|
Name |
Accession |
Description |
Interval |
E-value |
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
10-414 |
0e+00 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 671.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 10 DLRQEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGI 89
Cdd:PRK00197 1 DIMEYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 90 AAGLRQVAGLRDPVGEVLRGYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALV 169
Cdd:PRK00197 81 AEGLRQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 170 AVLRTALVGLELPADAVQLLSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLD 249
Cdd:PRK00197 161 AVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVDESADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 250 VAERILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPD------------EADLRREYLSLDIAV 317
Cdd:PRK00197 241 KALKIVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVELRGDEAalallpdvvpatEEDWDTEYLDLILAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 318 AVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLP 397
Cdd:PRK00197 321 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 400
|
410
....*....|....*..
gi 489507647 398 ELTSTKWIAWGAGHTRP 414
Cdd:PRK00197 401 ELTTYKYIVLGDGQIRA 417
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
29-414 |
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: 654.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 29 LASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLR 108
Cdd:COG0014 17 LATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEGLRQVAALPDPVGEVLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 109 GYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQL 188
Cdd:COG0014 97 GWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQEALEEAGLPEDAVQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 189 LSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNA 268
Cdd:COG0014 177 VPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRVVENATVPVIEHGDGNCHVYVDASADLEMAVDIVVNAKTQRPGVCNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 269 AETLLVDAAIAETALPRLLAALQHAGVTVHLDPD------------EADLRREYLSLDIAVAVVDGVDAAIAHINEYGTG 336
Cdd:COG0014 257 LETLLVHRDIAAEFLPRLAAALAEAGVELRGDERtrailpdvkpatEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSG 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489507647 337 HTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTKWIAWGAGHTRP 414
Cdd:COG0014 337 HTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYVVRGDGQIRP 414
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
29-408 |
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: 616.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 29 LASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLR 108
Cdd:cd07079 14 LATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQVAALPDPVGEVLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 109 GYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQL 188
Cdd:cd07079 94 GWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEALEEAGLPEDAVQL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 189 LSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNA 268
Cdd:cd07079 174 IPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIVVNAKTQRPSVCNA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 269 AETLLVDAAIAETALPRLLAALQHAGVTVHLDP------------DEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTG 336
Cdd:cd07079 254 LETLLVHRDIAEEFLPKLAEALREAGVELRGDEetlailpgakpaTEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSG 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489507647 337 HTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTKWIAWG 408
Cdd:cd07079 334 HTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYIVRG 405
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
29-403 |
6.26e-148 |
|
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: 425.35 E-value: 6.26e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 29 LASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLR 108
Cdd:TIGR00407 8 LAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELADPVGKVID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 109 GYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQL 188
Cdd:TIGR00407 88 GRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGLPVGAVQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 189 LSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNA 268
Cdd:TIGR00407 168 IETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQRPSTCNA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 269 AETLLVDAAIAETALPRLLAALQHAGVTVHLDP----------------DEADLRREYLSLDIAVAVVDGVDAAIAHINE 332
Cdd:TIGR00407 248 IETLLVNKAIAREFLPVLENQLLEKGVTIHADAyalkllelgpateaivCKTDFDKEFLSLDLSVKIVESLEAAIQHINQ 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489507647 333 YGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTK 403
Cdd:TIGR00407 328 YGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
29-411 |
5.31e-103 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 320.90 E-value: 5.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 29 LASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLR 108
Cdd:PLN02418 310 LQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLADMEDPIGRVLK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 109 GYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTAL---VGLELpada 185
Cdd:PLN02418 390 RTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIpktVGGKL---- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 186 VQLLSAadRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSV 265
Cdd:PLN02418 466 IGLVTS--RDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 266 CNAAETLLVDAAIAETA-LPRLLAALQHAGVTVH---------LDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGT 335
Cdd:PLN02418 544 CNAMETLLVHKDLVQNGgLNDLLVALRSAGVTLYggpraskllNIPEAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGS 623
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489507647 336 GHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTKWIAWGAGH 411
Cdd:PLN02418 624 AHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQ 699
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
13-411 |
3.59e-93 |
|
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: 295.28 E-value: 3.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 13 QEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAG 92
Cdd:TIGR01092 286 TGERDMAVAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 93 LRQVAGLRDPVGEVLRGYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVL 172
Cdd:TIGR01092 366 LRQLAAMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVI 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 173 RTALvGLELPADAVQLLSAadRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAE 252
Cdd:TIGR01092 446 TEAI-PIHVGKKLIGLVTS--REEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVDMAK 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 253 RILLNSKTRRPSVCNAAETLLVDAAIAETA-LPRLLAALQHAGVTVHLDPDEA-----------DLRREYLSLDIAVAVV 320
Cdd:TIGR01092 523 RIVRDAKCDYPAACNAMETLLVHKDLLRNGlLDDLIDMLRTEGVTIHGGPRFAayltfnisetkSFRTEYSSLACTVEIV 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 321 DGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELT 400
Cdd:TIGR01092 603 DDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLL 682
|
410
....*....|.
gi 489507647 401 STKWIAWGAGH 411
Cdd:TIGR01092 683 TTRWLLRGKGQ 693
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
29-406 |
3.49e-48 |
|
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: 168.94 E-value: 3.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 29 LASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAArEADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLR 108
Cdd:cd07077 10 LAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAY-IRSLIANWIAMMGCSESKLYKNIDTERGITASVGHIQDVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 109 gytlPNGLQLRQQRVPLGVVGMIYEGR-PNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALvAVLRTALVGLELPADAVQ 187
Cdd:cd07077 89 ----PDNGETYVRAFPIGVTMHILPSTnPLSGITSALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAADAAHGPKILVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 188 LLSAADRATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQ-VPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVC 266
Cdd:cd07077 164 YVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 267 NAAETLLVDAAIAETALPRLLAALQHAGVTVHLDP--------DEAD--LRREYLSLDIAVAVVDGVDA---AIAHINEY 333
Cdd:cd07077 243 ASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETkplskettPSFDdeALESMTPLECQFRVLDVISAvenAWMIIESG 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489507647 334 GTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARG-PMGLPELTSTKWIA 406
Cdd:cd07077 323 GGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRPLKRLV 396
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
30-405 |
1.30e-35 |
|
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: 134.28 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 30 ASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREAdtpaaMLDRlslnpqrVDGIAAGLRQVAGLRDPVGEVLRG 109
Cdd:cd06534 11 AALPPAERAAILRKIADLLEERREELAALETLETGKPIEE-----ALGE-------VARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 110 YTLPNGlQLRQQRVPLGVVGMIYEGRP--NVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALvgleLPADAVQ 187
Cdd:cd06534 79 SPDPGG-EAYVRREPLGVVGVITPWNFplLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 188 LLSAADRATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQVP----TIETGvGNCHVYVHQAADLDVAERILLNSKTR-R 262
Cdd:cd06534 154 VVPGGGDEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAENlkpvTLELG-GKSPVIVDEDADLDAAVEGAVFGAFFnA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 263 PSVCNAAETLLVDAAIAETALPRLlaalqhAGVTVHLDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIV 342
Cdd:cd06534 232 GQICTAASRLLVHESIYDEFVEKL------VTVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVF 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489507647 343 TTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQ-FGFGAEIGISTQKlharGPMGLPELTSTKWI 405
Cdd:cd06534 306 TRDLNRALRVAERLRAGTVYINDSSIGVGPEApFGGVKNSGIGREG----GPYGLEEYTRTKTV 365
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
123-369 |
2.80e-16 |
|
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: 80.23 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 123 VPLGVV-GMIYEGRPNVTVdAFG--LTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQLLSAADRATVTH 199
Cdd:cd07122 94 EPVGVIaALIPSTNPTSTA-IFKalIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 200 LIQARGlVDVVIPRGGAGLieavVRDAQ---VPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNAAE-TLLVD 275
Cdd:cd07122 173 LMKHPD-VDLILATGGPGM----VKAAYssgKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEqSVIVD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 276 AAIAETAL--------------------------------------PRLLAALqhAGVTV------------HLDPDEAd 305
Cdd:cd07122 248 DEIYDEVRaelkrrgayflneeekeklekalfddggtlnpdivgksAQKIAEL--AGIEVpedtkvlvaeetGVGPEEP- 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489507647 306 LRREYLSLDIAVAVV----DGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAF 369
Cdd:cd07122 325 LSREKLSPVLAFYRAedfeEALEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPSSL 392
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
34-405 |
9.75e-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: 72.24 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 34 TTVKDRA--LHAAADELLAHRDQILAANAEDLNAAREAdtpAAMldrlslnpqRVDGIAAGLRQVAGL-RDPVGEVLRgy 110
Cdd:cd07078 17 LPPAERAaiLRKLADLLEERREELAALETLETGKPIEE---ALG---------EVARAADTFRYYAGLaRRLHGEVIP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 111 TLPNGLQLRQQRVPLGVVGMI----YegrP-NVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALvgleLPADA 185
Cdd:cd07078 83 SPDPGELAIVRREPLGVVGAItpwnF---PlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 186 VQLLSAADRATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQVP----TIETGvGNCHVYVHQAADLDVAERILLNSKTR 261
Cdd:cd07078 156 LNVVTGDGDEVGAALASHPR-VDKISFTGSTAVGKAIMRAAAENlkrvTLELG-GKSPLIVFDDADLDAAVKGAVFGAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 262 RP-SVCNAAETLLVDAAIAETALPRLLAAL------------------------------------QHAGVTVHLDPDEA 304
Cdd:cd07078 234 NAgQVCTAASRLLVHESIYDEFVERLVERVkalkvgnpldpdtdmgplisaaqldrvlayiedakaEGAKLLCGGKRLEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 305 DLRREY---------LSLDIA----------VAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNA 365
Cdd:cd07078 314 GKGYFVpptvltdvdPDMPIAqeeifgpvlpVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489507647 366 STAFTDGEQ-FGFGAEIGIStqklHARGPMGLPELTSTKWI 405
Cdd:cd07078 394 YSVGAEPSApFGGVKQSGIG----REGGPYGLEEYTEPKTV 430
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-405 |
2.90e-12 |
|
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: 67.94 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 34 TTVKDRA--LHAAADELLAHRDQILAANAEDLNA-AREADTpaamldrlslnpqRVDGIAAGLRQVAGLrdpvGEVLRGY 110
Cdd:pfam00171 48 TPAAERAaiLRKAADLLEERKDELAELETLENGKpLAEARG-------------EVDRAIDVLRYYAGL----ARRLDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 111 TLP--NGLQLRQQRVPLGVVGMIyegRP-----NVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTAlvglELPA 183
Cdd:pfam00171 111 TLPsdPGRLAYTRREPLGVVGAI---TPwnfplLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEA----GLPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 184 DAVQLLSAADRATVTHLIQARGlVDVVI----PRGGAGLIEAVVRDAQVPTIETGvGNCHVYVHQAADLDVAERILLNSK 259
Cdd:pfam00171 184 GVLNVVTGSGAEVGEALVEHPD-VRKVSftgsTAVGRHIAEAAAQNLKRVTLELG-GKNPLIVLEDADLDAAVEAAVFGA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 260 TRRP-SVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPD---------------------------------EAD 305
Cdd:pfam00171 262 FGNAgQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDtdmgpliskaqlervlkyvedakeegaklltggEAG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 306 LRREYL-----------SLDIA----------VAVVDGVDAAIAHIN--EYgtGHTEAIVTTNLDAAQRFTEQIDAAAVM 362
Cdd:pfam00171 342 LDNGYFveptvlanvtpDMRIAqeeifgpvlsVIRFKDEEEAIEIANdtEY--GLAAGVFTSDLERALRVARRLEAGMVW 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489507647 363 VNASTAFT-DGEQF------GFGAEigistqklhaRGPMGLPELTSTKWI 405
Cdd:pfam00171 420 INDYTTGDaDGLPFggfkqsGFGRE----------GGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
34-407 |
5.70e-12 |
|
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: 67.07 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 34 TTVKDRA--LHAAADELLAHRDQILAANAEDLNAAReadtPAAMLDrlslnpqrVDGIAAGLRQVAGL-RDPVGEVLRGY 110
Cdd:COG1012 62 TPPAERAaiLLRAADLLEERREELAALLTLETGKPL----AEARGE--------VDRAADFLRYYAGEaRRLYGETIPSD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 111 tlPNGLQLRQQRVPLGVVGMI----YegrP-NVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTAlvglELPADA 185
Cdd:COG1012 130 --APGTRAYVRREPLGVVGAItpwnF---PlALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEA----GLPAGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 186 VQLLSAADRATVTHLIQARGlVDVVI----PRGGAGLIEAVVRDAQVPTIETGvGNCHVYVHQAADLDVAERILLNSKTR 261
Cdd:COG1012 201 LNVVTGDGSEVGAALVAHPD-VDKISftgsTAVGRRIAAAAAENLKRVTLELG-GKNPAIVLDDADLDAAVEAAVRGAFG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 262 RpS--VCNAAETLLVDAAIAETALPRLLAALQH----------------------------------AGVTVHLDPDEAD 305
Cdd:COG1012 279 N-AgqRCTAASRLLVHESIYDEFVERLVAAAKAlkvgdpldpgtdmgpliseaqlervlayiedavaEGAELLTGGRRPD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 306 LRREYL-----------SLDIA----------VAVVDGVDAAIAHIN--EYG-TGhteAIVTTNLDAAQRFTEQIDAAAV 361
Cdd:COG1012 358 GEGGYFveptvladvtpDMRIAreeifgpvlsVIPFDDEEEAIALANdtEYGlAA---SVFTRDLARARRVARRLEAGMV 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489507647 362 MVNASTAFTDGEQ-FG------FGAEigistqklhaRGPMGLPELTSTKWIAW 407
Cdd:COG1012 435 WINDGTTGAVPQApFGgvkqsgIGRE----------GGREGLEEYTETKTVTI 477
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
8-376 |
2.86e-10 |
|
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: 61.68 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 8 QLDLRQEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQIlaanAEDLnaAREADTPaamldrlslnpqRVD 87
Cdd:cd07094 16 PADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEF----AKII--ACEGGKP------------IKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 88 GIAAGLRQVAGLRDPVGEV--LRGYTLPNGLQLRQQ-------RVPLGVVGMI--YEGRPNVTVDAFGLTLKSGNAALLR 156
Cdd:cd07094 78 ARVEVDRAIDTLRLAAEEAerIRGEEIPLDATQGSDnrlawtiREPVGVVLAItpFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 157 GSSSAAKSNEALVAVLRTAlvglELPADAVQLLSAADRATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQVP--TIETG 234
Cdd:cd07094 158 PASKTPLSALELAKILVEA----GVPEGVLQVVTGEREVLGDAFAADER-VAMLSFTGSAAVGEALRANAGGKriALELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 235 vGNCHVYVHQAADLD-VAERILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLA------------------------- 288
Cdd:cd07094 233 -GNAPVIVDRDADLDaAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAavkklkvgdpldedtdvgpliseea 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 289 --------------------------ALQHAGVTVHLDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIV 342
Cdd:cd07094 312 aerverwveeaveagarllcggerdgALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430
....*....|....*....|....*....|....*
gi 489507647 343 TTNLDAAQRFTEQIDAAAVMVNASTAF-TDGEQFG 376
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFrTDWMPFG 426
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
39-371 |
6.69e-10 |
|
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: 60.73 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 39 RALHAAADELLAHRDQIlaanAEDLnaAREADTPAAmldrlslnpqrvDGIAAGLRQVAGLRDPVGEVLR--GYTLPN-- 114
Cdd:cd07097 63 DILDKAGDELEARKEEL----ARLL--TREEGKTLP------------EARGEVTRAGQIFRYYAGEALRlsGETLPStr 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 115 -GLQLRQQRVPLGVVGMIYEGRPNVTVDAFGL--TLKSGNAALLRGSSSAAKSNEALVAVLRTAlvglELPADAVQLLSA 191
Cdd:cd07097 125 pGVEVETTREPLGVVGLITPWNFPIAIPAWKIapALAYGNTVVFKPAELTPASAWALVEILEEA----GLPAGVFNLVMG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 192 ADRATVTHLIQARGlVDVVIPRG----GAGLIEAVVRDAQVPTIETGvGNCHVYVHQAADLDVAERILLNSKTRRP-SVC 266
Cdd:cd07097 201 SGSEVGQALVEHPD-VDAVSFTGstavGRRIAAAAAARGARVQLEMG-GKNPLVVLDDADLDLAVECAVQGAFFSTgQRC 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 267 NAAETLLVDAAIAETALPRLLAALQHAGVTVHLDP--------DEADLRREYLSLDIAV--------------------- 317
Cdd:cd07097 279 TASSRLIVTEGIHDRFVEALVERTKALKVGDALDEgvdigpvvSERQLEKDLRYIEIARsegaklvyggerlkrpdegyy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 318 ---AVVDGV------------------------DAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFT 370
Cdd:cd07097 359 lapALFAGVtndmriareeifgpvaavirvrdyDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGV 438
|
.
gi 489507647 371 D 371
Cdd:cd07097 439 D 439
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
104-381 |
6.02e-08 |
|
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: 54.66 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 104 GEVLRGYTLPNGLQLRQQ---RVPLGVVGMIYEGRPNVTVDAFGL--TLKSGNAALLRGSSSAAKSNEALVAVLRTAlvg 178
Cdd:cd07131 112 GRRLFGETVPSELPNKDAmtrRQPIGVVALITPWNFPVAIPSWKIfpALVCGNTVVFKPAEDTPACALKLVELFAEA--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 179 lELPADAVQLLSAADRATVTHLIQARGlVDVVIPRG----GAGLIEAVVRDAQVPTIETGvGNCHVYVHQAADLDVA-ER 253
Cdd:cd07131 189 -GLPPGVVNVVHGRGEEVGEALVEHPD-VDVVSFTGstevGERIGETCARPNKRVALEMG-GKNPIIVMDDADLDLAlEG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 254 ILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLAAL----------------------------------QHAGVTVHL 299
Cdd:cd07131 266 ALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAkrlrvgdgldeetdmgplineaqlekvlnyneigKEEGATLLL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 300 DPDEAD------------------------LRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQ 355
Cdd:cd07131 346 GGERLTgggyekgyfveptvftdvtpdmriAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRD 425
|
330 340
....*....|....*....|....*.
gi 489507647 356 IDAAAVMVNASTaftdgeqfgFGAEI 381
Cdd:cd07131 426 LEAGITYVNAPT---------IGAEV 442
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
107-382 |
4.26e-07 |
|
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: 51.80 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 107 LRGYTLPN---GLQLRQQRVPLGVVGMIYEGRPNVTVDA--FGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLEL 181
Cdd:cd07086 113 LYGLTIPSerpGHRLMEQWNPLGVVGVITAFNFPVAVPGwnAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 182 PADAVQLLSAadRATVTHLIQARGLVDVVIPRG----GAGLIEAVVRDAQVPTIETGvGNCHVYVHQAADLDVAER-ILL 256
Cdd:cd07086 193 PPGVVNLVTG--GGDGGELLVHDPRVPLVSFTGstevGRRVGETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRaVLF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 257 NS-KT--RRpsvCNAAETLLVDAAIAETALPRLLAA----------------------------------LQHAGVTVHL 299
Cdd:cd07086 270 AAvGTagQR---CTTTRRLIVHESVYDEFLERLVKAykqvrigdpldegtlvgplinqaavekylnaieiAKSQGGTVLT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 300 DPDEAD----------------------LRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQ-- 355
Cdd:cd07086 347 GGKRIDggepgnyveptivtgvtddariVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkg 426
|
330 340
....*....|....*....|....*..
gi 489507647 356 IDAAAVMVNASTAftdgeqfgfGAEIG 382
Cdd:cd07086 427 SDCGIVNVNIPTS---------GAEIG 444
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
102-376 |
5.83e-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: 48.36 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 102 PVGEVLRGYTLpnglqlrqqRVPLGVVGMI--YEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTAlvgl 179
Cdd:cd07149 110 PGGEGRIGFTI---------REPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEA---- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 180 ELPADAVQLLSAADRATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQVP--TIETGvGNCHVYVHQAADLD-VAERILL 256
Cdd:cd07149 177 GLPKGALNVVTGSGETVGDALVTDPR-VRMISFTGSPAVGEAIARKAGLKkvTLELG-SNAAVIVDADADLEkAVERCVS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 257 NSKTRRPSVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPD--------EADLRREYLSLDIAVA---------- 318
Cdd:cd07149 255 GAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDtdvgpmisEAEAERIEEWVEEAVEggarlltggk 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 319 ---------VVDGVDA------------------------AIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVN- 364
Cdd:cd07149 335 rdgaileptVLTDVPPdmkvvceevfapvvslnpfdtldeAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINd 414
|
330
....*....|..
gi 489507647 365 ASTAFTDGEQFG 376
Cdd:cd07149 415 SSTFRVDHMPYG 426
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
124-317 |
2.53e-05 |
|
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: 46.10 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 124 PLGVV-GMIYEGRPNVTVDAFGL-TLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQLLSAADRATVTHLI 201
Cdd:cd07081 95 PIGVVaSITPSTNPTSTVIFKSLiSLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 202 QARGlVDVVIPRGGAGLIEAVvRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNAAETLLVDAAIAET 281
Cdd:cd07081 175 KFPG-IGLLLATGGPAVVKAA-YSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYD 252
|
170 180 190
....*....|....*....|....*....|....*.
gi 489507647 282 ALPRLLAAlQHAgvtVHLDPDEADLRREYLSLDIAV 317
Cdd:cd07081 253 EVMRLFEG-QGA---YKLTAEELQQVQPVILKNGDV 284
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
296-385 |
3.03e-05 |
|
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: 45.87 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 296 TVHLDP-DEADL-RREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAF-TDG 372
Cdd:cd07148 345 TVLLDPpRDAKVsTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFrVDW 424
|
90
....*....|...
gi 489507647 373 EQFGFGAEIGIST 385
Cdd:cd07148 425 MPFAGRRQSGYGT 437
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
38-376 |
1.27e-04 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 43.89 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 38 DRALHAAAD--------------ELLAHRDQILAANAEDLNAAREADTPAAMldRLSLNPQrVDGIAAGLRQVAGLrdpV 103
Cdd:cd07108 22 DRAVAAAKAafpewaatparergKLLARIADALEARSEELARLLALETGNAL--RTQARPE-AAVLADLFRYFGGL---A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 104 GEvLRGYTLPNGLQLRQ--QRVPLGVVGMIYEGRPNVTVDAFGLTlksgnAALLRGSSSAAKSNE-ALVAVLRTA-LVGL 179
Cdd:cd07108 96 GE-LKGETLPFGPDVLTytVREPLGVVGAILPWNAPLMLAALKIA-----PALVAGNTVVLKAAEdAPLAVLLLAeILAQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 180 ELPADAVQLLSAADRATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQ---VP-TIETGvGNCHVYVHQAADLD--VAER 253
Cdd:cd07108 170 VLPAGVLNVITGYGEECGAALVDHPD-VDKVTFTGSTEVGKIIYRAAAdrlIPvSLELG-GKSPMIVFPDADLDdaVDGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 254 ILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLAAL----------------------QHAGVTVHLD----------- 300
Cdd:cd07108 248 IAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLsklkigdpldeatdigaiisekQFAKVCGYIDlglstsgatvl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 301 -----PDEADLRREYLSLDIAVAVVDG---------------------VDAAIAHINEYGTGHTEAIVTTNLDAAQRFTE 354
Cdd:cd07108 328 rggplPGEGPLADGFFVQPTIFSGVDNewrlareeifgpvlcaipwkdEDEVIAMANDSHYGLAAYVWTRDLGRALRAAH 407
|
410 420
....*....|....*....|..
gi 489507647 355 QIDAAAVMVNASTAFTDGEQFG 376
Cdd:cd07108 408 ALEAGWVQVNQGGGQQPGQSYG 429
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
115-364 |
1.80e-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: 43.39 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 115 GLQLRQQRVPLGVVGMI----YegrPN-VTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALvgleLPADAVQLL 189
Cdd:cd07102 107 GFERYIRREPLGVVLIIapwnY---PYlTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAG----LPEGVFQVL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 190 SAADrATVTHLIQARGlVDVVIPRGGAGLIEAVVRDAQVPTIETGV---GNCHVYVHQAADLD-VAERI----LLNSKtr 261
Cdd:cd07102 180 HLSH-ETSAALIADPR-IDHVSFTGSVAGGRAIQRAAAGRFIKVGLelgGKDPAYVRPDADLDaAAESLvdgaFFNSG-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 262 rpSVCNAAETLLVDAAIAET-------------------------------ALPRLLAALQHA---GVTVHLDPDEADLR 307
Cdd:cd07102 256 --QSCCSIERIYVHESIYDAfveafvavvkgyklgdpldpsttlgpvvsarAADFVRAQIADAiakGARALIDGALFPED 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 308 RE---YLSLDIAVAV--------------------VDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVN 364
Cdd:cd07102 334 KAggaYLAPTVLTNVdhsmrvmreetfgpvvgimkVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN 413
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
30-328 |
2.10e-04 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 43.41 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 30 ASLPTTVKDRALHAAADELLAHRDQILAAnaedlnAAREADTPaamldrLSLNPQRVDGIAAGLRQVAGL-RDPVGEVLR 108
Cdd:cd07088 52 ERLPAIERAAYLRKLADLIRENADELAKL------IVEEQGKT------LSLARVEVEFTADYIDYMAEWaRRIEGEIIP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 109 GyTLPNGlQLRQQRVPLGVVGMIYEGRPNVTVDA--FGLTLKSGNAALLRGSSSAAKSNEALVAVLRTAlvglELPADAV 186
Cdd:cd07088 120 S-DRPNE-NIFIFKVPIGVVAGILPWNFPFFLIArkLAPALVTGNTIVIKPSEETPLNALEFAELVDEA----GLPAGVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 187 QLL----SAADRATVTH----LIQARGLVdvvipRGGAGLIEAVVRDAQVPTIETGvGNCHVYVHQAADLDVAERILLNS 258
Cdd:cd07088 194 NIVtgrgSVVGDALVAHpkvgMISLTGST-----EAGQKIMEAAAENITKVSLELG-GKAPAIVMKDADLDLAVKAIVDS 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489507647 259 KTRRP-SVCNAAETLLVDAAIAETALPRLLAALqhAGVTVhLDPDEADLRREYLSLDIAVAVVDG-VDAAIA 328
Cdd:cd07088 268 RIINCgQVCTCAERVYVHEDIYDEFMEKLVEKM--KAVKV-GDPFDAATDMGPLVNEAALDKVEEmVERAVE 336
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
14-407 |
1.53e-03 |
|
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: 40.67 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 14 EVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREA-----DTPAAMLDRLSLNPQRVdg 88
Cdd:cd07099 19 EVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADaglevLLALEAIDWAARNAPRV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 89 iaaglrqvagLRDPvgEVLRGYTLPNgLQLRQQRVPLGVVGMI----YegrPNVTvdAFGLT---LKSGNAALLRGSSSA 161
Cdd:cd07099 97 ----------LAPR--KVPTGLLMPN-KKATVEYRPYGVVGVIspwnY---PLLT--PMGDIipaLAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 162 AKSNEALVAVLRTALvgleLPADAVQLLsAADRATVTHLIQARglVDVVIPRGGAGLIEAV-VRDAQVPT---IETGvGN 237
Cdd:cd07099 159 PLVGELLAEAWAAAG----PPQGVLQVV-TGDGATGAALIDAG--VDKVAFTGSVATGRKVmAAAAERLIpvvLELG-GK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 238 CHVYVHQAADLDVAER-ILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLA---ALQHAG------------------- 294
Cdd:cd07099 231 DPMIVLADADLERAAAaAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAkarALRPGAddigdadigpmttarqldi 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 295 --------------------------------VTVHLDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIV 342
Cdd:cd07099 311 vrrhvddavakgakaltggarsngggpfyeptVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489507647 343 TTNLDAAQRFTEQIDAAAVMVNASTAFT---DGEQFGFGAEIGISTQklharGPMGLPELTSTKWIAW 407
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINDVLLTAgipALPFGGVKDSGGGRRH-----GAEGLREFCRPKAIAR 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
2-376 |
3.04e-03 |
|
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: 39.64 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 2 TVPAPSqldlRQEVHDAARRARVAARRLASLPTTVKDRALHAAAdellahrdQILAANAEDLnaareadtpAAMLDRLSL 81
Cdd:cd07145 14 TVPSLS----REEVREAIEVAEKAKDVMSNLPAYKRYKILMKVA--------ELIERRKEEL---------AKLLTIEVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 82 NPQRvDGIAAGLRQVAGLRDPVGEV--LRGYTLP----NGLQLR---QQRVPLGVVGMI--YEGRPNVTVDAFGLTLKSG 150
Cdd:cd07145 73 KPIK-QSRVEVERTIRLFKLAAEEAkvLRGETIPvdayEYNERRiafTVREPIGVVGAItpFNFPANLFAHKIAPAIAVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 151 NAALLRGSSSAaksneALVAVLRTALV-GLELPADAVQLLSAADR----ATVTH----LIQARGLVDVviprgGAGLIEA 221
Cdd:cd07145 152 NSVVVKPSSNT-----PLTAIELAKILeEAGLPPGVINVVTGYGSevgdEIVTNpkvnMISFTGSTAV-----GLLIASK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 222 VVRDAQVPTIETGvGNCHVYVHQAADLDVAERILLNSK-TRRPSVCNAAETLLVDAAIAETALPRL-------------- 286
Cdd:cd07145 222 AGGTGKKVALELG-GSDPMIVLKDADLERAVSIAVRGRfENAGQVCNAVKRILVEEEVYDKFLKLLvekvkklkvgdpld 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 287 -------LAALQHA-------------GVTVHL------------------DPDEADLRREYLSLDIAVAVVDGVDAA-- 326
Cdd:cd07145 301 estdlgpLISPEAVermenlvndavekGGKILYggkrdegsffpptvlendTPDMIVMKEEVFGPVLPIAKVKDDEEAve 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489507647 327 IAHINEYGTghTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAF-TDGEQFG 376
Cdd:cd07145 381 IANSTEYGL--QASVFTNDINRALKVARELEAGGVVINDSTRFrWDNLPFG 429
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
12-406 |
3.32e-03 |
|
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: 39.62 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 12 RQEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAR-EADTPAAMLDRLslnpqrvdgia 90
Cdd:cd07150 20 RQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYgKAWFETTFTPEL----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 91 agLRQVAGL-RDPVGEVLRgyTLPNGLQLRQQRVPLGVVGMI--YEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEA 167
Cdd:cd07150 89 --LRAAAGEcRRVRGETLP--SDSPGTVSMSVRRPLGVVAGItpFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 168 LVAVLRTAlvglELPADAVQLLSAAdRATVTHLIQARGLVDVVIPRG----GAGLIEAVVRDAQVPTIETGvGNCHVYVH 243
Cdd:cd07150 165 IAEIMEEA----GLPKGVFNVVTGG-GAEVGDELVDDPRVRMVTFTGstavGREIAEKAGRHLKKITLELG-GKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 244 QAADLDVAERILLNSK-TRRPSVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPDE------ADLRREYLS--LD 314
Cdd:cd07150 239 ADADLDYAVRAAAFGAfMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTvigpliSPRQVERIKrqVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 315 IAVA-------------------VVDGVDA--------------------------AIAHINEYGTghTEAIVTTNLDAA 349
Cdd:cd07150 319 DAVAkgaklltggkydgnfyqptVLTDVTPdmrifreetfgpvtsvipakdaeealELANDTEYGL--SAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489507647 350 QRFTEQIDAAAVMVNASTaFTDGEQFGFGA--EIGISTQKlharGPMGLPELTSTKWIA 406
Cdd:cd07150 397 FKLAERLESGMVHINDPT-ILDEAHVPFGGvkASGFGREG----GEWSMEEFTELKWIT 450
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
30-363 |
5.02e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 39.47 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 30 ASLPTTVKDRALHAAADELLAHRDQILAANAED--LNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVL 107
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGalLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 108 RGYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQ 187
Cdd:COG3321 941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 188 LLSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCN 267
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 268 AAETLLVDAAIAETALPRLLAALQHAGVTVHLDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLD 347
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
|
330
....*....|....*.
gi 489507647 348 AAQRFTEQIDAAAVMV 363
Cdd:COG3321 1181 LAAALAAALAGLAALL 1196
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3-360 |
5.81e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 39.09 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 3 VPAPSQLDLRQEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLN 82
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 83 PQRVDGIAAGLRQVAGLRDPVGEVLRGYTLPNGLQLRQQRVPLGVVG-MIYEGRPNVTVDAFGLTLKSGNAALLRGSSSA 161
Cdd:COG3321 941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAaAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 162 AKSNEALVAVLRTALVGLELPADAVQLLSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVY 241
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 242 VHQAADLDVAERILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPDEADLRREYLSLDIAVAVVD 321
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
|
330 340 350
....*....|....*....|....*....|....*....
gi 489507647 322 GVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAA 360
Cdd:COG3321 1181 LAAALAAALAGLAALLLAALLAALLAALLALALAALAAA 1219
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
300-382 |
8.86e-03 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 38.19 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507647 300 DPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVN------ASTAFTDGE 373
Cdd:cd07113 372 SADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfldPAVPFGGMK 451
|
....*....
gi 489507647 374 QFGFGAEIG 382
Cdd:cd07113 452 QSGIGREFG 460
|
|
| |
