASGLAE 170
Cdd:pfam00171 106 rLDGETLP---SDPGRLAYTRREPLGVVGAItpWNFPLLLPAWKIAPALAAGNTVVLKPSELTP----LTALLLAELFEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 171 AGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKS---LIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIA 247
Cdd:pfam00171 179 AGLPAGVLNVV-TGSGAEVGEALVEHPDVRKVSFTGSTAvgrHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 248 MNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQY-------------------TAKNVElrgclKTCSLIKNAV---- 303
Cdd:pfam00171 258 VFGAFGNAGqVCTATSRLLVHESIYDEFVEKLVEAAkklkvgdpldpdtdmgpliSKAQLE-----RVLKYVEDAKeega 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 304 ------RATEED------------------WHTEYLAPILAIKIVADIDEAIAHIN--HYssAHTEAIVTEDYTLARRFL 357
Cdd:pfam00171 333 klltggEAGLDNgyfveptvlanvtpdmriAQEEIFGPVLSVIRFKDEEEAIEIANdtEY--GLAAGVFTSDLERALRVA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 998903496 358 REVDSSSVMVNASTRFAD------GF-EYGLGAEigistdklhaRGPVGLHGLTSLKFI 409
Cdd:pfam00171 411 RRLEAGMVWINDYTTGDAdglpfgGFkQSGFGRE----------GGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
14-376 |
3.80e-20 |
|
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: 92.11 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIA---SenrkdLEAGKqngmdPASLDRLEltparIQAMIEGLKQVAA 90
Cdd:COG1012 52 ARAAFPAWAATPPAERAAILLRAADLLEERREELAallT-----LETGK-----PLAEARGE-----VDRAADFLRYYAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 91 LPDPV-GEITNLNYQPSGIQVgqMRVPLGVIGII----YesrP-NVTVDAAALCLKSGNACILRGGSESIYSnraiAAAI 164
Cdd:COG1012 117 EARRLyGETIPSDAPGTRAYV--RREPLGVVGAItpwnF---PlALAAWKLAPALAAGNTVVLKPAEQTPLS----ALLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 165 ASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIV----PRGGKsLIERISAEATIPVIKHLDGICHVYIDGKADI 240
Cdd:COG1012 188 AELLEEAGLPAGVLNVV-TGDGSEVGAALVAHPDVDKISftgsTAVGR-RIAAAAAENLKRVTLELGGKNPAIVLDDADL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 241 DKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQY--------TAKNVELrGCL-------KTCSLIKNAV- 303
Cdd:COG1012 266 DAAVEAAVRGAFGNAGqRCTAASRLLVHESIYDEFVERLVAAAkalkvgdpLDPGTDM-GPLiseaqleRVLAYIEDAVa 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 304 ----------RATEED------------------WHTEYLAPILAIKIVADIDEAIAHINhyssaHTE-----AIVTEDY 350
Cdd:COG1012 345 egaelltggrRPDGEGgyfveptvladvtpdmriAREEIFGPVLSVIPFDDEEEAIALAN-----DTEyglaaSVFTRDL 419
|
410 420
....*....|....*....|....*.
gi 998903496 351 TLARRFLREVDSSSVMVNASTRFADG 376
Cdd:COG1012 420 ARARRVARRLEAGMVWINDGTTGAVP 445
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
12-375 |
3.96e-19 |
|
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: 88.80 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 12 QQARAAGREISKAESGRknnALLKIAEAIAAGSAEIAS----ENRKDLEAGKqngMD-PASLDRLELTpARIQAMIEGLK 86
Cdd:cd07078 8 RAAFKAWAALPPAERAA---ILRKLADLLEERREELAAletlETGKPIEEAL---GEvARAADTFRYY-AGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 87 QVAALPDPVGEITnlnyqpsgiqvgqmRVPLGVIGII----YesrP-NVTVDAAALCLKSGNACILRGGSESIYSnraiA 161
Cdd:cd07078 81 IPSPDPGELAIVR--------------REPLGVVGAItpwnF---PlLLAAWKLAPALAAGNTVVLKPSELTPLT----A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 162 AAIASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIV----PRGGKSLIeRISAEATIPVIKHLDGICHVYIDGK 237
Cdd:cd07078 140 LLLAELLAEAGLPPGVLNVV-TGDGDEVGAALASHPRVDKISftgsTAVGKAIM-RAAAENLKRVTLELGGKSPLIVFDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 238 ADIDKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQYTA--------KNVEL------RGCLKTCSLIKNA 302
Cdd:cd07078 218 ADLDAAVKGAVFGAFGNAGqVCTAASRLLVHESIYDEFVERLVERVKAlkvgnpldPDTDMgplisaAQLDRVLAYIEDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 303 VRA---------------------------TEED--WHTEYLAPILAIKIVADIDEAIAHIN--HYS-SAhteAIVTEDY 350
Cdd:cd07078 298 KAEgakllcggkrleggkgyfvpptvltdvDPDMpiAQEEIFGPVLPVIPFKDEEEAIELANdtEYGlAA---GVFTRDL 374
|
410 420
....*....|....*....|....*
gi 998903496 351 TLARRFLREVDSSSVMVNASTRFAD 375
Cdd:cd07078 375 ERALRVAERLEAGTVWINDYSVGAE 399
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
114-380 |
3.36e-14 |
|
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: 74.01 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 114 RVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVeTTDRAAVGE 191
Cdd:cd07094 121 REPVGVVLAItpFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS----ALELAKILVEAGVPEGVLQVV-TGEREVLGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 192 LITMKDYVDVIVPRGGKSLIERISAEATIP-VIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETLLVAES 269
Cdd:cd07094 196 AFAADERVAMLSFTGSAAVGEALRANAGGKrIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 270 IAATVLPILAEQYTAKNV--------------ELRGCLKTCSLIKNAVRA----------------------TEED---W 310
Cdd:cd07094 276 LYDEFIEAFVAAVKKLKVgdpldedtdvgpliSEEAAERVERWVEEAVEAgarllcggerdgalfkptvledVPRDtklS 355
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998903496 311 HTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRF-ADGFEYG 380
Cdd:cd07094 356 TEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFrTDWMPFG 426
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
10-380 |
1.17e-12 |
|
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: 69.16 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 10 LGQQARAAGRE----ISKAESGRKNNALLKIAE--AIAAGSAEIASENRKD------LEAGKqngmdPASLDRLELTPAr 77
Cdd:cd07149 12 IGRVPVASEEDvekaIAAAKEGAKEMKSLPAYEraEILERAAQLLEERREEfartiaLEAGK-----PIKDARKEVDRA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 78 IQAMI---EGLKQVAalpdpvGEITNLNYQPSGIQ-VG-QMRVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRGG 150
Cdd:cd07149 86 IETLRlsaEEAKRLA------GETIPFDASPGGEGrIGfTIREPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 151 SESIYSnraiAAAIASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATI-PVIKHLDGI 229
Cdd:cd07149 160 SQTPLS----ALKLAELLLEAGLPKGALNVV-TGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLkKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 230 CHVYIDGKADIDKAVA-IAMNAKTHRYGVCNAMETLLVAESI---------AAT--------------VLPIL------- 278
Cdd:cd07149 235 AAVIVDADADLEKAVErCVSGAFANAGQVCISVQRIFVHEDIydeflerfvAATkklvvgdpldedtdVGPMIseaeaer 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 279 AEQYTAKNVE-----LRGCLKTCSLIKNAV-RATEED---WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTED 349
Cdd:cd07149 315 IEEWVEEAVEggarlLTGGKRDGAILEPTVlTDVPPDmkvVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND 394
|
410 420 430
....*....|....*....|....*....|..
gi 998903496 350 YTLARRFLREVDSSSVMVNASTRF-ADGFEYG 380
Cdd:cd07149 395 LQKALKAARELEVGGVMINDSSTFrVDHMPYG 426
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
31-373 |
1.23e-12 |
|
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: 69.30 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 31 NALLKIAEAIAAGSAEIAseNRKDLEAGKqngmdPASLDRLELTPArIQAMIEGLKQVAALPDPVGEITNLNYQPSGIQV 110
Cdd:cd07145 47 KILMKVAELIERRKEELA--KLLTIEVGK-----PIKQSRVEVERT-IRLFKLAAEEAKVLRGETIPVDAYEYNERRIAF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 111 GQmRVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRGGSESiysnRAIAAAIASGLAEAGLPQQAVQVVeTTDRAA 188
Cdd:cd07145 119 TV-REPIGVVGAItpFNFPANLFAHKIAPAIAVGNSVVVKPSSNT----PLTAIELAKILEEAGLPPGVINVV-TGYGSE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 189 VGELITMKDYVDVIVPRGGKSLIERISAEATIP---VIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETL 264
Cdd:cd07145 193 VGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTgkkVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGqVCNAVKRI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 265 LVAESIAATVLPILAEQYTAKNV--------------ELRGCLKTCSLIKNA-----------------------VRATE 307
Cdd:cd07145 273 LVEEEVYDKFLKLLVEKVKKLKVgdpldestdlgpliSPEAVERMENLVNDAvekggkilyggkrdegsffpptvLENDT 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998903496 308 ED---WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRF 373
Cdd:cd07145 353 PDmivMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRF 421
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
78-371 |
1.65e-11 |
|
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: 65.68 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 78 IQAMIEGLKQVAALPDPVGEitnlNYQPSGIQvGQ----MRVPLGVI-GIIYESRP-NVTVDAAALCLKSGNACILRGGS 151
Cdd:cd07105 61 VDLAAGMLREAASLITQIIG----GSIPSDKP-GTlamvVKEPVGVVlGIAPWNAPvILGTRAIAYPLAAGNTVVLKASE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 152 ESIYSNRAIAAAiasgLAEAGLPQQAVQVVET--TDRAAVGELITMKDYVDVI-------VPRggksLIERISAEATIPV 222
Cdd:cd07105 136 LSPRTHWLIGRV----FHEAGLPKGVLNVVTHspEDAPEVVEALIAHPAVRKVnftgstrVGR----IIAETAAKHLKPV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 223 IKHLDGICHVYIDGKADIDKAV-AIAMNAKTHRYGVCNAMETLLVAESIA-----------------ATVLPILAEQYTA 284
Cdd:cd07105 208 LLELGGKAPAIVLEDADLDAAAnAALFGAFLNSGQICMSTERIIVHESIAdefveklkaaaeklfagPVVLGSLVSAAAA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 285 KNVElrgclktcSLIKNAVR-----------ATEED------------------WHTEYLAPILAIKIVADIDEAIAHIN 335
Cdd:cd07105 288 DRVK--------ELVDDALSkgaklvvgglaDESPSgtsmpptildnvtpdmdiYSEESFGPVVSIIRVKDEEEAVRIAN 359
|
330 340 350
....*....|....*....|....*....|....*.
gi 998903496 336 HYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNAST 371
Cdd:cd07105 360 DSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
78-368 |
2.51e-11 |
|
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: 64.85 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 78 IQAMIEGLKQVAAlPDPVGeiTNLNYQPSGIQVgqMRVPLGVIGII----YesrP-NVTVDAAALCLKSGNACILRGgSE 152
Cdd:cd07087 67 IDHALKHLKKWMK-PRRVS--VPLLLQPAKAYV--IPEPLGVVLIIgpwnY---PlQLALAPLIGAIAAGNTVVLKP-SE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 153 siYSnRAIAAAIASGLAEAgLPQQAVQVVETTDRAAVgELITMKdyVDVIV----PRGGKsLIERISAEATIPVIKHLDG 228
Cdd:cd07087 138 --LA-PATSALLAKLIPKY-FDPEAVAVVEGGVEVAT-ALLAEP--FDHIFftgsPAVGK-IVMEAAAKHLTPVTLELGG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 229 ICHVYIDGKADIDKAVA-IA----MNAkthryG-VCNAMETLLVAESIAATVLPILAEQYTA---KNVELRGCL------ 293
Cdd:cd07087 210 KSPCIVDKDANLEVAARrIAwgkfLNA-----GqTCIAPDYVLVHESIKDELIEELKKAIKEfygEDPKESPDYgriine 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 294 ----KTCSLIKNAVRA-----------------TEEDW-----HTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVT 347
Cdd:cd07087 285 rhfdRLASLLDDGKVViggqvdkeeryiaptilDDVSPdsplmQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFS 364
|
330 340
....*....|....*....|.
gi 998903496 348 EDYTLARRFLREVDSSSVMVN 368
Cdd:cd07087 365 EDKAVQERVLAETSSGGVCVN 385
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-371 |
2.86e-11 |
|
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: 64.96 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 12 QQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASEnrKDLEAGKqngmdPASLDRLELTPAriqamIEGLKQVAal 91
Cdd:cd07097 44 AAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL--LTREEGK-----TLPEARGEVTRA-----GQIFRYYA-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 92 pdpvGEITNL--NYQPS---GIQVGQMRVPLGVIGIIyeSRPNVTVD------AAALClkSGNACILRGGSESIysnrAI 160
Cdd:cd07097 110 ----GEALRLsgETLPStrpGVEVETTREPLGVVGLI--TPWNFPIAipawkiAPALA--YGNTVVFKPAELTP----AS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 161 AAAIASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIK---HLDGICHVYIDGK 237
Cdd:cd07097 178 AWALVEILEEAGLPAGVFNLV-MGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARvqlEMGGKNPLVVLDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 238 ADIDKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQYTAKNV-----------------ELRGCLKTCSLI 299
Cdd:cd07097 257 ADLDLAVECAVQGAFFSTGqRCTASSRLIVTEGIHDRFVEALVERTKALKVgdaldegvdigpvvserQLEKDLRYIEIA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 300 KN--AVRAT-----EEDWHTEYLA--------------------PILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTL 352
Cdd:cd07097 337 RSegAKLVYggerlKRPDEGYYLApalfagvtndmriareeifgPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKH 416
|
410
....*....|....*....
gi 998903496 353 ARRFLREVDSSSVMVNAST 371
Cdd:cd07097 417 ATHFKRRVEAGVVMVNLPT 435
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
107-411 |
4.43e-11 |
|
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: 64.18 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 107 GIQVGQMRVPLGVIG-IIYESRP-NVTVDAAALCLKSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVETT 184
Cdd:cd07109 108 GYFVYTVREPHGVTGhIIPWNYPlQITGRSVAPALAAGNAVVVKPAEDAPLT----ALRLAELAEEAGLPAGALNVVTGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 185 DRAAVGELITMKDyVDVIV----PRGGKsLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCN 259
Cdd:cd07109 184 GAEAGAALVAHPG-VDHISftgsVETGI-AVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGqTCS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 260 AMETLLVAESIAATVLPILAEQYTAKNV-------------------ELRGCLKT------------------------- 295
Cdd:cd07109 262 AGSRLLVHRSIYDEVLERLVERFRALRVgpgledpdlgplisakqldRVEGFVARarargarivaggriaegapaggyfv 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 296 CSLIKNAVRATEEDWHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNastrfad 375
Cdd:cd07109 342 APTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVN------- 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 998903496 376 gfEYGLGAEI----------GISTDKlharGPVGLHGLTSLKFIVL 411
Cdd:cd07109 415 --NYGAGGGIelpfggvkksGHGREK----GLEALYNYTQTKTVAV 454
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
113-385 |
6.05e-11 |
|
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: 63.91 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIGIIYESRPNVTVDAAALC--LKSGNACILRGGSESiysnRAIAAAIASGLAEAGLPQQAVQVVETTDrAAVG 190
Cdd:cd07131 132 RRQPIGVVALITPWNFPVAIPSWKIFpaLVCGNTVVFKPAEDT----PACALKLVELFAEAGLPPGVVNVVHGRG-EEVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 191 ELITMKDYVDVIVPRGGKSLIERI---SAEATIPVIKHLDGICHVYIDGKADIDKAV--AIAMNAKT--HRygvCNAMET 263
Cdd:cd07131 207 EALVEHPDVDVVSFTGSTEVGERIgetCARPNKRVALEMGGKNPIIVMDDADLDLALegALWSAFGTtgQR---CTATSR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 264 LLVAESI----------AATVL-------------PILAEQYT---------AKNVELRGCLKTCSLIKNA--------- 302
Cdd:cd07131 284 LIVHESVydeflkrfveRAKRLrvgdgldeetdmgPLINEAQLekvlnyneiGKEEGATLLLGGERLTGGGyekgyfvep 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 303 -----VRATEEDWHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTrfadgf 377
Cdd:cd07131 364 tvftdVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPT------ 437
|
....*...
gi 998903496 378 eygLGAEI 385
Cdd:cd07131 438 ---IGAEV 442
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
115-368 |
6.86e-11 |
|
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: 63.66 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 115 VPLGVI-GIIYESRPNVTVDAAAL-CLKSGNACILRGGSESIYSNRAIAAAIASGLAEAGLPQQAVQVVETTDRAAVGEL 192
Cdd:cd07122 94 EPVGVIaALIPSTNPTSTAIFKALiALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 193 ITMKDyVDVIVPRGGKSLIERISAEATiPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYGV-CNAMETLLVAESIA 271
Cdd:cd07122 174 MKHPD-VDLILATGGPGMVKAAYSSGK-PAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTiCASEQSVIVDDEIY 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 272 ATVLPILAEQ--YTAKNVELR----------GCLKT----CSLIKNAVRA-------------------TEEDWHTEYLA 316
Cdd:cd07122 252 DEVRAELKRRgaYFLNEEEKEklekalfddgGTLNPdivgKSAQKIAELAgievpedtkvlvaeetgvgPEEPLSREKLS 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 998903496 317 PILAIKIVADIDEAI----AHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVN 368
Cdd:cd07122 332 PVLAFYRAEDFEEALekarELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVN 387
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
113-411 |
1.02e-10 |
|
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: 63.13 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRGGSESiysnRAIAAAIASGLAEA-GLPQQAVQVVeTTDRAAV 189
Cdd:cd07120 114 LREPMGVAGIIvpWNSPVVLLVRSLAPALAAGCTVVVKPAGQT----AQINAAIIRILAEIpSLPAGVVNLF-TESGSEG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 190 GELITMKDYVDVIVPRGGKSLIERISAEATiPVIK----HLDG-ICHVYIDgKADIDKAVAIAMNAKTHRYG-VCNAMET 263
Cdd:cd07120 189 AAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKrlglELGGkTPCIVFD-DADLDAALPKLERALTIFAGqFCMAGSR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 264 LLVAESIAATVLPILAEQYTAKNVE------------------------------------LRGCLKTCSLIKNA----- 302
Cdd:cd07120 267 VLVQRSIADEVRDRLAARLAAVKVGpgldpasdmgplidranvdrvdrmveraiaagaevvLRGGPVTEGLAKGAflrpt 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 303 ---VRATEEDW-HTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFADGFE 378
Cdd:cd07120 347 lleVDDPDADIvQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAE 426
|
330 340 350
....*....|....*....|....*....|...
gi 998903496 379 YGLGAEIGIStdKLHarGPVGLHGLTSLKFIVL 411
Cdd:cd07120 427 EGGYRQSGLG--RLH--GVAALEDFIEYKHIYL 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
113-386 |
2.10e-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: 62.20 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIGIIyeSRPN--VTVDA--AALCLKSGNACILRGGSESIYSNRAIAAAIASGLAEAGLPQQAVQVVetTDRAA 188
Cdd:cd07086 130 QWNPLGVVGVI--TAFNfpVAVPGwnAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV--TGGGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 189 VGELITMKDYVDVIVPRG----GKsLIERISAEATIPVIKHLDGICHVYIDGKADIDKAV-AIAMNA-KT--HRygvCNA 260
Cdd:cd07086 206 GGELLVHDPRVPLVSFTGstevGR-RVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVrAVLFAAvGTagQR---CTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 261 METLLVAESIAATVLPILAEQYtaKNVE---------LRGCL---KTCSLIKNAVR-ATEED------------------ 309
Cdd:cd07086 282 TRRLIVHESVYDEFLERLVKAY--KQVRigdpldegtLVGPLinqAAVEKYLNAIEiAKSQGgtvltggkridggepgny 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 310 ---------------WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSS--VMVNASTr 372
Cdd:cd07086 360 veptivtgvtddariVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSDCgiVNVNIPT- 438
|
330
....*....|....
gi 998903496 373 fadgfeygLGAEIG 386
Cdd:cd07086 439 --------SGAEIG 444
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
114-368 |
2.16e-08 |
|
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: 55.83 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 114 RVPLGVI-GIIYESRP-NVTVDAAALCLKSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVeTTDRAAVGE 191
Cdd:cd07146 118 REPLGVVlAITPFNHPlNQVAHKIAPAIAANNRIVLKPSEKTPLS----AIYLADLLYEAGLPPDMLSVV-TGEPGEIGD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 192 LITMKDYVDVIVPRGGKSLIERISAEAT-IPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYGV-CNAMETLLVAES 269
Cdd:cd07146 193 ELITHPDVDLVTFTGGVAVGKAIAATAGyKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQrCTAVKRILVHES 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 270 IAATVLPILAEQYTAKNV-------ELRGCL---KTCSLIKNAVRATEED---------------WHT------------ 312
Cdd:cd07146 273 VADEFVDLLVEKSAALVVgdpmdpaTDMGTVideEAAIQIENRVEEAIAQgarvllgnqrqgalyAPTvldhvppdaelv 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 998903496 313 --EYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVN 368
Cdd:cd07146 353 teETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN 410
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
12-371 |
3.92e-08 |
|
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: 54.84 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 12 QQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASENRKdlEAGKqngmdpasldrleltpARIQAMIEG------L 85
Cdd:cd07104 7 AAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIR--ESGS----------------TRPKAAFEVgaaiaiL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 86 KQVAALP-DPVGEItnlnyQPSGIQvGQM----RVPLGVIGIIyeSRPNV----TVDAAALCLKSGNACILRGGSESIYS 156
Cdd:cd07104 69 REAAGLPrRPEGEI-----LPSDVP-GKEsmvrRVPLGVVGVI--SPFNFplilAMRSVAPALALGNAVVLKPDSRTPVT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 157 nraIAAAIASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATipviKHLDGIC------ 230
Cdd:cd07104 141 ---GGLLIAEIFEEAGLPKGVLNVV-PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG----RHLKKVAlelggn 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 231 --HVYIDGkADIDKAV-AIAMNAKTHRYGVCNAMETLLVAESIaatvlpilAEQYTAKNVELRGCLKT------------ 295
Cdd:cd07104 213 npLIVLDD-ADLDLAVsAAAFGAFLHQGQICMAAGRILVHESV--------YDEFVEKLVAKAKALPVgdprdpdtvigp 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 296 ----------CSLIKNAVRA--------TEED-----------------WHTEYLAPILAIKIVADIDEAIAHINHYSSA 340
Cdd:cd07104 284 linerqvdrvHAIVEDAVAAgarlltggTYEGlfyqptvlsdvtpdmpiFREEIFGPVAPVIPFDDDEEAVELANDTEYG 363
|
410 420 430
....*....|....*....|....*....|.
gi 998903496 341 HTEAIVTEDYTLARRFLREVDSSSVMVNAST 371
Cdd:cd07104 364 LSAAVFTRDLERAMAFAERLETGMVHINDQT 394
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
14-387 |
4.06e-08 |
|
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: 54.96 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIAseNRKDLEAGKqngmdPASLDRLEL--TPARIQAMIEGLKQVaal 91
Cdd:cd07088 44 AEAAQKAWERLPAIERAAYLRKLADLIRENADELA--KLIVEEQGK-----TLSLARVEVefTADYIDYMAEWARRI--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 92 pdpVGEItnLNYQPSGIQVGQMRVPLGVI-GIIYESRPNVTV-DAAALCLKSGNACILRGGSESIYSnraiAAAIASGLA 169
Cdd:cd07088 114 ---EGEI--IPSDRPNENIFIFKVPIGVVaGILPWNFPFFLIaRKLAPALVTGNTIVIKPSEETPLN----ALEFAELVD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 170 EAGLPQQAVQVVeTTDRAAVGE---------LITMKDYVdvivpRGGKSLIERiSAEATIPVIKHLDGICHVYIDGKADI 240
Cdd:cd07088 185 EAGLPAGVLNIV-TGRGSVVGDalvahpkvgMISLTGST-----EAGQKIMEA-AAENITKVSLELGGKAPAIVMKDADL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 241 DKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQY--------TAKNVEL------RGCLKTCSLIKNA--- 302
Cdd:cd07088 258 DLAVKAIVDSRIINCGqVCTCAERVYVHEDIYDEFMEKLVEKMkavkvgdpFDAATDMgplvneAALDKVEEMVERAvea 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 303 --------------------------VRATEEDWHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRF 356
Cdd:cd07088 338 gatlltggkrpegekgyfyeptvltnVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRA 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 998903496 357 LREVDSSSVMVN-----ASTRFADGF-EYGLGAEIGI 387
Cdd:cd07088 418 TNELEFGETYINrenfeAMQGFHAGWkKSGLGGADGK 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
113-372 |
6.21e-08 |
|
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: 54.50 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIGII----YesrP-NVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAiasgLAEAGLPQQAVQVVeTTDRA 187
Cdd:cd07082 138 RREPLGVVLAIgpfnY---PlNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEA----FHDAGFPKGVVNVV-TGRGR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 188 AVGELITMKDYVDVIVPRGGKSLIERISAEA-TIPVIKHLDG--ICHVYIDgkADIDKAVA-IAMNAKTHRYGVCNAMET 263
Cdd:cd07082 210 EIGDPLVTHGRIDVISFTGSTEVGNRLKKQHpMKRLVLELGGkdPAIVLPD--ADLELAAKeIVKGALSYSGQRCTAIKR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 264 LLVAESIAATVLPILAEQYTAKNV--------------------ELRGclktcsLIKNAV-----------RATE----- 307
Cdd:cd07082 288 VLVHESVADELVELLKEEVAKLKVgmpwdngvditplidpksadFVEG------LIDDAVakgatvlngggREGGnliyp 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998903496 308 -------ED---WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTR 372
Cdd:cd07082 362 tlldpvtPDmrlAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQ 436
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
52-368 |
1.18e-07 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 53.49 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 52 RKDLeaGKQngMDPASLDRLELTPARIQAMIEGLKQVAAlPDPVgEITNLNYQPSG-IQvgqmRVPLGVIGII----Yes 126
Cdd:PTZ00381 54 HKDL--GRH--PFETKMTEVLLTVAEIEHLLKHLDEYLK-PEKV-DTVGVFGPGKSyII----PEPLGVVLVIgawnY-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 127 rP-NVTVDAAALCLKSGNACILRggsESIYSnRAIAAAIAsGLAEAGLPQQAVQVVETtDRAAVGELITMKdyVDVIV-- 203
Cdd:PTZ00381 122 -PlNLTLIPLAGAIAAGNTVVLK---PSELS-PHTSKLMA-KLLTKYLDPSYVRVIEG-GVEVTTELLKEP--FDHIFft 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 204 --PRGGKsLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAE 280
Cdd:PTZ00381 193 gsPRVGK-LVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGqTCVAPDYVLVHRSIKDKFIEALKE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 281 QYTA------KNVELRGCLKTCS-------LIKN----AVRATEEDWHTEYLA--------------------PILAIKI 323
Cdd:PTZ00381 272 AIKEffgedpKKSEDYSRIVNEFhtkrlaeLIKDhggkVVYGGEVDIENKYVAptiivnpdldsplmqeeifgPILPILT 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 998903496 324 VADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVN 368
Cdd:PTZ00381 352 YENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
114-374 |
6.03e-07 |
|
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: 51.54 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 114 RVPLGVIGII----YesrP-NVTVDAAALCLKSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVeTTDRAA 188
Cdd:cd07101 116 RRPKGVVGVIspwnY---PlTLAVSDAIPALLAGNAVVLKPDSQTALT----ALWAVELLIEAGLPRDLWQVV-TGPGSE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 189 VGE-LITMKDYVDVI-VPRGGKSLIERiSAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETLL 265
Cdd:cd07101 188 VGGaIVDNADYVMFTgSTATGRVVAER-AGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGqLCVSIERIY 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 266 VAESIAATVLPILAEQytAKNVELRGCL----KTCSLIKNA----VRATEED---------------------------- 309
Cdd:cd07101 267 VHESVYDEFVRRFVAR--TRALRLGAALdygpDMGSLISQAqldrVTAHVDDavakgatvlaggrarpdlgpyfyeptvl 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998903496 310 ---------WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFA 374
Cdd:cd07101 345 tgvtedmelFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAA 418
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
78-281 |
7.66e-07 |
|
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: 51.14 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 78 IQAMIEGLKQVAALP-DPVGEITnlnyqPSgiQVGQM----RVPLGVIGIIyeSRPN----VTVDAAALCLKSGNACILR 148
Cdd:cd07152 74 VGAAIGELHEAAGLPtQPQGEIL-----PS--APGRLslarRVPLGVVGVI--SPFNfpliLAMRSVAPALALGNAVVLK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 149 GGSESIYSNRAIaaaIASGLAEAGLPQQAVQVVetTDRAAVGELITMKDYVDVIVPRGGKSlIERISAEATIPVIK---- 224
Cdd:cd07152 145 PDPRTPVSGGVV---IARLFEEAGLPAGVLHVL--PGGADAGEALVEDPNVAMISFTGSTA-VGRKVGEAAGRHLKkvsl 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 998903496 225 HLDGICHVYIDGKADIDKAV-AIAMNAKTHRYGVCNAMETLLVAESIAATVLPILAEQ 281
Cdd:cd07152 219 ELGGKNALIVLDDADLDLAAsNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAK 276
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
12-368 |
9.57e-07 |
|
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: 50.71 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 12 QQARAAGREISKAESGRKNNALLKIAEAIAAGSAEIASEnrKDLEAGKqngmdPASLDRLEL--TPARIQAMIEGLKQVA 89
Cdd:cd07102 25 ERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEE--LTWQMGR-----PIAQAGGEIrgMLERARYMISIAEEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 90 AlPDPVGEitnlnyqPSGIQVGQMRVPLGVIGIIyeSRPN----VTVDAAALCLKSGNACILRGGSESIysnrAIAAAIA 165
Cdd:cd07102 98 A-DIRVPE-------KDGFERYIRREPLGVVLII--APWNypylTAVNAVIPALLAGNAVILKHSPQTP----LCGERFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 166 SGLAEAGLPQQAVQVVETTDraAVGELITMKDYVDVIV----PRGGKSlIERISAEATIPVIKHLDGICHVYIDGKADID 241
Cdd:cd07102 164 AAFAEAGLPEGVFQVLHLSH--ETSAALIADPRIDHVSftgsVAGGRA-IQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 242 KAVA-IAMNAKTHRYGVCNAMETLLVAESI----------------------AATVLPILAEQYTAKNVELRgclktcsl 298
Cdd:cd07102 241 AAAEsLVDGAFFNSGQSCCSIERIYVHESIydafveafvavvkgyklgdpldPSTTLGPVVSARAADFVRAQ-------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 299 IKNAVRA-----------TEEDWHTEYLA--------------------PILAIKIVADIDEAIAHINHYSSAHTEAIVT 347
Cdd:cd07102 313 IADAIAKgaralidgalfPEDKAGGAYLAptvltnvdhsmrvmreetfgPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420
....*....|....*....|.
gi 998903496 348 EDYTLARRFLREVDSSSVMVN 368
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMN 413
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
114-370 |
9.86e-07 |
|
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: 50.81 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 114 RVPLGVIGIIYE-SRPNVTvdAA---ALCLKSGNACILRGGSESIYSNRAIAAaIAsglAEAGLPQQAVQVVeTTDRAAV 189
Cdd:cd07110 118 REPVGVVGLITPwNFPLLM--AAwkvAPALAAGCTVVLKPSELTSLTELELAE-IA---AEAGLPPGVLNVV-TGTGDEA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 190 GELITMKDYVDVIVPRGGKSLIERI--SAEATI-PVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETLL 265
Cdd:cd07110 191 GAPLAAHPGIDKISFTGSTATGSQVmqAAAQDIkPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGqICSATSRLL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 266 VAESIAATVLPILAEQYTA--------KNVELrGCL-------KTCSLIKNA---------------------------- 302
Cdd:cd07110 271 VHESIADAFLERLATAAEAirvgdpleEGVRL-GPLvsqaqyeKVLSFIARGkeegarllcggrrpahlekgyfiaptvf 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 303 --VRATEEDWHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNAS 370
Cdd:cd07110 350 adVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCS 419
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
134-368 |
1.56e-06 |
|
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: 50.12 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 134 AAALClkSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRG----GKS 209
Cdd:cd07103 139 APALA--AGCTVVLKPAEETPLS----ALALAELAEEAGLPAGVLNVV-TGSPAEIGEALCASPRVRKISFTGstavGKL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 210 LIeRISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQYTA---- 284
Cdd:cd07103 212 LM-AQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGqTCVCANRIYVHESIYDEFVEKLVERVKKlkvg 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 285 ----KNVEL------RGCLKTCSLIKNAV-----------RATEEDW-----------------HTEYLAPILAIKIVAD 326
Cdd:cd07103 291 ngldEGTDMgplineRAVEKVEALVEDAVakgakvltggkRLGLGGYfyeptvltdvtddmlimNEETFGPVAPIIPFDT 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 998903496 327 IDEAIAHINhyssaHTEA-----IVTEDYTLARRFLREVDSSSVMVN 368
Cdd:cd07103 371 EDEVIARAN-----DTPYglaayVFTRDLARAWRVAEALEAGMVGIN 412
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
25-368 |
2.05e-06 |
|
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: 49.72 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 25 ESGRKNNA------LLKIAEAIAAGSAEIASENRKDLeaGKQNGmdPASLDRLELTPARIQAMIEGLKQVAAlpdPVGEI 98
Cdd:cd07137 13 RSGRTRSAewrksqLKGLLRLVDENEDDIFAALRQDL--GKPSA--ESFRDEVSVLVSSCKLAIKELKKWMA---PEKVK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 99 TNLNYQPSGIQVgqMRVPLGVIGIIyeSRPNV----TVDAAALCLKSGNACILRGgSEsiysnraIAAAIASGLA---EA 171
Cdd:cd07137 86 TPLTTFPAKAEI--VSEPLGVVLVI--SAWNFpfllSLEPVIGAIAAGNAVVLKP-SE-------LAPATSALLAkliPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 172 GLPQQAVQVVETTdrAAVGElITMKDYVDVIVPRGGkSLIERI----SAEATIPVIKHLDGICHVYIDGKADIDKAVAIA 247
Cdd:cd07137 154 YLDTKAIKVIEGG--VPETT-ALLEQKWDKIFFTGS-PRVGRIimaaAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 248 MNAKthrYGVCN-----AMETLLVAESIAATVLPILA---EQYTAKN----------------VELRGCLKTCSLIKNAV 303
Cdd:cd07137 230 AGGK---WGCNNgqaciAPDYVLVEESFAPTLIDALKntlEKFFGENpkeskdlsrivnshhfQRLSRLLDDPSVADKIV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 304 RATEEDWHTEYLAP--------------------ILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSS 363
Cdd:cd07137 307 HGGERDEKNLYIEPtilldppldssimteeifgpLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSG 386
|
....*
gi 998903496 364 SVMVN 368
Cdd:cd07137 387 GVTFN 391
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
114-374 |
2.78e-06 |
|
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: 49.14 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 114 RVPLGVIGII----YE-SRPNVTVDAAalcLKSGNACILRgGSEsiYSNRaIAAAIASGLAEAGLPQQAVQVVetTDRAA 188
Cdd:cd07099 117 YRPYGVVGVIspwnYPlLTPMGDIIPA---LAAGNAVVLK-PSE--VTPL-VGELLAEAWAAAGPPQGVLQVV--TGDGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 189 VGE-LItmKDYVDVIV----PRGGKSLIERiSAEATIPVIKHLDGICHVYIDGKADIDKAVAIA-----MNAkthryG-V 257
Cdd:cd07099 188 TGAaLI--DAGVDKVAftgsVATGRKVMAA-AAERLIPVVLELGGKDPMIVLADADLERAAAAAvwgamVNA-----GqT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 258 CNAMETLLVAESIAATVLPILAEQ-------------------YTAKNVEL----------RGCLKTCSLIKNAVRA--- 305
Cdd:cd07099 260 CISVERVYVHESVYDEFVARLVAKaralrpgaddigdadigpmTTARQLDIvrrhvddavaKGAKALTGGARSNGGGpfy 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998903496 306 -----TEED-----WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRFA 374
Cdd:cd07099 340 eptvlTDVPhdmdvMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTA 418
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
106-416 |
3.00e-06 |
|
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: 49.05 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 106 SGIQVGQMRVPLGVIGIIYESR-----PNVTVDAAALClksGNACILRGgsesiySNRAIAAA--IASGLAEAGLPQQAV 178
Cdd:cd07085 126 RGIDTYSYRQPLGVVAGITPFNfpamiPLWMFPMAIAC---GNTFVLKP------SERVPGAAmrLAELLQEAGLPDGVL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 179 QVVeTTDRAAVGELITMKDyvdvivprggkslIERISAEATIPVIKHL--DGICHvyidGK-----------------AD 239
Cdd:cd07085 197 NVV-HGGKEAVNALLDHPD-------------IKAVSFVGSTPVGEYIyeRAAAN----GKrvqalggaknhavvmpdAD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 240 IDKAVAIAMNAKthrYGV----CNAMETLLVAESIAATVLPILAEQytAKNVELRGCL----------------KTCSLI 299
Cdd:cd07085 259 LEQTANALVGAA---FGAagqrCMALSVAVAVGDEADEWIPKLVER--AKKLKVGAGDdpgadmgpvispaakeRIEGLI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 300 KNAVRA-------------------------------TEED-WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVT 347
Cdd:cd07085 334 ESGVEEgaklvldgrgvkvpgyengnfvgptildnvtPDMKiYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFT 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998903496 348 EDYTLARRFLREVDSSSVMVNastrfadgfeyglgaeIGISTdklhargPVGLHGLTSLKFIVLGDGHI 416
Cdd:cd07085 414 RSGAAARKFQREVDAGMVGIN----------------VPIPV-------PLAFFSFGGWKGSFFGDLHF 459
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
116-368 |
4.15e-06 |
|
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: 48.84 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 116 PLGVIGII----YesrP--NVTVDAAAlCLKSGNACILRGGSESIYSNRAIAAAIASGLAEAGLPQQAVQVVetTDRAAV 189
Cdd:cd07098 120 PLGVVGAIvswnY---PfhNLLGPIIA-ALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLV--TCLPET 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 190 GELITMKDYVDVIV----PRGGKsLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYGV-CNAMETL 264
Cdd:cd07098 194 AEALTSHPVIDHITfigsPPVGK-KVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQnCIGIERV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 265 LVAESIAATVLPILAE--------QYTAKNVELRGCL------KTCSLIKNA---------------------------- 302
Cdd:cd07098 273 IVHEKIYDKLLEILTDrvqalrqgPPLDGDVDVGAMIsparfdRLEELVADAvekgarllaggkryphpeypqghyfppt 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 303 ----VRATEEDWHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVN 368
Cdd:cd07098 353 llvdVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
113-387 |
5.86e-06 |
|
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: 48.32 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRgGSEsiysnraIAAAIASGLA----EAGLPQQAVQVVeTTDR 186
Cdd:cd07114 116 RREPLGVVAAItpWNSPLLLLAKKLAPALAAGNTVVLK-PSE-------HTPASTLELAklaeEAGFPPGVVNVV-TGFG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 187 AAVGELITMKDYVDVIV----PRGGKSLIeRISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMnakthrYGV----- 257
Cdd:cd07114 187 PETGEALVEHPLVAKIAftggTETGRHIA-RAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVV------AGIfaaag 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 258 --CNAMETLLVAESIAATVLPILAEQytAKNVEL---------RGCL-------KTCSLIKNAV-----------RATEE 308
Cdd:cd07114 260 qtCVAGSRLLVQRSIYDEFVERLVAR--ARAIRVgdpldpetqMGPLaterqleKVERYVARAReegarvltggeRPSGA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 309 D---------------------WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMV 367
Cdd:cd07114 338 DlgagyffeptiladvtndmriAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWV 417
|
330 340
....*....|....*....|....*.
gi 998903496 368 NASTRFA-----DGF-EYGLGAEIGI 387
Cdd:cd07114 418 NTYRALSpsspfGGFkDSGIGRENGI 443
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
116-389 |
6.06e-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: 48.03 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 116 PLGVI-GIIYESRPNVTVDAAAL-CLKSGNACILRGGSESI-YSNRAIA----AAIASGLAEAGLPQQAVQVVETTDRaa 188
Cdd:cd07081 95 PIGVVaSITPSTNPTSTVIFKSLiSLKTRNSIIFSPHPRAKkVTQRAATlllqAAVAAGAPENLIGWIDNPSIELAQR-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 189 vgelITMKDYVDVIVPRGGKSLIERiSAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYGV-CNAMETLLVA 267
Cdd:cd07081 173 ----LMKFPGIGLLLATGGPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGViCASEQSVIVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 268 ESIAATVLPILAEQ--YTAKNVELRGC----LKTCSL----------------------------IKNAVRATEEDWHTE 313
Cdd:cd07081 248 DSVYDEVMRLFEGQgaYKLTAEELQQVqpviLKNGDVnrdivgqdaykiaaaaglkvpqetriliGEVTSLAEHEPFAHE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 314 YLAPILAIKIVADIDEAIAH----INHYSSAHTEAIVT-EDYTLAR--RFLREVDSSSVMVNASTRFA---DGFEYGLGA 383
Cdd:cd07081 328 KLSPVLAMYRAANFADADAKalalKLEGGCGHTSAMYSdNIKAIENmnQFANAMKTSRFVKNGPCSQGglgDLYNFRGWP 407
|
....*.
gi 998903496 384 EIGIST 389
Cdd:cd07081 408 SMTLGC 413
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
114-271 |
5.26e-05 |
|
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: 45.37 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 114 RVPLGVIGIIyesRP-----NVTVDAAALCLKSGNACILRGGSESIYSNRAIAAAIasgLAEAGLPQQAVQVVeTTDRAA 188
Cdd:cd07151 128 REPLGVVGVI---SPwnfplHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKI---FEEAGLPKGVLNVV-VGAGSE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 189 VGElitmkDYVDVIVPRggkslieRISAEATIPVIKHLDGIC----------------HVYIDgKADIDKAV-AIAMNAK 251
Cdd:cd07151 201 IGD-----AFVEHPVPR-------LISFTGSTPVGRHIGELAgrhlkkvalelggnnpFVVLE-DADIDAAVnAAVFGKF 267
|
170 180
....*....|....*....|
gi 998903496 252 THRYGVCNAMETLLVAESIA 271
Cdd:cd07151 268 LHQGQICMAINRIIVHEDVY 287
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
310-370 |
7.67e-05 |
|
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: 44.71 E-value: 7.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998903496 310 WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNAS 370
Cdd:cd07144 385 VKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS 445
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
14-380 |
1.19e-04 |
|
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: 44.16 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 14 ARAAGREISKAESGRKNNALLKIAEAIAAGSAEIAseNRKDLEAGKqngmdPASLDRLELtpARIQAMIeglkQVAA--L 91
Cdd:cd07147 30 AVKAFRPMRALPAHRRAAILLHCVARLEERFEELA--ETIVLEAGK-----PIKDARGEV--ARAIDTF----RIAAeeA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 92 PDPVGEITNLNYQPSGI--QVGQMRVPLGVIGII--YESRPNVTVDAAALCLKSGNACILRGGSESIYSnraiAAAIASG 167
Cdd:cd07147 97 TRIYGEVLPLDISARGEgrQGLVRRFPIGPVSAItpFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLS----ALILGEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 168 LAEAGLPQQAVQVVETTDRAAvgELITMKDYVDVIV----PRGGKSLIERISAEatiPVIKHLDGICHVYIDGKADIDKA 243
Cdd:cd07147 173 LAETGLPKGAFSVLPCSRDDA--DLLVTDERIKLLSftgsPAVGWDLKARAGKK---KVVLELGGNAAVIVDSDADLDFA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 244 VA-IAMNAKTHRYGVCNAMETLLVAESIAATVLPILAEQ-------------------YTAKNVElrgclKTCSLIKNAV 303
Cdd:cd07147 248 AQrIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARvkalktgdpkddatdvgpmISESEAE-----RVEGWVNEAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 304 RA----------------------TEED---WHTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLR 358
Cdd:cd07147 323 DAgaklltggkrdgalleptiledVPPDmevNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWD 402
|
410 420
....*....|....*....|...
gi 998903496 359 EVDSSSVMVNASTRF-ADGFEYG 380
Cdd:cd07147 403 ELEVGGVVINDVPTFrVDHMPYG 425
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
313-411 |
1.52e-04 |
|
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: 43.95 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 313 EYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVNASTRF-ADGFEYGLGAEIGISTDK 391
Cdd:cd07148 360 EIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFrVDWMPFAGRRQSGYGTGG 439
|
90 100
....*....|....*....|
gi 998903496 392 LhargPVGLHGLTSLKFIVL 411
Cdd:cd07148 440 I----PYTMHDMTQEKMAVI 455
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
45-279 |
1.76e-04 |
|
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: 43.72 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 45 AEIASENRKDL------EAGK--QNGMDPAS--LDRLELTPARIQAmiegLKQVAALPDPVGEITNLNYQPSG------- 107
Cdd:cd07125 101 ADLLEANRGELialaaaEAGKtlADADAEVReaIDFCRYYAAQARE----LFSDPELPGPTGELNGLELHGRGvfvcisp 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 108 ------IQVGQMrvplgvigiiyesrpnvtvdAAALClkSGNACILRGGSESIYsnraIAAAIASGLAEAGLPQQAVQVV 181
Cdd:cd07125 177 wnfplaIFTGQI--------------------AAALA--AGNTVIAKPAEQTPL----IAARAVELLHEAGVPRDVLQLV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 182 eTTDRAAVGELITMKDYVDVIVPRGG--------KSLIERisAEATIPVIKHLDGICHVYIDGKADIDKAVA-IAMNAKT 252
Cdd:cd07125 231 -PGDGEEIGEALVAHPRIDGVIFTGStetaklinRALAER--DGPILPLIAETGGKNAMIVDSTALPEQAVKdVVQSAFG 307
|
250 260
....*....|....*....|....*..
gi 998903496 253 HRYGVCNAMETLLVAESIAATVLPILA 279
Cdd:cd07125 308 SAGQRCSALRLLYLQEEIAERFIEMLK 334
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
109-281 |
1.88e-04 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 43.71 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 109 QVGQMRVPLGVIGII----YesrP-NVTVDAAALCLKSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVeT 183
Cdd:PRK09407 147 KTTELRQPKGVVGVIspwnY---PlTLAVSDAIPALLAGNAVVLKPDSQTPLT----ALAAVELLYEAGLPRDLWQVV-T 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 184 TDRAAVG-ELITMKDYVD---------VIVPRGGKSLIErISAEatipvikhLDGICHVYIDGKADIDKAVAIAMNAKTH 253
Cdd:PRK09407 219 GPGPVVGtALVDNADYLMftgstatgrVLAEQAGRRLIG-FSLE--------LGGKNPMIVLDDADLDKAAAGAVRACFS 289
|
170 180
....*....|....*....|....*....
gi 998903496 254 RYG-VCNAMETLLVAESIAATVLPILAEQ 281
Cdd:PRK09407 290 NAGqLCISIERIYVHESIYDEFVRAFVAA 318
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
12-290 |
1.95e-04 |
|
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: 43.58 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 12 QQARAAGREISKAESGRknnALLKIAEAIAAGSAEIASenRKDLEAGK-----QNGMDPASLDRLELTpARIQAMIEGlk 86
Cdd:cd07115 29 RAAFEAWSAMDPAERGR---ILWRLAELILANADELAR--LESLDTGKpiraaRRLDVPRAADTFRYY-AGWADKIEG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 87 QVAALPDPVgeitnLNYQpsgiqvgqMRVPLGVIG-IIYESRP-NVTVDAAALCLKSGNACILRGGSESIYSnraiAAAI 164
Cdd:cd07115 101 EVIPVRGPF-----LNYT--------VREPVGVVGaIVPWNFPlMFAAWKVAPALAAGNTVVLKPAELTPLS----ALRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 165 ASGLAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKSL---IERISAEATIPVIKHLDGICHVYIDGKADID 241
Cdd:cd07115 164 AELMAEAGFPAGVLNVV-TGFGEVAGAALVEHPDVDKITFTGSTAVgrkIMQGAAGNLKRVSLELGGKSANIVFADADLD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 998903496 242 KAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLpilaEQYTAKNVELR 290
Cdd:cd07115 243 AAVRAAATGIFYNQGqMCTAGSRLLVHESIYDEFL----ERFTSLARSLR 288
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
168-289 |
2.59e-04 |
|
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: 43.07 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 168 LAEAGLPQQAVQVVeTTDRAAVGELITMKDYVDVIVPRGGKSLIERISAEATIPVIKhldgiCHVYIDGK--------AD 239
Cdd:cd07119 184 IEEAGLPAGVVNLV-TGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK-----VALELGGKnpnivfadAD 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 998903496 240 IDKAVAIAMNAKTHRYG-VCNAMETLLVAESIAATVLPILAEQytAKNVEL 289
Cdd:cd07119 258 FETAVDQALNGVFFNAGqVCSAGSRLLVEESIHDKFVAALAER--AKKIKL 306
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| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
12-380 |
1.08e-03 |
|
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: 41.19 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 12 QQARAAGREISKAESGRknnALLKIAEAIAAGSAE----IASENRKDLEagkqngmdpasldrlelTPARIQA--MIEGL 85
Cdd:cd07108 29 KAAFPEWAATPARERGK---LLARIADALEARSEElarlLALETGNALR-----------------TQARPEAavLADLF 88
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 86 KQVAALpdpVGEITNLNYqPSGIQVGQM--RVPLGVIGIIYesrP-NVTVDAAAL----CLKSGNACILRGGSESIYSNR 158
Cdd:cd07108 89 RYFGGL---AGELKGETL-PFGPDVLTYtvREPLGVVGAIL---PwNAPLMLAALkiapALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 159 AIAAAIASGL------------AEAGLP---QQAVQVVETTDRAAVGELItMKDYVDVIVP----RGGKSlierisaeat 219
Cdd:cd07108 162 LLAEILAQVLpagvlnvitgygEECGAAlvdHPDVDKVTFTGSTEVGKII-YRAAADRLIPvsleLGGKS---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 220 iPVIkhldgichVYIDgkADIDKAVAIAMNA-KTHRYG-VCNAMETLLVAESIAATVLpilaEQYTAKNVELR------- 290
Cdd:cd07108 231 -PMI--------VFPD--ADLDDAVDGAIAGmRFTRQGqSCTAGSRLFVHEDIYDAFL----EKLVAKLSKLKigdplde 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 291 ----GCL-------KTCSLIKNAVRATE------------------------------EDWHT---EYLAPILAIKIVAD 326
Cdd:cd07108 296 atdiGAIisekqfaKVCGYIDLGLSTSGatvlrggplpgegpladgffvqptifsgvdNEWRLareEIFGPVLCAIPWKD 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 998903496 327 IDEAIAHIN--HYSSAHTeaIVTEDYTLARRFLREVDSSSVMVNASTRFADGFEYG 380
Cdd:cd07108 376 EDEVIAMANdsHYGLAAY--VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYG 429
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| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
33-270 |
2.73e-03 |
|
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: 39.78 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 33 LLKIAEAIAAGSAEIASenrkdLEAgkQNGMDPASLDRLeltpARIQAMIEGLKQVAALPDPVGEITNLNYQPsgIQVGQ 112
Cdd:cd07142 71 LLRFADLLEKHADELAA-----LET--WDNGKPYEQARY----AEVPLAARLFRYYAGWADKIHGMTLPADGP--HHVYT 137
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIG-IIYESRPNVTVD-AAALCLKSGNACILRGGSESIYSnraiAAAIASGLAEAGLPQQAVQVVETTDRAAVG 190
Cdd:cd07142 138 LHEPIGVVGqIIPWNFPLLMFAwKVGPALACGNTIVLKPAEQTPLS----ALLAAKLAAEAGLPDGVLNIVTGFGPTAGA 213
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 191 ELITMKDyVDVIVPRG----GKSLIERISAEATIPVIKHLDGICHVYIDGKADIDKAVAIAMNAKTHRYG-VCNAMETLL 265
Cdd:cd07142 214 AIASHMD-VDKVAFTGstevGKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGqCCCAGSRTF 292
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....*
gi 998903496 266 VAESI 270
Cdd:cd07142 293 VHESI 297
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| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
113-271 |
6.27e-03 |
|
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: 38.47 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 113 MRVPLGVIGIIYE-SRPNVTV-DAAALCLKSGNACILRgGSESIYSNRAIAAAIasgLAEAGLPQQAVQVVeTTDRAAVG 190
Cdd:cd07118 116 LREPIGVVGIITPwNFPFLILsQKLPFALAAGCTVVVK-PSEFTSGTTLMLAEL---LIEAGLPAGVVNIV-TGYGATVG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 191 ELITMKDYVDVIVPRG----GKSLIeRISAEATIPVIKHLDGICHVYIDGKADIDKAV-AIAMNAKTHRYGVCNAMETLL 265
Cdd:cd07118 191 QAMTEHPDVDMVSFTGstrvGKAIA-AAAARNLKKVSLELGGKNPQIVFADADLDAAAdAVVFGVYFNAGECCNSGSRLL 269
|
....*.
gi 998903496 266 VAESIA 271
Cdd:cd07118 270 VHESIA 275
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| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
116-280 |
8.84e-03 |
|
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: 38.36 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 116 PLGVIGII----YESRPNVTVDAAALClkSGNACILRGGSESIYsnraIAAAIASGLAEAGLPQQAVQVVeTTDRAAVGE 191
Cdd:cd07124 166 PLGVGAVIspwnFPLAILAGMTTAALV--TGNTVVLKPAEDTPV----IAAKLVEILEEAGLPPGVVNFL-PGPGEEVGD 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998903496 192 LITMKDYVDVIVPRGGKSLIERISAEATI---------PVIKHLDGICHVYIDGKADIDKAV-AIAMNAkthrYGV---- 257
Cdd:cd07124 239 YLVEHPDVRFIAFTGSREVGLRIYERAAKvqpgqkwlkRVIAEMGGKNAIIVDEDADLDEAAeGIVRSA----FGFqgqk 314
|
170 180
....*....|....*....|...
gi 998903496 258 CNAMETLLVAESIAATVLPILAE 280
Cdd:cd07124 315 CSACSRVIVHESVYDEFLERLVE 337
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| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
311-368 |
9.95e-03 |
|
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: 37.97 E-value: 9.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 998903496 311 HTEYLAPILAIKIVADIDEAIAHINHYSSAHTEAIVTEDYTLARRFLREVDSSSVMVN 368
Cdd:cd07132 328 QEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
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