|
Name |
Accession |
Description |
Interval |
E-value |
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
52-420 |
0e+00 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 734.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 52 ANEQDLAAGRANGLEPAMLDRLALTPARIDDMIEGLRQVATLPDPIGEIRDMRYVPSGIQIGKMRVPLGVVGIIYESRPN 131
Cdd:PRK00197 49 ANAKDLAAARANGLSAAMLDRLLLTEARIEGIAEGLRQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 132 VTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVETTDRAAVGALISMPEYVDVIVPRGGKG 211
Cdd:PRK00197 129 VTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 212 LIERISREAKVPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLLVHAGIAERVLPPLATIYREKGVEL 291
Cdd:PRK00197 209 LIRRVVENATVPVIEHGDGICHIYVDESADLDKALKIVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEALAEAGVEL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 292 RGDAATRALLgADVLEATEEDWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMVN 371
Cdd:PRK00197 289 RGDEAALALL-PDVVPATEEDWDTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVN 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15599202 372 ASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEKYVVFGDGHVR 420
Cdd:PRK00197 368 ASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYIVLGDGQIR 416
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
52-420 |
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: 726.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 52 ANEQDLAAGRANGLEPAMLDRLALTPARIDDMIEGLRQVATLPDPIGEIRDMRYVPSGIQIGKMRVPLGVVGIIYESRPN 131
Cdd:COG0014 46 ANAKDLEAARENGLSEALLDRLKLTEERIEAMAEGLRQVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 132 VTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVETTDRAAVGALISMPEYVDVIVPRGGKG 211
Cdd:COG0014 126 VTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVIQEALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 212 LIERISREAKVPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLLVHAGIAERVLPPLATIYREKGVEL 291
Cdd:COG0014 206 LIRRVVENATVPVIEHGDGNCHVYVDASADLEMAVDIVVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAEAGVEL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 292 RGDAATRALLgADVLEATEEDWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMVN 371
Cdd:COG0014 286 RGDERTRAIL-PDVKPATEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVN 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15599202 372 ASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEKYVVFGDGHVR 420
Cdd:COG0014 365 ASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYVVRGDGQIR 413
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
52-416 |
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: 673.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 52 ANEQDLAAGRANGLEPAMLDRLALTPARIDDMIEGLRQVATLPDPIGEIRDMRYVPSGIQIGKMRVPLGVVGIIYESRPN 131
Cdd:cd07079 43 ANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQVAALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 132 VTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVETTDRAAVGALISMPEYVDVIVPRGGKG 211
Cdd:cd07079 123 VTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQEALEEAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 212 LIERISREAKVPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLLVHAGIAERVLPPLATIYREKGVEL 291
Cdd:cd07079 203 LIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIVVNAKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGVEL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 292 RGDAATRALLGaDVLEATEEDWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMVN 371
Cdd:cd07079 283 RGDEETLAILP-GAKPATEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVN 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15599202 372 ASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEKYVVFGD 416
Cdd:cd07079 362 ASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYIVRGD 406
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
28-410 |
5.63e-172 |
|
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: 486.99 E-value: 5.63e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 28 TAQKNRALLAAADALDAARAELSHANEQDLAAGRANGLEPAMLDRLALTPARIDDMIEGLRQVATLPDPIGEIRDMRYVP 107
Cdd:TIGR00407 13 TAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELADPVGKVIDGRELD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 108 SGIQIGKMRVPLGVVGIIYESRPNVTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVETTD 187
Cdd:TIGR00407 93 SGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTGLPVGAVQLIETPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 188 RAAVGALISMPEYVDVIVPRGGKGLIERISREAKVPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLL 267
Cdd:TIGR00407 173 RELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVLGHGDGICHIYLDESADLIKAIKVIVNAKTQRPSTCNAIETLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 268 VHAGIAERVLPPLATIYREKGVELRGDAATRALL---GADVLEATEEDWRTEYNAPILSIRIVDGLDAAIEHINTYGSQH 344
Cdd:TIGR00407 253 VNKAIAREFLPVLENQLLEKGVTIHADAYALKLLelgPATEAIVCKTDFDKEFLSLDLSVKIVESLEAAIQHINQYGTQH 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599202 345 TDAIITENFSDARRFLAEVDSASVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEK 410
Cdd:TIGR00407 333 SDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK 398
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
52-419 |
1.46e-109 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 338.24 E-value: 1.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 52 ANEQDLAAGRANGLEPAMLDRLALTPARIDDMIEGLRQVATLPDPIGEIRDMRYVPSGIQIGKMRVPLGVVGIIYESRPN 131
Cdd:PLN02418 339 ENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLADMEDPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPD 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 132 VTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEA--GLPAAAVqvvetTDRAAVGALISMPEYVDVIVPRGG 209
Cdd:PLN02418 419 ALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTvgGKLIGLV-----TSRDEIPDLLKLDDVIDLVIPRGS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 210 KGLIERISREAKVPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLLVHAGIAER-VLPPLATIYREKG 288
Cdd:PLN02418 494 NKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAACNAMETLLVHKDLVQNgGLNDLLVALRSAG 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 289 VELRGDAATRALLGadVLEATEedWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASV 368
Cdd:PLN02418 574 VTLYGGPRASKLLN--IPEAQS--FHHEYSSLACTVEIVDDVHAAIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAV 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15599202 369 MVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEKYVVFGDGHV 419
Cdd:PLN02418 650 FHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQV 700
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
48-419 |
1.70e-102 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 319.93 E-value: 1.70e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 48 ELSHANEQDLAAGRANGLEPAMLDRLALTPARIDDMIEGLRQVATLPDPIGEIRDMRYVPSGIQIGKMRVPLGVVGIIYE 127
Cdd:TIGR01092 327 EILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAISLRQLAAMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 128 SRPNVTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLpAAAVQVVetTDRAAVGALISMPEYVDVIVPR 207
Cdd:TIGR01092 407 SRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVG-KKLIGLV--TSREEIPDLLKLDDVIDLVIPR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 208 GGKGLIERISREAKVPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLLVHAGIAER-VLPPLATIYRE 286
Cdd:TIGR01092 484 GSNKLVSQIKKSTKIPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAMETLLVHKDLLRNgLLDDLIDMLRT 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 287 KGVELRGDAATRALLGADVLEAteEDWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSA 366
Cdd:TIGR01092 564 EGVTIHGGPRFAAYLTFNISET--KSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSA 641
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15599202 367 SVMVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEKYVVFGDGHV 419
Cdd:TIGR01092 642 AVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQV 694
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
65-413 |
2.71e-47 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 166.63 E-value: 2.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 65 LEPAMLDRLALTPARIDDMIEGLRQVatlPDPIGEIRDmRYVPSGIQIGKMRVPLGVVGIIYESR-PNVTIDAASLCLKS 143
Cdd:cd07077 51 LIANWIAMMGCSESKLYKNIDTERGI---TASVGHIQD-VLLPDNGETYVRAFPIGVTMHILPSTnPLSGITSALRGIAT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 144 GNATILRGGSEAIHSNQAIARCIQQGLAeAGLPAAAVQVVETTDRAAVGALISMPEyVDVIVPRGGKGLIERISREAK-V 222
Cdd:cd07077 127 RNQCIFRPHPSAPFTNRALALLFQAADA-AHGPKILVLYVPHPSDELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPhI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 223 PVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAPCNTMETLLVHAGIAERVLPPLATIYREKGVELRgdAATRALLG 302
Cdd:cd07077 205 PVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVP--QETKPLSK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 303 aDVLEATEEDWRTEYNAPILSIRIVDGLDA---AIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMVNASTRFADG 379
Cdd:cd07077 283 -ETTPSFDDEALESMTPLECQFRVLDVISAvenAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRG 361
|
330 340 350
....*....|....*....|....*....|....*
gi 15599202 380 FEYGLGAEIGISTDKLHARG-PVGLEGLTSEKYVV 413
Cdd:cd07077 362 AFAGKGVERIVTSGMNNIFGaGVGHDALRPLKRLV 396
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
78-414 |
2.52e-37 |
|
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: 139.29 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 78 ARIDDMIEGLRQVATLPDPIGEIRdmryvpsgiqigkmRVPLGVVGIIYESRP--NVTIDAASLCLKSGNATILRGGSEA 155
Cdd:cd06534 66 AGLADKLGGPELPSPDPGGEAYVR--------------REPLGVVGVITPWNFplLLAAWKLAPALAAGNTVVLKPSELT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 156 IHSNQAIARCIQqglaEAGLPAAAVQVVETTDRAAVGALISMPEyVDVIVPRGGKGLIERISREAK---VPVIKHLDGIC 232
Cdd:cd06534 132 PLTALALAELLQ----EAGLPPGVVNVVPGGGDEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAenlKPVTLELGGKS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 233 HVYIDVAADLDKAIRVADNAKT----QRyapCNTMETLLVHAGIAERVLPPLATIYrekgvelrgdaatrallgADVLEA 308
Cdd:cd06534 207 PVIVDEDADLDAAVEGAVFGAFfnagQI---CTAASRLLVHESIYDEFVEKLVTVL------------------VDVDPD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 309 TEEdWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMVNASTRFA-DGFEYGLGAE 387
Cdd:cd06534 266 MPI-AQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKN 344
|
330 340
....*....|....*....|....*..
gi 15599202 388 IGISTDKlharGPVGLEGLTSEKYVVF 414
Cdd:cd06534 345 SGIGREG----GPYGLEEYTRTKTVVI 367
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
116-378 |
7.03e-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: 79.17 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVVGIIyeSRPN--VTIDAASLC--LKSGNATILRGGSEAIHSNQAIARCIqqglAEAGLPAAAVQVVeTTDRAAV 191
Cdd:cd07078 94 REPLGVVGAI--TPWNfpLLLAAWKLApaLAAGNTVVLKPSELTPLTALLLAELL----AEAGLPPGVLNVV-TGDGDEV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 192 GALISMPEYVDVIV----PRGGKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVADNAKT----QRyapCNTM 263
Cdd:cd07078 167 GAALASHPRVDKISftgsTAVGKAIMRAAAENLK-RVTLELGGKSPLIVFDDADLDAAVKGAVFGAFgnagQV---CTAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 264 ETLLVHAGIAERVL-------------PPL-----------ATIYR--EKGVELRGDAATRALLGAD------------- 304
Cdd:cd07078 243 SRLLVHESIYDEFVerlvervkalkvgNPLdpdtdmgplisAAQLDrvLAYIEDAKAEGAKLLCGGKrleggkgyfvppt 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599202 305 VLEATEED---WRTEYNAPILSIRIVDGLDAAIEHIN--TYGSqhTDAIITENFSDARRFLAEVDSASVMVNASTRFAD 378
Cdd:cd07078 323 VLTDVDPDmpiAQEEIFGPVLPVIPFKDEEEAIELANdtEYGL--AAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
115-389 |
1.45e-15 |
|
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: 78.37 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 115 MRVPLGVVGIIyeSRPN--VTIDA--ASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVetTDRAA 190
Cdd:cd07086 130 QWNPLGVVGVI--TAFNfpVAVPGwnAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV--TGGGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 191 VGALISMPEYVDVIVPRG----GKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVADNA--KT--QRyapCNT 262
Cdd:cd07086 206 GGELLVHDPRVPLVSFTGstevGRRVGETVARRFG-RVLLELGGNNAIIVMDDADLDLAVRAVLFAavGTagQR---CTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 263 METLLVHAGIAERVLPPLATIYR-------------------EKGVELRGDAATRA-------LLGADVLEATEEDW--- 313
Cdd:cd07086 282 TRRLIVHESVYDEFLERLVKAYKqvrigdpldegtlvgplinQAAVEKYLNAIEIAksqggtvLTGGKRIDGGEPGNyve 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 314 --------------RTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFL--AEVDSASVMVNASTrfa 377
Cdd:cd07086 362 ptivtgvtddarivQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNIPT--- 438
|
330
....*....|..
gi 15599202 378 dgfeygLGAEIG 389
Cdd:cd07086 439 ------SGAEIG 444
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
80-379 |
1.79e-15 |
|
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: 77.86 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 80 IDDMIEGLRQVATLPDPI-GEIRDMryVPSGIQIGKMRVPLGVVGIIyeSRPNVTIDAASL----CLKSGNATILRGGSE 154
Cdd:COG1012 104 VDRAADFLRYYAGEARRLyGETIPS--DAPGTRAYVRREPLGVVGAI--TPWNFPLALAAWklapALAAGNTVVLKPAEQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 155 AIHSNQAIARCiqqgLAEAGLPAAAVQVVETTDRAAVGALISMPEyVDVIV----PRGGKGLIERISREAKvPVIKHLDG 230
Cdd:COG1012 180 TPLSALLLAEL----LEEAGLPAGVLNVVTGDGSEVGAALVAHPD-VDKISftgsTAVGRRIAAAAAENLK-RVTLELGG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 231 ICHVYIDVAADLDKAIRVADNAKT----QRyapCNTMETLLVHAGIAERVLP----------------------PLAT-- 282
Cdd:COG1012 254 KNPAIVLDDADLDAAVEAAVRGAFgnagQR---CTAASRLLVHESIYDEFVErlvaaakalkvgdpldpgtdmgPLISea 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 283 ----------IYREKGVEL-----RGDAATRALLGADVLEATEED---WRTEYNAPILSIRIVDGLDAAIEHINtygsqH 344
Cdd:COG1012 331 qlervlayieDAVAEGAELltggrRPDGEGGYFVEPTVLADVTPDmriAREEIFGPVLSVIPFDDEEEAIALAN-----D 405
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15599202 345 TD-----AIITENFSDARRFLAEVDSASVMVNASTRFADG 379
Cdd:COG1012 406 TEyglaaSVFTRDLARARRVARRLEAGMVWINDGTTGAVP 445
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
80-412 |
3.08e-14 |
|
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: 74.10 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 80 IDDMIEGLRQVATLPDPI-GEIRDMRYvpsGIQIGKMRVPLGVVGII--YESRPNVTIDAASLCLKSGNATILRGGSEAI 156
Cdd:pfam00171 90 VDRAIDVLRYYAGLARRLdGETLPSDP---GRLAYTRREPLGVVGAItpWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 157 HSNQAIARCIQqglaEAGLPAAAVQVVeTTDRAAVGALISMPEYVDVIVPRGGKGLIERISREAKVPVIKH---LDGICH 233
Cdd:pfam00171 167 LTALLLAELFE----EAGLPAGVLNVV-TGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVtleLGGKNP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 234 VYIDVAADLDKAIRVADNAKT----QRyapCNTMETLLVHAGIAERVLP----------------------PLAT----- 282
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFgnagQV---CTATSRLLVHESIYDEFVEklveaakklkvgdpldpdtdmgPLISkaqle 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 283 -------IYREKGVEL----RGDAATRALLGADVLEATEED---WRTEYNAPILSIRIVDGLDAAIEHINT--YGsqHTD 346
Cdd:pfam00171 319 rvlkyveDAKEEGAKLltggEAGLDNGYFVEPTVLANVTPDmriAQEEIFGPVLSVIRFKDEEEAIEIANDteYG--LAA 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599202 347 AIITENFSDARRFLAEVDSASVMVNASTRFAD------GF-EYGLGAEigistdklhaRGPVGLEGLTSEKYV 412
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDAdglpfgGFkQSGFGRE----------GGPYGLEEYTEVKTV 459
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
116-383 |
2.21e-10 |
|
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: 62.23 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVVGII--YESRPNVTIDAASLCLKSGNATILRGGSEAIHSNQAIArciqQGLAEAGLPAAAVQVVeTTDRAAVG- 192
Cdd:cd07149 121 REPIGVVAAItpFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLA----ELLLEAGLPKGALNVV-TGSGETVGd 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 193 ALISMPEyVDVIVPRGGKGLIERISREAKV-PVIKHLDGICHVYIDVAADLDKAIRVADNAKTqRYA--PCNTMETLLVH 269
Cdd:cd07149 196 ALVTDPR-VRMISFTGSPAVGEAIARKAGLkKVTLELGSNAAVIVDADADLEKAVERCVSGAF-ANAgqVCISVQRIFVH 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 270 AGIAERVLP-------------PL-------------ATIYREKGVELRGDAATRALLGAD---------VLEATEED-- 312
Cdd:cd07149 274 EDIYDEFLErfvaatkklvvgdPLdedtdvgpmiseaEAERIEEWVEEAVEGGARLLTGGKrdgaileptVLTDVPPDmk 353
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599202 313 -WRTEYNAPILSIRIVDGLDAAIEHINT--YGSQHtdAIITENFSDARRFLAEVDSASVMVNASTRF-ADGFEYG 383
Cdd:cd07149 354 vVCEEVFAPVVSLNPFDTLDEAIAMANDspYGLQA--GVFTNDLQKALKAARELEVGGVMINDSSTFrVDHMPYG 426
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
115-388 |
2.27e-10 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 62.36 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 115 MRVPLGVVGIIYESRPNVTIDAASLC--LKSGNATILRGGSEAIHSNQAIARCiqqgLAEAGLPAAAVQVVETTDRAAVG 192
Cdd:cd07131 132 RRQPIGVVALITPWNFPVAIPSWKIFpaLVCGNTVVFKPAEDTPACALKLVEL----FAEAGLPPGVVNVVHGRGEEVGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 193 ALISMPEyVDVIVPRG----GKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVA--DNAKT--QRyapCNTME 264
Cdd:cd07131 208 ALVEHPD-VDVVSFTGstevGERIGETCARPNK-RVALEMGGKNPIIVMDDADLDLALEGAlwSAFGTtgQR---CTATS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 265 TLLVHAGIAERVLP----------------------PLAT------------IYREKGVEL--------RGDAATRALLG 302
Cdd:cd07131 283 RLIVHESVYDEFLKrfverakrlrvgdgldeetdmgPLINeaqlekvlnyneIGKEEGATLllggerltGGGYEKGYFVE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 303 ADVLEATEEDWR---TEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMVNASTrfadg 379
Cdd:cd07131 363 PTVFTDVTPDMRiaqEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPT----- 437
|
....*....
gi 15599202 380 feygLGAEI 388
Cdd:cd07131 438 ----IGAEV 442
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
79-414 |
5.64e-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: 60.91 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 79 RIDDMIEGLRQVATLPDPIGEIRDMR--YVPSGIQIGK-------MRVPLGVVGII--YESRPNVTIDAASLCLKSGNAT 147
Cdd:cd07094 75 IKDARVEVDRAIDTLRLAAEEAERIRgeEIPLDATQGSdnrlawtIREPVGVVLAItpFNFPLNLVAHKLAPAIATGCPV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 148 ILRGGSEAIHSNQAIARCiqqgLAEAGLPAAAVQVVeTTDRAAVGALISMPEYVDVIVPRGGKGLIERISREAKVP-VIK 226
Cdd:cd07094 155 VLKPASKTPLSALELAKI----LVEAGVPEGVLQVV-TGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKrIAL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 227 HLDGICHVYIDVAADLDKAI-RVADNAKTQRYAPCNTMETLLVHAGIAERVLP----------------------PLATI 283
Cdd:cd07094 230 ELGGNAPVIVDRDADLDAAIeALAKGGFYHAGQVCISVQRIYVHEELYDEFIEafvaavkklkvgdpldedtdvgPLISE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 284 YREKGVELRGDAATR-------------ALLGADVLEATEED---WRTEYNAPILSIRIVDGLDAAIEHINT--YGSQht 345
Cdd:cd07094 310 EAAERVERWVEEAVEagarllcggerdgALFKPTVLEDVPRDtklSTEETFGPVVPIIRYDDFEEAIRIANStdYGLQ-- 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 346 DAIITENFSDARRFLAEVDSASVMVNASTRF-ADGFEYGLGAEIGISTDKLhargPVGLEGLTSEKYVVF 414
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFrTDWMPFGGVKESGVGREGV----PYAMEEMTEEKTVVI 453
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
100-371 |
8.20e-10 |
|
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: 60.20 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 100 IRDMRYVpsGI-------QIGKMRVPLGVV-GIIYESRPNVT-IDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGL 170
Cdd:cd07122 72 IKDMKTV--GVieedeekGIVEIAEPVGVIaALIPSTNPTSTaIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 171 AEAGLPAAAVQVVETTDRAAVGALISMPEyVDVIVPRGGKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVAD 250
Cdd:cd07122 150 VAAGAPEGLIQWIEEPSIELTQELMKHPD-VDLILATGGPGMVKAAYSSGK-PAIGVGPGNVPAYIDETADIKRAVKDII 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 251 NAKTQRYAP-CNTMETLLVHAGIAERVLPPL-----------------ATIYREKGVeLRGDAATR------ALLGADVL 306
Cdd:cd07122 228 LSKTFDNGTiCASEQSVIVDDEIYDEVRAELkrrgayflneeekekleKALFDDGGT-LNPDIVGKsaqkiaELAGIEVP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 307 EAT------------EEDWRTEYNAPILSIRIV----DGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEVDSASVMV 370
Cdd:cd07122 307 EDTkvlvaeetgvgpEEPLSREKLSPVLAFYRAedfeEALEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILV 386
|
.
gi 15599202 371 N 371
Cdd:cd07122 387 N 387
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
56-374 |
2.78e-08 |
|
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: 55.66 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 56 DLAAGRANGLEPAMLDRLALTPA----RIDDMIEGLRQVATLPDPIGEirdmRYVPSGIQiGK----MRVPLGVV-GIIY 126
Cdd:cd07105 33 DLLESRRDEFIEAMMEETGATAAwagfNVDLAAGMLREAASLITQIIG----GSIPSDKP-GTlamvVKEPVGVVlGIAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 127 ESRPnVTIDAASLC--LKSGNATILRGGSEAIHSNQAIARCiqqgLAEAGLPAAAVQVVETT-DRAA--VGALISMPEYV 201
Cdd:cd07105 108 WNAP-VILGTRAIAypLAAGNTVVLKASELSPRTHWLIGRV----FHEAGLPKGVLNVVTHSpEDAPevVEALIAHPAVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 202 DV------IVPRggkgLIERISREAKVPVIKHLDGICHVYIDVAADLDKAIR-VADNAKTQRYAPCNTMETLLVHAGIAE 274
Cdd:cd07105 183 KVnftgstRVGR----IIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANaALFGAFLNSGQICMSTERIIVHESIAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 275 R-----------------VLPPLATI------------YREKGVELRGDAATRALLGADVLEAT-----EED---WRTEY 317
Cdd:cd07105 259 EfveklkaaaeklfagpvVLGSLVSAaaadrvkelvddALSKGAKLVVGGLADESPSGTSMPPTildnvTPDmdiYSEES 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599202 318 NAPILSIRIVDGLDAAIEHINT--YGSqhTDAIITENFSDARRFLAEVDSASVMVNAST 374
Cdd:cd07105 339 FGPVVSIIRVKDEEEAVRIANDseYGL--SAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
116-376 |
3.68e-08 |
|
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: 55.05 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVVGII--YESRPNVTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQqglaEAGLPAAAVQVVeTTDRAAVGA 193
Cdd:cd07145 121 REPIGVVGAItpFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILE----EAGLPPGVINVV-TGYGSEVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 194 LISMPEYVDVIVPRGGKGLIERISREAKVP---VIKHLDGICHVYIDVAADLDKAIRVADNAKTQrYAP--CNTMETLLV 268
Cdd:cd07145 196 EIVTNPKVNMISFTGSTAVGLLIASKAGGTgkkVALELGGSDPMIVLKDADLERAVSIAVRGRFE-NAGqvCNAVKRILV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 269 HAGIAERVLP-------------PLAT-------IYRE--------------KG--VELRGDAATRALLGADVLEATEED 312
Cdd:cd07145 275 EEEVYDKFLKllvekvkklkvgdPLDEstdlgplISPEavermenlvndaveKGgkILYGGKRDEGSFFPPTVLENDTPD 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599202 313 ---WRTEYNAPILSIRIVDGLDAAIEHINT--YGSQhtDAIITENFSDARRFLAEVDSASVMVNASTRF 376
Cdd:cd07145 355 mivMKEEVFGPVLPIAKVKDDEEAVEIANSteYGLQ--ASVFTNDINRALKVARELEAGGVVINDSTRF 421
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
115-276 |
4.48e-08 |
|
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: 55.04 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 115 MRVPLGVVGIIYESRPNVTIDAASL--CLKSGNATILRGGSEAIHSNQAIARCiqqgLAEA-GLPAAAVQVVeTTDRAAV 191
Cdd:cd07120 114 LREPMGVAGIIVPWNSPVVLLVRSLapALAAGCTVVVKPAGQTAQINAAIIRI----LAEIpSLPAGVVNLF-TESGSEG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 192 GA-LISMPEyVDVIVPRGGKGLIERISREAkVPVIK----HLDG-ICHVYIDvAADLDKAIRVADNAKT----QRyapCN 261
Cdd:cd07120 189 AAhLVASPD-VDVISFTGSTATGRAIMAAA-APTLKrlglELGGkTPCIVFD-DADLDAALPKLERALTifagQF---CM 262
|
170
....*....|....*
gi 15599202 262 TMETLLVHAGIAERV 276
Cdd:cd07120 263 AGSRVLVQRSIADEV 277
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
92-374 |
1.17e-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: 53.79 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 92 TLPDPIGE----IRDMRY------------VPS---GIQIGKMRVPLGVVGIIYE-----SRPNVTIDAAslcLKSGNAT 147
Cdd:cd07097 90 TLPEARGEvtraGQIFRYyagealrlsgetLPStrpGVEVETTREPLGVVGLITPwnfpiAIPAWKIAPA---LAYGNTV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 148 ILRGGSEAIHSNQAIARCIqqglAEAGLPAAAVQVVETTDRAAVGALISMPEyVDVIVPRGGKGLIERISREAKVPVIK- 226
Cdd:cd07097 167 VFKPAELTPASAWALVEIL----EEAGLPAGVFNLVMGSGSEVGQALVEHPD-VDAVSFTGSTAVGRRIAAAAAARGARv 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 227 --HLDGICHVYIDVAADLDKAIRVADN----AKTQRyapCNTMETLLVHAGIAERVLP---------------------- 278
Cdd:cd07097 242 qlEMGGKNPLVVLDDADLDLAVECAVQgaffSTGQR---CTASSRLIVTEGIHDRFVEalvertkalkvgdaldegvdig 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 279 PLAT------------IYREKGVELR--GDAATRA----LLGADVLEATEEDWRT---EYNAPILSIRIVDGLDAAIEHI 337
Cdd:cd07097 319 PVVSerqlekdlryieIARSEGAKLVygGERLKRPdegyYLAPALFAGVTNDMRIareEIFGPVAAVIRVRDYDEALAIA 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 15599202 338 NT--YGsqHTDAIITENFSDARRFLAEVDSASVMVNAST 374
Cdd:cd07097 399 NDteFG--LSAGIVTTSLKHATHFKRRVEAGVVMVNLPT 435
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
116-388 |
2.12e-07 |
|
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: 52.62 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVVGIIYESRPNVTIDAASLC--LKSGNATILRGGSEAIHSNQAIARCiqqgLAEAGLPAAAVQVVETTDRAAVGA 193
Cdd:cd07109 115 REPHGVTGHIIPWNYPLQITGRSVApaLAAGNAVVVKPAEDAPLTALRLAEL----AEEAGLPAGALNVVTGLGAEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 194 LISMPEyVDVIV----PRGGKgLIERISREAKVPVIKHLDG----IchVYIDvaADLDKAIRVADNAKTQRYAP-CNTME 264
Cdd:cd07109 191 LVAHPG-VDHISftgsVETGI-AVMRAAAENVVPVTLELGGkspqI--VFAD--ADLEAALPVVVNAIIQNAGQtCSAGS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 265 TLLVHAGIAERVLPPLATIYREKGV--------------------------ELRGDAATRALLGADVLEATEEDW----- 313
Cdd:cd07109 265 RLLVHRSIYDEVLERLVERFRALRVgpgledpdlgplisakqldrvegfvaRARARGARIVAGGRIAEGAPAGGYfvapt 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 314 ------------RTEYNAPILSIRIVDGLDAAIEHINTygsqhTD-----AIITENFSDARRFLAEVDSASVMVNastrf 376
Cdd:cd07109 345 llddvppdsrlaQEEIFGPVLAVMPFDDEAEAIALANG-----TDyglvaGVWTRDGDRALRVARRLRAGQVFVN----- 414
|
330
....*....|..
gi 15599202 377 adgfEYGLGAEI 388
Cdd:cd07109 415 ----NYGAGGGI 422
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
118-389 |
4.70e-06 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 48.74 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 118 PLGVVGIIyeSRPN--VTIDA--ASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVetTDRAAVGA 193
Cdd:cd07130 132 PLGVVGVI--TAFNfpVAVWGwnAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLV--CGGADVGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 194 LISMPEYVDVIVPRG----GKGLIERIS-REAKVpvIKHLDGICHVYIDVAADLDKAIRVADNAKT----QRyapCNTME 264
Cdd:cd07130 208 ALVKDPRVPLVSFTGstavGRQVGQAVAaRFGRS--LLELGGNNAIIVMEDADLDLAVRAVLFAAVgtagQR---CTTTR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 265 TLLVHAGIAERVLPPLATIYR-------------------EKGVELRGDAATRA-------LLGADVLE----------- 307
Cdd:cd07130 283 RLIVHESIYDEVLERLKKAYKqvrigdplddgtlvgplhtKAAVDNYLAAIEEAksqggtvLFGGKVIDgpgnyveptiv 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 308 ---ATEEDWRTEYNAPILSIRIVDGLDAAIEHINTYGSQHTDAIITENFSDARRFLAEV--DSASVMVNASTRfadgfey 382
Cdd:cd07130 363 eglSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTS------- 435
|
....*..
gi 15599202 383 glGAEIG 389
Cdd:cd07130 436 --GAEIG 440
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
118-392 |
4.93e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.42 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 118 PLGVV-GIIYESRPNVT-IDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVVETTDRAAVGALI 195
Cdd:cd07081 95 PIGVVaSITPSTNPTSTvIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 196 SMPEyVDVIVPRGGKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVADNAKT-QRYAPCNTMETLLVHAGIAE 274
Cdd:cd07081 175 KFPG-IGLLLATGGPAVVKAAYSSGK-PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTfDNGVICASEQSVIVVDSVYD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 275 RVLPPLAT--IYREKGVELR-----------------GDAA--------------TRALLGADVLEATEEDWRTEYNAPI 321
Cdd:cd07081 253 EVMRLFEGqgAYKLTAEELQqvqpvilkngdvnrdivGQDAykiaaaaglkvpqeTRILIGEVTSLAEHEPFAHEKLSPV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 322 LSIRIVDGLDAAIEH----INTYGSQHTDAIITENFS---DARRFLAEVDSASVMVNASTRFA---DGFEYGLGAEIGIS 391
Cdd:cd07081 333 LAMYRAANFADADAKalalKLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKNGPCSQGglgDLYNFRGWPSMTLG 412
|
.
gi 15599202 392 T 392
Cdd:cd07081 413 C 413
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
96-371 |
9.94e-06 |
|
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: 47.52 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 96 PIGEIRDMR------------YVPSGIQIGKMRV---PLGVVGII----YesrP-NVTIDAASLCLKSGNATILRGgSEa 155
Cdd:cd07087 63 VLGEIDHALkhlkkwmkprrvSVPLLLQPAKAYVipePLGVVLIIgpwnY---PlQLALAPLIGAIAAGNTVVLKP-SE- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 156 iHSnQAIARCIQQGLAEAgLPAAAVQVVETTDRAAVgALISMPeyVDVIV----PRGGKgLIERISREAKVPVIKHLDGI 231
Cdd:cd07087 138 -LA-PATSALLAKLIPKY-FDPEAVAVVEGGVEVAT-ALLAEP--FDHIFftgsPAVGK-IVMEAAAKHLTPVTLELGGK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 232 CHVYIDVAADLDKAI-RVA----DNAKTQRYAPcntmETLLVHAGIAERVLPPLatiyREKGVELRGD------------ 294
Cdd:cd07087 211 SPCIVDKDANLEVAArRIAwgkfLNAGQTCIAP----DYVLVHESIKDELIEEL----KKAIKEFYGEdpkespdygrii 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 295 ------------AATRALLGADVLEA---------TEEDW-----RTEYNAPILSIRIVDGLDAAIEHINTYgsQHTDA- 347
Cdd:cd07087 283 nerhfdrlasllDDGKVVIGGQVDKEeryiaptilDDVSPdsplmQEEIFGPILPILTYDDLDEAIEFINSR--PKPLAl 360
|
330 340
....*....|....*....|....*
gi 15599202 348 -IITENFSDARRFLAEVDSASVMVN 371
Cdd:cd07087 361 yLFSEDKAVQERVLAETSSGGVCVN 385
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
115-374 |
1.16e-05 |
|
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: 47.32 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 115 MRVPLGVVGIIyeSRPNV----TIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQqglaEAGLPAAAVQVVeTTDRAA 190
Cdd:cd07150 116 VRRPLGVVAGI--TPFNYplilATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIME----EAGLPKGVFNVV-TGGGAE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 191 VGALISMPEYVDVIVPRG----GKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVAD-NAKTQRYAPCNTMET 265
Cdd:cd07150 189 VGDELVDDPRVRMVTFTGstavGREIAEKAGRHLK-KITLELGGKNPLIVLADADLDYAVRAAAfGAFMHQGQICMSASR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 266 LLVHAGIAERVLPPLATIYREKGVELRGDAAT----------RALL----------GADVLEATEED------------- 312
Cdd:cd07150 268 IIVEEPVYDEFVKKFVARASKLKVGDPRDPDTvigplisprqVERIkrqvedavakGAKLLTGGKYDgnfyqptvltdvt 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599202 313 -----WRTEYNAPILSIRIVDGLDAAIEHINT--YGSqhTDAIITENFSDARRFLAEVDSASVMVNAST 374
Cdd:cd07150 348 pdmriFREETFGPVTSVIPAKDAEEALELANDteYGL--SAAILTNDLQRAFKLAERLESGMVHINDPT 414
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
83-204 |
1.43e-05 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 47.14 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 83 MIEGLRQVATLP-DPIGEIrdmryVPSGIQiGKM----RVPLGVVGIIyeSRPNV----TIDAASLCLKSGNATILRGGS 153
Cdd:cd07104 64 AIAILREAAGLPrRPEGEI-----LPSDVP-GKEsmvrRVPLGVVGVI--SPFNFplilAMRSVAPALALGNAVVLKPDS 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15599202 154 E-AIHSNQAIARCiqqgLAEAGLPAAAVQVVeTTDRAAVG-ALISMPEyVDVI 204
Cdd:cd07104 136 RtPVTGGLLIAEI----FEEAGLPKGVLNVV-PGGGSEIGdALVEHPR-VRMI 182
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
81-375 |
7.06e-05 |
|
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: 44.87 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 81 DDMIEGLRQVATLPDPIGEIRDMR--YVPSGIQIGK-------MRVPLGVVGII----YesrP-NVTIDAASLCLKSGNA 146
Cdd:cd07082 95 DALKEVDRTIDYIRDTIEELKRLDgdSLPGDWFPGTkgkiaqvRREPLGVVLAIgpfnY---PlNLTVSKLIPALIMGNT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 147 TILRGGSEAIHSNQAIARCiqqgLAEAGLPAAAVQVVeTTDRAAVGALISMPEYVDVIVPRGGKGLIERISREA-KVPVI 225
Cdd:cd07082 172 VVFKPATQGVLLGIPLAEA----FHDAGFPKGVVNVV-TGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHpMKRLV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 226 KHLDGichvyIDVA-----ADLDKAI-RVADNAKT---QRyapCNTMETLLVHAGIAERVLP----------------PL 280
Cdd:cd07082 247 LELGG-----KDPAivlpdADLELAAkEIVKGALSysgQR---CTAIKRVLVHESVADELVEllkeevaklkvgmpwdNG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 281 ATI------------------YREKGVEL--RGDAATRALLGADVLEATEEDWRT---EYNAPILSIRIVDGLDAAIEHI 337
Cdd:cd07082 319 VDItplidpksadfvegliddAVAKGATVlnGGGREGGNLIYPTLLDPVTPDMRLaweEPFGPVLPIIRVNDIEEAIELA 398
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15599202 338 NT--YGSQhtDAIITENFSDARRFLAEVDSASVMVNASTR 375
Cdd:cd07082 399 NKsnYGLQ--ASIFTKDINKARKLADALEVGTVNINSKCQ 436
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
104-275 |
8.35e-05 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 44.73 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 104 RYVPS---GIQIGKMRVPLGVVGIIyesRP------NVT--IDAAslcLKSGNATILRGGSEAIHSNQAIARCIQqglaE 172
Cdd:cd07103 100 RTIPSpapGKRILVIKQPVGVVAAI---TPwnfpaaMITrkIAPA---LAAGCTVVLKPAEETPLSALALAELAE----E 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 173 AGLPAAAVQVVeTTDRAAVG-ALISMPeyvdviVPRG---------GKGLIE-------RISRE----AkvPVIkhldgi 231
Cdd:cd07103 170 AGLPAGVLNVV-TGSPAEIGeALCASP------RVRKisftgstavGKLLMAqaadtvkRVSLElggnA--PFI------ 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599202 232 chVYIDvaADLDKAIRVADNAKTQryapcNTMET------LLVHAGIAER 275
Cdd:cd07103 235 --VFDD--ADLDKAVDGAIASKFR-----NAGQTcvcanrIYVHESIYDE 275
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
106-371 |
1.93e-04 |
|
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: 43.66 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 106 VPSGIQIGKMRVPLGVVGIIYESR-----PNVTIDAASLClksGNATILRGGSEAIHSNQAIARCIQqglaEAGLPAAAV 180
Cdd:cd07085 124 VARGIDTYSYRQPLGVVAGITPFNfpamiPLWMFPMAIAC---GNTFVLKPSERVPGAAMRLAELLQ----EAGLPDGVL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 181 QVVeTTDRAAVGALISMPEyVDVIVPRG----GKGLIERISREAKvPVIKHLDGICHVYIDVAADLDKAIRVADNAKT-- 254
Cdd:cd07085 197 NVV-HGGKEAVNALLDHPD-IKAVSFVGstpvGEYIYERAAANGK-RVQALGGAKNHAVVMPDADLEQTANALVGAAFga 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 255 --QRyapCNTMETLLVHAGIAERVLPPLAtiyrEKGVELRGDAAT-----------------------RAL--------- 300
Cdd:cd07085 274 agQR---CMALSVAVAVGDEADEWIPKLV----ERAKKLKVGAGDdpgadmgpvispaakerieglieSGVeegaklvld 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 301 --------------LGADVLEATEED---WRTEYNAPILSIRIVDGLDAAIEHINT--YGsqHTDAIITENFSDARRFLA 361
Cdd:cd07085 347 grgvkvpgyengnfVGPTILDNVTPDmkiYKEEIFGPVLSIVRVDTLDEAIAIINAnpYG--NGAAIFTRSGAAARKFQR 424
|
330
....*....|
gi 15599202 362 EVDSASVMVN 371
Cdd:cd07085 425 EVDAGMVGIN 434
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
82-373 |
2.01e-04 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 43.49 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 82 DMIEGLRQVATLPDPIGEIRDMRYVpsgiqigkMRVPLGVVGIIYE-SRPNVTidAA---SLCLKSGNATILRGGSEAIH 157
Cdd:cd07110 92 DLAEQLDAKAERAVPLPSEDFKARV--------RREPVGVVGLITPwNFPLLM--AAwkvAPALAAGCTVVLKPSELTSL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 158 SNQAIARCIqqglAEAGLPAAAVQVVeTTDRAAVGALISMPEYVDVIVPRGGKGLIERISREAKV---PVIKHLDGICHV 234
Cdd:cd07110 162 TELELAEIA----AEAGLPPGVLNVV-TGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQdikPVSLELGGKSPI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 235 YIDVAADLDKAIRVA------DNAKTqryapCNTMETLLVHAGIAERVLPPLATIYR--------EKGVEL--------- 291
Cdd:cd07110 237 IVFDDADLEKAVEWAmfgcfwNNGQI-----CSATSRLLVHESIADAFLERLATAAEairvgdplEEGVRLgplvsqaqy 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 292 --------RG-DAATRALLGADVLEATEED-----------------WRTEYNAPILSIRIVDGLDAAIEHINT--YGSq 343
Cdd:cd07110 312 ekvlsfiaRGkEEGARLLCGGRRPAHLEKGyfiaptvfadvptdsriWREEIFGPVLCVRSFATEDEAIALANDseYGL- 390
|
330 340 350
....*....|....*....|....*....|
gi 15599202 344 hTDAIITENFSDARRFLAEVDSASVMVNAS 373
Cdd:cd07110 391 -AAAVISRDAERCDRVAEALEAGIVWINCS 419
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
116-272 |
6.78e-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: 41.85 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVVGII------YESRPNVTIDAaslcLKSGNATILRggseaiHSNQA--IARCIQQGLAEAGLPAAAVQVVETTD 187
Cdd:cd07102 114 REPLGVVLIIapwnypYLTAVNAVIPA----LLAGNAVILK------HSPQTplCGERFAAAFAEAGLPEGVFQVLHLSH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 188 rAAVGALISMPeYVDVIV----PRGGKglieRISREAKVPVIK---HLDGICHVYIDVAADLDKAI-RVADNAKTQRYAP 259
Cdd:cd07102 184 -ETSAALIADP-RIDHVSftgsVAGGR----AIQRAAAGRFIKvglELGGKDPAYVRPDADLDAAAeSLVDGAFFNSGQS 257
|
170
....*....|...
gi 15599202 260 CNTMETLLVHAGI 272
Cdd:cd07102 258 CCSIERIYVHESI 270
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
84-281 |
7.73e-04 |
|
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: 41.51 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 84 IEGLRQVATLP-DPIGEIrdmryVPSgiQIGKM----RVPLGVVGIIyeSRPN----VTIDAASLCLKSGNATILRGGSE 154
Cdd:cd07152 78 IGELHEAAGLPtQPQGEI-----LPS--APGRLslarRVPLGVVGVI--SPFNfpliLAMRSVAPALALGNAVVLKPDPR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 155 -AIHSNQAIARCiqqgLAEAGLPAAAVQVVeTTDRAAVGALISMPEyVDVIVPRGGKGLIERISREA-----KVPVikHL 228
Cdd:cd07152 149 tPVSGGVVIARL----FEEAGLPAGVLHVL-PGGADAGEALVEDPN-VAMISFTGSTAVGRKVGEAAgrhlkKVSL--EL 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599202 229 DGICHVYIDVAADLDKAIR-VADNAKTQRYAPCNTMETLLVHAGIAERVLPPLA 281
Cdd:cd07152 221 GGKNALIVLDDADLDLAASnGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLA 274
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
115-390 |
1.34e-03 |
|
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: 40.61 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 115 MRVPLGVVGIIYESRPNVTIDAASL--CLKSGNATILRGGSEAIHSNQAIARCIQqglaEAGLPAAAVQVVeTTDRAAVG 192
Cdd:cd07114 116 RREPLGVVAAITPWNSPLLLLAKKLapALAAGNTVVLKPSEHTPASTLELAKLAE----EAGFPPGVVNVV-TGFGPETG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 193 -ALISMPEyVDVIV----PRGGKGLIE-------RISREA--KVPVIkhldgichVYIDvaADLDKAIR--VADN--AKT 254
Cdd:cd07114 191 eALVEHPL-VAKIAftggTETGRHIARaaaenlaPVTLELggKSPNI--------VFDD--ADLDAAVNgvVAGIfaAAG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 255 QryaPCNTMETLLVHAGIAERVL--------------P--------PLAT------------IYREKGVELR--GDAATR 298
Cdd:cd07114 260 Q---TCVAGSRLLVQRSIYDEFVerlvararairvgdPldpetqmgPLATerqlekveryvaRAREEGARVLtgGERPSG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 299 ALLGAD------VLEATEED---WRTEYNAPILSIRIVDGLDAAIEHIN--TYGSqhTDAIITENFSDARRFLAEVDSAS 367
Cdd:cd07114 337 ADLGAGyffeptILADVTNDmriAQEEVFGPVLSVIPFDDEEEAIALANdsEYGL--AAGIWTRDLARAHRVARAIEAGT 414
|
330 340
....*....|....*....|....*....
gi 15599202 368 VMVNASTRFA-----DGF-EYGLGAEIGI 390
Cdd:cd07114 415 VWVNTYRALSpsspfGGFkDSGIGRENGI 443
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
118-283 |
2.45e-03 |
|
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: 39.98 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 118 PLGVVGII----YesrP--NVtIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQQGLAEAGLPAAAVQVV----ETTD 187
Cdd:cd07098 120 PLGVVGAIvswnY---PfhNL-LGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVtclpETAE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 188 raavgALISMPEyVDVIVPRGGKGLIERISREAK---VPVIKHLDGICHVYIDVAADLDKAIRVADNAKTQRYAP-CNTM 263
Cdd:cd07098 196 -----ALTSHPV-IDHITFIGSPPVGKKVMAAAAeslTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQnCIGI 269
|
170 180
....*....|....*....|
gi 15599202 264 ETLLVHAGIAERVLPPLATI 283
Cdd:cd07098 270 ERVIVHEKIYDKLLEILTDR 289
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
116-390 |
3.36e-03 |
|
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: 39.56 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVV-GIIYESRPNVTIdAASL--CLKSGNATILRGGSEAIHSNQAIARCIQqglaEAGLPAAAVQVVeTTDRAAVG 192
Cdd:cd07088 131 KVPIGVVaGILPWNFPFFLI-ARKLapALVTGNTIVIKPSEETPLNALEFAELVD----EAGLPAGVLNIV-TGRGSVVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 193 ALISMPEYVDVIVPRGGKGLIERISREAKVPVIK---HLDGICHVYIDVAADLDKAIRVADNAKT----QryaPCNTMET 265
Cdd:cd07088 205 DALVAHPKVGMISLTGSTEAGQKIMEAAAENITKvslELGGKAPAIVMKDADLDLAVKAIVDSRIincgQ---VCTCAER 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 266 LLVHAGIAERVLPPLATIYREKGVELRGDAATR--ALLGADVLEATEE------------------------DW------ 313
Cdd:cd07088 282 VYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDmgPLVNEAALDKVEEmveraveagatlltggkrpegekgYFyeptvl 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 314 ----------RTEYNAPILSIRIVDGLDAAIEHIN--TYGSqhTDAIITENFSDARRFLAEVDSASVMVN-----ASTRF 376
Cdd:cd07088 362 tnvrqdmeivQEEIFGPVLPVVKFSSLDEAIELANdsEYGL--TSYIYTENLNTAMRATNELEFGETYINrenfeAMQGF 439
|
330
....*....|....*
gi 15599202 377 ADGF-EYGLGAEIGI 390
Cdd:cd07088 440 HAGWkKSGLGGADGK 454
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
111-311 |
4.51e-03 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 39.14 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 111 QIGKMRVPLGVVGIIYESR-P--NVTIDAASlCLKSGNATILRGGSEAIHSNQAIARCIQQGLAeagLPAAAVQVVEtTD 187
Cdd:cd07084 93 QSHGYRWPYGPVLVIGAFNfPlwIPLLQLAG-ALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPEDVTLIN-GD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 188 RAAVGALISMPEyVDVIVPRGGKGLIERISREAK-VPVIKHLDGICHVYIDVAADLDKAirVADNAKTQRYA----PCNT 262
Cdd:cd07084 168 GKTMQALLLHPN-PKMVLFTGSSRVAEKLALDAKqARIYLELAGFNWKVLGPDAQAVDY--VAWQCVQDMTAcsgqKCTA 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599202 263 METLLVHA------------GIAERVLPPLATIYREKGVE-LRGDAATRALLGADVLEATEE 311
Cdd:cd07084 245 QSMLFVPEnwsktplveklkALLARRKLEDLLLGPVQTFTtLAMIAHMENLLGSVLLFSGKE 306
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
116-285 |
6.05e-03 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 38.57 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 116 RVPLGVVGIIYESRPNVTIDAASL--CLKSGNATILRGGSEAIHSNQAIARCiqqgLAEAGLPAAAVQVVETTDRAAVGA 193
Cdd:cd07115 115 REPVGVVGAIVPWNFPLMFAAWKVapALAAGNTVVLKPAELTPLSALRIAEL----MAEAGFPAGVLNVVTGFGEVAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599202 194 LISMPEyVDVIVPRGGKGLIERISREAKVPVIK---HLDGICHVYIDVAADLDKAIRVADNA----KTQRyapCNTMETL 266
Cdd:cd07115 191 LVEHPD-VDKITFTGSTAVGRKIMQGAAGNLKRvslELGGKSANIVFADADLDAAVRAAATGifynQGQM---CTAGSRL 266
|
170
....*....|....*....
gi 15599202 267 LVHAGIAERVLPPLATIYR 285
Cdd:cd07115 267 LVHESIYDEFLERFTSLAR 285
|
|
| |
