|
Name |
Accession |
Description |
Interval |
E-value |
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
1-417 |
0e+00 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 734.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 1 MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDV 80
Cdd:PRK00197 5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGIAEGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 81 RQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQ 160
Cdd:PRK00197 85 RQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 161 DALKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESAEIAEALK 240
Cdd:PRK00197 165 EALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVDESADLDKALK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 241 VIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLqagpAKVVAVKAEEYDDEFLSLDLNV 320
Cdd:PRK00197 245 IVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVELRGDEAALALL----PDVVPATEEDWDTEYLDLILAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 321 KIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLE 400
Cdd:PRK00197 321 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 400
|
410
....*....|....*..
gi 446816049 401 ALTTYKWIGIGDYTIRA 417
Cdd:PRK00197 401 ELTTYKYIVLGDGQIRA 417
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
1-417 |
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: 696.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 1 MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDV 80
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 81 RQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQ 160
Cdd:COG0014 82 RQVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 161 DALKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESAEIAEALK 240
Cdd:COG0014 162 EALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRVVENATVPVIEHGDGNCHVYVDASADLEMAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 241 VIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLqagpAKVVAVKAEEYDDEFLSLDLNV 320
Cdd:COG0014 242 IVVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAEAGVELRGDERTRAIL----PDVKPATEEDWGTEYLDLILAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 321 KIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLE 400
Cdd:COG0014 318 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 397
|
410
....*....|....*..
gi 446816049 401 ALTTYKWIGIGDYTIRA 417
Cdd:COG0014 398 ELTTYKYVVRGDGQIRP 414
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
9-406 |
0e+00 |
|
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: 671.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 9 AKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVCNLAD 88
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 89 PVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGL 168
Cdd:TIGR00407 81 PVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 169 PAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESAEIAEALKVIVNAKTQ 248
Cdd:TIGR00407 161 PVGAVQLIETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 249 RPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLQAGPAKVVAVKAEEYDDEFLSLDLNVKIVSDLDD 328
Cdd:TIGR00407 241 RPSTCNAIETLLVNKAIAREFLPVLENQLLEKGVTIHADAYALKLLELGPATEAIVCKTDFDKEFLSLDLSVKIVESLEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446816049 329 AIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYK 406
Cdd:TIGR00407 321 AIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
3-412 |
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: 665.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 3 EQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQ 82
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 83 VCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDA 162
Cdd:cd07079 81 VAALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 163 LKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESAEIAEALKVI 242
Cdd:cd07079 161 LEEAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 243 VNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLqagpAKVVAVKAEEYDDEFLSLDLNVKI 322
Cdd:cd07079 241 VNAKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGVELRGDEETLAIL----PGAKPATEEDWGTEYLDLILAVKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 323 VSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEAL 402
Cdd:cd07079 317 VDSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEEL 396
|
410
....*....|
gi 446816049 403 TTYKWIGIGD 412
Cdd:cd07079 397 TTYKYIVRGD 406
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
5-408 |
2.70e-110 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 339.78 E-value: 2.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 5 MGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVC 84
Cdd:PLN02418 299 MAVAARESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 85 NLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALK 164
Cdd:PLN02418 379 DMEDPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 165 --SCGLPAGAVQAidnpdRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESAEIAEALKVI 242
Cdd:PLN02418 459 ktVGGKLIGLVTS-----RDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIV 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 243 VNAKTQRPSTCNTVETLLVNKNIADS-FLPALSKQMAESGVTLHadaaalaqlqAGP---AKVVAVKAEEYDDEFLSLDL 318
Cdd:PLN02418 534 VDAKTDYPAACNAMETLLVHKDLVQNgGLNDLLVALRSAGVTLY----------GGPrasKLLNIPEAQSFHHEYSSLAC 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 319 NVKIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMG 398
Cdd:PLN02418 604 TVEIVDDVHAAIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVG 683
|
410
....*....|
gi 446816049 399 LEALTTYKWI 408
Cdd:PLN02418 684 VEGLLTTRWI 693
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
5-408 |
2.62e-102 |
|
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: 319.16 E-value: 2.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 5 MGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVC 84
Cdd:TIGR01092 291 MAVAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAISLRQLA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 85 NLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALK 164
Cdd:TIGR01092 371 AMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIP 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 165 SCGLPAgAVQAIDNpdRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESAEIAEALKVIVN 244
Cdd:TIGR01092 451 IHVGKK-LIGLVTS--REEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVDMAKRIVRD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 245 AKTQRPSTCNTVETLLVNKNIADS-FLPALSKQMAESGVTLHADAAALAQLQAGPAKVvavkaEEYDDEFLSLDLNVKIV 323
Cdd:TIGR01092 528 AKCDYPAACNAMETLLVHKDLLRNgLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISET-----KSFRTEYSSLACTVEIV 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 324 SDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALT 403
Cdd:TIGR01092 603 DDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLL 682
|
....*
gi 446816049 404 TYKWI 408
Cdd:TIGR01092 683 TTRWL 687
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
8-408 |
3.52e-52 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 179.73 E-value: 3.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANgLSEAMLDRLALTPARLKGIADDVRQVCNLA 87
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRS-LIANWIAMMGCSESKLYKNIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 DPVGQVIDGgvlDSGLrLERRRVPLGVIGVIYEAR-PNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALkSC 166
Cdd:cd07077 81 GHIQDVLLP---DNGE-TYVRAFPIGVTMHILPSTnPLSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAD-AA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 167 GLPAGAVQAIDNPDRALVSEMLRMDKyIDMLIPRGGAGLHKLCREQST-IPVITGGIGVCHIYVDESAEIAEALKVIVNA 245
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 246 KTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAalaqlqagPAKVVAVKAEEYDDEFLSLDLN-----V 320
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETK--------PLSKETTPSFDDEALESMTPLEcqfrvL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 321 KIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARG-PMGL 399
Cdd:cd07077 307 DVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGH 386
|
....*....
gi 446816049 400 EALTTYKWI 408
Cdd:cd07077 387 DALRPLKRL 395
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
8-408 |
1.58e-31 |
|
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: 123.49 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEamldrLALTPARLKGIADDVRqvcnla 87
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGE-----VARAIDTFRYAAGLAD------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 DPVGQVIDGGvlDSGLRLERRRVPLGVIGVI----YearP-NVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDA 162
Cdd:cd06534 71 KLGGPELPSP--DPGGEAYVRREPLGVVGVItpwnF---PlLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 163 lkscGLPAGAVQAIDNPDRALVSEMLRMDKyIDMLIPRGGAGLHKLCRE---QSTIPVITGGIGVCHIYVDESAEIAEAL 239
Cdd:cd06534 146 ----GLPPGVVNVVPGGGDEVGAALLSHPR-VDKISFTGSTAVGKAIMKaaaENLKPVTLELGGKSPVIVDEDADLDAAV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 240 KVIVNAKT----QRpstCNTVETLLVNKNIADSFLPALskqmaesgVTLHAdaaalaqlqagpakVVAVKAEEYDDEFLS 315
Cdd:cd06534 221 EGAVFGAFfnagQI---CTAASRLLVHESIYDEFVEKL--------VTVLV--------------DVDPDMPIAQEEIFG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 316 LDLNVKIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTD-------GGQFGLGAEVavst 388
Cdd:cd06534 276 PVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpeapfggVKNSGIGREG---- 351
|
410 420
....*....|....*....|
gi 446816049 389 qklharGPMGLEALTTYKWI 408
Cdd:cd06534 352 ------GPYGLEEYTRTKTV 365
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
110-276 |
7.08e-18 |
|
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: 85.24 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 110 VPLGVI-GVIYEARPNVTVDVASL-CLKTGNAVIL---RGGKETCrtnAATVAVIQDALKSCGLPAGAVQAIDNPDRALV 184
Cdd:cd07122 94 EPVGVIaALIPSTNPTSTAIFKALiALKTRNAIIFsphPRAKKCS---IEAAKIMREAAVAAGAPEGLIQWIEEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 185 SEMLRmDKYIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIYVDESAEIAEALKVIVNAKTQRPST-CNTVETLLVNK 263
Cdd:cd07122 171 QELMK-HPDVDLILATGGPGMVKAAY-SSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTiCASEQSVIVDD 248
|
170
....*....|...
gi 446816049 264 NIADSFLPALSKQ 276
Cdd:cd07122 249 EIYDEVRAELKRR 261
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
8-410 |
1.82e-14 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 74.78 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDvadaraNG--LSEAMLDrlaltparLKGIADDVRQVCN 85
Cdd:COG1012 51 AARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLE------TGkpLAEARGE--------VDRAADFLRYYAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 86 LADPvgqvIDGGVLDSGLRLER---RRVPLGVIGVIyeaRP-NVTVDVASL----CLKTGNAVILRGGKETCRTNAATVA 157
Cdd:COG1012 117 EARR----LYGETIPSDAPGTRayvRREPLGVVGAI---TPwNFPLALAAWklapALAAGNTVVLKPAEQTPLSALLLAE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 158 VIQDAlkscGLPAGAVQAIDNPDRALVSEMLRmDKYIDMLI----PRGGAGLHKLCREQStIPVITGGIGVCHIYVDESA 233
Cdd:COG1012 190 LLEEA----GLPAGVLNVVTGDGSEVGAALVA-HPDVDKISftgsTAVGRRIAAAAAENL-KRVTLELGGKNPAIVLDDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 234 EIAEALKVIVNAKT----QRpstCNTVETLLVNKNIADSFLPALSKQMA--------ESGVTLhadaaalaqlqaGP--- 298
Cdd:COG1012 264 DLDAAVEAAVRGAFgnagQR---CTAASRLLVHESIYDEFVERLVAAAKalkvgdplDPGTDM------------GPlis 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 299 ------------------AKVVA--VKAEEYDDEFLS---LD-----------------LNVKIVSDLDDAIAHIRehGT 338
Cdd:COG1012 329 eaqlervlayiedavaegAELLTggRRPDGEGGYFVEptvLAdvtpdmriareeifgpvLSVIPFDDEEEAIALAN--DT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 339 QH--SDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQ-FG------LGAEvavstqklhaRGPMGLEALTTYKWIG 409
Cdd:COG1012 407 EYglAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQApFGgvkqsgIGRE----------GGREGLEEYTETKTVT 476
|
.
gi 446816049 410 I 410
Cdd:COG1012 477 I 477
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
8-408 |
2.21e-14 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 74.55 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARanglsEAMLDRLALTPARLKGIADDVRqvcnla 87
Cdd:cd07078 6 AARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPI-----EEALGEVARAADTFRYYAGLAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 DPVGQVIDGGVLDSglRLERRRVPLGVIGVIyeARPNVTVDVASL----CLKTGNAVILRGGKETCRTNAATVAVIQDAl 163
Cdd:cd07078 75 RLHGEVIPSPDPGE--LAIVRREPLGVVGAI--TPWNFPLLLAAWklapALAAGNTVVLKPSELTPLTALLLAELLAEA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 164 kscGLPAGAVQAIdNPDRALVSEMLRMDKYIDMLI----PRGGAGLHKLCrEQSTIPVI--TGgiGVCHIYVDESAEIAE 237
Cdd:cd07078 150 ---GLPPGVLNVV-TGDGDEVGAALASHPRVDKISftgsTAVGKAIMRAA-AENLKRVTleLG--GKSPLIVFDDADLDA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 238 ALKVIVNAKT----QRpstCNTVETLLVNKNIADSFLPALSKQMAEsgvtLHADAAALAQLQAGP--AKVVAVKAEEYDD 311
Cdd:cd07078 223 AVKGAVFGAFgnagQV---CTAASRLLVHESIYDEFVERLVERVKA----LKVGNPLDPDTDMGPliSAAQLDRVLAYIE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 312 E---------------------------FLSLDLNVKI--------------VSDLDDAIAHI-REHGTQHSdAILTRDM 349
Cdd:cd07078 296 DakaegakllcggkrleggkgyfvpptvLTDVDPDMPIaqeeifgpvlpvipFKDEEEAIELAnDTEYGLAA-GVFTRDL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446816049 350 RNAQRFVNEVDSSAVYVNASTRFTD-----GG--QFGLGAEvavstqklhaRGPMGLEALTTYKWI 408
Cdd:cd07078 375 ERALRVAERLEAGTVWINDYSVGAEpsapfGGvkQSGIGRE----------GGPYGLEEYTEPKTV 430
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
8-408 |
3.07e-13 |
|
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: 71.02 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEaqsesilnANAQDVAD--ARANG--LSEAMLDrlaltparLKGIADDVRQV 83
Cdd:pfam00171 37 AARAAFPAWRKTPAAERAAILRKAADLLE--------ERKDELAEleTLENGkpLAEARGE--------VDRAIDVLRYY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 84 CNLAD-PVGQVIDggvLDSGLRLERRRVPLGVIGVIyeaRP-NVTVDVASL----CLKTGNAVILRGGKETcrtnAATVA 157
Cdd:pfam00171 101 AGLARrLDGETLP---SDPGRLAYTRREPLGVVGAI---TPwNFPLLLPAWkiapALAAGNTVVLKPSELT----PLTAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 158 VIQDALKSCGLPAGAVQAIdNPDRALVSEMLRMDKYIDMLI----PRGGAGLHKLCrEQSTIPVI--TGgiGVCHIYVDE 231
Cdd:pfam00171 171 LLAELFEEAGLPAGVLNVV-TGSGAEVGEALVEHPDVRKVSftgsTAVGRHIAEAA-AQNLKRVTleLG--GKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 232 SAEIAEALKVIVNAKT----QRpstCNTVETLLVNKNIADSFLPALSKQMAesgvTLHADAAALAQLQAGP--------- 298
Cdd:pfam00171 247 DADLDAAVEAAVFGAFgnagQV---CTATSRLLVHESIYDEFVEKLVEAAK----KLKVGDPLDPDTDMGPliskaqler 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 299 ------------AKVVAVKAEEYDDEFL----SLD-----------------LNVKIVSDLDDAIAhiREHGTQ--HSDA 343
Cdd:pfam00171 320 vlkyvedakeegAKLLTGGEAGLDNGYFveptVLAnvtpdmriaqeeifgpvLSVIRFKDEEEAIE--IANDTEygLAAG 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446816049 344 ILTRDMRNAQRFVNEVDSSAVYVNASTRFTD-----GG--QFGLGAEVavstqklharGPMGLEALTTYKWI 408
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDAdglpfGGfkQSGFGREG----------GPYGLEEYTEVKTV 459
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
82-384 |
5.14e-11 |
|
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: 64.12 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 82 QVCNLADPVGQVIDGGVLDS---GLRLERRRVPLGVIGVIyeaRP-NVTVDV----ASLCLKTGNAVILRGGKETCRTNA 153
Cdd:cd07086 101 DICDYAVGLSRMLYGLTIPSerpGHRLMEQWNPLGVVGVI---TAfNFPVAVpgwnAAIALVCGNTVVWKPSETTPLTAI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 154 ATVAVIQDALKSCGLPAGAVQAIDnpDRALVSEMLRMDKYIDMLIPRG----GAGLHKLCREQSTIPVITGGiGVCHIYV 229
Cdd:cd07086 178 AVTKILAEVLEKNGLPPGVVNLVT--GGGDGGELLVHDPRVPLVSFTGstevGRRVGETVARRFGRVLLELG-GNNAIIV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 230 DESAEIAEALKVIVNA--KT--QRpstCNTVETLLVNKNIADSFLPALSK------------------------------ 275
Cdd:cd07086 255 MDDADLDLAVRAVLFAavGTagQR---CTTTRRLIVHESVYDEFLERLVKaykqvrigdpldegtlvgplinqaavekyl 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 276 ----QMAESGVTLHADAAALAQLQAG----PAKV--VAVKAEEYDDEFLSLDLNVKIVSDLDDAIAHIREHGTQHSDAIL 345
Cdd:cd07086 332 naieIAKSQGGTVLTGGKRIDGGEPGnyvePTIVtgVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIF 411
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446816049 346 TRDMRNAQRFVNEVDSSA--VYVNASTrftdggqfgLGAEV 384
Cdd:cd07086 412 TEDLREAFRWLGPKGSDCgiVNVNIPT---------SGAEI 443
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
111-281 |
1.45e-09 |
|
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: 59.59 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 111 PLGVI-GVIYEARPNVTVDVASL-CLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPDRALvSEML 188
Cdd:cd07081 95 PIGVVaSITPSTNPTSTVIFKSLiSLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIEL-AQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 189 RMDKYIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIYVDESAEIAEALKVIVNAKT-QRPSTCNTVETLLVNKNIAD 267
Cdd:cd07081 174 MKFPGIGLLLATGGPAVVKAAY-SSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTfDNGVICASEQSVIVVDSVYD 252
|
170
....*....|....
gi 446816049 268 sflpALSKQMAESG 281
Cdd:cd07081 253 ----EVMRLFEGQG 262
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
2-185 |
3.03e-09 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 58.71 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 2 LEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILnanaqdvadARAN---GLSEAMLD-RLALTPARLKGIA 77
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELV---------ARAHaetGLPEARLQgELGRTTGQLRLFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 78 DDVRQvcnlADPVGQVIDGGVLDSGL----RLERRRVPLGVIGVIyeARPNVTV-------DVASlCLKTGNAVILRGGK 146
Cdd:cd07129 72 DLVRE----GSWLDARIDPADPDRQPlprpDLRRMLVPLGPVAVF--GASNFPLafsvaggDTAS-ALAAGCPVVVKAHP 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446816049 147 ETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPDR----ALVS 185
Cdd:cd07129 145 AHPGTSELVARAIRAALRATGLPAGVFSLLQGGGRevgvALVK 187
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
8-273 |
1.09e-07 |
|
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: 53.59 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEamLDRLALTparLKGIADDVRQVcnla 87
Cdd:cd07094 29 TARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE--VDRAIDT---LRLAAEEAERI---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 dpVGQVIDGGVLD-SGLRLE-RRRVPLGVIGVI--YEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDAl 163
Cdd:cd07094 100 --RGEEIPLDATQgSDNRLAwTIREPVGVVLAItpFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEA- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 164 kscGLPAGAVQAIdNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVIT---GGIGVChiYVDESAEIAEALK 240
Cdd:cd07094 177 ---GVPEGVLQVV-TGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIAlelGGNAPV--IVDRDADLDAAIE 250
|
250 260 270
....*....|....*....|....*....|....
gi 446816049 241 VIVN-AKTQRPSTCNTVETLLVNKNIADSFLPAL 273
Cdd:cd07094 251 ALAKgGFYHAGQVCISVQRIYVHEELYDEFIEAF 284
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-372 |
1.37e-07 |
|
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: 53.37 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAmlDRLALTparLKGIADDVRQVcnla 87
Cdd:cd07149 29 AAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV--DRAIET---LRLSAEEAKRL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 dpVGQVIDggvLDSGLRLERR-----RVPLGVIGVI--YEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQ 160
Cdd:cd07149 100 --AGETIP---FDASPGGEGRigftiREPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 161 DAlkscGLPAGAVQAIDNPdRALVSEMLRMDKYIDMLIPRGG----------AGLHKLCRE-QSTIPVItggigvchiyV 229
Cdd:cd07149 175 EA----GLPKGALNVVTGS-GETVGDALVTDPRVRMISFTGSpavgeaiarkAGLKKVTLElGSNAAVI----------V 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 230 DESAEIAEALKVIVN-AKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAesgvTLHADAAALAQLQAGP--AKVVAVKA 306
Cdd:cd07149 240 DADADLEKAVERCVSgAFANAGQVCISVQRIFVHEDIYDEFLERFVAATK----KLVVGDPLDEDTDVGPmiSEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 307 EEYDDEFLSL-----------------------DLNVKIV--------------SDLDDAIAHIRE--HGTQHsdAILTR 347
Cdd:cd07149 316 EEWVEEAVEGgarlltggkrdgaileptvltdvPPDMKVVceevfapvvslnpfDTLDEAIAMANDspYGLQA--GVFTN 393
|
410 420
....*....|....*....|....*
gi 446816049 348 DMRNAQRFVNEVDSSAVYVNASTRF 372
Cdd:cd07149 394 DLQKALKAARELEVGGVMINDSSTF 418
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
8-388 |
1.58e-07 |
|
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: 53.12 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVA----DARANglseamLDRLALTparLKGIADDVRQV 83
Cdd:cd07145 29 VAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGkpikQSRVE------VERTIRL---FKLAAEEAKVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 84 cnladpVGQVIDggvLDSGLRLERR-----RVPLGVIGVI--YEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATV 156
Cdd:cd07145 100 ------RGETIP---VDAYEYNERRiaftvREPIGVVGAItpFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 157 AVIQDAlkscGLPAGAVQAIDNPDRALVSEMLRMDKyIDMLIPRGGA--GLHKLCREQSTIPVITGGIG-VCHIYVDESA 233
Cdd:cd07145 171 KILEEA----GLPPGVINVVTGYGSEVGDEIVTNPK-VNMISFTGSTavGLLIASKAGGTGKKVALELGgSDPMIVLKDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 234 EIAEALKVIVNAK-TQRPSTCNTVETLLVNKNIADSFL-----------------------PALSKQMAE---------- 279
Cdd:cd07145 246 DLERAVSIAVRGRfENAGQVCNAVKRILVEEEVYDKFLkllvekvkklkvgdpldestdlgPLISPEAVErmenlvndav 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 280 -SGVTLHADAAALAQLQAGPAKVVAVKAEE--YDDEFLSLDLNVKIVSDLDDA--IAHIREHGTQHSdaILTRDMRNAQR 354
Cdd:cd07145 326 eKGGKILYGGKRDEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDEEAveIANSTEYGLQAS--VFTNDINRALK 403
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446816049 355 FVNEVDSSAVYVNASTRF-TD----GG--QFGLGAEVAVST 388
Cdd:cd07145 404 VARELEAGGVVINDSTRFrWDnlpfGGfkKSGIGREGVRYT 444
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
8-279 |
1.79e-07 |
|
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: 52.97 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGL---SEAmLDRLALTPARLKGIADDVRqvc 84
Cdd:cd07125 77 IAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADaevREA-IDFCRYYAAQARELFSDPE--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 85 nLADPVGQVidggvldSGLRLERRRV---------PLGV-IGVIYEArpnvtvdvaslcLKTGNAVILRGGKETCRTNAA 154
Cdd:cd07125 153 -LPGPTGEL-------NGLELHGRGVfvcispwnfPLAIfTGQIAAA------------LAAGNTVIAKPAEQTPLIAAR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 155 TVAVIQDAlkscGLPAGAVQAIDnPDRALVSEMLRMDKYIDMLIPRGG----AGLHKLC--REQSTIPVI--TGGIGVch 226
Cdd:cd07125 213 AVELLHEA----GVPRDVLQLVP-GDGEEIGEALVAHPRIDGVIFTGStetaKLINRALaeRDGPILPLIaeTGGKNA-- 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446816049 227 IYVDESAEIAEALK-VIVNAKT---QRpstCNTVETLLVNKNIADSFLPALSKQMAE 279
Cdd:cd07125 286 MIVDSTALPEQAVKdVVQSAFGsagQR---CSALRLLYLQEEIAERFIEMLKGAMAS 339
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
8-384 |
2.32e-07 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 52.73 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESIlnanAQDVADARANGLSEAmldrlaltparlKGiadDVRQVCNLA 87
Cdd:cd07131 45 AAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEEL----ARLVTREMGKPLAEG------------RG---DVQEAIDMA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 DPV---GQVIDGGVLDSGLR---LERRRVPLGVIGVIYE-----ARPNVTVDVASLClktGNAVILRGGKETCRTNAATV 156
Cdd:cd07131 106 QYAageGRRLFGETVPSELPnkdAMTRRQPIGVVALITPwnfpvAIPSWKIFPALVC---GNTVVFKPAEDTPACALKLV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 157 AVIQDAlkscGLPAGAVQAIDNPDRAlVSEMLRMDKYIDMLIPRG----GAGLHKLCREQSTIPVITGGiGVCHIYVDES 232
Cdd:cd07131 183 ELFAEA----GLPPGVVNVVHGRGEE-VGEALVEHPDVDVVSFTGstevGERIGETCARPNKRVALEMG-GKNPIIVMDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 233 AEIAEALK-VIVNA-KT--QRpstCNTVETLLVNKNIADSFL-----------------------PALSKQMAES----- 280
Cdd:cd07131 257 ADLDLALEgALWSAfGTtgQR---CTATSRLIVHESVYDEFLkrfverakrlrvgdgldeetdmgPLINEAQLEKvlnyn 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 281 ----GVTLHADAAALAQLQAGPAK----------VVAVKAEEYDDEFLSLDLNVKIVSDLDDAIAHIREHGTQHSDAILT 346
Cdd:cd07131 334 eigkEEGATLLLGGERLTGGGYEKgyfveptvftDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYT 413
|
410 420 430
....*....|....*....|....*....|....*...
gi 446816049 347 RDMRNAQRFVNEVDSSAVYVNASTrftdggqfgLGAEV 384
Cdd:cd07131 414 EDVNKAFRARRDLEAGITYVNAPT---------IGAEV 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
27-371 |
4.64e-07 |
|
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: 51.80 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 27 VLEKIADELEAQSESILNANAQDVADARANGLSE--AMLDRLALTPARLKGIaddvrqvcnlaDPVGQVIDGGVLDSGLR 104
Cdd:cd07082 66 CLHKFADLLKENKEEVANLLMWEIGKTLKDALKEvdRTIDYIRDTIEELKRL-----------DGDSLPGDWFPGTKGKI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 105 LERRRVPLGVIGVI----YearP-NVTVDVASLCLKTGNAVILRggketcrtnAATVAVIQ-----DALKSCGLPAGAVQ 174
Cdd:cd07082 135 AQVRREPLGVVLAIgpfnY---PlNLTVSKLIPALIMGNTVVFK---------PATQGVLLgiplaEAFHDAGFPKGVVN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 175 AIDNPDRAlVSEMLRMDKYIDMLIPRGG-AGLHKLCREQSTIPVITG-GIGVCHIyVDESAEIAEALKVIVNAKT----Q 248
Cdd:cd07082 203 VVTGRGRE-IGDPLVTHGRIDVISFTGStEVGNRLKKQHPMKRLVLElGGKDPAI-VLPDADLELAAKEIVKGALsysgQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 249 RpstCNTVETLLVNKNIADSFLPALSKQMA----------------------------------ESGVTLHADAAALAQL 294
Cdd:cd07082 281 R---CTAIKRVLVHESVADELVELLKEEVAklkvgmpwdngvditplidpksadfvegliddavAKGATVLNGGGREGGN 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 295 QAGPAKVVAVKAEEY---DDEFLSLdLNVKIVSDLDDAIAHI--REHGTQHSdaILTRDMRNAQRFVNEVDSSAVYVNAS 369
Cdd:cd07082 358 LIYPTLLDPVTPDMRlawEEPFGPV-LPIIRVNDIEEAIELAnkSNYGLQAS--IFTKDINKARKLADALEVGTVNINSK 434
|
..
gi 446816049 370 TR 371
Cdd:cd07082 435 CQ 436
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
8-176 |
2.16e-06 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 49.45 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEaqsesilnANAQDVAD--ARANG--LSEAMLDrlaltparLKGIADDVRQV 83
Cdd:cd07106 27 AAKAAFPGWSATPLEERRAALLAIADAIE--------ANAEELARllTLEQGkpLAEAQFE--------VGGAVAWLRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 84 CNLADPVgQVIDggvLDSGLRLERRRVPLGVIGVIYearP-NVTVDVASL----CLKTGNAVILRGGKETCRTNAATVAV 158
Cdd:cd07106 91 ASLDLPD-EVIE---DDDTRRVELRRKPLGVVAAIV---PwNFPLLLAAWkiapALLAGNTVVLKPSPFTPLCTLKLGEL 163
|
170
....*....|....*...
gi 446816049 159 IQDAlkscgLPAGAVQAI 176
Cdd:cd07106 164 AQEV-----LPPGVLNVV 176
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
8-176 |
9.05e-06 |
|
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: 47.63 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESIlnanaqdvadarANGLSEAMLDRLALTPARLKGIADDVRQVCNLA 87
Cdd:cd07102 26 RARAAQKGWRAVPLEERKAIVTRAVELLAANTDEI------------AEELTWQMGRPIAQAGGEIRGMLERARYMISIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 DPVGQVIDGGvLDSGLRLERRRVPLGVIGVIyeARPN----VTVDVASLCLKTGNAVILrggKETCRTnAATVAVIQDAL 163
Cdd:cd07102 94 EEALADIRVP-EKDGFERYIRREPLGVVLII--APWNypylTAVNAVIPALLAGNAVIL---KHSPQT-PLCGERFAAAF 166
|
170
....*....|...
gi 446816049 164 KSCGLPAGAVQAI 176
Cdd:cd07102 167 AEAGLPEGVFQVL 179
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
8-174 |
2.52e-05 |
|
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: 46.37 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAmldrlALTPARLKGIADDVRQVcnla 87
Cdd:cd07104 8 AAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEV-----GAAIAILREAAGLPRRP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 dpvgqviDGGVLDSGL--RLER-RRVPLGVIGVIyeaRP-----NVTVDVASLCLKTGNAVILRGGKETCRTNAATVA-V 158
Cdd:cd07104 79 -------EGEILPSDVpgKESMvRRVPLGVVGVI---SPfnfplILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAeI 148
|
170
....*....|....*.
gi 446816049 159 IQDAlkscGLPAGAVQ 174
Cdd:cd07104 149 FEEA----GLPKGVLN 160
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
4-278 |
4.34e-05 |
|
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: 45.41 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 4 QMGIAAKQASYKLAQLSS--REKNRVLEKIADELEAQSESILNANAQDvadaraNG--LSEAMLDrlaltparLKGIADD 79
Cdd:cd07120 22 EAAIAAARRAFDETDWAHdpRLRARVLLELADAFEANAERLARLLALE------NGkiLGEARFE--------ISGAISE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 80 VRQVCNLADPV-GQVID--GGVLDSGLrlerrRVPLGVIGVIYEARPNVTVDVASL--CLKTGNAVILRGGKETCRTNAA 154
Cdd:cd07120 88 LRYYAGLARTEaGRMIEpePGSFSLVL-----REPMGVAGIIVPWNSPVVLLVRSLapALAAGCTVVVKPAGQTAQINAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 155 tVAVIQDALKScgLPAGAVQAIDNPdRALVSEMLRMDKYIDML-----------IPRGGAG-LHKLCREqstipviTGGi 222
Cdd:cd07120 163 -IIRILAEIPS--LPAGVVNLFTES-GSEGAAHLVASPDVDVIsftgstatgraIMAAAAPtLKRLGLE-------LGG- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 223 GVCHIyVDESAEIAEALKVIVNAKT----QRpstCNTVETLLVNKNIADSFLPALSKQMA 278
Cdd:cd07120 231 KTPCI-VFDDADLDAALPKLERALTifagQF---CMAGSRVLVQRSIADEVRDRLAARLA 286
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
83-275 |
1.41e-04 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 43.73 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 83 VCNLAdpVGQ--VIDGGVLDS---GLRLERRRVPLGVIGVIyeARPNVTVDV----ASLCLKTGNAVILRGGKETCRTNA 153
Cdd:cd07130 101 ICDFA--VGLsrQLYGLTIPSerpGHRMMEQWNPLGVVGVI--TAFNFPVAVwgwnAAIALVCGNVVVWKPSPTTPLTAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 154 ATVAVIQDALKSCGLPAGAVQAI-----------DNPDRALVS-----EMLRmdKYIDMLIPRGGAGLHKLcreqstipv 217
Cdd:cd07130 177 AVTKIVARVLEKNGLPGAIASLVcggadvgealvKDPRVPLVSftgstAVGR--QVGQAVAARFGRSLLEL--------- 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446816049 218 itGGIGVchIYVDESAEIAEALKVIVNAKT----QRpstCNTVETLLVNKNIADSFLPALSK 275
Cdd:cd07130 246 --GGNNA--IIVMEDADLDLAVRAVLFAAVgtagQR---CTTTRRLIVHESIYDEVLERLKK 300
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
8-370 |
1.80e-04 |
|
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: 43.33 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAqsesilnanaqdvadaRANGLSEAMLDRLALTPA----RLKGIADDVRQV 83
Cdd:cd07105 8 AAAAAFPAWSKTPPSERRDILLKAADLLES----------------RRDEFIEAMMEETGATAAwagfNVDLAAGMLREA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 84 CNLADpvgQVIDGGV--LDSGLRLERRRVPLGVIGVIyeARPN--VTVDVASLC--LKTGNAVILRGGKETCRTNAATVA 157
Cdd:cd07105 72 ASLIT---QIIGGSIpsDKPGTLAMVVKEPVGVVLGI--APWNapVILGTRAIAypLAAGNTVVLKASELSPRTHWLIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 158 VIQDAlkscGLPAGAVQAIDN-PDRAlvsemlrmDKYIDMLIPrggaglHKLCRE----QSTIpviTGGI---------- 222
Cdd:cd07105 147 VFHEA----GLPKGVLNVVTHsPEDA--------PEVVEALIA------HPAVRKvnftGSTR---VGRIiaetaakhlk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 223 -------GVCHIYVDESAEIAEALKVIV-NAKTQRPSTCNTVETLLVNKNIADSFLPAL---SKQMAESGVTLHADAAAL 291
Cdd:cd07105 206 pvllelgGKAPAIVLEDADLDAAANAALfGAFLNSGQICMSTERIIVHESIADEFVEKLkaaAEKLFAGPVVLGSLVSAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 292 AQLQAGP---------AKVVAVKAEE----------------------YDDEFLSLDLNVKIVSDLDDAIAHIREHGTQH 340
Cdd:cd07105 286 AADRVKElvddalskgAKLVVGGLADespsgtsmpptildnvtpdmdiYSEESFGPVVSIIRVKDEEEAVRIANDSEYGL 365
|
410 420 430
....*....|....*....|....*....|
gi 446816049 341 SDAILTRDMRNAQRFVNEVDSSAVYVNAST 370
Cdd:cd07105 366 SAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
8-173 |
3.33e-04 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 42.55 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADArangLSEAM---LDRLAltpARLKGIADDVRQVC 84
Cdd:cd07093 27 AAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKP----ITLARtrdIPRAA---ANFRFFADYILQLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 85 NLADPVgqviDGGVLDSGLrlerrRVPLGVIGVIyeaRP-NV-----TVDVASlCLKTGNAVILRGGKETCRTNAATVAV 158
Cdd:cd07093 100 GESYPQ----DGGALNYVL-----RQPVGVAGLI---TPwNLplmllTWKIAP-ALAFGNTVVLKPSEWTPLTAWLLAEL 166
|
170
....*....|....*
gi 446816049 159 IQDAlkscGLPAGAV 173
Cdd:cd07093 167 ANEA----GLPPGVV 177
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
8-176 |
3.54e-04 |
|
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: 42.73 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESIlnanAQDVADARANGLSeamldrlalTPAR--LKGIADDVRQVCN 85
Cdd:cd07108 27 AAKAAFPEWAATPARERGKLLARIADALEARSEEL----ARLLALETGNALR---------TQARpeAAVLADLFRYFGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 86 LADPV-GQVIDGGvldSGLRLERRRVPLGVIGVIYearP-NVTVDVASL----CLKTGNAVILRGGKEtcrtnaATVAVI 159
Cdd:cd07108 94 LAGELkGETLPFG---PDVLTYTVREPLGVVGAIL---PwNAPLMLAALkiapALVAGNTVVLKAAED------APLAVL 161
|
170
....*....|....*...
gi 446816049 160 QDA-LKSCGLPAGAVQAI 176
Cdd:cd07108 162 LLAeILAQVLPAGVLNVI 179
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
1-276 |
4.83e-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: 42.23 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 1 MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARAngLSEAMLDRLALTparLKGIADDV 80
Cdd:cd07147 22 DIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIK--DARGEVARAIDT---FRIAAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 81 RQvcnladpvgqvIDGGVLD-------SGLRLERRRVPLGVIGVI--YEARPNVTVDVASLCLKTGNAVILrggKETCRT 151
Cdd:cd07147 97 TR-----------IYGEVLPldisargEGRQGLVRRFPIGPVSAItpFNFPLNLVAHKVAPAIAAGCPFVL---KPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 152 nAATVAVIQDALKSCGLPAGAVQAI--DNPDralvSEMLRMDKYIDMLI----PRGG------AGLHKLCREqstipviT 219
Cdd:cd07147 163 -PLSALILGEVLAETGLPKGAFSVLpcSRDD----ADLLVTDERIKLLSftgsPAVGwdlkarAGKKKVVLE-------L 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446816049 220 GGIGVChiYVDESAEIAEALKVIVN-AKTQRPSTCNTVETLLVNKNIADSFLPALSKQ 276
Cdd:cd07147 231 GGNAAV--IVDSDADLDFAAQRIIFgAFYQAGQSCISVQRVLVHRSVYDEFKSRLVAR 286
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
100-244 |
6.78e-04 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 41.84 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 100 DSGLRLERRrVPLGVIGVIYEA-RPNVTVDVASL-CLKTGNAVILR---GGKETCrtnAATVAVIQDALKSCGLPAGAVQ 174
Cdd:cd07121 87 DNGLTLVEY-APFGVIGAITPStNPTETIINNSIsMLAAGNAVVFNphpGAKKVS---AYAVELINKAIAEAGGPDNLVV 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 175 AIDNPDRALVSEMLRMDKyIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIYVDESAEIAEALKVIVN 244
Cdd:cd07121 163 TVEEPTIETTNELMAHPD-INLLVVTGGPAVVKAAL-SSGKKAIGAGAGNPPVVVDETADIEKAARDIVQ 230
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
8-173 |
2.54e-03 |
|
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: 39.92 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSEsilnanaqdvadaranglseamldRLALTPARLKGIAddvrqvcnLA 87
Cdd:cd07097 45 AAAAAFPAWRRTSPEARADILDKAGDELEARKE------------------------ELARLLTREEGKT--------LP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 DPVGQV----------------IDGGVLDS---GLRLERRRVPLGVIGVI-----------YEARPnvtvdvaslCLKTG 137
Cdd:cd07097 93 EARGEVtragqifryyagealrLSGETLPStrpGVEVETTREPLGVVGLItpwnfpiaipaWKIAP---------ALAYG 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 446816049 138 NAVILRGGKETcrtnAATVAVIQDALKSCGLPAGAV 173
Cdd:cd07097 164 NTVVFKPAELT----PASAWALVEILEEAGLPAGVF 195
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
8-196 |
2.55e-03 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 39.97 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDVADARANGLSEAmldRLALTparlkgiadDVRQVCNLA 87
Cdd:cd07152 21 RAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEV---GAAIG---------ELHEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 88 -DPVGQVIDGGvldSGLRLERRRVPLGVIGVIYEARPNVTVDVASL--CLKTGNAVILrggKETCRTNAATVAVIQDALK 164
Cdd:cd07152 89 tQPQGEILPSA---PGRLSLARRVPLGVVGVISPFNFPLILAMRSVapALALGNAVVL---KPDPRTPVSGGVVIARLFE 162
|
170 180 190
....*....|....*....|....*....|..
gi 446816049 165 SCGLPAGAVQAIdnPDRALVSEMLRMDKYIDM 196
Cdd:cd07152 163 EAGLPAGVLHVL--PGGADAGEALVEDPNVAM 192
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
8-173 |
4.22e-03 |
|
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: 39.26 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 8 AAKQASYKLAQLSSREKNRVLEKIADELEAQSESILNANAQDvadaraNG--LSEAM--LDRLALTPARLKGIADDVRQV 83
Cdd:cd07110 27 AARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARD------NGkpLDEAAwdVDDVAGCFEYYADLAEQLDAK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 84 CNLADPVGqvidggvlDSGLRLERRRVPLGVIGVI----YearPNVTV--DVASlCLKTGNAVILRGGKETCRTNAATVA 157
Cdd:cd07110 101 AERAVPLP--------SEDFKARVRREPVGVVGLItpwnF---PLLMAawKVAP-ALAAGCTVVLKPSELTSLTELELAE 168
|
170
....*....|....*.
gi 446816049 158 VIQDAlkscGLPAGAV 173
Cdd:cd07110 169 IAAEA----GLPPGVL 180
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
100-244 |
6.26e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 38.73 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 100 DSGLRLERRrVPLGVIGVIYEA-RPNVTVDVASL-CLKTGNAVILR---GGKETCrtnAATVAVIQDALKSCGLPAGAVQ 174
Cdd:PRK15398 119 DNGLTLIEY-APFGVIGAVTPStNPTETIINNAIsMLAAGNSVVFSphpGAKKVS---LRAIELLNEAIVAAGGPENLVV 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 175 AIDNPDRALVSEMLRMDKyIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIYVDESAEIAEALKVIVN 244
Cdd:PRK15398 195 TVAEPTIETAQRLMKHPG-IALLVVTGGPAVVKAAM-KSGKKAIGAGAGNPPVVVDETADIEKAARDIVK 262
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
7-273 |
7.18e-03 |
|
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: 38.49 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 7 IAAKQASYKlAQLSSREKNRVLEKIADELEAQSEsilnanaqDVAD--ARANGLSeamldrlaltparLKGIADDVRQVC 84
Cdd:cd07146 26 ALALAASYR-STLTRYQRSAILNKAAALLEARRE--------EFARliTLESGLC-------------LKDTRYEVGRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 85 NLADPV---GQVIDGGVLDSGL---RLERR----RVPLGVIGVIYE-ARP-NVTVDVASLCLKTGNAVILRGGKETcrtn 152
Cdd:cd07146 84 DVLRFAaaeALRDDGESFSCDLtanGKARKiftlREPLGVVLAITPfNHPlNQVAHKIAPAIAANNRIVLKPSEKT---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446816049 153 AATVAVIQDALKSCGLPAGAVQAIdNPDRALVSEMLRMDKYIDMLIPRGG----------AGLHKLCREqstipviTGGI 222
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVV-TGEPGEIGDELITHPDVDLVTFTGGvavgkaiaatAGYKRQLLE-------LGGN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446816049 223 GVchIYVDESAEIAEALKVIVNAKT----QRpstCNTVETLLVNKNIADSFLPAL 273
Cdd:cd07146 232 DP--LIVMDDADLERAATLAVAGSYansgQR---CTAVKRILVHESVADEFVDLL 281
|
|
| |
