|
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: 746.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 1 MLEQMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDV 80
Cdd:PRK00197 5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGIAEGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 81 RQVCNLADPVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQ 160
Cdd:PRK00197 85 RQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 161 QALQECGLPAAAVQAIESPDRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIPPALK 240
Cdd:PRK00197 165 EALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVDESADLDKALK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 241 IIVNAKTQRPSTCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPSALPALqngpAKVEPVKAEQYDDEYLSLDLNV 320
Cdd:PRK00197 245 IVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVELRGDEAALALL----PDVVPATEEDWDTEYLDLILAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 321 KVVTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLE 400
Cdd:PRK00197 321 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 400
|
410
....*....|....*..
gi 1513931114 401 ALTTYKWIGFGDDTIRA 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: 707.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 1 MLEQMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDV 80
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 81 RQVCNLADPVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQ 160
Cdd:COG0014 82 RQVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 161 QALQECGLPAAAVQAIESPDRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIPPALK 240
Cdd:COG0014 162 EALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRVVENATVPVIEHGDGNCHVYVDASADLEMAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 241 IIVNAKTQRPSTCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPSALPALQNgpakVEPVKAEQYDDEYLSLDLNV 320
Cdd:COG0014 242 IVVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAEAGVELRGDERTRAILPD----VKPATEEDWGTEYLDLILAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 321 KVVTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLE 400
Cdd:COG0014 318 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 397
|
410
....*....|....*..
gi 1513931114 401 ALTTYKWIGFGDDTIRA 417
Cdd:COG0014 398 ELTTYKYVVRGDGQIRP 414
|
|
| 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: 675.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 3 EQMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDVRQ 82
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 83 VCNLADPVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQA 162
Cdd:cd07079 81 VAALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 163 LQECGLPAAAVQAIESPDRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIPPALKII 242
Cdd:cd07079 161 LEEAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 243 VNAKTQRPSTCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPSALPALQNgpakVEPVKAEQYDDEYLSLDLNVKV 322
Cdd:cd07079 241 VNAKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGVELRGDEETLAILPG----AKPATEEDWGTEYLDLILAVKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 323 VTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEAL 402
Cdd:cd07079 317 VDSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEEL 396
|
410
....*....|
gi 1513931114 403 TTYKWIGFGD 412
Cdd:cd07079 397 TTYKYIVRGD 406
|
|
| 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: 633.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 9 AKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDVRQVCNLAD 88
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 89 PVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQECGL 168
Cdd:TIGR00407 81 PVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 169 PAAAVQAIESPDRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIPPALKIIVNAKTQ 248
Cdd:TIGR00407 161 PVGAVQLIETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 249 RPSTCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPSALPALQNGPAKVEPVKAEQYDDEYLSLDLNVKVVTDMDE 328
Cdd:TIGR00407 241 RPSTCNAIETLLVNKAIAREFLPVLENQLLEKGVTIHADAYALKLLELGPATEAIVCKTDFDKEFLSLDLSVKIVESLEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513931114 329 AIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYK 406
Cdd:TIGR00407 321 AIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
5-408 |
5.22e-112 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 344.40 E-value: 5.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 5 MGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDVRQVC 84
Cdd:PLN02418 299 MAVAARESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 85 NLADPVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQ 164
Cdd:PLN02418 379 DMEDPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 165 EC--GLPAAAVQAiespdRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIPPALKII 242
Cdd:PLN02418 459 KTvgGKLIGLVTS-----RDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIV 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 243 VNAKTQRPSTCNTVETLLVHRNIADT-FLPALSKQMAESGVTLHAAPSALPALQNgpakvepVKAEQYDDEYLSLDLNVK 321
Cdd:PLN02418 534 VDAKTDYPAACNAMETLLVHKDLVQNgGLNDLLVALRSAGVTLYGGPRASKLLNI-------PEAQSFHHEYSSLACTVE 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 322 VVTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEA 401
Cdd:PLN02418 607 IVDDVHAAIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEG 686
|
....*..
gi 1513931114 402 LTTYKWI 408
Cdd:PLN02418 687 LLTTRWI 693
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
5-415 |
2.39e-106 |
|
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: 329.56 E-value: 2.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 5 MGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDVRQVC 84
Cdd:TIGR01092 291 MAVAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAISLRQLA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 85 NLADPVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQ 164
Cdd:TIGR01092 371 AMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIP 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 165 ECGLpAAAVQAIESpdRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIPPALKIIVN 244
Cdd:TIGR01092 451 IHVG-KKLIGLVTS--REEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVDMAKRIVRD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 245 AKTQRPSTCNTVETLLVHRNIADT-FLPALSKQMAESGVTLHAAPSaLPALQngpaKVEPVKAEQYDDEYLSLDLNVKVV 323
Cdd:TIGR01092 528 AKCDYPAACNAMETLLVHKDLLRNgLLDDLIDMLRTEGVTIHGGPR-FAAYL----TFNISETKSFRTEYSSLACTVEIV 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 324 TDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALT 403
Cdd:TIGR01092 603 DDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLL 682
|
410
....*....|..
gi 1513931114 404 TYKWIGFGDDTI 415
Cdd:TIGR01092 683 TTRWLLRGKGQV 694
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
8-408 |
2.77e-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: 2.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANgLSEAMLDRLALTPARLSGIASDVRQVCNLA 87
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRS-LIANWIAMMGCSESKLYKNIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 88 DPVGQVidggLLDSGLRIERRRVPLGVIGVIYEAR-PNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQEC 166
Cdd:cd07077 81 GHIQDV----LLPDNGETYVRAFPIGVTMHILPSTnPLSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 167 GlPAAAVQAIESPDRALVGEMLKMDKyIDMLIPRGGAGLHKLCREQST-IPVITGGIGVCHIFVDETAEIPPALKIIVNA 245
Cdd:cd07077 157 G-PKILVLYVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 246 KTQRPSTCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPsaLPALQNGPAKVEPVKAEQYDDeyLSLDLNVKVVTD 325
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQET--KPLSKETTPSFDDEALESMTP--LECQFRVLDVIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 326 MDE-AIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARG-PMGLEALT 403
Cdd:cd07077 311 AVEnAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALR 390
|
....*
gi 1513931114 404 TYKWI 408
Cdd:cd07077 391 PLKRL 395
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
8-408 |
1.98e-30 |
|
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: 120.41 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEamldrLALTPARLSGIASDVRqvcnla 87
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGE-----VARAIDTFRYAAGLAD------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 88 DPVGQVIDggLLDSGLRIERRRVPLGVIGVI----YearP-NVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQA 162
Cdd:cd06534 71 KLGGPELP--SPDPGGEAYVRREPLGVVGVItpwnF---PlLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 163 lqecGLPAAAVQAIESPDRALVGEMLKMDKyIDMLIPRGGAGLHKLCRE---QSTIPVITGGIGVCHIFVDETAEIPPAL 239
Cdd:cd06534 146 ----GLPPGVVNVVPGGGDEVGAALLSHPR-VDKISFTGSTAVGKAIMKaaaENLKPVTLELGGKSPVIVDEDADLDAAV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 240 KIIVNAKT----QRpstCNTVETLLVHRNIADTFLPALskqmaesgVTLHAAPSALPALqngpAKVE---PVkaeqydde 312
Cdd:cd06534 221 EGAVFGAFfnagQI---CTAASRLLVHESIYDEFVEKL--------VTVLVDVDPDMPI----AQEEifgPV-------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 313 ylsldLNVKVVTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQF-------GLGAEVa 385
Cdd:cd06534 278 -----LPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPfggvknsGIGREG- 351
|
410 420
....*....|....*....|...
gi 1513931114 386 vstqklharGPMGLEALTTYKWI 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 |
5.58e-17 |
|
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: 82.15 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 110 VPLGVI-GVIYEARPNVTVDVASL-CLKTGNAAILRGGKETWRTNAATVKVIQQALQECGLPAAAVQAIESPDRALVGEM 187
Cdd:cd07122 94 EPVGVIaALIPSTNPTSTAIFKALiALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 188 LKmDKYIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIFVDETAEIPPALKIIVNAKTQRPST-CNTVETLLVHRNIA 266
Cdd:cd07122 174 MK-HPDVDLILATGGPGMVKAAY-SSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTiCASEQSVIVDDEIY 251
|
170
....*....|
gi 1513931114 267 DTFLPALSKQ 276
Cdd:cd07122 252 DEVRAELKRR 261
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
8-408 |
2.31e-15 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 77.57 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAA--SWqlALLSSREKNQVLEKIADyleaqtddILRANAEDLA--EARANG--LSEAMLDrlaltparLSGIASDVR 81
Cdd:pfam00171 37 AARAAfpAW--RKTPAAERAAILRKAAD--------LLEERKDELAelETLENGkpLAEARGE--------VDRAIDVLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 82 QVCNLADPV-GQVIDgglLDSGLRIERRRVPLGVIGVIYearP-NVTVDVASL----CLKTGNAAILRGGKETwrtnAAT 155
Cdd:pfam00171 99 YYAGLARRLdGETLP---SDPGRLAYTRREPLGVVGAIT---PwNFPLLLPAWkiapALAAGNTVVLKPSELT----PLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 156 VKVIQQALQECGLPAAAVQAIeSPDRALVGEMLKMDKYIDMLI----PRGGAGLHKLCrEQSTIPVI--TGGigVCHIFV 229
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVV-TGSGAEVGEALVEHPDVRKVSftgsTAVGRHIAEAA-AQNLKRVTleLGG--KNPLIV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 230 DETAEIPPALKIIVNAKT----QRpstCNTVETLLVHRNIADTFLPALSKQMAesgvTLHAAPSALPALQNGP------- 298
Cdd:pfam00171 245 LEDADLDAAVEAAVFGAFgnagQV---CTATSRLLVHESIYDEFVEKLVEAAK----KLKVGDPLDPDTDMGPliskaql 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 299 ----AKVEPVKAE----------QYDDEYL---SLDLNVK-------------VVT-----DMDEAIAhiREHGTQ--HS 341
Cdd:pfam00171 318 ervlKYVEDAKEEgaklltggeaGLDNGYFvepTVLANVTpdmriaqeeifgpVLSvirfkDEEEAIE--IANDTEygLA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513931114 342 DAILTRTLRNANRFINEVDSSAVYVNASTRFTD-----GG--QFGLGAEVavstqklharGPMGLEALTTYKWI 408
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDAdglpfGGfkQSGFGREG----------GPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
8-408 |
1.86e-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: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAA--SWqlALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARanglsEAMLDRLALTPARLSGIASDVRqvcn 85
Cdd:cd07078 6 AARAAfkAW--AALPPAERAAILRKLADLLEERREELAALETLETGKPI-----EEALGEVARAADTFRYYAGLAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 86 laDPVGQVIDggLLDSGLRIERRRVPLGVIGVIyeARPNVTVDVASL----CLKTGNAAILRGGKETWRTNAATVKVIQQ 161
Cdd:cd07078 75 --RLHGEVIP--SPDPGELAIVRREPLGVVGAI--TPWNFPLLLAAWklapALAAGNTVVLKPSELTPLTALLLAELLAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 162 AlqecGLPAAAVQAIESpDRALVGEMLKMDKYIDMLI----PRGGAGLHKLCrEQSTIPVI--TGGigVCHIFVDETAEI 235
Cdd:cd07078 149 A----GLPPGVLNVVTG-DGDEVGAALASHPRVDKISftgsTAVGKAIMRAA-AENLKRVTleLGG--KSPLIVFDDADL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 236 PPALKIIVNAKT----QRpstCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPSALPALQNGPAKVEPVKAE---- 307
Cdd:cd07078 221 DAAVKGAVFGAFgnagQV---CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYieda 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 308 -------QYDDEYLSLD----------------------------LNVKVVTDMDEAIAHI-REHGTQHSdAILTRTLRN 351
Cdd:cd07078 298 kaegaklLCGGKRLEGGkgyfvpptvltdvdpdmpiaqeeifgpvLPVIPFKDEEEAIELAnDTEYGLAA-GVFTRDLER 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513931114 352 ANRFINEVDSSAVYVNASTRFTD-----GG--QFGLGAEvavstqklhaRGPMGLEALTTYKWI 408
Cdd:cd07078 377 ALRVAERLEAGTVWINDYSVGAEpsapfGGvkQSGIGRE----------GGPYGLEEYTEPKTV 430
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
8-408 |
2.37e-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: 74.39 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRanaedlAEARANG--LSEAMLDrlaltparLSGIASDVRQVCN 85
Cdd:COG1012 51 AARAAFPAWAATPPAERAAILLRAADLLEERREELAA------LLTLETGkpLAEARGE--------VDRAADFLRYYAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 86 LADPV-GQVIDGGLldSGLRIERRRVPLGVIGVIyeaRP-NVTVDVASL----CLKTGNAAILRGGKETwrtnAATVKVI 159
Cdd:COG1012 117 EARRLyGETIPSDA--PGTRAYVRREPLGVVGAI---TPwNFPLALAAWklapALAAGNTVVLKPAEQT----PLSALLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 160 QQALQECGLPAAAVQAIESPDRAlVGEMLKMDKYIDMLI----PRGGAGLHKLCREQStIPVITGGIGVCHIFVDETAEI 235
Cdd:COG1012 188 AELLEEAGLPAGVLNVVTGDGSE-VGAALVAHPDVDKISftgsTAVGRRIAAAAAENL-KRVTLELGGKNPAIVLDDADL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 236 PPALKIIVNAKT----QRpstCNTVETLLVHRNIADTFLPALSKQMA--------------------------------- 278
Cdd:COG1012 266 DAAVEAAVRGAFgnagQR---CTAASRLLVHESIYDEFVERLVAAAKalkvgdpldpgtdmgpliseaqlervlayieda 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 279 -ESGVTLHAAPSALPAlqNGPAKVEPV-------KAEQYDDEY----LSldlnVKVVTDMDEAIAHIRehGTQH--SDAI 344
Cdd:COG1012 343 vAEGAELLTGGRRPDG--EGGYFVEPTvladvtpDMRIAREEIfgpvLS----VIPFDDEEEAIALAN--DTEYglAASV 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513931114 345 LTRTLRNANRFINEVDSSAVYVNASTRFTDGGQ-FG------LGAEvavstqklhaRGPMGLEALTTYKWI 408
Cdd:COG1012 415 FTRDLARARRVARRLEAGMVWINDGTTGAVPQApFGgvkqsgIGRE----------GGREGLEEYTETKTV 475
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
108-384 |
4.84e-13 |
|
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: 70.29 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 108 RRVPLGVIGVIyeaRP-NVTVDV----ASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQECGLPAAAVQAIESPDRa 182
Cdd:cd07086 130 QWNPLGVVGVI---TAfNFPVAVpgwnAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGD- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 183 lVGEMLKMDKYIDMLIPRG----GAGLHKLCREQSTIPVITGGiGVCHIFVDETAEIPPALKIIVNA--KT--QRpstCN 254
Cdd:cd07086 206 -GGELLVHDPRVPLVSFTGstevGRRVGETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRAVLFAavGTagQR---CT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 255 TVETLLVHRNIADTFLPALSK----------------------------------QMAESGVTLHAAPSALPALQNG--- 297
Cdd:cd07086 281 TTRRLIVHESVYDEFLERLVKaykqvrigdpldegtlvgplinqaavekylnaieIAKSQGGTVLTGGKRIDGGEPGnyv 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 298 -PAKVEPV--KAEQYDDEYLSLDLNVKVVTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSA--VYVNASTrf 372
Cdd:cd07086 361 ePTIVTGVtdDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSDCgiVNVNIPT-- 438
|
330
....*....|..
gi 1513931114 373 tdggqfgLGAEV 384
Cdd:cd07086 439 -------SGAEI 443
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
2-188 |
9.40e-11 |
|
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: 63.33 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 2 LEQMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDIL-RANAED-LAEARANGlsEamLDRlalTPARLSGIASD 79
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVaRAHAETgLPEARLQG--E--LGR---TTGQLRLFADL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 80 VRQvcnlADPVGQVIDGGLLDSGL----RIERRRVPLGVIGVIyeARPNVTV-------DVASlCLKTGNAAILRGGKET 148
Cdd:cd07129 74 VRE----GSWLDARIDPADPDRQPlprpDLRRMLVPLGPVAVF--GASNFPLafsvaggDTAS-ALAAGCPVVVKAHPAH 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1513931114 149 WRTNAATVKVIQQALQECGLPAAAVQAIESPDRAlVGEML 188
Cdd:cd07129 147 PGTSELVARAIRAALRATGLPAGVFSLLQGGGRE-VGVAL 185
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
8-384 |
5.73e-10 |
|
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: 60.82 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAED----LAEARANgLSEA--MLDRlaltparlsgIASDVR 81
Cdd:cd07131 45 AAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREmgkpLAEGRGD-VQEAidMAQY----------AAGEGR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 82 QvcnladPVGQVIDGGLLDSGLRIerRRVPLGVIGVIYE-----ARPNVTVDVASLClktGNAAILRGGKETwrtNAATV 156
Cdd:cd07131 114 R------LFGETVPSELPNKDAMT--RRQPIGVVALITPwnfpvAIPSWKIFPALVC---GNTVVFKPAEDT---PACAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 157 KVIQqALQECGLPAAAVQAIESPDRAlVGEMLKMDKYIDMLIPRG----GAGLHKLCREQSTIPVITGGiGVCHIFVDET 232
Cdd:cd07131 180 KLVE-LFAEAGLPPGVVNVVHGRGEE-VGEALVEHPDVDVVSFTGstevGERIGETCARPNKRVALEMG-GKNPIIVMDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 233 AEippaLKIIVNA------KT--QRpstCNTVETLLVHRNIADTFL-----------------------PALSKQMAES- 280
Cdd:cd07131 257 AD----LDLALEGalwsafGTtgQR---CTATSRLIVHESVYDEFLkrfverakrlrvgdgldeetdmgPLINEAQLEKv 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 281 ----------GVTLHAAPSALPalQNGPAK---VEPV-------KAEQYDDEYLSLDLNVKVVTDMDEAIAHIREHGTQH 340
Cdd:cd07131 330 lnyneigkeeGATLLLGGERLT--GGGYEKgyfVEPTvftdvtpDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGL 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1513931114 341 SDAILTRTLRNANRFINEVDSSAVYVNASTrftdggqfgLGAEV 384
Cdd:cd07131 408 SSAIYTEDVNKAFRARRDLEAGITYVNAPT---------IGAEV 442
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
111-379 |
9.57e-08 |
|
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: 53.75 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 111 PLGVIGVIyeARPNVTVDV----ASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQECGLPAAAVQAIESPdrALVGE 186
Cdd:cd07130 132 PLGVVGVI--TAFNFPVAVwgwnAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGG--ADVGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 187 MLKMDKYIDMLIPRGGAGLHKLCREQstipvITGGIGVC--------HIFVDETAEIPPALKIIVNAKT----QRpstCN 254
Cdd:cd07130 208 ALVKDPRVPLVSFTGSTAVGRQVGQA-----VAARFGRSllelggnnAIIVMEDADLDLAVRAVLFAAVgtagQR---CT 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 255 TVETLLVHRNIADTFLPALSK----------------------------------QMAESGVTLHAAPSAL--------P 292
Cdd:cd07130 280 TTRRLIVHESIYDEVLERLKKaykqvrigdplddgtlvgplhtkaavdnylaaieEAKSQGGTVLFGGKVIdgpgnyveP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 293 ALQNGPAKVEPVKAEQYddeylSLDLNVKVVTDMDEAIAHIREHGTQHSDAILTRTLRNANRFINEV--DSSAVYVNAST 370
Cdd:cd07130 360 TIVEGLSDAPIVKEETF-----APILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGT 434
|
330
....*....|
gi 1513931114 371 RFTD-GGQFG 379
Cdd:cd07130 435 SGAEiGGAFG 444
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
111-281 |
1.56e-07 |
|
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: 53.04 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 111 PLGVI-GVIYEARPNVTVDVASL-CLKTGNAAILRGGKETWRTNAATVKVIQQALQECGLPAAAVQAIESPDRALVGEML 188
Cdd:cd07081 95 PIGVVaSITPSTNPTSTVIFKSLiSLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 189 KMDKyIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIFVDETAEIPPALKIIVNAKT-QRPSTCNTVETLLVHRNIAD 267
Cdd:cd07081 175 KFPG-IGLLLATGGPAVVKAAY-SSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTfDNGVICASEQSVIVVDSVYD 252
|
170
....*....|....
gi 1513931114 268 tflpALSKQMAESG 281
Cdd:cd07081 253 ----EVMRLFEGQG 262
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
22-298 |
6.46e-07 |
|
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: 51.19 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 22 REKNQVLEKIADYLEAqtddilraNAEDLAE--ARANG--LSEAMLDrlaltparLSGIASDVRQVCNLADPV-GQVID- 95
Cdd:cd07120 42 RLRARVLLELADAFEA--------NAERLARllALENGkiLGEARFE--------ISGAISELRYYAGLARTEaGRMIEp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 96 -GGLLDSGLRierrrVPLGVIGVIYEARPNVTVDVASL--CLKTGNAAILRGGKETWRTNAATVKVIQQAlqeCGLPAAA 172
Cdd:cd07120 106 ePGSFSLVLR-----EPMGVAGIIVPWNSPVVLLVRSLapALAAGCTVVVKPAGQTAQINAAIIRILAEI---PSLPAGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 173 VQAIESPdRALVGEMLKMDKYIDML-----------IPRGGAG-LHKLCREqstipviTGGIGVCHIFVDetAEIPPALK 240
Cdd:cd07120 178 VNLFTES-GSEGAAHLVASPDVDVIsftgstatgraIMAAAAPtLKRLGLE-------LGGKTPCIVFDD--ADLDAALP 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513931114 241 IIVNAKT----QRpstCNTVETLLVHRNIADTFLPALSKQMAesgvTLHAAPSALPALQNGP 298
Cdd:cd07120 248 KLERALTifagQF---CMAGSRVLVQRSIADEVRDRLAARLA----AVKVGPGLDPASDMGP 302
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
8-188 |
8.35e-07 |
|
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: 50.99 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAA--SWqlALLSSREKNQVLEKIADyleaqtddILRANAEDLAE--ARANG--LSEAMLDrlaltparLSGIASDVR 81
Cdd:cd07106 27 AAKAAfpGW--SATPLEERRAALLAIAD--------AIEANAEELARllTLEQGkpLAEAQFE--------VGGAVAWLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 82 QVCNLADPVgQVIDgglLDSGLRIERRRVPLGVIGVIYearP-NVTVDVASL----CLKTGNAAILRGGKETWRTNAATV 156
Cdd:cd07106 89 YTASLDLPD-EVIE---DDDTRRVELRRKPLGVVAAIV---PwNFPLLLAAWkiapALLAGNTVVLKPSPFTPLCTLKLG 161
|
170 180 190
....*....|....*....|....*....|..
gi 1513931114 157 KVIQQAlqecgLPAAAVQAIESPDRalVGEML 188
Cdd:cd07106 162 ELAQEV-----LPPGVLNVVSGGDE--LGPAL 186
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
8-279 |
1.24e-06 |
|
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: 50.66 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGL---SEAmLDRLALTPARLSGIASDVRqvc 84
Cdd:cd07125 77 IAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADaevREA-IDFCRYYAAQARELFSDPE--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 85 nLADPVGQVidgglldSGLRIERRRV---------PLGV-IGVIYEArpnvtvdvaslcLKTGNAAILRGGKETWRTNAA 154
Cdd:cd07125 153 -LPGPTGEL-------NGLELHGRGVfvcispwnfPLAIfTGQIAAA------------LAAGNTVIAKPAEQTPLIAAR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 155 TVkviqQALQECGLPAAAVQAIeSPDRALVGEMLKMDKYIDMLIPRGG----AGLHKLC--REQSTIPVI--TGGIGVch 226
Cdd:cd07125 213 AV----ELLHEAGVPRDVLQLV-PGDGEEIGEALVAHPRIDGVIFTGStetaKLINRALaeRDGPILPLIaeTGGKNA-- 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513931114 227 IFVDETAEIPPALKIIV----NAKTQRpstCNTVETLLVHRNIADTFLPALSKQMAE 279
Cdd:cd07125 286 MIVDSTALPEQAVKDVVqsafGSAGQR---CSALRLLYLQEEIAERFIEMLKGAMAS 339
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
3-278 |
1.35e-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: 50.38 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 3 EQMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEArangLSEAMLDRLALTPARLSGIASDVRQ 82
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT----MVDASLGEILVTCEKIRWTLKHGEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 83 VcnLADpvgQVIDGGLLDSGLRIERRRVPLGVIGVI----YearP--NVTVDVASlCLKTGNAAILRGGKETWRTNAATV 156
Cdd:cd07098 97 A--LRP---ESRPGGLLMFYKRARVEYEPLGVVGAIvswnY---PfhNLLGPIIA-ALFAGNAIVVKVSEQVAWSSGFFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 157 KVIQQALQECGLPAAAVQAIesPDRALVGEMLKMDKYIDMLIPRGGAGLHKL---CREQSTIPVIT--GGIGVCHIFVDe 231
Cdd:cd07098 168 SIIRECLAACGHDPDLVQLV--TCLPETAEALTSHPVIDHITFIGSPPVGKKvmaAAAESLTPVVLelGGKDPAIVLDD- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1513931114 232 tAEIPPALKIIVNAKTQRP-STCNTVETLLVHRNIADTFLPALSKQMA 278
Cdd:cd07098 245 -ADLDQIASIIMRGTFQSSgQNCIGIERVIVHEKIYDKLLEILTDRVQ 291
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-279 |
7.93e-06 |
|
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: 47.98 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAED----LAEARANglseamLDRLALTpARLSgiASDVRQV 83
Cdd:cd07149 29 AAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEagkpIKDARKE------VDRAIET-LRLS--AEEAKRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 84 cnladpVGQVIDgglLDSGLRIERR-----RVPLGVIGVI--YEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATV 156
Cdd:cd07149 100 ------AGETIP---FDASPGGEGRigftiREPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 157 KVIQQAlqecGLPAAAVQAIESPdRALVGEMLKMDKYIDMLIPRGG----------AGLHKLCRE-QSTIPVItggigvc 225
Cdd:cd07149 171 ELLLEA----GLPKGALNVVTGS-GETVGDALVTDPRVRMISFTGSpavgeaiarkAGLKKVTLElGSNAAVI------- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1513931114 226 hifVDETAEIPPALKIIVN-AKTQRPSTCNTVETLLVHRNIADTFLPALSKQMAE 279
Cdd:cd07149 239 ---VDADADLEKAVERCVSgAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK 290
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
8-196 |
9.69e-06 |
|
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: 47.67 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEamldrlaltparLSGIASDVRQVCNLA 87
Cdd:cd07152 21 RAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFE------------VGAAIGELHEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 88 -DPVGQVIDGGlldSGLRIERRRVPLGVIGVIYEARPNVTVDVASL--CLKTGNAAILrggKETWRTNAATVKVIQQALQ 164
Cdd:cd07152 89 tQPQGEILPSA---PGRLSLARRVPLGVVGVISPFNFPLILAMRSVapALALGNAVVL---KPDPRTPVSGGVVIARLFE 162
|
170 180 190
....*....|....*....|....*....|..
gi 1513931114 165 ECGLPAAAVQAIesPDRALVGEMLKMDKYIDM 196
Cdd:cd07152 163 EAGLPAGVLHVL--PGGADAGEALVEDPNVAM 192
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
19-388 |
9.75e-06 |
|
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: 47.73 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 19 LSSREKNQVLEKIADyleaqtddILRANAEDLAE--ARANGL----SEAMLDRlALTPARLSgiASDVRQVcnladpVGQ 92
Cdd:cd07145 40 LPAYKRYKILMKVAE--------LIERRKEELAKllTIEVGKpikqSRVEVER-TIRLFKLA--AEEAKVL------RGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 93 VIDgglLDSGLRIERR-----RVPLGVIGVI--YEARPNVTVDVASLCLKTGNAAILRGGKETwrtnAATVKVIQQALQE 165
Cdd:cd07145 103 TIP---VDAYEYNERRiaftvREPIGVVGAItpFNFPANLFAHKIAPAIAVGNSVVVKPSSNT----PLTAIELAKILEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 166 CGLPAAAVQAIeSPDRALVG-EMLKMDKyIDMLIPRGGA--GLHKLCREQSTIPVIT---GGIGVCHIFVDetAEIPPAL 239
Cdd:cd07145 176 AGLPPGVINVV-TGYGSEVGdEIVTNPK-VNMISFTGSTavGLLIASKAGGTGKKVAlelGGSDPMIVLKD--ADLERAV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 240 KIIVNAK-TQRPSTCNTVETLLVHRNIADTFL-----------------------PALSKQMAE-----------SGVTL 284
Cdd:cd07145 252 SIAVRGRfENAGQVCNAVKRILVEEEVYDKFLkllvekvkklkvgdpldestdlgPLISPEAVErmenlvndaveKGGKI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 285 HAAPSALPALQNGPAKVEPVKAEQ--YDDEYLSLDLNVKVVTDMDEA--IAHIREHGTQHSdaILTRTLRNANRFINEVD 360
Cdd:cd07145 332 LYGGKRDEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDEEAveIANSTEYGLQAS--VFTNDINRALKVARELE 409
|
410 420 430
....*....|....*....|....*....|....*
gi 1513931114 361 SSAVYVNASTRF-TD----GG--QFGLGAEVAVST 388
Cdd:cd07145 410 AGGVVINDSTRFrWDnlpfGGfkKSGIGREGVRYT 444
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
8-196 |
1.41e-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: 47.14 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSE-----AMLDRLALTPARLSG--IASDV 80
Cdd:cd07104 8 AAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEvgaaiAILREAAGLPRRPEGeiLPSDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 81 RQVCNLAdpvgqvidgglldsglrierRRVPLGVIGVIyeaRP-----NVTVDVASLCLKTGNAAILrggKETWRTNAAT 155
Cdd:cd07104 88 PGKESMV--------------------RRVPLGVVGVI---SPfnfplILAMRSVAPALALGNAVVL---KPDSRTPVTG 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1513931114 156 VKVIQQALQECGLPAAAVQAIeSPDRALVGEMLKMDKYIDM 196
Cdd:cd07104 142 GLLIAEIFEEAGLPKGVLNVV-PGGGSEIGDALVEHPRVRM 181
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
17-273 |
6.02e-05 |
|
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: 45.02 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 17 ALLSSREKNQVLEKIADYLEAQTDDILRANAED----LAEARANGLSEAMLDRLALTPAR-LSGIASDvrqvcNL-ADPV 90
Cdd:cd07118 38 PRMSGAERAAVLLKVADLIRARRERLALIETLEsgkpISQARGEIEGAADLWRYAASLARtLHGDSYN-----NLgDDML 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 91 GQVIdgglldsglrierrRVPLGVIGVIyeaRP-NVTVDVAS----LCLKTGNAAILrggKETWRTNAATVKVIQQALqE 165
Cdd:cd07118 113 GLVL--------------REPIGVVGII---TPwNFPFLILSqklpFALAAGCTVVV---KPSEFTSGTTLMLAELLI-E 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 166 CGLPAAAVQaIESPDRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQST-----IPVITGGIGVCHIFVD---ETAEIPP 237
Cdd:cd07118 172 AGLPAGVVN-IVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAArnlkkVSLELGGKNPQIVFADadlDAAADAV 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 1513931114 238 ALKIIVNAKtqrpSTCNTVETLLVHRNIADTFLPAL 273
Cdd:cd07118 251 VFGVYFNAG----ECCNSGSRLLVHESIADAFVAAV 282
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-273 |
7.48e-05 |
|
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: 44.66 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 3 EQMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLdrlALTPARLSgiASDVRQ 82
Cdd:cd07146 21 EALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR---AADVLRFA--AAEALR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 83 vcnladpvgqvIDGGLLDSGL-------RIERRRVPLGVIGVIYE-ARP-NVTVDVASLCLKTGNAAILRGGKETWRTNA 153
Cdd:cd07146 96 -----------DDGESFSCDLtangkarKIFTLREPLGVVLAITPfNHPlNQVAHKIAPAIAANNRIVLKPSEKTPLSAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 154 ATVKViqqaLQECGLPAAAVQAIeSPDRALVGEMLKMDKYIDMLIPRGG----------AGLHKLCREqstipviTGGIG 223
Cdd:cd07146 165 YLADL----LYEAGLPPDMLSVV-TGEPGEIGDELITHPDVDLVTFTGGvavgkaiaatAGYKRQLLE-------LGGND 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1513931114 224 VchIFVDETAEIPPALKIIVNAKT----QRpstCNTVETLLVHRNIADTFLPAL 273
Cdd:cd07146 233 P--LIVMDDADLERAATLAVAGSYansgQR---CTAVKRILVHESVADEFVDLL 281
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
8-370 |
2.41e-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: 42.99 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADyleaqtddILRANAEDLAEAranGLSEAMLDRLALTPARLSGIASDVRQVCNLa 87
Cdd:cd07121 12 AAKAAQKQYRKCTLADREKIIEAIRE--------ALLSNAEELAEM---AVEETGMGRVEDKIAKNHLAAEKTPGTEDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 88 dpVGQVIDGgllDSGLRIERRrVPLGVIGVIYEA-RPNVTVDVASL-CLKTGNAAILR---GGKetwRTNAATVKVIQQA 162
Cdd:cd07121 80 --TTTAWSG---DNGLTLVEY-APFGVIGAITPStNPTETIINNSIsMLAAGNAVVFNphpGAK---KVSAYAVELINKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 163 LQECGLPAAAVQAIESPDRALVGEMLKMDKyIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHIFVDETAEIPPALKII 242
Cdd:cd07121 151 IAEAGGPDNLVVTVEEPTIETTNELMAHPD-INLLVVTGGPAVVKAAL-SSGKKAIGAGAGNPPVVVDETADIEKAARDI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 243 VN-AKTQRPSTCNTVETLLVHRNIADTFLPALSK------------QMAESGVTLHAAPSALPAL----------QNG-- 297
Cdd:cd07121 229 VQgASFDNNLPCIAEKEVIAVDSVADYLIAAMQRngayvlndeqaeQLLEVVLLTNKGATPNKKWvgkdaskilkAAGie 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 298 -PAKVEPVKAEQYDD------EYLSLDLNVKVVTDMDEAI--AHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNA 368
Cdd:cd07121 309 vPADIRLIIVETDKDhpfvveEQMMPILPVVRVKNFDEAIelAVELEHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNG 388
|
..
gi 1513931114 369 ST 370
Cdd:cd07121 389 PS 390
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
8-176 |
2.71e-04 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 43.00 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDIlranaedlaearANGLSEAMLDRLALTPARLSGIASDVRQVCNLA 87
Cdd:cd07102 26 RARAAQKGWRAVPLEERKAIVTRAVELLAANTDEI------------AEELTWQMGRPIAQAGGEIRGMLERARYMISIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 88 DPVGQVIDGGLlDSGLRIERRRVPLGVIGVIyeARPN----VTVDVASLCLKTGNAAILRGGKETwrtnAATVKVIQQAL 163
Cdd:cd07102 94 EEALADIRVPE-KDGFERYIRREPLGVVLII--APWNypylTAVNAVIPALLAGNAVILKHSPQT----PLCGERFAAAF 166
|
170
....*....|...
gi 1513931114 164 QECGLPAAAVQAI 176
Cdd:cd07102 167 AEAGLPEGVFQVL 179
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
111-273 |
2.75e-03 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 39.82 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 111 PLGVIGVIYEArpNVTVDV----ASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQECGLPAAAVQAIESPdrALVGE 186
Cdd:PLN02315 154 PLGIVGVITAF--NFPCAVlgwnACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGG--AEIGE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 187 MLKMDKYIDMLIPRGGAGLHKLCREQstipvITGGIGVC--------HIFVDETAEIPPALKII----VNAKTQRpstCN 254
Cdd:PLN02315 230 AIAKDTRIPLVSFTGSSKVGLMVQQT-----VNARFGKCllelsgnnAIIVMDDADIQLAVRSVlfaaVGTAGQR---CT 301
|
170
....*....|....*....
gi 1513931114 255 TVETLLVHRNIADTFLPAL 273
Cdd:PLN02315 302 TCRRLLLHESIYDDVLEQL 320
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
8-244 |
3.06e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 39.50 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADyleaqtddILRANAEDLAEARAN----GLSEAML--DRLA---------LTPAR 72
Cdd:PRK15398 44 AAKVAQQRYQQKSLAMRQRIIDAIRE--------ALLPHAEELAELAVEetgmGRVEDKIakNVAAaektpgvedLTTEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 73 LSGiasdvrqvcnladpvgqviDGGLLdsglRIERrrVPLGVIGVIYEA-RPNVTVDVASL-CLKTGNAAILR---GGKe 147
Cdd:PRK15398 116 LTG-------------------DNGLT----LIEY--APFGVIGAVTPStNPTETIINNAIsMLAAGNSVVFSphpGAK- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 148 twRTNAATVKVIQQALQECGLPAAAVQAIESPDRALVGEMLKMDKyIDMLIPRGGAGLHKLCReQSTIPVITGGIGVCHI 227
Cdd:PRK15398 170 --KVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPG-IALLVVTGGPAVVKAAM-KSGKKAIGAGAGNPPV 245
|
250
....*....|....*..
gi 1513931114 228 FVDETAEIPPALKIIVN 244
Cdd:PRK15398 246 VVDETADIEKAARDIVK 262
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
8-273 |
4.80e-03 |
|
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: 38.96 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 8 AAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAED----LAEARANGLSEAmldrlALTPARLSGIASDVRqv 83
Cdd:cd07115 27 AARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDtgkpIRAARRLDVPRA-----ADTFRYYAGWADKIE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 84 cnladpvGQVI--DGGLLDSglrieRRRVPLGVIGVIYearP-NVTVDVASL----CLKTGNAAILRGGKETWRTNAAtv 156
Cdd:cd07115 100 -------GEVIpvRGPFLNY-----TVREPVGVVGAIV---PwNFPLMFAAWkvapALAAGNTVVLKPAELTPLSALR-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513931114 157 kvIQQALQECGLPAAAVQAIESPDRAlVGEMLKMDKYIDML-----------IPRGGAG-LHKLCREqstipviTGGIGV 224
Cdd:cd07115 163 --IAELMAEAGFPAGVLNVVTGFGEV-AGAALVEHPDVDKItftgstavgrkIMQGAAGnLKRVSLE-------LGGKSA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1513931114 225 CHIFVD---ETAEIPPALKIIVNAKtqrpSTCNTVETLLVHRNIADTFLPAL 273
Cdd:cd07115 233 NIVFADadlDAAVRAAATGIFYNQG----QMCTAGSRLLVHESIYDEFLERF 280
|
|
| |
