|
Name |
Accession |
Description |
Interval |
E-value |
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
4-421 |
0e+00 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 756.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 4 SIEQYMQKVGQQAREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMDKGRSNQLDSALLDRLELTPARFKGM 83
Cdd:PRK00197 1 DIMEYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 84 LQGLKDVIALVDPIGEITDLAYRPTGIQIGKMRVPLGVVGMIYESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIA 163
Cdd:PRK00197 81 AEGLRQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 164 EAIKHGLKVAGLPEHSVQVIETSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQ 243
Cdd:PRK00197 161 AVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVDESADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 244 KALPITLNAKTHRYGVCNAMETLLVDEKIADVFLPHIAELYAEKQVELRGCPETRRILgASVKPATEEDWYTEYLGPILA 323
Cdd:PRK00197 241 KALKIVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVELRGDEAALALL-PDVVPATEEDWDTEYLDLILA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 324 VKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARGPVGL 403
Cdd:PRK00197 320 VKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGL 399
|
410
....*....|....*...
gi 491207823 404 EGLTSQKWIVLGDGQIRQ 421
Cdd:PRK00197 400 EELTTYKYIVLGDGQIRA 417
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
7-421 |
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: 751.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 7 QYMQKVGQQAREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMDKGRSNQLDSALLDRLELTPARFKGMLQG 86
Cdd:COG0014 1 AYLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 87 LKDVIALVDPIGEITDLAYRPTGIQIGKMRVPLGVVGMIYESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAI 166
Cdd:COG0014 81 LRQVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 167 KHGLKVAGLPEHSVQVIETSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKAL 246
Cdd:COG0014 161 QEALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRVVENATVPVIEHGDGNCHVYVDASADLEMAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 247 PITLNAKTHRYGVCNAMETLLVDEKIADVFLPHIAELYAEKQVELRGCPETRRILgASVKPATEEDWYTEYLGPILAVKV 326
Cdd:COG0014 241 DIVVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAEAGVELRGDERTRAIL-PDVKPATEEDWGTEYLDLILAVKV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 327 VSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGL 406
Cdd:COG0014 320 VDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEEL 399
|
410
....*....|....*
gi 491207823 407 TSQKWIVLGDGQIRQ 421
Cdd:COG0014 400 TTYKYVVRGDGQIRP 414
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
10-416 |
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: 688.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 10 QKVGQQAREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMDKGRSNQLDSALLDRLELTPARFKGMLQGLKD 89
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 90 VIALVDPIGEITDLAYRPTGIQIGKMRVPLGVVGMIYESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHG 169
Cdd:cd07079 81 VAALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 170 LKVAGLPEHSVQVIETSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKALPIT 249
Cdd:cd07079 161 LEEAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 250 LNAKTHRYGVCNAMETLLVDEKIADVFLPHIAELYAEKQVELRGCPETRRILGAsVKPATEEDWYTEYLGPILAVKVVSG 329
Cdd:cd07079 241 VNAKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGVELRGDEETLAILPG-AKPATEEDWGTEYLDLILAVKVVDS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 330 IDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSQ 409
Cdd:cd07079 320 LDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTY 399
|
....*..
gi 491207823 410 KWIVLGD 416
Cdd:cd07079 400 KYIVRGD 406
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
16-410 |
2.06e-167 |
|
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: 475.43 E-value: 2.06e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 16 AREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMDKGRSNQLDSALLDRLELTPARFKGMLQGLKDVIALVD 95
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 96 PIGEITDLAYRPTGIQIGKMRVPLGVVGMIYESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHGLKVAGL 175
Cdd:TIGR00407 81 PVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 176 PEHSVQVIETSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKALPITLNAKTH 255
Cdd:TIGR00407 161 PVGAVQLIETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 256 RYGVCNAMETLLVDEKIADVFLPHIAELYAEKQVELRGCPETRRIL---GASVKPATEEDWYTEYLGPILAVKVVSGIDE 332
Cdd:TIGR00407 241 RPSTCNAIETLLVNKAIAREFLPVLENQLLEKGVTIHADAYALKLLelgPATEAIVCKTDFDKEFLSLDLSVKIVESLEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491207823 333 AIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARGPVGLEGLTSQK 410
Cdd:TIGR00407 321 AIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
16-419 |
2.23e-106 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 329.76 E-value: 2.23e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 16 AREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMDKGRSNQLDSALLDRLELTPARFKGMLQGLKDVIALVD 95
Cdd:PLN02418 303 ARESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLADMED 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 96 PIGEI---TDLAyrpTGIQIGKMRVPLGVVGMIYESRPNVTLEAASLAIKSGNAIILRGGSEALESN----KAIAEAIKH 168
Cdd:PLN02418 383 PIGRVlkrTEVA---DGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNailhKVITDAIPK 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 169 --GLKVAGLpehsvqvieTSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKAL 246
Cdd:PLN02418 460 tvGGKLIGL---------VTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAK 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 247 PITLNAKTHRYGVCNAMETLLVDEKIAD--VFLPHIAELYAEKqVELRGCPETRRILGAsvkPATEEdWYTEYLGPILAV 324
Cdd:PLN02418 531 RIVVDAKTDYPAACNAMETLLVHKDLVQngGLNDLLVALRSAG-VTLYGGPRASKLLNI---PEAQS-FHHEYSSLACTV 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 325 KVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARGPVGLE 404
Cdd:PLN02418 606 EIVDDVHAAIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVE 685
|
410
....*....|....*
gi 491207823 405 GLTSQKWIVLGDGQI 419
Cdd:PLN02418 686 GLLTTRWILRGNGQV 700
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
6-419 |
3.28e-100 |
|
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: 313.77 E-value: 3.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 6 EQYMQKVGQQAREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMDKGRSNQLDSALLDRLELTPARFKGMLQ 85
Cdd:TIGR01092 285 QTGERDMAVAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 86 GLKDVIALVDPIGEITDLAYRPTGIQIGKMRVPLGVVGMIYESRPNVTLEAASLAIKSGNAIILRGGSEALESNkaiaeA 165
Cdd:TIGR01092 365 SLRQLAAMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSN-----A 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 166 IKHGLKVAGLPEHSVQ--VIETSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQ 243
Cdd:TIGR01092 440 ILHKVITEAIPIHVGKklIGLVTSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVD 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 244 KALPITLNAKTHRYGVCNAMETLLVDEKIADV-FLPHIAELYAEKQVELRGCPetRRILGASVKPATEEDWYTEYLGPIL 322
Cdd:TIGR01092 520 MAKRIVRDAKCDYPAACNAMETLLVHKDLLRNgLLDDLIDMLRTEGVTIHGGP--RFAAYLTFNISETKSFRTEYSSLAC 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 323 AVKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARGPVG 402
Cdd:TIGR01092 598 TVEIVDDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVG 677
|
410
....*....|....*..
gi 491207823 403 LEGLTSQKWIVLGDGQI 419
Cdd:TIGR01092 678 VEGLLTTRWLLRGKGQV 694
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
16-414 |
2.60e-49 |
|
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: 172.02 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 16 AREASRVLTSASTSLKNHALSAIYTALENNQAAILAANQIDMdKGRSNQLDSALLDRLELTPARFKGMLQGLKDVIALVD 95
Cdd:cd07077 3 AKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSER-GAYIRSLIANWIAMMGCSESKLYKNIDTERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 96 PIGEITdlayRPTGIQIGKMRVPLGVVGMIYESR-PNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHGLKvAG 174
Cdd:cd07077 82 HIQDVL----LPDNGETYVRAFPIGVTMHILPSTnPLSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADA-AH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 175 LPEHSVQVIETSDRAAVGHLITMAEyVDVIVPRGGKSLIERVTNEAR-IPVIKHLDGNCHVFVEAQADLQKALPITLNAK 253
Cdd:cd07077 157 GPKILVLYVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 254 THRYGVCNAMETLLVDEKIADVFLPHIAELYAEKQVELrgcPETRRILGASVKPaTEEDWYTEYLGPIL----AVKVVSG 329
Cdd:cd07077 236 FFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKV---PQETKPLSKETTP-SFDDEALESMTPLEcqfrVLDVISA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 330 IDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFADGFEYGLGAEIGISTDKIHARG-PVGLEGLTS 408
Cdd:cd07077 312 VENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRP 391
|
....*.
gi 491207823 409 QKWIVL 414
Cdd:cd07077 392 LKRLVR 397
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
81-414 |
6.08e-34 |
|
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: 130.04 E-value: 6.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 81 KGMLQGLKDVIALVDPIGEITDLAYRPTGIQI-----GKM----RVPLGVVGMIYESRP--NVTLEAASLAIKSGNAIIL 149
Cdd:cd06534 46 KPIEEALGEVARAIDTFRYAAGLADKLGGPELpspdpGGEayvrREPLGVVGVITPWNFplLLAAWKLAPALAAGNTVVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 150 RGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRAAVGHLITMAEYVDVIVPRGGKSLIERV---TNEARIPVIK 226
Cdd:cd06534 126 KPSELTPLTALALAELLQE----AGLPPGVVNVV-PGGGDEVGAALLSHPRVDKISFTGSTAVGKAImkaAAENLKPVTL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 227 HLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLLVDEKIADVFLPHIAELYAEkqvelrgcpetrrilgasV 305
Cdd:cd06534 201 ELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGqICTAASRLLVHESIYDEFVEKLVTVLVD------------------V 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 306 KPATEEdWYTEYLGPILAVKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFA-DGFEYGL 384
Cdd:cd06534 263 DPDMPI-AQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGG 341
|
330 340 350
....*....|....*....|....*....|
gi 491207823 385 GAEIGISTDKiharGPVGLEGLTSQKWIVL 414
Cdd:cd06534 342 VKNSGIGREG----GPYGLEEYTRTKTVVI 367
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
111-371 |
3.23e-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: 86.01 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 111 QIGKMRVPLGVV-GMIYESRPNVTLEAASL-AIKSGNAIILRGGSEALESNKAIAEAIKHGLKVAGLPEHSVQVIETSDR 188
Cdd:cd07122 88 GIVEIAEPVGVIaALIPSTNPTSTAIFKALiALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 189 AAVGHLITmAEYVDVIVPRGGKSLIeRVTNEARIPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYGV-CNAMETLL 267
Cdd:cd07122 168 ELTQELMK-HPDVDLILATGGPGMV-KAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTiCASEQSVI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 268 VDEKIADVFlphIAELyaekqvELRGC------------------------------------------PETRRILGASV 305
Cdd:cd07122 246 VDDEIYDEV---RAEL------KRRGAyflneeekeklekalfddggtlnpdivgksaqkiaelagievPEDTKVLVAEE 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207823 306 KPATEEDWYT-EYLGPILAVKVVSGIDEAID---HINKYGSH-HTDAIVTENYTLARQFLARVDSSSVVIN 371
Cdd:cd07122 317 TGVGPEEPLSrEKLSPVLAFYRAEDFEEALEkarELLEYGGAgHTAVIHSNDEEVIEEFALRMPVSRILVN 387
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
102-414 |
4.09e-17 |
|
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: 82.87 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 102 DLAYRPTGIQIGKMRVPLGVVGMI--YESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHS 179
Cdd:cd07094 107 DATQGSDNRLAWTIREPVGVVLAItpFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVE----AGVPEGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 180 VQVIeTSDRAAVGHLITMAEYVDVIVPRGGKSLIERVTNEARIP-VIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG 258
Cdd:cd07094 183 LQVV-TGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKrIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 259 -VCNAMETLLVDEKIADVFL-----------------------PHIAELYA---EKQVElRGCPETRRIL------GASV 305
Cdd:cd07094 262 qVCISVQRIYVHEELYDEFIeafvaavkklkvgdpldedtdvgPLISEEAAervERWVE-EAVEAGARLLcggerdGALF 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 306 KPATEED-------WYTEYLGPILAVKVVSGIDEAIDHIN--KYGSHhtDAIVTENYTLARQFLARVDSSSVVINASTRF 376
Cdd:cd07094 341 KPTVLEDvprdtklSTEETFGPVVPIIRYDDFEEAIRIANstDYGLQ--AGIFTRDLNVAFKAAEKLEVGGVMVNDSSAF 418
|
330 340 350
....*....|....*....|....*....|....*....
gi 491207823 377 -ADGFEYGLGAEIGISTDKIhargPVGLEGLTSQKWIVL 414
Cdd:cd07094 419 rTDWMPFGGVKESGVGREGV----PYAMEEMTEEKTVVI 453
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
115-412 |
1.43e-16 |
|
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: 81.42 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMI--YESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRAAVG 192
Cdd:pfam00171 123 RREPLGVVGAItpWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEE----AGLPAGVLNVV-TGSGAEVG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 193 HLITMAEYVDVIV----PRGGKSLIERVTnEARIPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLL 267
Cdd:pfam00171 198 EALVEHPDVRKVSftgsTAVGRHIAEAAA-QNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGqVCTATSRLL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 268 VDEKIADVFLPHIAELYA-------------------EKQVE----------------LRGCPETRRiLGASVKPATEED 312
Cdd:pfam00171 277 VHESIYDEFVEKLVEAAKklkvgdpldpdtdmgplisKAQLErvlkyvedakeegaklLTGGEAGLD-NGYFVEPTVLAN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 313 -------WYTEYLGPILAVKVVSGIDEAIDHIN--KYGshHTDAIVTENYTLARQFLARVDSSSVVINASTRFAD----- 378
Cdd:pfam00171 356 vtpdmriAQEEIFGPVLSVIRFKDEEEAIEIANdtEYG--LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdglpf 433
|
330 340 350
....*....|....*....|....*....|....*.
gi 491207823 379 -GF-EYGLGAEigistdkihaRGPVGLEGLTSQKWI 412
Cdd:pfam00171 434 gGFkQSGFGRE----------GGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
116-414 |
3.89e-16 |
|
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: 79.94 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIyeSRPNVTLE------AASLAikSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRA 189
Cdd:cd07078 94 REPLGVVGAI--TPWNFPLLlaawklAPALA--AGNTVVLKPSELTPLTALLLAELLAE----AGLPPGVLNVV-TGDGD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 190 AVGHLITMAEYVDVIV----PRGGKSLIERVTNEArIPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAME 264
Cdd:cd07078 165 EVGAALASHPRVDKISftgsTAVGKAIMRAAAENL-KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGqVCTAAS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 265 TLLVDEKIADVFLPHIAELYA--------------------------EKQVELRGCPETRRILGAS---------VKPAT 309
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKalkvgnpldpdtdmgplisaaqldrvLAYIEDAKAEGAKLLCGGKrleggkgyfVPPTV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 310 EED-------WYTEYLGPILAVKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRFAD---- 378
Cdd:cd07078 324 LTDvdpdmpiAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEpsap 403
|
330 340 350
....*....|....*....|....*....|....*....
gi 491207823 379 --GF-EYGLGAEigistdkihaRGPVGLEGLTSQKWIVL 414
Cdd:cd07078 404 fgGVkQSGIGRE----------GGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
116-376 |
2.52e-15 |
|
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: 77.39 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMI--YESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRAAVGH 193
Cdd:cd07145 121 REPIGVVGAItpFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEE----AGLPPGVINVV-TGYGSEVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 194 LITMAEYVDVIVPRGGKSLIERVTNEARIP---VIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLLVD 269
Cdd:cd07145 196 EIVTNPKVNMISFTGSTAVGLLIASKAGGTgkkVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGqVCNAVKRILVE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 270 EKIADVFLPHIAE--------------------------LYAEKQVE---------LRGcpeTRRILGASVKPATEED-- 312
Cdd:cd07145 276 EEVYDKFLKLLVEkvkklkvgdpldestdlgplispeavERMENLVNdavekggkiLYG---GKRDEGSFFPPTVLENdt 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207823 313 -----WYTEYLGPILAVKVVSGIDEAIDHIN--KYGSHhtDAIVTENYTLARQFLARVDSSSVVINASTRF 376
Cdd:cd07145 353 pdmivMKEEVFGPVLPIAKVKDDEEAVEIANstEYGLQ--ASVFTNDINRALKVARELEAGGVVINDSTRF 421
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
98-414 |
1.67e-14 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 75.16 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 98 GEITDLAYRPTGIQIgkMRVPLGVVGMI----YesrP-NVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHglkv 172
Cdd:COG1012 123 GETIPSDAPGTRAYV--RREPLGVVGAItpwnF---PlALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEE---- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 173 AGLPEHSVQVIeTSDRAAVGHLITMAEYVDVIV----PRGGKSLIERVtNEARIPVIKHLDGNCHVFVEAQADLQKALPI 248
Cdd:COG1012 194 AGLPAGVLNVV-TGDGSEVGAALVAHPDVDKISftgsTAVGRRIAAAA-AENLKRVTLELGGKNPAIVLDDADLDAAVEA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 249 TLNAKTHRYG-VCNAMETLLVDEKIADVFLPHIAELYA-------------------EKQVEL------RGCPETRRILG 302
Cdd:COG1012 272 AVRGAFGNAGqRCTAASRLLVHESIYDEFVERLVAAAKalkvgdpldpgtdmgplisEAQLERvlayieDAVAEGAELLT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 303 ASVKPATEEDWY-----------------TEYLGPILAVKVVSGIDEAIDHIN--KYG--ShhtdAIVTENYTLARQFLA 361
Cdd:COG1012 352 GGRRPDGEGGYFveptvladvtpdmriarEEIFGPVLSVIPFDDEEEAIALANdtEYGlaA----SVFTRDLARARRVAR 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 362 RVDSSSVVINASTRFAD------GF-EYGLGAEigistdkihaRGPVGLEGLTSQKWIVL 414
Cdd:COG1012 428 RLEAGMVWINDGTTGAVpqapfgGVkQSGIGRE----------GGREGLEEYTETKTVTI 477
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
103-374 |
8.44e-14 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 72.75 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 103 LAYRPTGIQI-----GK----MRVPLGVVGMIyeSRPNV----TLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHg 169
Cdd:cd07150 95 ECRRVRGETLpsdspGTvsmsVRRPLGVVAGI--TPFNYplilATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEE- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 170 lkvAGLPEHSVQVIeTSDRAAVGHLITMAEYVDVIVPRG----GKSLIERVTNEARiPVIKHLDGNCHVFVEAQADLQKA 245
Cdd:cd07150 172 ---AGLPKGVFNVV-TGGGAEVGDELVDDPRVRMVTFTGstavGREIAEKAGRHLK-KITLELGGKNPLIVLADADLDYA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 246 LPI-TLNAKTHRYGVCNAMETLLVDEKIADVFL--------------PH-----IAELYAEKQVEL------RGCPETRR 299
Cdd:cd07150 247 VRAaAFGAFMHQGQICMSASRIIVEEPVYDEFVkkfvarasklkvgdPRdpdtvIGPLISPRQVERikrqveDAVAKGAK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 300 IL------GASVKPATEED-------WYTEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVD 364
Cdd:cd07150 327 LLtggkydGNFYQPTVLTDvtpdmriFREETFGPVTSVIPAKDAEEALELANdtEYGL--SAAILTNDLQRAFKLAERLE 404
|
330
....*....|
gi 491207823 365 SSSVVINAST 374
Cdd:cd07150 405 SGMVHINDPT 414
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
116-383 |
7.07e-13 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 69.93 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMI--YESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAikhgLKVAGLPEHSVQVIeTSDRAAVGH 193
Cdd:cd07149 121 REPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL----LLEAGLPKGALNVV-TGSGETVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 194 LITMAEYVDVIVPRGGKSLIERVTNEARI-PVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLLVDEK 271
Cdd:cd07149 196 ALVTDPRVRMISFTGSPAVGEAIARKAGLkKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGqVCISVQRIFVHED 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 272 IADVFLPHIAElYAEKQVelRGCP--------------ETRRIL--------------------GASVKPATEED----- 312
Cdd:cd07149 276 IYDEFLERFVA-ATKKLV--VGDPldedtdvgpmiseaEAERIEewveeaveggarlltggkrdGAILEPTVLTDvppdm 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491207823 313 --WYTEYLGPILAVKVVSGIDEAIDHINK--YGSHHtdAIVTENYTLARQFLARVDSSSVVINASTRF-ADGFEYG 383
Cdd:cd07149 353 kvVCEEVFAPVVSLNPFDTLDEAIAMANDspYGLQA--GVFTNDLQKALKAARELEVGGVMINDSSTFrVDHMPYG 426
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
115-374 |
2.09e-11 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 65.29 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVV-GMIYESRPnVTLEAASLA--IKSGNAIILRGGSEALESNKAIAEAikhgLKVAGLPEHSVQVIETS-DRAA 190
Cdd:cd07105 95 VKEPVGVVlGIAPWNAP-VILGTRAIAypLAAGNTVVLKASELSPRTHWLIGRV----FHEAGLPKGVLNVVTHSpEDAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 191 vghlitmaEYVDVIVPRGgksLIERV-----TNEARI----------PVIKHLDGNCHVFVEAQADLQKA-LPITLNAKT 254
Cdd:cd07105 170 --------EVVEALIAHP---AVRKVnftgsTRVGRIiaetaakhlkPVLLELGGKAPAIVLEDADLDAAaNAALFGAFL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 255 HRYGVCNAMETLLVDEKIADVFL------------------PHIAELYAEKQVEL------------RGCPETRRILGAS 304
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVeklkaaaeklfagpvvlgSLVSAAAADRVKELvddalskgaklvVGGLADESPSGTS 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491207823 305 VKPATEED-------WYTEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINAST 374
Cdd:cd07105 319 MPPTILDNvtpdmdiYSEESFGPVVSIIRVKDEEEAVRIANdsEYGL--SAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
115-388 |
6.10e-11 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 63.91 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIyesRP-NVTLEAASL----AIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIETSDrA 189
Cdd:cd07131 132 RRQPIGVVALI---TPwNFPVAIPSWkifpALVCGNTVVFKPAEDTPACALKLVELFAE----AGLPPGVVNVVHGRG-E 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 190 AVGHLITMAEYVDVIVPRGGKSLIERVTNEA---RIPVIKHLDGNCHVFVEAQADLQKALPITLNA--KT--HRygvCNA 262
Cdd:cd07131 204 EVGEALVEHPDVDVVSFTGSTEVGERIGETCarpNKRVALEMGGKNPIIVMDDADLDLALEGALWSafGTtgQR---CTA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 263 METLLVDEKIADVFLPHIAE-------------------LYAEKQVE--LR----GCPETRRIL--GASVKPATEEDWY- 314
Cdd:cd07131 281 TSRLIVHESVYDEFLKRFVErakrlrvgdgldeetdmgpLINEAQLEkvLNyneiGKEEGATLLlgGERLTGGGYEKGYf 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 315 -----------------TEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINASTr 375
Cdd:cd07131 361 veptvftdvtpdmriaqEEIFGPVVALIEVSSLEEAIEIANdtEYGL--SSAIYTEDVNKAFRARRDLEAGITYVNAPT- 437
|
330
....*....|...
gi 491207823 376 fadgfeygLGAEI 388
Cdd:cd07131 438 --------IGAEV 442
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
116-392 |
3.51e-10 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 61.48 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIYESRPNVTLEAASL--AIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRAAVGH 193
Cdd:cd07109 115 REPHGVTGHIIPWNYPLQITGRSVapALAAGNAVVVKPAEDAPLTALRLAELAEE----AGLPAGALNVV-TGLGAEAGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 194 LITMAEYVDVIV----PRGGKsLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLLV 268
Cdd:cd07109 190 ALVAHPGVDHISftgsVETGI-AVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGqTCSAGSRLLV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 269 DEKIADVFLPHIAELY------------------AEKQVEL------RGCPETRRIL--GASVKPATEEDWY-------- 314
Cdd:cd07109 269 HRSIYDEVLERLVERFralrvgpgledpdlgpliSAKQLDRvegfvaRARARGARIVagGRIAEGAPAGGYFvaptlldd 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 315 ---------TEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINastrfadgfEYG 383
Cdd:cd07109 349 vppdsrlaqEEIFGPVLAVMPFDDEAEAIALANgtDYGL--VAGVWTRDGDRALRVARRLRAGQVFVN---------NYG 417
|
....*....
gi 491207823 384 LGAeiGIST 392
Cdd:cd07109 418 AGG--GIEL 424
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
115-389 |
4.08e-10 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 61.43 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIyeSRPN----VTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHGLKVAGLPEHSVQVIetSDRAA 190
Cdd:cd07086 130 QWNPLGVVGVI--TAFNfpvaVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV--TGGGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 191 VGHLITMAEYVDVIVPRG----GKSLIERVtnEARI-PVIKHLDGNCHVFVEAQADLQKALPITLNA--KT--HRygvCN 261
Cdd:cd07086 206 GGELLVHDPRVPLVSFTGstevGRRVGETV--ARRFgRVLLELGGNNAIIVMDDADLDLAVRAVLFAavGTagQR---CT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 262 AMETLLVDEKIADVFLPHIAELYA-------------------EKQVEL------RGCPETRRIL-GASVKPATEEDWY- 314
Cdd:cd07086 281 TTRRLIVHESVYDEFLERLVKAYKqvrigdpldegtlvgplinQAAVEKylnaieIAKSQGGTVLtGGKRIDGGEPGNYv 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 315 ----------------TEYLGPILAVKVVSGIDEAIdHIN---KYGShhTDAIVTENYTLARQFLARVDSSS--VVINAS 373
Cdd:cd07086 361 eptivtgvtddarivqEETFAPILYVIKFDSLEEAI-AINndvPQGL--SSSIFTEDLREAFRWLGPKGSDCgiVNVNIP 437
|
330
....*....|....*.
gi 491207823 374 TrfadgfeygLGAEIG 389
Cdd:cd07086 438 T---------SGAEIG 444
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
118-392 |
5.56e-10 |
|
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: 60.74 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 118 PLGVV-GMIYESRPNVTLEAASL-AIKSGNAIILRGGSEALESNKAIAEAIKHGLKVAGLPEHSVQVIETSDRAAVGHLI 195
Cdd:cd07081 95 PIGVVaSITPSTNPTSTVIFKSLiSLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 196 TMAEyVDVIVPRGGKSLIERVTNEARiPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYGV-CNAMETLLVDEKIAD 274
Cdd:cd07081 175 KFPG-IGLLLATGGPAVVKAAYSSGK-PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGViCASEQSVIVVDSVYD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 275 ------------------------VFL------PHIAELYAEKQVELRG--CPETRRIL-GASVKPATEEDWYTEYLGPI 321
Cdd:cd07081 253 evmrlfegqgaykltaeelqqvqpVILkngdvnRDIVGQDAYKIAAAAGlkVPQETRILiGEVTSLAEHEPFAHEKLSPV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 322 LAVKVVSGIDEAIDH----INKYGSHHTDAIVTENYTL---ARQFLARVDSSSVVINASTRFA---DGFEYGLGAEIGIS 391
Cdd:cd07081 333 LAMYRAANFADADAKalalKLEGGCGHTSAMYSDNIKAienMNQFANAMKTSRFVKNGPCSQGglgDLYNFRGWPSMTLG 412
|
.
gi 491207823 392 T 392
Cdd:cd07081 413 C 413
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
115-375 |
1.45e-09 |
|
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: 59.51 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIyeSRPNVTL-EAASL---AIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRAA 190
Cdd:cd07082 138 RREPLGVVLAI--GPFNYPLnLTVSKlipALIMGNTVVFKPATQGVLLGIPLAEAFHD----AGFPKGVVNVV-TGRGRE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 191 VGHLITMAEYVDVIVPRGGKSLIERVTNEA-RIPVIKHLDGNCHVFVEAQADLQKALP-ITLNAKTHRYGVCNAMETLLV 268
Cdd:cd07082 211 IGDPLVTHGRIDVISFTGSTEVGNRLKKQHpMKRLVLELGGKDPAIVLPDADLELAAKeIVKGALSYSGQRCTAIKRVLV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 269 DEKIADVFLPHIAELYAEKQV--------------------ELRG------------CPETRRILGASVKPA-----TEE 311
Cdd:cd07082 291 HESVADELVELLKEEVAKLKVgmpwdngvditplidpksadFVEGliddavakgatvLNGGGREGGNLIYPTlldpvTPD 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491207823 312 ---DWyTEYLGPILAVKVVSGIDEAIDHINK--YGSHhtDAIVTENYTLARQFLARVDSSSVVINASTR 375
Cdd:cd07082 371 mrlAW-EEPFGPVLPIIRVNDIEEAIELANKsnYGLQ--ASIFTKDINKARKLADALEVGTVNINSKCQ 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
35-371 |
1.65e-09 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 59.46 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 35 LSAIYTALENNQAAILAANQIDMDKGRSnqldSALLDRLELTPARFKGMLQGLKDVIAL--VDpigeiTDLAYRPtgiqi 112
Cdd:cd07087 26 LKALKRMLTENEEEIAAALYADLGKPPA----EAYLTEIAVVLGEIDHALKHLKKWMKPrrVS-----VPLLLQP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 113 GKMRV---PLGVVGMI----YesrP-NVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHGLkvaglPEHSVQVIE 184
Cdd:cd07087 92 AKAYVipePLGVVLIIgpwnY---PlQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYF-----DPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 185 tSDRAAVGHLItmAEYVDVIV----PRGGKsLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKALP-I----TLNAkth 255
Cdd:cd07087 164 -GGVEVATALL--AEPFDHIFftgsPAVGK-IVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARrIawgkFLNA--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 256 ryG-VCNAMETLLVDEKIADVFLP----HIAELYAEKQ------------------VEL----------RGCPETRRILG 302
Cdd:cd07087 237 --GqTCIAPDYVLVHESIKDELIEelkkAIKEFYGEDPkespdygriinerhfdrlASLlddgkvviggQVDKEERYIAP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491207823 303 ASVKPATEED--WYTEYLGPILAVKVVSGIDEAIDHINKYgsHHTDA--IVTENYTLARQFLARVDSSSVVIN 371
Cdd:cd07087 315 TILDDVSPDSplMQEEIFGPILPILTYDDLDEAIEFINSR--PKPLAlyLFSEDKAVQERVLAETSSGGVCVN 385
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
116-371 |
5.19e-07 |
|
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: 51.59 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIYE-SRP-NVTLEAASLAIKSGNAIILRGGsealESNKAIAEAIKHGLKVAGLPEHSVQVIeTSDRAAVGH 193
Cdd:cd07146 118 REPLGVVLAITPfNHPlNQVAHKIAPAIAANNRIVLKPS----EKTPLSAIYLADLLYEAGLPPDMLSVV-TGEPGEIGD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 194 LITMAEYVDVIVPRGGKSLIERVTNEA-RIPVIKHLDGNCHVFVEAQADLQKALPItlnAKTHRYGV----CNAMETLLV 268
Cdd:cd07146 193 ELITHPDVDLVTFTGGVAVGKAIAATAgYKRQLLELGGNDPLIVMDDADLERAATL---AVAGSYANsgqrCTAVKRILV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 269 DEKIADVFLPHIAELYAEKQVELRGCPET---------------RRIL----------------GASVKPA-------TE 310
Cdd:cd07146 270 HESVADEFVDLLVEKSAALVVGDPMDPATdmgtvideeaaiqieNRVEeaiaqgarvllgnqrqGALYAPTvldhvppDA 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491207823 311 EDWYTEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVIN 371
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNstAYGL--SSGVCTNDLDTIKRLVERLDVGTVNVN 410
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
106-374 |
6.10e-07 |
|
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: 51.48 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 106 RPtGIQIGKMRVPLGVVGMI-----------YESRPnvtleaaslAIKSGNAIILRGGSEALESNKAIAEAIKHglkvAG 174
Cdd:cd07097 124 RP-GVEVETTREPLGVVGLItpwnfpiaipaWKIAP---------ALAYGNTVVFKPAELTPASAWALVEILEE----AG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 175 LPEHSVQVIeTSDRAAVGHLITMAEYVDVIVPRG----GKSLIERVTNE-ARIPVikHLDGNCHVFVEAQADLQKALPIT 249
Cdd:cd07097 190 LPAGVFNLV-MGSGSEVGQALVEHPDVDAVSFTGstavGRRIAAAAAARgARVQL--EMGGKNPLVVLDDADLDLAVECA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 250 LNAKTHRYG-VCNAMETLLVDEKIADVFL-----------------------PHIAELYAEK---QVELRGCPETRRILG 302
Cdd:cd07097 267 VQGAFFSTGqRCTASSRLIVTEGIHDRFVealvertkalkvgdaldegvdigPVVSERQLEKdlrYIEIARSEGAKLVYG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 303 ASVKPATEEDWYT-----------------EYLGPILAVKVVSGIDEAIDHIN--KYGshHTDAIVTENYTLARQFLARV 363
Cdd:cd07097 347 GERLKRPDEGYYLapalfagvtndmriareEIFGPVAAVIRVRDYDEALAIANdtEFG--LSAGIVTTSLKHATHFKRRV 424
|
330
....*....|.
gi 491207823 364 DSSSVVINAST 374
Cdd:cd07097 425 EAGVVMVNLPT 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
116-366 |
7.45e-07 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 51.09 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIyeSRPN----VTLEAASLAIKSGNAIILRGGSEALesnkAIAEAIKHGLKVAGLPEHSVQVIETSDrAAV 191
Cdd:cd07102 114 REPLGVVLII--APWNypylTAVNAVIPALLAGNAVILKHSPQTP----LCGERFAAAFAEAGLPEGVFQVLHLSH-ETS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 192 GHLITMAeYVDVIV----PRGGKSlIERVTNEARIPVIKHLDGNCHVFVEAQADLQKAlpitlnAKTHRYGV-------C 260
Cdd:cd07102 187 AALIADP-RIDHVSftgsVAGGRA-IQRAAAGRFIKVGLELGGKDPAYVRPDADLDAA------AESLVDGAffnsgqsC 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 261 NAMETLLVDEKIADVFLPH-IAELYAEKqvelrgcpetrriLGASVKPATeedwyteYLGPIL----AVKVVSGIDEAID 335
Cdd:cd07102 259 CSIERIYVHESIYDAFVEAfVAVVKGYK-------------LGDPLDPST-------TLGPVVsaraADFVRAQIADAIA 318
|
250 260 270
....*....|....*....|....*....|....*.
gi 491207823 336 -----HINkyGSHHTDAIVTENYtLARQFLARVDSS 366
Cdd:cd07102 319 kgaraLID--GALFPEDKAGGAY-LAPTVLTNVDHS 351
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
103-374 |
1.14e-06 |
|
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: 50.61 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 103 LAYRPTG-----IQIGKM----RVPLGVVGMIyeSRPNVTLeaaSLAIKS-------GNAIILRGGSE-ALESNKAIAEA 165
Cdd:cd07104 74 LPRRPEGeilpsDVPGKEsmvrRVPLGVVGVI--SPFNFPL---ILAMRSvapalalGNAVVLKPDSRtPVTGGLLIAEI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 166 IKHglkvAGLPEHSVQVIeTSDRAAVGHLITMAEYVDVIVPRG----GKSLIE-------RVTNEaripvikhLDGNCHV 234
Cdd:cd07104 149 FEE----AGLPKGVLNVV-PGGGSEIGDALVEHPRVRMISFTGstavGRHIGElagrhlkKVALE--------LGGNNPL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 235 FVEAQADLQKALPITLNAK-THRYGVCNAMETLLVDEKIADVF----------LP---------HIAELYAEKQVE-LRG 293
Cdd:cd07104 216 IVLDDADLDLAVSAAAFGAfLHQGQICMAAGRILVHESVYDEFveklvakakaLPvgdprdpdtVIGPLINERQVDrVHA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 294 CPETRRILGASVKPATEED------------------WYTEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENY 353
Cdd:cd07104 296 IVEDAVAAGARLLTGGTYEglfyqptvlsdvtpdmpiFREEIFGPVAPVIPFDDDEEAVELANdtEYGL--SAAVFTRDL 373
|
330 340
....*....|....*....|.
gi 491207823 354 TLARQFLARVDSSSVVINAST 374
Cdd:cd07104 374 ERAMAFAERLETGMVHINDQT 394
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
108-371 |
1.23e-06 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 50.59 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 108 TGIQIGKMRVPLGVVG---------MIyesrPNVTLeaaSLAIKSGNAIILRGGSEALESNKAIAEAikhgLKVAGLPEH 178
Cdd:cd07085 126 RGIDTYSYRQPLGVVAgitpfnfpaMI----PLWMF---PMAIACGNTFVLKPSERVPGAAMRLAEL----LQEAGLPDG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 179 SVQVIeTSDRAAVGHLITmAEYVDVIVPRG----GKSLIERVTNEARiPVIKHLDGNCHVFVEAQADLQKALPITLNAKt 254
Cdd:cd07085 195 VLNVV-HGGKEAVNALLD-HPDIKAVSFVGstpvGEYIYERAAANGK-RVQALGGAKNHAVVMPDADLEQTANALVGAA- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 255 hrYGV----CNAMETLLVDEKIADVFLPHIAELYAEKQVELRGCPET-----------RRILGA---------------- 303
Cdd:cd07085 271 --FGAagqrCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGAdmgpvispaakERIEGLiesgveegaklvldgr 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 304 SVKPATEEDWY------------------TEYLGPILAVKVVSGIDEAIDHINK--YGshHTDAIVTENYTLARQFLARV 363
Cdd:cd07085 349 GVKVPGYENGNfvgptildnvtpdmkiykEEIFGPVLSIVRVDTLDEAIAIINAnpYG--NGAAIFTRSGAAARKFQREV 426
|
....*...
gi 491207823 364 DSSSVVIN 371
Cdd:cd07085 427 DAGMVGIN 434
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
35-371 |
2.39e-06 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 49.33 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 35 LSAIYTALENNQAAILAANQIDMDKgrsNQLDSaLLDRLELTPARFKGMLQGLKDVIAlvdPIGEITDLAYRPTGIQIgk 114
Cdd:cd07137 27 LKGLLRLVDENEDDIFAALRQDLGK---PSAES-FRDEVSVLVSSCKLAIKELKKWMA---PEKVKTPLTTFPAKAEI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIyeSRPNV----TLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKhglkvAGLPEHSVQVIETSdrAA 190
Cdd:cd07137 98 VSEPLGVVLVI--SAWNFpfllSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIP-----EYLDTKAIKVIEGG--VP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 191 VGHlITMAEYVDVIVPRGGkSLIERVTNEAR----IPVIKHLDGNCHVFVEAQADLQKALPITLNAKthrYGVCN----- 261
Cdd:cd07137 169 ETT-ALLEQKWDKIFFTGS-PRVGRIIMAAAakhlTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGK---WGCNNgqaci 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 262 AMETLLVDEKIA----DVFLPHIAELYAEKQVELRgcpETRRILGAS--------VKPA------------TEEDWYT-- 315
Cdd:cd07137 244 APDYVLVEESFAptliDALKNTLEKFFGENPKESK---DLSRIVNSHhfqrlsrlLDDPsvadkivhggerDEKNLYIep 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207823 316 ---------------EYLGPILAVKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVIN 371
Cdd:cd07137 321 tilldppldssimteEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
116-377 |
3.69e-06 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 48.76 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIyeSRPN--VTLEAASL--AIKSGNAIILRgGSEAlesNKAIAEAIKHGLKVAGLPEHSVQVIeTSDRAAV 191
Cdd:cd07099 117 YRPYGVVGVI--SPWNypLLTPMGDIipALAAGNAVVLK-PSEV---TPLVGELLAEAWAAAGPPQGVLQVV-TGDGATG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 192 GHLItmAEYVDVIV----PRGGKSLIERVTnEARIPVIKHLDGNCHVFVEAQADLQKAlpitlnAKTHRYG-------VC 260
Cdd:cd07099 190 AALI--DAGVDKVAftgsVATGRKVMAAAA-ERLIPVVLELGGKDPMIVLADADLERA------AAAAVWGamvnagqTC 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 261 NAMETLLVDEKIADVFLPHIAE-------------------LYAEKQVEL----------RG----CPETRRILGASVKP 307
Cdd:cd07099 261 ISVERVYVHESVYDEFVARLVAkaralrpgaddigdadigpMTTARQLDIvrrhvddavaKGakalTGGARSNGGGPFYE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 308 AT-------------EEDWyteylGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINA 372
Cdd:cd07099 341 PTvltdvphdmdvmrEETF-----GPVLPVMPVADEDEAIALANdsRYGL--SASVFSRDLARAEAIARRLEAGAVSIND 413
|
....*
gi 491207823 373 STRFA 377
Cdd:cd07099 414 VLLTA 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
116-382 |
6.15e-06 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 48.21 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIYESRPNVTLEAASL--AIKSGNAIILR----GGSEALEsnkaiaeaIKHGLKVAGLPEHSVQVIeTSDRA 189
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIapALIAGNAVVLKpptqGAVAALH--------MVHCFHLAGFPKGLISCV-TGKGS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 190 AVGHLITMAEYVDVIVPRGGKSLIERVTNEARIPVIKHLDGNCHVFVEAQADLQ-KALPITLNAKTHRYGVCNAMETLLV 268
Cdd:PLN00412 227 EIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDlAAANIIKGGFSYSGQRCTAVKVVLV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 269 DEKIADVFLPHIAELYAE-------------------------------KQVELRGCPETRR-------ILGASVKPATE 310
Cdd:PLN00412 307 MESVADALVEKVNAKVAKltvgppeddcditpvvsessanfieglvmdaKEKGATFCQEWKRegnliwpLLLDNVRPDMR 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491207823 311 EDWyTEYLGPILAVKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVIN-ASTRFADGFEY 382
Cdd:PLN00412 387 IAW-EEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINsAPARGPDHFPF 458
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
115-414 |
1.82e-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: 46.57 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIYESRPNVTLEAASL--AIKSGNAIILRGGSEALESNKAIAEAIKhglKVAGLPEHSVQVIETSDRAAVG 192
Cdd:cd07120 114 LREPMGVAGIIVPWNSPVVLLVRSLapALAAGCTVVVKPAGQTAQINAAIIRILA---EIPSLPAGVVNLFTESGSEGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 193 HLITMAEyVDVIVPRGGKSLIERVTNEArIPVIK----HLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLL 267
Cdd:cd07120 191 HLVASPD-VDVISFTGSTATGRAIMAAA-APTLKrlglELGGKTPCIVFDDADLDAALPKLERALTIFAGqFCMAGSRVL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 268 VDEKIADVFLPHIAE------------------------------------LYAEKQVELRGCPETRRIL-GASVKPATE 310
Cdd:cd07120 269 VQRSIADEVRDRLAArlaavkvgpgldpasdmgplidranvdrvdrmveraIAAGAEVVLRGGPVTEGLAkGAFLRPTLL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 311 EDWYT-------EYLGPILAVKVVSGIDEAIDHINkygshHTD-----AIVTENytLARQF-LAR-VDSSSVVINASTRF 376
Cdd:cd07120 349 EVDDPdadivqeEIFGPVLTLETFDDEAEAVALAN-----DTDyglaaSVWTRD--LARAMrVARaIRAGTVWINDWNKL 421
|
330 340 350
....*....|....*....|....*....|....*...
gi 491207823 377 ADGFEYGLGAEIGIStdkiHARGPVGLEGLTSQKWIVL 414
Cdd:cd07120 422 FAEAEEGGYRQSGLG----RLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
105-388 |
2.02e-05 |
|
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: 46.52 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 105 YRPTGIQIG--KMRV---PLGVVGMI----YesrP--NVtLEAASLAIKSGNAIILRGGSEALESNKAIAEAIKHGLKVA 173
Cdd:cd07098 102 SRPGGLLMFykRARVeyePLGVVGAIvswnY---PfhNL-LGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAAC 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 174 GLPEHSVQVI----ETSDraavgHLITmAEYVDVIV----PRGGKsLIERVTNEARIPVIKHLDGNCHVFVEAQADLQKA 245
Cdd:cd07098 178 GHDPDLVQLVtclpETAE-----ALTS-HPVIDHITfigsPPVGK-KVMAAAAESLTPVVLELGGKDPAIVLDDADLDQI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 246 LPITLNAKTHRYGV-CNAMETLLVDEKIADVFLphiaELYAEKQVELR-GCPETRRI-LGASVKPATeedwyteylgpil 322
Cdd:cd07098 251 ASIIMRGTFQSSGQnCIGIERVIVHEKIYDKLL----EILTDRVQALRqGPPLDGDVdVGAMISPAR------------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 323 AVKVVSGIDEAID------------HINKYGSHH-------TDaiVTENYTLARQFL-ARVdssSVVINAST-----RFA 377
Cdd:cd07098 314 FDRLEELVADAVEkgarllaggkryPHPEYPQGHyfpptllVD--VTPDMKIAQEEVfGPV---MVVMKASDdeeavEIA 388
|
330
....*....|.
gi 491207823 378 DGFEYGLGAEI 388
Cdd:cd07098 389 NSTEYGLGASV 399
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
115-373 |
4.76e-05 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 45.48 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIYesrP-NVTLEAASL----AIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRA 189
Cdd:cd07144 141 LHEPYGVCGQII---PwNYPLAMAAWklapALAAGNTVVIKPAENTPLSLLYFANLVKE----AGFPPGVVNII-PGYGA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 190 AVGHLITMAEYVDVIVPRG----GKSLIERVTNEARiPVIKHLDGNCHVFVEAQADLQKALP-ITLNAKTHRYGVCNAME 264
Cdd:cd07144 213 VAGSALAEHPDVDKIAFTGstatGRLVMKAAAQNLK-AVTLECGGKSPALVFEDADLDQAVKwAAAGIMYNSGQNCTATS 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 265 TLLVDEKIADVFLphiaELYAE--KQVELRGCP-----------------------------ETRRILGASVKPATEEDW 313
Cdd:cd07144 292 RIYVQESIYDKFV----EKFVEhvKQNYKVGSPfdddtvvgpqvsktqydrvlsyiekgkkeGAKLVYGGEKAPEGLGKG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 314 Y------------------TEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINAS 373
Cdd:cd07144 368 YfipptiftdvpqdmrivkEEIFGPVVVISKFKTYEEAIKKANdtTYGL--AAAVFTKDIRRAHRVARELEAGMVWINSS 445
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
116-335 |
1.92e-04 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 43.45 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIyesRP-----NVTLEAASLAIKSGNAIILRGGSE-ALESNKAIAEAIKHglkvAGLPEHSVQVI-----E 184
Cdd:cd07151 128 REPLGVVGVI---SPwnfplHLSMRSVAPALALGNAVVLKPASDtPITGGLLLAKIFEE----AGLPKGVLNVVvgagsE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 185 TSDrAAVGH----LITMAEYVDVivprgGKSLIERVTNEARIPVIKhLDGNCHVFVEAQADLQKALPITLNAK-THRYGV 259
Cdd:cd07151 201 IGD-AFVEHpvprLISFTGSTPV-----GRHIGELAGRHLKKVALE-LGGNNPFVVLEDADIDAAVNAAVFGKfLHQGQI 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491207823 260 CNAMETLLVDEKIADVFLphiaELYAEKQVELRgcpetrriLGASVKPATEedwyteyLGPILAVKVVSGIDEAID 335
Cdd:cd07151 274 CMAINRIIVHEDVYDEFV----EKFVERVKALP--------YGDPSDPDTV-------VGPLINESQVDGLLDKIE 330
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
115-390 |
2.12e-04 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 43.31 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIYESRPNVTLEAASL--AIKSGNAIILRGGSEALESNKAIAEAIKHglkvAGLPEHSVQVIeTSDRAAVG 192
Cdd:cd07114 116 RREPLGVVAAITPWNSPLLLLAKKLapALAAGNTVVLKPSEHTPASTLELAKLAEE----AGFPPGVVNVV-TGFGPETG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 193 HLITMAEYVDVIV----PRGGKSLIERVtneAR--IPVIKHLDGNCHVFVEAQADLQKAlpitlnAKTHRYGV------- 259
Cdd:cd07114 191 EALVEHPLVAKIAftggTETGRHIARAA---AEnlAPVTLELGGKSPNIVFDDADLDAA------VNGVVAGIfaaagqt 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 260 CNAMETLLVDEKIADVFL--------------P-----HIAELYAEKQVE------LRGCPETRRIL------------- 301
Cdd:cd07114 262 CVAGSRLLVQRSIYDEFVerlvararairvgdPldpetQMGPLATERQLEkveryvARAREEGARVLtggerpsgadlga 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 302 GASVKPATEED-------WYTEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINA 372
Cdd:cd07114 342 GYFFEPTILADvtndmriAQEEVFGPVLSVIPFDDEEEAIALANdsEYGL--AAGIWTRDLARAHRVARAIEAGTVWVNT 419
|
330 340
....*....|....*....|....
gi 491207823 373 STRFA-----DGF-EYGLGAEIGI 390
Cdd:cd07114 420 YRALSpsspfGGFkDSGIGRENGI 443
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
115-414 |
4.11e-04 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 42.41 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMI--YESRPNVTLEAASLAIKSGNAIILRGGSEALESNKAIAEAikhgLKVAGLPEHSVQVIETSDRAAvG 192
Cdd:cd07148 121 TREPIGVVVAIsaFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDL----LHEAGLPEGWCQAVPCENAVA-E 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 193 HLIT--MAEYVDVI-VPRGGKSLIERVTNEARIpVIKHlDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLLV 268
Cdd:cd07148 196 KLVTdpRVAFFSFIgSARVGWMLRSKLAPGTRC-ALEH-GGAAPVIVDRSADLDAMIPPLVKGGFYHAGqVCVSVQRVFV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 269 DEKIADVFlphiAELYAEKQVELRgcpetrriLGASVKPATE-------------EDWYT-------------------- 315
Cdd:cd07148 274 PAEIADDF----AQRLAAAAEKLV--------VGDPTDPDTEvgplirprevdrvEEWVNeavaagarllcggkrlsdtt 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 316 ------------------EYLGPILAVKVVSGIDEAIDHINKYGSHHTDAIVTENYTLARQFLARVDSSSVVINASTRF- 376
Cdd:cd07148 342 yaptvlldpprdakvstqEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFr 421
|
330 340 350
....*....|....*....|....*....|....*...
gi 491207823 377 ADGFEYGLGAEIGISTDKIhargPVGLEGLTSQKWIVL 414
Cdd:cd07148 422 VDWMPFAGRRQSGYGTGGI----PYTMHDMTQEKMAVI 455
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
116-383 |
4.50e-04 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 42.36 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIYESRPNVTLEAASLA--IKSGNAIILRGGSEALESNKAIAEAIKHGLkvaglPEHSVQVIeTSDRAAVGH 193
Cdd:cd07107 114 REPYGVVARIVAFNHPLMFAAAKIAapLAAGNTVVVKPPEQAPLSALRLAELAREVL-----PPGVFNIL-PGDGATAGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 194 LITMAEYVDVI-----VPRGGKslIERVTNEARIPVIKHLDGNCHVFVEAQADLQK-ALPITLNAKTHRYG-VCNAMETL 266
Cdd:cd07107 188 ALVRHPDVKRIaligsVPTGRA--IMRAAAEGIKHVTLELGGKNALIVFPDADPEAaADAAVAGMNFTWCGqSCGSTSRL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 267 LVDEKIADVFLPHIAELYAEKQVELRGCPETR-----------RIL---------GASV--------KPATEEDWYT--- 315
Cdd:cd07107 266 FVHESIYDEVLARVVERVAAIKVGDPTDPATTmgplvsrqqydRVMhyidsakreGARLvtgggrpeGPALEGGFYVept 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 316 --------------EYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINASTRFADG 379
Cdd:cd07107 346 vfadvtpgmriareEIFGPVLSVLRWRDEAEMVAQANgvEYGL--TAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLG 423
|
....
gi 491207823 380 FEYG 383
Cdd:cd07107 424 APFG 427
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
116-377 |
2.11e-03 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 39.98 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIyeSRPNVTLE-AASLAIK---SGNAIILRGGSEALESNKAIAEAikhgLKVAGLPEHSVQVIeTSDRAAV 191
Cdd:cd07101 116 RRPKGVVGVI--SPWNYPLTlAVSDAIPallAGNAVVLKPDSQTALTALWAVEL----LIEAGLPRDLWQVV-TGPGSEV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 192 GH-LITMAEYVDVI-VPRGGKSLIERVtneAR--IPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETL 266
Cdd:cd07101 189 GGaIVDNADYVMFTgSTATGRVVAERA---GRrlIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGqLCVSIERI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 267 LVDEKIADVFLPHIAE-------------------LYAEKQVE-LRGCPETRRILGASV---------------KPATEE 311
Cdd:cd07101 266 YVHESVYDEFVRRFVArtralrlgaaldygpdmgsLISQAQLDrVTAHVDDAVAKGATVlaggrarpdlgpyfyEPTVLT 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491207823 312 D-------WYTEYLGPILAVKVVSGIDEAIDHINkygshHTD-----AIVTENYTLARQFLARVDSSSVVINASTRFA 377
Cdd:cd07101 346 GvtedmelFAEETFGPVVSIYRVADDDEAIELAN-----DTDyglnaSVWTRDGARGRRIAARLRAGTVNVNEGYAAA 418
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
116-412 |
2.61e-03 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 39.97 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 116 RVPLGVVGMIyeSRPN----VTLEAASLAIKSGNAIILRGGSE-ALESNKAIAEAikhgLKVAGLPEHSVQVIETSdrAA 190
Cdd:cd07152 108 RVPLGVVGVI--SPFNfpliLAMRSVAPALALGNAVVLKPDPRtPVSGGVVIARL----FEEAGLPAGVLHVLPGG--AD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 191 VGHLITMAEYVDVIVPRGGKSLIERVtNEARIPVIK----HLDGNCHVFVEAQADLQKALP-ITLNAKTHRYGVCNAMET 265
Cdd:cd07152 180 AGEALVEDPNVAMISFTGSTAVGRKV-GEAAGRHLKkvslELGGKNALIVLDDADLDLAASnGAWGAFLHQGQICMAAGR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 266 LLVDEKIADVFLPHIAE-------------------LYAEKQVE--LRGCPETRRiLGASVK------------------ 306
Cdd:cd07152 259 HLVHESVADAYTAKLAAkakhlpvgdpatgqvalgpLINARQLDrvHAIVDDSVA-AGARLEaggtydglfyrptvlsgv 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 307 ----PATEEdwytEYLGPILAVKVVSGIDEAIDHIN--KYGShhTDAIVTENYTLARQFLARVDSSSVVINASTRFADGF 380
Cdd:cd07152 338 kpgmPAFDE----EIFGPVAPVTVFDSDEEAVALANdtEYGL--SAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPH 411
|
330 340 350
....*....|....*....|....*....|....*....
gi 491207823 381 -------EYGLGAEIGistdkiharGPVGLEGLTSQKWI 412
Cdd:cd07152 412 npfggmgASGNGSRFG---------GPANWEEFTQWQWV 441
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
35-371 |
3.97e-03 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 39.39 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 35 LSAIYTALENNQAAILAAnqIDMDKGRSNQLDSALLDRLeltparfkGMLQGLKDVIALVD----PIGEITDLAYRPTGI 110
Cdd:cd07133 26 LDRLKALLLDNQDALAEA--ISADFGHRSRHETLLAEIL--------PSIAGIKHARKHLKkwmkPSRRHVGLLFLPAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 111 QIgkMRVPLGVVGMI----YesrP-NVTLEAASLAIKSGNAIILRGgSE-ALESNKAIAEAIKhglkvAGLPEHSVQVIE 184
Cdd:cd07133 96 EV--EYQPLGVVGIIvpwnY---PlYLALGPLIAALAAGNRVMIKP-SEfTPRTSALLAELLA-----EYFDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 185 -TSDRAA-----------------VGHLItMAEYVDVIVP----RGGKSliervtneariPVIkhldgnchvfVEAQADL 242
Cdd:cd07133 165 gGADVAAafsslpfdhllftgstaVGRHV-MRAAAENLTPvtleLGGKS-----------PAI----------IAPDADL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 243 QKALPITLNAKTHRYG-VCNAMETLLVDEKIADVFLPHIAELYAEKQVELRGCPETRRI------------------LGA 303
Cdd:cd07133 223 AKAAERIAFGKLLNAGqTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYTSIinerhyarlqglledaraKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 304 ---SVKPATEEDWYT--------------------EYLGPILAVKVVSGIDEAIDHINK-------YgshhtdaIVTENY 353
Cdd:cd07133 303 rviELNPAGEDFAATrklpptlvlnvtddmrvmqeEIFGPILPILTYDSLDEAIDYINArprplalY-------YFGEDK 375
|
410
....*....|....*...
gi 491207823 354 TLARQFLARVDSSSVVIN 371
Cdd:cd07133 376 AEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
115-390 |
9.46e-03 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 38.09 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 115 MRVPLGVVGMIYE-SRPNVTL-EAASLAIKSGNAIILRGGsealESNKAIAEAIKHGLKVAGLPEHSVQVIeTSDRAAVG 192
Cdd:cd07118 116 LREPIGVVGIITPwNFPFLILsQKLPFALAAGCTVVVKPS----EFTSGTTLMLAELLIEAGLPAGVVNIV-TGYGATVG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 193 HLITMAEYVDVIVPRG----GKSLIERVTNEARiPVIKHLDGNCHVFVEAQADLQKALPITLNAKTHRYG-VCNAMETLL 267
Cdd:cd07118 191 QAMTEHPDVDMVSFTGstrvGKAIAAAAARNLK-KVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGeCCNSGSRLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 268 VDEKIADVFLPHIAELYAEKQVELRGCPETR-----------RILG--------------------------------AS 304
Cdd:cd07118 270 VHESIADAFVAAVVARSRKVRVGDPLDPETKvgaiineaqlaKITDyvdagraegatlllggerlasaaglfyqptifTD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207823 305 VKP----ATEedwytEYLGPILAVKVVSGIDEAIDHINK--YGShhTDAIVTENYTLARQFLARVDSSSVVINastRFAD 378
Cdd:cd07118 350 VTPdmaiARE-----EIFGPVLSVLTFDTVDEAIALANDtvYGL--SAGVWSKDIDTALTVARRIRAGTVWVN---TFLD 419
|
330 340
....*....|....*....|.
gi 491207823 379 GF---------EYGLGAEIGI 390
Cdd:cd07118 420 GSpelpfggfkQSGIGRELGR 440
|
|
| |
