|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-277 |
0e+00 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 575.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 10 KAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK----------- 78
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKlwctfhekglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ----------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEK 130
Cdd:cd19107 81 kgacqktlsdlkldyldlylihwptgfkPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 131 LLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQVL 210
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615417 211 IRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFDAEY 277
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-260 |
3.99e-143 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 404.07 E-value: 3.99e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 7 LSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQE-KAVKREDLFIVSK------- 78
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKlwntkhh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 --------------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHF 126
Cdd:cd19106 81 pedvepalrktlkdlqldyldlylihwpyafeRGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 127 QIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTA 206
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462615417 207 AQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRAC 260
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-277 |
1.40e-126 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 361.97 E-value: 1.40e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK------------- 78
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKlwctchkkslvkt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 --------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 132
Cdd:cd19110 83 actrslkalklnyldlylihwpmgfkPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 133 NKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIR 212
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 213 FHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFDAEY 277
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-258 |
1.22e-119 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 344.60 E-value: 1.22e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 3 TFVELSTKAKMPIVGLGTWKS---PLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK- 78
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 --------------------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGV 120
Cdd:cd19108 81 wctfhrpelvrpalekslkklqldyvdlylihfpvalkPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 121 SNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIA 199
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615417 200 AKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-250 |
4.41e-117 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 335.99 E-value: 4.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqekaVKREDLFIVSK--SGD--------- 81
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKlwPTDhgyervrea 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 -------------DLF----PKDDKGnaIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPglKYKPVTN 144
Cdd:cd19071 77 leeslkdlgldylDLYlihwPVPGKE--GGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAA--RIKPAVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 145 QVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPK 224
Cdd:cd19071 153 QIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPK 224
|
250 260
....*....|....*....|....*.
gi 2462615417 225 SVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19071 225 SSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-273 |
1.08e-112 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 327.14 E-value: 1.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTW----KSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK---------- 78
Cdd:cd19109 4 IPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKlwntchppel 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 -----------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIE 129
Cdd:cd19109 84 vrptlertlkvlqldyvdlyiiempmafkPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 130 KLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQ 208
Cdd:cd19109 164 LILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKTAAQ 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 209 VLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPF 273
Cdd:cd19109 244 VVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-258 |
6.32e-110 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 318.15 E-value: 6.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 11 AKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK------SGD--- 81
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS----GVPREELFVTTKvwndnhGYDdtl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 ---------------DLF----PKDDKgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGlkYKPV 142
Cdd:COG0656 79 aafeeslerlgldylDLYlihwPGPGP---------YVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG--VKPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 143 TNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVI 222
Cdd:COG0656 148 VNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVI 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462615417 223 PKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:COG0656 218 PKSVTPERIRENLDAFDFELSDEDMAAIDALDRGER 253
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-260 |
7.18e-109 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 316.53 E-value: 7.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKS-PLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKSGD--------- 81
Cdd:cd19116 10 EIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNsyhereqve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 ---------------DL----FP---KDDKGNAIGGKAT-----FLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNk 134
Cdd:cd19116 90 palreslkrlgldyvDLylihWPvafKENNDSESNGDGSlsdidYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLS- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 135 pGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLlEDPKIKEIAAKHKKTAAQVLIRFH 214
Cdd:cd19116 169 -NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPRL-DDPTLVAIAKKYGKTTAQIVLRYL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462615417 215 IQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRAC 260
Cdd:cd19116 247 IDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-260 |
1.41e-103 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 303.56 E-value: 1.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 2 ATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKSG- 80
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 81 --------------------------------------DDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSN 122
Cdd:cd19154 81 hehapedveealreslkklqleyvdlylihapaafkddEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 123 FSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPED-----PSLLEDPKIKE 197
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615417 198 IAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRAC 260
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-258 |
6.21e-103 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 302.02 E-value: 6.21e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 1 MATFvELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK-- 78
Cdd:cd19123 1 MKTL-PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKlw 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 --------------------------------------------SGDDLFPKDDKGNAiggkatflDAWEAMEELVDEGL 114
Cdd:cd19123 80 nnshapedvlpalektladlqldyldlylmhwpvalkkgvgfpeSGEDLLSLSPIPLE--------DTWRAMEELVDKGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 115 VKALGVSNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWA-KPED-PSLLED 192
Cdd:cd19123 152 CRHIGVSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLED 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615417 193 PKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19123 230 PVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-248 |
2.03e-95 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 282.31 E-value: 2.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 3 TFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKS-GD 81
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLwCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 DLFPKD----------------------------DKGNAIGGKATFL-----DAWEAMEELVDEGLVKALGVSNFSHFQI 128
Cdd:cd19125 81 DHAPEDvppalektlkdlqldyldlylihwpvrlKKGAHMPEPEEVLppdipSTWKAMEKLVDSGKVRAIGVSNFSVKKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 129 EKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEdpsLLEDPKIKEIAAKHKKTAAQ 208
Cdd:cd19125 161 EDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGKTPAQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462615417 209 VLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMA 248
Cdd:cd19125 236 VALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFA 275
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-260 |
1.61e-87 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 262.85 E-value: 1.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 4 FVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK----- 78
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKlppgg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 -----------------------------------SGDDLFPKDDKGNAIGGKAT-FLDAWEAMEELVDEGLVKALGVSN 122
Cdd:cd19155 83 nrrekvekfllksleklqldyvdlylihfpvgslsKEDDSGKLDPTGEHKQDYTTdLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 123 FSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKP-------EDPSLLEDPKI 195
Cdd:cd19155 163 FNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 196 KEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRAC 260
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-258 |
9.94e-87 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 260.12 E-value: 9.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK------------- 78
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKlppvylefkdtek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 -----------SGDDLF----P-----KDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPglK 138
Cdd:cd19111 83 slekslenlklPYVDLYlihhPcgfvnKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA--K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 YKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRP--WAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQ 216
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQVLLRFVLQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462615417 217 RNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19111 241 RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-252 |
1.33e-84 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 254.09 E-value: 1.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKspLGKVKEAVKV---AIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKSGD-------- 81
Cdd:cd19136 1 MPILGLGTFR--LRGEEEVRQAvdaALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPkdqgyeka 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 ----------------DLF----------PKDDKGNAIGGKATfldaWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKP 135
Cdd:cd19136 79 raaclgslerlgtdylDLYlihwpgvqglKPSDPRNAELRRES----WRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 136 glKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedPSLLEDPKIKEIAAKHKKTAAQVLIRFHI 215
Cdd:cd19136 155 --EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPTVLAIAKKYGRTPAQVLLRWAL 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462615417 216 QRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILS 252
Cdd:cd19136 225 QQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-250 |
1.20e-82 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 249.72 E-value: 1.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 7 LSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK-------- 78
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDS----GVPREEIFITTKlwctwhrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 -------------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQ 127
Cdd:cd19117 84 veealdqslkklgldyvdlylmhwpvpldpdGNDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSIKN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 128 IEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHKKTAA 207
Cdd:cd19117 164 LEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKTPA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462615417 208 QVLIRFHIQRNVIVIPKSVTPARIVENIQVFDfkLSDEEMATI 250
Cdd:cd19117 236 QVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEI 276
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-258 |
2.50e-81 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 247.40 E-value: 2.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK--SGD- 81
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKlwNSDh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 -------------------DL----FPKDDKGNAIGGKATFLD---------------AWEAMEELVDEGLVKALGVSNF 123
Cdd:cd19112 83 ghvieackdslkklqldylDLylvhFPVATKHTGVGTTGSALGedgvldidvtisletTWHAMEKLVSAGLVRSIGISNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 124 SHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLG--SPDRPWAKPEDPslLEDPKIKEIAAK 201
Cdd:cd19112 163 DIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615417 202 HKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-258 |
2.89e-80 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 243.07 E-value: 2.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 4 FVELSTKAKMPIVGLGTWKSPLGK-VKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqekaVKREDLFIVSK--SG 80
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG----IPREELFITSKvwNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 81 D----------------------DLF----PKDDKgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNK 134
Cdd:cd19157 77 DqgydstlkafeaslerlgldylDLYlihwPVKGK---------YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 135 PglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKHKKTAAQVLIRFH 214
Cdd:cd19157 148 A--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNKSVAQVILRWD 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462615417 215 IQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19157 216 LQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-250 |
5.63e-80 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 243.09 E-value: 5.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 7 LSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEK-AVKREDLFIVSK------- 78
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKlwnnshr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 --------------------------------SGDDLFPK----DDKGN-AIGGKATFLDAWEAMEELVDEGLVKALGVS 121
Cdd:cd19118 81 peyvepalddtlkelgldyldlylihwpvafkPTGDLNPLtavpTNGGEvDLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 122 NFSHFQIEKLLNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwAKPEDPSLLEDPKIKEIAAK 201
Cdd:cd19118 161 NFSIDHLQAIIEETGVV--PAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462615417 202 HKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDfkLSDEEMATI 250
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAV 280
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-254 |
1.73e-79 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 240.80 E-value: 1.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLG-KVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK----- 78
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES----GVPREELFVTTKlwndd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ----SGDDLFpkDDKGNAIG------------GKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPglKYKPV 142
Cdd:cd19126 77 qrarRTEDAF--QESLDRLGldyvdlylihwpGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA--DVVPA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 143 TNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVI 222
Cdd:cd19126 153 VNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTI 222
|
250 260 270
....*....|....*....|....*....|..
gi 2462615417 223 PKSVTPARIVENIQVFDFKLSDEEMATILSFN 254
Cdd:cd19126 223 PKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-254 |
3.48e-78 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 237.47 E-value: 3.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWK-SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqekaVKREDLFIVSKsgddL 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTK----L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 84 FPKDDKGNAIggKATF-----------LD-------------AWEAMEELVDEGLVKALGVSNFSHFQIEKLLnkPGLKY 139
Cdd:cd19133 73 WIQDAGYEKA--KKAFerslkrlgldyLDlylihqpfgdvygAWRAMEELYKEGKIRAIGVSNFYPDRLVDLI--LHNEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 140 KPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNV 219
Cdd:cd19133 149 KPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE--------GRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGI 220
|
250 260 270
....*....|....*....|....*....|....*
gi 2462615417 220 IVIPKSVTPARIVENIQVFDFKLSDEEMATILSFN 254
Cdd:cd19133 221 VVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-250 |
2.10e-77 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 235.34 E-value: 2.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK--SGD- 81
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS----GVPREELFITTKlwNSDq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 ---------------------DLF------PKDDKgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNK 134
Cdd:cd19131 78 gydstlrafdeslrklgldyvDLYlihwpvPAQDK---------YVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 135 PGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKTAAQVLIRFH 214
Cdd:cd19131 149 TGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----------GLLSDPVIGEIAEKHGKTPAQVVIRWH 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462615417 215 IQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19131 217 LQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-250 |
3.58e-76 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 233.18 E-value: 3.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 14 PIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK--------------- 78
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKlwptmhqpenvkeql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ------------------------SGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNK 134
Cdd:cd19128 82 litlqdlqleyldlflihwplafdMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 135 pgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKpedpSLLEDPKIKEIAAKHKKTAAQVLIRFH 214
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462615417 215 IQR---NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-258 |
7.60e-76 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 233.47 E-value: 7.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 1 MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK-- 78
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKlw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ----SGD------------------DL----FP----------------KDDKGNAIGGKATFLDAWEAMEELVDEGLVK 116
Cdd:cd19115 81 ntfhDGErvepicrkqladwgidyfDLflihFPialkyvdpavryppgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 117 ALGVSNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGsP------DRPWAKpEDPSLL 190
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615417 191 EDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-253 |
1.17e-75 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 231.44 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 4 FVELSTKAKMPIVGLGTWKSPlGKVKEAVKVAI-DAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKsgdd 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKES----GVPREDLFLTTK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 83 LFPKD------------------------------DKGNAIGG-KATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKL 131
Cdd:cd19135 75 LWPSDygyestkqafeaslkrlgvdyldlyllhwpDCPSSGKNvKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 132 LNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrPWakpedpSLLEDPKIKEIAAKHKKTAAQVLI 211
Cdd:cd19135 155 LEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KG------KALEEPTVTELAKKYQKTPAQILI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462615417 212 RFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSF 253
Cdd:cd19135 223 RWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
2-247 |
4.32e-75 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 230.50 E-value: 4.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 2 ATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqEKAVKREDLFIVSK--- 78
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKlws 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ------------------------------------SGDDLFPKDDKGN-AIGGKATFLDAWEAMEELVDEGLVKALGVS 121
Cdd:cd19121 80 tyhrrvelcldrslkslgldyvdlylvhwpvllnpnGNHDLFPTLPDGSrDLDWDWNHVDTWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 122 NFSHFQIEKLLnkPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAK 201
Cdd:cd19121 160 NYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAKK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462615417 202 HKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFklSDEEM 247
Cdd:cd19121 230 HNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDM 273
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-258 |
1.23e-74 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 228.94 E-value: 1.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLGKVKE-AVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK--SGD 81
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKlwNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 DLFPK-----DDKGNAIG------------GKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKpgLKYKPVTN 144
Cdd:cd19156 77 QGYEStlaafEESLEKLGldyvdlylihwpVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKS--CKVAPMVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 145 QVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPK 224
Cdd:cd19156 155 QIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPK 224
|
250 260 270
....*....|....*....|....*....|....
gi 2462615417 225 SVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19156 225 SVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-250 |
1.84e-72 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 222.52 E-value: 1.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 11 AKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKSGDDLFPKDDKG 90
Cdd:cd19140 6 VRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAAS----GVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 91 NAI--------------------GGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYkpVTNQVECHP 150
Cdd:cd19140 82 ASVeeslrklrtdyvdllllhwpNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPL--FTNQVEYHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 151 YLTQEKLIQYCHSKGITVTAYSPLGspdrpwakpeDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQR-NVIVIPKSVTPA 229
Cdd:cd19140 160 YLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPE 229
|
250 260
....*....|....*....|.
gi 2462615417 230 RIVENIQVFDFKLSDEEMATI 250
Cdd:cd19140 230 RLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-250 |
6.65e-72 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 221.37 E-value: 6.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK-SGD--------- 81
Cdd:cd19132 6 QIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRS----GVPREELFVTTKlPGRhhgyeealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 --------------DLF------PKDDKgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKykP 141
Cdd:cd19132 82 tieeslyrlgldyvDLYlihwpnPSRDL---------YVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVT--P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 142 VTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIV 221
Cdd:cd19132 151 AVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVP 221
|
250 260
....*....|....*....|....*....
gi 2462615417 222 IPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19132 222 IPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-250 |
1.50e-71 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 219.83 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSK-SGDDLFPK----- 86
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKvWRDHLRPEdlkks 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 87 -DDKGNAIGGKatFLDA----W-----------EAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKykPVTNQVECHP 150
Cdd:cd19073 77 vDRSLEKLGTD--YVDLllihWpnptvpleetlGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP--IAVNQVEFHP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 151 YLTQEKLIQYCHSKGITVTAYSPLgspdrpwAKPEdpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPAR 230
Cdd:cd19073 153 FLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDH 222
|
250 260
....*....|....*....|
gi 2462615417 231 IVENIQVFDFKLSDEEMATI 250
Cdd:cd19073 223 LKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-258 |
2.74e-71 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 221.55 E-value: 2.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKSGD--- 81
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNnfh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 ---------------------DLF-----------PKDDK---GNAIGGKATF-------LDAWEAMEELVDEGLVKALG 119
Cdd:cd19113 83 dpknvetalnktlsdlkldyvDLFlihfpiafkfvPIEEKyppGFYCGDGDNFvyedvpiLDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 120 VSNFSHFQIEKLLNkpGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-----DRPWAKpEDPSLLEDPK 194
Cdd:cd19113 163 VSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462615417 195 IKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-250 |
3.69e-70 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 217.27 E-value: 3.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKsgddLF 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTK----LW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 85 PKD-DKGNAIGG----------------------KATF---LDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLK 138
Cdd:cd19127 73 ISDyGYDKALRGfdaslrrlgldyvdlyllhwpvPNDFdrtIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 ykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAK--PEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQ 216
Cdd:cd19127 153 --PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgpTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQ 230
|
250 260 270
....*....|....*....|....*....|....
gi 2462615417 217 RNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19127 231 NGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-250 |
1.96e-69 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 215.56 E-value: 1.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGT----WKSPLG----KVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKSGD-- 81
Cdd:cd19120 3 KIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSPgi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 -------------------DLF----PKDDKGnaigGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPglK 138
Cdd:cd19120 79 kdprealrkslaklgvdyvDLYlihsPFFAKE----GGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTA--K 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 YKPVTNQVECHPYLT--QEKLIQYCHSKGITVTAYSPLGspdrPWAKPEDPSLleDPKIKEIAAKHKKTAAQVLIRFHIQ 216
Cdd:cd19120 153 IKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLS----PLTRDAGGPL--DPVLEKIAEKYGVTPAQVLLRWALQ 226
|
250 260 270
....*....|....*....|....*....|....
gi 2462615417 217 RNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19120 227 KGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-250 |
6.74e-67 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 209.43 E-value: 6.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 11 AKMPIVGLGTWKSPLGK--VKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVK-REDLFIVSK------SGD 81
Cdd:cd19124 3 QTMPVIGMGTASDPPSPedIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKlwcsdaHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 DLFP-------------------------KDDKGNAIGGKATFLD-----AWEAMEELVDEGLVKALGVSNFSHFQIEKL 131
Cdd:cd19124 83 LVLPalkkslrnlqleyvdlylihwpvslKPGKFSFPIEEEDFLPfdikgVWEAMEECQRLGLTKAIGVSNFSCKKLQEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 132 LNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAkpeDPSLLEDPKIKEIAAKHKKTAAQVLI 211
Cdd:cd19124 163 LSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKEIAAAKGKTVAQVSL 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462615417 212 RFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19124 238 RWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-255 |
2.21e-63 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 200.80 E-value: 2.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWkSP---LGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK--- 78
Cdd:cd19119 4 FKLNTGASIPALGLGTA-SPhedRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKvwp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ---------------------------------------SGDDLFPKDDKGNAIGGKAT-FLDAWEAMEELVDEGLVKAL 118
Cdd:cd19119 83 tfydeversldeslkalgldyvdlllvhwpvcfekdsddSGKPFTPVNDDGKTRYAASGdHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 119 GVSNFSHFQIEKLLNKpgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEI 198
Cdd:cd19119 163 GVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVKKI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615417 199 AAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVfdFKLSDEEMATILSFNR 255
Cdd:cd19119 233 AEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
13-254 |
6.90e-62 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 195.90 E-value: 6.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKSGDDLFPKDDKGNA 92
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 93 IG---------------------GKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKykPVTNQVECHPY 151
Cdd:cd19130 86 FAeslaklgldqvdlylvhwptpAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVV--PAVNQIELHPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 152 LTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARI 231
Cdd:cd19130 164 YQQRTIRDWAQAHDVKIEAWSPLGQG----------KLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERM 233
|
250 260
....*....|....*....|...
gi 2462615417 232 VENIQVFDFKLSDEEMATILSFN 254
Cdd:cd19130 234 EDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-250 |
2.72e-61 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 195.75 E-value: 2.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK-------------- 78
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKlwntnhrpervkpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 -------------------------SGDDLFPKDDKGNAIGGKA-TFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 132
Cdd:cd19129 86 feaslkrlqldyldlylihtpfafqPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 133 NKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpSLLEDPKIKEIAAKHKKTAAQVLIR 212
Cdd:cd19129 166 EAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEP-------KLLEDPVITAIARRVNKTPAQVLLA 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462615417 213 FHIQRNVIVIPKSVTPARIVENiqvFDFK-LSDEEMATI 250
Cdd:cd19129 237 WAIQRGTALLTTSKTPSRIREN---FDIStLPEDAMREI 272
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-258 |
2.84e-60 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 193.16 E-value: 2.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKSGDDLFPKD---- 87
Cdd:cd19114 3 KMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDhvre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 88 --DK--------------------------------GNAIGGKATF-------LDAWEAMEELVDEGLVKALGVSNFSHF 126
Cdd:cd19114 83 afDRqlkdygldyidlylihfpipaayvdpaenypfLWKDKELKKFpleqspmQECWREMEKLVDAGLVRNIGIANFNVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 127 QIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP---DRPWAKPEDPSLLEDPKIKEIAAKHK 203
Cdd:cd19114 163 LILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 204 KTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-250 |
1.57e-59 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 190.28 E-value: 1.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 3 TFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKsgdd 82
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 83 LFpKDDKGNA------------------------IGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLK 138
Cdd:PRK11565 77 LW-NDDHKRPrealeeslkklqldyvdlylmhwpVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 ykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedpSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRN 218
Cdd:PRK11565 156 --PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYGKTPAQIVIRWHLDSG 225
|
250 260 270
....*....|....*....|....*....|..
gi 2462615417 219 VIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:PRK11565 226 LVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-250 |
1.88e-56 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 183.21 E-value: 1.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 7 LSTKAKMPIVGLGTWKS--PLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEK-AVKREDLFIVSK----- 78
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKvwnhl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 --------SGD-----------DLF--------PKDDKGNA-IG--GKATFLDA--------WEAMEELVDEGLVKALGV 120
Cdd:cd19122 83 hepedvkwSIDnslknlkldyiDLFlvhwpiaaEKNDQRSPkLGpdGKYVILKDltenpeptWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 121 SNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSllEDPKIKEIAA 200
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462615417 201 KHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDfkLSDEEMATI 250
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAI 286
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-250 |
3.90e-56 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 182.13 E-value: 3.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWKSPLG-------KVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekAVKREDLFIVSKSGDDLFP 85
Cdd:pfam00248 1 IGLGTWQLGGGwgpiskeEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVPDGDGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 86 KDDKGNA--------------------------IGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPglKY 139
Cdd:pfam00248 77 WPSGGSKenirksleeslkrlgtdyidlyylhwPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKG--KI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 140 KPVTNQVECHPY--LTQEKLIQYCHSKGITVTAYSPLGS-----------------PDRPWAKPEDPSLLEDPKIKEIAA 200
Cdd:pfam00248 155 PIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRRLLKKGTPLNLEALEALEEIAK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462615417 201 KHKKTAAQVLIRFHIQ--RNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:pfam00248 235 EHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-250 |
1.36e-55 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 179.47 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSK------SGDDLFPK 86
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKiwidnlSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 87 -DDKGNAIGGKATFL---------------DAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGlKYKPVTNQVECHP 150
Cdd:cd19139 77 lEESLEKLRTDYVDLtlihwpspndevpveEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG-AGAIATNQIELSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 151 YLTQEKLIQYCHSKGITVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPAR 230
Cdd:cd19139 156 YLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREH 225
|
250 260
....*....|....*....|
gi 2462615417 231 IVENIQVFDFKLSDEEMATI 250
Cdd:cd19139 226 LRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-250 |
1.58e-52 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 171.96 E-value: 1.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKsgddlF 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTK-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 85 PKDDKGN--------------------------AIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGlk 138
Cdd:cd19134 74 ATPDQGFtasqaacraslerlgldyvdlylihwPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTF-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 YKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRN 218
Cdd:cd19134 152 FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG----------RLLDNPAVTAIAAAHGRTPAQVLLRWSLQLG 221
|
250 260 270
....*....|....*....|....*....|..
gi 2462615417 219 VIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19134 222 NVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-250 |
4.48e-51 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 168.18 E-value: 4.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 10 KAKMPIVGLGTWK------SPLGKVKEAVKV---AIDAGYRHIDCAYVYQN---EHEVGEAIqekiqeKAVKREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmsKDYSDDKKAIEAlryAIELGINLIDTAEMYGGghaEELVGKAI------KGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 78 KSGDDLFPKDDKGNAIGG-----KATFLD---------------AWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGl 137
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKEslkrlGTDYIDlylihwpnpsipieeTLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 138 KYKPVTNQVECHpYLTQE---KLIQYCHSKGITVTAYSPLGSPDRPWAKPedpslleDPKIKEIAAKHKKTAAQVLIRFH 214
Cdd:cd19072 154 KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------SPLLDEIAKKYGKTPAQIALNWL 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462615417 215 IQR-NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19072 226 ISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-250 |
1.31e-49 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 164.73 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 5 VELSTKAKMPIVGLGTW-----KSPLGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 77 SKsgddLFPkddkGNAiGGKATF--------------LDA----W----------EAMEELVDEGLVKALGVSNFSHFQI 128
Cdd:cd19138 76 SK----VLP----SNA-SRQGTVracerslrrlgtdyLDLyllhWrggvplaetvAAMEELKKEGKIRAWGVSNFDTDDM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 129 EKLLNKPGLKyKPVTNQVECHpyLTQE----KLIQYCHSKGITVTAYSPLGSPDRPwakpeDPSLLEDPKIKEIAAKHKK 204
Cdd:cd19138 147 EELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLENPTLKEIAARHGA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462615417 205 TAAQVLIRFHI-QRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19138 219 TPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-258 |
6.95e-47 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 157.49 E-value: 6.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKSGDDLFPKDD--- 88
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLAKDKlip 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 89 --KGNAIGGKATFLDA----W----------EAMEELVD---EGLVKALGVSNFSHFQIEKLLNKPGlKYKPVTNQVECH 149
Cdd:PRK11172 78 slKESLQKLRTDYVDLtlihWpspndevsveEFMQALLEakkQGLTREIGISNFTIALMKQAIAAVG-AENIATNQIELS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 150 PYLTQEKLIQYCHSKGITVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPA 229
Cdd:PRK11172 157 PYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRE 226
|
250 260
....*....|....*....|....*....
gi 2462615417 230 RIVENIQVFDFKLSDEEMATILSFNRNWR 258
Cdd:PRK11172 227 NLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-250 |
7.00e-40 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 139.24 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWK---------SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHE---VGEAIqekiqeKAVKREDLFIVSKS 79
Cdd:cd19137 3 KIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGGGHTeelVGKAI------KDFPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 80 GDDLFPKDDKGNAIGGKATFLDA---------W-----------EAMEELVDEGLVKALGVSNFSHFQIEKLLNKpgLKY 139
Cdd:cd19137 77 WPTNLRYDDLLRSLQNSLRRLDTdyidlylihWpnpnipleetlSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK--SQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 140 KPVTNQVECHPY---LTQEKLIQYCHSKGITVTAYSPLgspDRPWAKPEDpslledpKIKEIAAKHKKTAAQVLIRFHIQ 216
Cdd:cd19137 155 PIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNR-------TLEEIAKNYGKTIAQIALAWLIQ 224
|
250 260 270
....*....|....*....|....*....|....*
gi 2462615417 217 R-NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19137 225 KpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-250 |
2.84e-36 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 131.45 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWksPLGKV------KEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIqekiqeKAVKREDLFIVSKSGddl 83
Cdd:COG0667 16 LGLGTM--TFGGPwggvdeAEAIAIldaALDAGINFFDTADVYgpgRSEELLGEAL------KGRPRDDVVIATKVG--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 84 FPKDDKGNAIGGKATFL-------------------------------DAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 132
Cdd:COG0667 85 RRMGPGPNGRGLSREHIrraveaslrrlgtdyidlyqlhrpdpdtpieETLGALDELVREGKIRYIGVSNYSAEQLRRAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 133 NKPGLKYKPVTNQVEchpY--LTQ---EKLIQYCHSKGITVTAYSPLGS---------------PDR-------PWAKPE 185
Cdd:COG0667 165 AIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGglltgkyrrgatfpeGDRaatnfvqGYLTER 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615417 186 DPSLLEdpKIKEIAAKHKKTAAQVLIRFHIQR--NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:COG0667 242 NLALVD--ALRAIAAEHGVTPAQLALAWLLAQpgVTSVIPGARSPEQLEENLAAADLELSAEDLAAL 306
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-248 |
5.90e-36 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 130.04 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWK---------SPLGK--VKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekaVKREDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgyGEYGDedLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 78 K-------SGDDLFPKDDKGNAIGGKATFLD----------------AWEAMEELVDEGLVKALGVSNFSHFQIEK---L 131
Cdd:cd19093 76 KfaplpwrLTRRSVVKALKASLERLGLDSIDlyqlhwpgpwysqieaLMDGLADAVEEGLVRAVGVSNYSADQLRRahkA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 132 LNKPGlkYKPVTNQVE---CHPYLTQEKLIQYCHSKGITVTAYSPLG--------SPDRP-----------WAKPEDPSL 189
Cdd:cd19093 156 LKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPppggrrrlfgrKNLEKVQPL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615417 190 LEdpKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMA 248
Cdd:cd19093 234 LD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVA 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-250 |
6.10e-30 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 114.16 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWksPLG----------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIVSK 78
Cdd:cd19084 3 KVSRIGLGTW--AIGgtwwgevddqESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 SGddLFPKDDKGNAIGGKATFL-------------------------------DAWEAMEELVDEGLVKALGVSNFSHFQ 127
Cdd:cd19084 74 CG--LRWDGGKGVTKDLSPESIrkeveqslrrlqtdyidlyqihwpdpntpieETAEALEKLKKEGKIRYIGVSNFSVEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 128 IEKLlnkpgLKY-KPVTNQVechPY--LTQ---EKLIQYCHSKGITVTAYSPLG--------------SPD--------- 178
Cdd:cd19084 152 LEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAqglltgkykkeptfPPDdrrsrfpff 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615417 179 RPWAKPEDPSLLEdpKIKEIAAKHKKTAAQVLIRFHIQRN----VIVIPKsvTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19084 224 RGENFEKNLEIVD--KLKEIAEKYGKSLAQLAIAWTLAQPgvtsAIVGAK--NPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-246 |
1.23e-26 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 104.95 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 17 GLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekAVKREDLFIVSKSGddLFPKDDKGNAI 93
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKCG--IRLGDDPRPGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 94 GG-----KA---------------------------TFLDAWE---AMEELVDEGLVKALGVSNFSHFQIEkLLNKpGLK 138
Cdd:cd19092 89 IKhydtsKEhilasvegslkrlgtdyldllllhrpdPLMDPEEvaeAFDELVKSGKVRYFGVSNFTPSQIE-LLQS-YLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 YKPVTNQVEC---HPYLTQEKLIQYCHSKGITVTAYSPLG-----SPDRpwakPEDPSLLEdpKIKEIAAKHKKTAAQVL 210
Cdd:cd19092 167 QPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGggrlfGGFD----ERFQRLRA--ALEELAEEYGVTIEAIA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462615417 211 IRFhIQR---NVIVIPKSVTPARIVENIQVFDFKLSDEE 246
Cdd:cd19092 241 LAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-250 |
1.29e-25 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 102.28 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 14 PIVGLGTW----KSPLGKVKE-----AVKVAIDAGYRHIDCAYVYQNEHE---VGEAIQEKiqekavkREDLFIVSKSGD 81
Cdd:cd19085 2 SRLGLGCWqfggGYWWGDQDDeesiaTIHAALDAGINFFDTAEAYGDGHSeevLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 DLFPKDDKGNAI--------------------GGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLnKPGlkyKP 141
Cdd:cd19085 75 DNLTPEDVRKSCerslkrlgtdyidlyqihwpSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL-DAG---RI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 142 VTNQVECHPYLTQ-EK-LIQYCHSKGITVTAYSPL------GSPDRPWAKPED------PSLLEDP----------KIKE 197
Cdd:cd19085 151 DSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlFRHFEPGaeeetfealeKLKE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 198 IAAKHKKTAAQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19085 231 IADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-236 |
1.02e-24 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 98.74 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWK-SPLGKVKEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekaVKREDLFIVSKSGddlFPKDD 88
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALldaALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGG---HPPGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 89 KGNAIGGKATFL-------------------------------DAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN--KP 135
Cdd:cd06660 75 DPSRSRLSPEHIrrdleeslrrlgtdyidlyylhrddpstpveETLEALNELVREGKIRYIGVSNWSAERLAEALAyaKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 136 GLKYKPVTNQVE---CHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpedpslledpkikeiaakhkkTAAQVLIR 212
Cdd:cd06660 155 HGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR----------------------------GPAQLALA 206
|
250 260
....*....|....*....|....*.
gi 2462615417 213 FHIQR--NVIVIPKSVTPARIVENIQ 236
Cdd:cd06660 207 WLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-250 |
1.20e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 94.66 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWksPLG--------------KVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavkREDLFIVSK 78
Cdd:cd19102 4 IGLGTW--AIGgggwgggwgpqddrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 SGddLFPkDDKGNAIGG--KATFL------------------------------DAWEAMEELVDEGLVKALGVSNFSHF 126
Cdd:cd19102 75 CG--LLW-DEEGRIRRSlkPASIRaeceaslrrlgvdvidlyqihwpdpdepieEAWGALAELKEEGKVRAIGVSNFSVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 127 QIEKLlnkpgLKYKPVT-NQVechPY--LTQE---KLIQYCHSKGITVTAYSPLGS--------PDRPWAKPED------ 186
Cdd:cd19102 152 QMKRC-----QAIHPIAsLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmtPERVASLPADdwrrrs 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 187 -----PSLLEDPKI----KEIAAKHKKTAAQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19102 224 pffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEI 298
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-243 |
4.34e-21 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 89.58 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 13 MPIVGLGTWKSPLGKvKEAVKV---AIDAGYRHIDCAYVYqnehevGEAIQEKIQEKAVK--REDLFIVSK-----SGDD 82
Cdd:cd19088 9 MRLTGPGIWGPPADR-EEAIAVlrrALELGVNFIDTADSY------GPDVNERLIAEALHpyPDDVVIATKgglvrTGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 83 LFPKDDK---------GNA---------------IGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLk 138
Cdd:cd19088 82 WWGPDGSpeylrqaveASLrrlgldridlyqlhrIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 139 ykpVTNQVECHPYLTQ-EKLIQYCHSKGITVTAYSPLGSpdRPWAKPEdpslledPKIKEIAAKHKKTAAQVLIRFHIQR 217
Cdd:cd19088 161 ---VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQPG-------GLLAEVAARLGATPAQVALAWLLAR 228
|
250 260
....*....|....*....|....*...
gi 2462615417 218 --NVIVIPKSVTPARIVENIQVFDFKLS 243
Cdd:cd19088 229 spVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-252 |
3.38e-20 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 87.86 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 29 KEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavKREDLFIVSKSGDDlfpKDDKGNAIGGKATFL----- 100
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHK---FGGDGSVLNNSPEFLrsave 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 101 --------------------------DAWEAMEELVDEGLVKALGVSNFSHFQIeKLLNKPGLkykpvTNQVEcHPY-LT 153
Cdd:cd19083 107 kslkrlntdyidlyyihfpdgetpkaEAVGALQELKDEGKIRAIGVSNFSLEQL-KEANKDGY-----VDVLQ-GEYnLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 154 Q----EKLIQYCHSKGITVTAYSPLGS-------------PDRPWAKpeDPSLLEDP----------KIKEIAAKHKKTA 206
Cdd:cd19083 180 QreaeEDILPYCVENNISFIPYFPLASgllagkytkdtkfPDNDLRN--DKPLFKGErfsenldkvdKLKSIADEKGVTV 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462615417 207 AQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDEEMATILS 252
Cdd:cd19083 258 AHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
19-250 |
3.07e-19 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 85.33 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 19 GTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIqekavKREDLFIVSKSGddlFPKDDKGNAIG- 94
Cdd:cd19079 28 RPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVY---FPMGDGPNGRGl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 95 -GKATF--LDA-----------------W----------EAMEELVDEGLVKALGVSNFSHFQIEKLLN---KPGLKyKP 141
Cdd:cd19079 100 sRKHIMaeVDAslkrlgtdyidlyqihrWdyetpieetlEALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKNGWT-KF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 142 VTNQvecHPY--LTQE---KLIQYCHSKGITVTAYSPL----------GSPDRPWAKPEDPSLLED----------PKIK 196
Cdd:cd19079 179 VSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLargrlarpwgDTTERRRSTTDTAKLKYDyfteadkeivDRVE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615417 197 EIAAKHKKTAAQVLIRFHIQRNVIVIP--KSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19079 256 EVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
35-250 |
1.43e-17 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 80.72 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 35 AIDAGYRHIDCAYVYQ---NEHEVGEAIQEKiqekavkREDLFIVSKSGDDlFPKDDKGNAIGGKATFL----------- 100
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKFGIV-RDPGSGFRGVDGRPEYVraaceaslkrl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 101 --------------------DAWEAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPVTN-QVECHPYLT--QEKL 157
Cdd:cd19076 113 gtdvidlyyqhrvdpnvpieETVGAMAELVEEGKVRYIGLSEASADTIRR-----AHAVHPITAvQSEYSLWTRdiEDEV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 158 IQYCHSKGITVTAYSPL------GSPDRPWAKPEDPSLLEDP---------------KIKEIAAKHKKTAAQVLIRFHIQ 216
Cdd:cd19076 188 LPTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDFRRNNPrfqgenfdknlklveKLEAIAAEKGCTPAQLALAWVLA 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462615417 217 R--NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19076 268 QgdDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-252 |
4.86e-17 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 79.24 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTW---------KSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHevgeaiQEKIQEKAVK--REDLFIVSKSG---- 80
Cdd:cd19149 14 IGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFGH------SEEIVGKAIKgrRDKVVLATKCGlrwd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 81 --DDLFPKDDKGNAI---GGKATFL------------------------------DAWEAMEELVDEGLVKALGVSNFSH 125
Cdd:cd19149 88 reGGSFFFVRDGVTVyknLSPESIReeveqslkrlgtdyidlyqthwqdvetpieETMEALEELKRQGKIRAIGASNVSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 126 FQIEKLLNKPGL-----KYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLGS--------PDR-----------PW 181
Cdd:cd19149 168 EQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLEQglltgkitPDRefdagdarsgiPW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615417 182 AKPEDPS----LLEdpKIKEIAAKHKKTAAQVLIRFHIQR--NVIVIPKSVTPARIVENIQVFDFKLSDEEMATILS 252
Cdd:cd19149 241 FSPENREkvlaLLE--KWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
16-250 |
4.87e-17 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 79.21 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLG----TWK---SPLGKVKEAVKVAIDAGYRHIDCAYVY------QNEHEVGEAIqEKIQEKavkREDLFIVSKSG-- 80
Cdd:cd19077 8 IGLGlmglTWRpnpTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFF-RKYPEY---ADKVVLSVKGGld 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 81 -DDLFPKDDKGN----------AIGGKAtFLDAWE---------------AMEELVDEGLVKALGVSNFSHFQIEKllnk 134
Cdd:cd19077 84 pDTLRPDGSPEAvrksienilrALGGTK-KIDIFEparvdpnvpieetikALKELVKEGKIRGIGLSEVSAETIRR---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 135 pGLKYKPVT-NQVECHPyLTQEKL----IQYCHSKGITVTAYSPL------GSPDRPWAKPEDPSLLEDP---------- 193
Cdd:cd19077 159 -AHAVHPIAaVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLgrglltGRIKSLADIPEGDFRRHLDrfngenfekn 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615417 194 -----KIKEIAAKHKKTAAQVLIRFHIQRN---VIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19077 237 lklvdALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-237 |
1.99e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 76.47 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 9 TKAKMPIVGLGTWKSPlGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIqekiqeKAVKREDLFIVSKS--GDDL 83
Cdd:cd19105 9 TGLKVSRLGFGGGGLP-RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEAL------KGLRRDKVFLATKAspRLDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 84 FPKDDKGNAIGG-----KATFLDAW------------------EAMEELVDEGLVKALGVSnfSHFQIEKLLN---KPG- 136
Cdd:cd19105 82 KDKAELLKSVEEslkrlQTDYIDIYqlhgvdtpeerllneellEALEKLKKEGKVRFIGFS--THDNMAEVLQaaiESGw 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 137 -----LKYKPVtnqvecHPYLTQEKLIQYCHSKGITVTAYSPLGS-PDRPWAKPEDPSLLEDPkikeiaakhkktaAQVL 210
Cdd:cd19105 160 fdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGgYLQPALLSVLKAKGFSL-------------PQAA 220
|
250 260
....*....|....*....|....*....
gi 2462615417 211 IRFHIQRNVI--VIPKSVTPARIVENIQV 237
Cdd:cd19105 221 LKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-250 |
2.16e-16 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 77.65 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGT--------WKSPLGKV--KEA---VKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavkREDLFI 75
Cdd:cd19091 12 KVSELALGTmtfgggggFFGAWGGVdqEEAdrlVDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 76 VSKSGddlFPKDDKGNAIGG----------------KATFLD-----AW----------EAMEELVDEGLVKALGVSNFS 124
Cdd:cd19091 85 ATKVR---GRMGEGPNDVGLsrhhiiraveaslkrlGTDYIDlyqlhGFdaltpleetlRALDDLVRQGKVRYIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 125 HFQIEKLL---NKPGLKyKPVTNQVechpYLT------QEKLIQYCHSKGITVTAYSPLG--------SPDRPWAK---- 183
Cdd:cd19091 162 AWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAggllsgkyRRGQPAPEgsrl 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615417 184 --------PEDPSLLED--PKIKEIAAKHKKTAAQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19091 237 rrtgfdfpPVDRERGYDvvDALREIAKETGATPAQVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-187 |
1.50e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 70.97 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 8 STKAKMPIVGLGTWksPLGKV--KEAVKV---AIDAGYRHIDCAYVYQNEHE-VGEAIQEkiqekavKREDLFIVSKSGD 81
Cdd:cd19100 6 RTGLKVSRLGFGGG--PLGRLsqEEAAAIirrALDLGINYFDTAPSYGDSEEkIGKALKG-------RRDKVFLATKTGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 ----------------------DLF------PKDDKGNAIGGKAtfldAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN 133
Cdd:cd19100 77 rdyegakrdlerslkrlgtdyiDLYqlhavdTEEDLDQVFGPGG----ALEALLEAKEEGKIRFIGISGHSPEVLLRALE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 134 KPglkykPV------TNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDP 187
Cdd:cd19100 153 TG-----EFdvvlfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
35-250 |
1.77e-13 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 69.39 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 35 AIDAGYRHIDCAYVYQ-NEHEVGEAIQEKIQekavKREDLFIVSKSGDDLFPKDDKGNA--------------------- 92
Cdd:cd19144 43 AFELGCTFWDTADIYGdSEELIGRWFKQNPG----KREKIFLATKFGIEKNVETGEYSVdgspeyvkkacetslkrlgvd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 93 ---------IGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPVTN-QVECHPYLT-----QEKL 157
Cdd:cd19144 119 yidlyyqhrVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRR-----AHAVHPIAAvQIEYSPFSLdierpEIGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 158 IQYCHSKGITVTAYSPLG---------SPD----------RPWAKPED-PSLLE--DpKIKEIAAKHKKTAAQVLIRFHI 215
Cdd:cd19144 194 LDTCRELGVAIVAYSPLGrgfltgairSPDdfeegdfrrmAPRFQAENfPKNLElvD-KIKAIAKKKNVTAGQLTLAWLL 272
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462615417 216 QR--NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19144 273 AQgdDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
99-250 |
2.66e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 68.39 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 99 FLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPglkYKPVTNQVEC-----HPyltQEKLIQYCHSKGITVTAYSP 173
Cdd:cd19101 121 YLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 174 ----------LGSPDRPWAKPEDPSLLEDPKI-----------------KEIAAKHKKTAAQVLIRFHIQR----NVIVi 222
Cdd:cd19101 195 laggllsekyLGVPEPTGPALETRSLQKYKLMidewggwdlfqellrtlKAIADKHGVSIANVAVRWVLDQpgvaGVIV- 273
|
170 180
....*....|....*....|....*....
gi 2462615417 223 pkSVTPAR-IVENIQVFDFKLSDEEMATI 250
Cdd:cd19101 274 --GARNSEhIDDNVRAFSFRLDDEDRAAI 300
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-245 |
9.31e-13 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 66.85 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWKSPLGKV-----KEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEkiqekaVKREDLFIVSK----SGDDl 83
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKvfwpTGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 84 fpKDDKG-------NAIGG-----KATFLDAW---------------EAMEELVDEGLVKALGVSNFSHFQIEK---LLN 133
Cdd:cd19074 80 --PNDRGlsrkhifESIHAslkrlQLDYVDIYychrydpetpleetvRAMDDLIRQGKILYWGTSEWSAEQIAEahdLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 134 KPGLkYKPVTNQVECHpYLTQEK---LIQYCHSKGITVTAYSPLGS-------------PDRPWAKPEDP-----SLLED 192
Cdd:cd19074 158 QFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQglltgkyrdgippPSRSRATDEDNrdkkrRLLTD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615417 193 P------KIKEIAAKHKKTAAQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDE 245
Cdd:cd19074 236 EnlekvkKLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
36-250 |
1.02e-12 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 66.85 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 36 IDAGYRHIDCAYVY---QNEHEVGEAiqEKI----QEKAVKREDLFIVSKSGddlFPKDDKGNAIGGKAT---------- 98
Cdd:cd19081 36 VDAGGNFIDTADVYsawVPGNAGGES--ETIigrwLKSRGKRDRVVIATKVG---FPMGPNGPGLSRKHIrraveaslrr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 99 ---------FLDAW----------EAMEELVDEGLVKALGVSNFSHFQIEKLLN---KPGLKyKPVTNQVEchpY----- 151
Cdd:cd19081 111 lqtdyidlyQAHWDdpatpleetlGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQPE---Ynlvdr 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 152 -LTQEKLIQYCHSKGITVTAYSPLGS--------PDRPWAK----PEDPSLLEDPK-------IKEIAAKHKKTAAQVLI 211
Cdd:cd19081 187 eSFEGELLPLCREEGIGVIPYSPLAGgfltgkyrSEADLPGstrrGEAAKRYLNERglrildaLDEVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462615417 212 RFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19081 267 AWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-250 |
2.33e-12 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 66.00 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWKSPLGKVKEAVKV---AIDAGYRHIDCAYVY-QNEHEVGEAIQEkiqekavKREDLFIVSKSgdDLFPKD 87
Cdd:COG1453 12 EVSVLGFGGMRLPRKDEEEAEALirrAIDNGINYIDTARGYgDSEEFLGKALKG-------PRDKVILATKL--PPWVRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 88 DKG----------------------NAIGGKATF------LDAWEAMEELVDEGLVKALGVSnfSHFQ---IEKLLNkpg 136
Cdd:COG1453 83 PEDmrkdleeslkrlqtdyidlyliHGLNTEEDLekvlkpGGALEALEKAKAEGKIRHIGFS--THGSlevIKEAID--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 137 lkykpvTNQVEC---------HPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwakpeDPSLLEDP-KIKEIaAKHKKTA 206
Cdd:COG1453 158 ------TGDFDFvqlqynyldQDNQAGEEALEAAAEKGIGVIIMKPLK----------GGRLANPPeKLVEL-LCPPLSP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462615417 207 AQVLIRF--HIQRNVIVIPKSVTPARIVENIQVFD--FKLSDEEMATI 250
Cdd:COG1453 221 AEWALRFllSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAIL 268
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-245 |
6.36e-12 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 64.11 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 14 PIVGLGTwkSPLGKVK---------EAVKVAIDAGYRHIDCAYVYQN-EHEVGEAIQEkiqekaVKREDLFIVSK----- 78
Cdd:cd19090 1 SALGLGT--AGLGGVFggvdddeavATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKvgrlp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 79 ------SGD------------------DLF-------PKDDKGNAIGGkatfldAWEAMEELVDEGLVKALGVSNFSHFQ 127
Cdd:cd19090 73 edtadySADrvrrsveeslerlgrdriDLLmihdperVPWVDILAPGG------ALEALLELKEEGLIKHIGLGGGPPDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 128 IEKLLNkpglkykpvTNQVEC----HPY--LTQE---KLIQYCHSKGITVTAYSPLGS-------PDRPWAKPEDPSLLE 191
Cdd:cd19090 147 LRRAIE---------TGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGMgllagrpPERVRYTYRWLSPEL 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615417 192 DP---KIKEIAAKHKKTAAQVLIRFHIQ--RNVIVIPKSVTPARIVENIQVFDFKLSDE 245
Cdd:cd19090 218 LDrakRLYELCDEHGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-250 |
1.10e-11 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 63.87 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWKspLG-------KVKEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekaVKREDLFIVSKSG-- 80
Cdd:cd19148 7 IALGTWA--IGgwmwggtDEKEAIETihkALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVGle 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 81 ---DDLFPKDDKGNAI------------------------GGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLln 133
Cdd:cd19148 80 wdeGGEVVRNSSPARIrkevedslrrlqtdyidlyqvhwpDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETF-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 134 kpgLKYKPV-TNQVechPY-----LTQEKLIQYCHSKGITVTAYSPL------GSPDRPWAKPEDPSLLEDPKIKE---- 197
Cdd:cd19148 158 ---RKVAPLhTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGALcrgllsGKMTKDTKFEGDDLRRTDPKFQEprfs 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615417 198 --IAA----------KHKKTAAQVLIRFHIQRNVIVIpkSVTPARIVENIQ----VFDFKLSDEEMATI 250
Cdd:cd19148 232 qyLAAveeldklaqeRYGKSVIHLAVRWLLDQPGVSI--ALWGARKPEQLDavdeVFGWSLNDEDMKEI 298
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-250 |
2.32e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 62.74 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWK--SPL-------------GKVKEAVKVAIDAGYRHIDCAYVYqnehevGEAIQEKIQE---KAVKREDL 73
Cdd:cd19103 3 KLPKIALGTWSwgSGGaggdqvfgnhldeDTLKAVFDKAMAAGLNLWDTAAVY------GMGASEKILGeflKRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 74 FIVSK--------SGD---DLFPKDDKGNAIGgkatFLD-----------AW-EAMEELVDEGLVKALGVSNFSHFQIEK 130
Cdd:cd19103 77 IISTKftpqiagqSADpvaDMLEGSLARLGTD----YIDiywihnpadveRWtPELIPLLKSGKVKHVGVSNHNLAEIKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 131 ---LLNKPGLKYKPVTNqvecH---PYLTQEK--LIQYCHSKGITVTAYSPL------GSPDRPWAKPEDPSLLED---- 192
Cdd:cd19103 153 aneILAKAGVSLSAVQN----HyslLYRSSEEagILDYCKENGITFFAYMVLeqgalsGKYDTKHPLPEGSGRAETynpl 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615417 193 -PKI-------KEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19103 229 lPQLeeltavmAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKEL 294
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
27-239 |
4.79e-11 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 61.42 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 27 KVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIqekiqeKAVKREDLFIVSKSGDDLFPKDDKGNAI---------- 93
Cdd:cd19096 22 KAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEAL------KEGPREKFYLATKLPPWSVKSAEDFRRIleeslkrlgv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 94 ----------GGKATFLD------AWEAMEELVDEGLVKALGVSnfSHFQ---IEKLLNkpglkykpvTNQVEC----HP 150
Cdd:cd19096 96 dyidfyllhgLNSPEWLEkarkggLLEFLEKAKKEGLIRHIGFS--FHDSpelLKEILD---------SYDFDFvqlqYN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 151 YLTQE-----KLIQYCHSKGITVTAYSPL--GspdrpwAKPEDPslledPKIKEIAAKHKKTAAQVLIRFHI-QRNVIVI 222
Cdd:cd19096 165 YLDQEnqagrPGIEYAAKKGMGVIIMEPLkgG------GLANNP-----PEALAILCGAPLSPAEWALRFLLsHPEVTTV 233
|
250 260
....*....|....*....|
gi 2462615417 223 pkSV---TPARIVENIQVFD 239
Cdd:cd19096 234 --LSgmsTPEQLDENIAAAD 251
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
29-250 |
5.08e-11 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 61.87 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 29 KEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIqekiqekAVKREDLFIVSKSGDDLFPKDDKG-----------N 91
Cdd:cd19078 25 EEMIELirkAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFGFKIDGGKPGPlgldsrpehirK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 92 AIGG-----KATFLDAW---------------EAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPVTN-QVECH- 149
Cdd:cd19078 98 AVEGslkrlQTDYIDLYyqhrvdpnvpieevaGTMKELIKEGKIRHWGLSEAGVETIRR-----AHAVCPVTAvQSEYSm 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 150 ----PyltQEKLIQYCHSKGITVTAYSPLGS--------PDRPWAKPEDPSLLedPK---------------IKEIAAKH 202
Cdd:cd19078 173 mwreP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidENTKFDEGDDRASL--PRftpealeanqalvdlLKEFAEEK 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462615417 203 KKTAAQVLIRF--HIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19078 248 GATPAQIALAWllAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-237 |
5.57e-11 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 60.95 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWksPLG----------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIVSKSG-- 80
Cdd:cd19086 6 IGFGTW--GLGgdwwgdvddaEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGnr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 81 -------DDLFPKDD------------KGNAI------GGKATFL---DAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 132
Cdd:cd19086 77 fdggperPQDFSPEYireaveaslkrlGTDYIdlyqlhNPPDEVLdndELFEALEKLKQEGKIRAYGVSVGDPEEALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 133 NKPGLK-----YkpvtNQVECHPYltqEKLIQYCHSKGITVTAYSPLGSpdrpwakpedpSLLEDpkikeiaakhkkTAA 207
Cdd:cd19086 157 RRGGIDvvqviY----NLLDQRPE---EELFPLAEEHGVGVIARVPLAS-----------GLLTG------------KLA 206
|
250 260 270
....*....|....*....|....*....|..
gi 2462615417 208 QVLIRFHIQRNVI--VIPKSVTPARIVENIQV 237
Cdd:cd19086 207 QAALRFILSHPAVstVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-213 |
2.23e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 60.02 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTWKSPLGK-----VKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIQEKAVKREDLFIVSKSG---DDLF 84
Cdd:cd19099 6 LGLGTYRGDSDDetdeeYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAGyipGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 85 PKDDKGNAIGGKA-------------------TFL-----------------------------------------DAWE 104
Cdd:cd19099 86 EPLRPLKYLEEKLgrglidvadsaglrhcispAYLedqierslkrlgldtidlyllhnpeeqllelgeeefydrleEAFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 105 AMEELVDEGLVKALGVS----------NFSHFQIEKLL--------NKPGLKYkpVtnQVECHPYLTQ------------ 154
Cdd:cd19099 166 ALEEAVAEGKIRYYGIStwdgfrappaLPGHLSLEKLVaaaeevggDNHHFKV--I--QLPLNLLEPEaltekntvkgea 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615417 155 EKLIQYCHSKGITVTAYSPL--GSPDRPWAKPEDPSLLEDpkikeiaakhkKTAAQVLIRF 213
Cdd:cd19099 242 LSLLEAAKELGLGVIASRPLnqGQLLGELRLADLLALPGG-----------ATLAQRALQF 291
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
35-175 |
2.49e-10 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 59.89 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 35 AIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIVSKSGddlFPKDDKGNAIG----------------- 94
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVF---GPMGDDPNDRGlsrrhirraveaslrrl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 95 --------------GKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN---KPGL--------KYKPVTNQVECH 149
Cdd:cd19087 109 qtdyidlyqmhhfdRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGLlrfvseqpMYNLLKRQAELE 188
|
170 180
....*....|....*....|....*.
gi 2462615417 150 pyltqekLIQYCHSKGITVTAYSPLG 175
Cdd:cd19087 189 -------ILPAARAYGLGVIPYSPLA 207
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
104-236 |
2.88e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 59.65 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 104 EAMEELVDEGLVKALGVSNFSHFQIEK---LLNKPGL-KYKPVTNQvecHPYL--------------TQEkLIQYCHSKG 165
Cdd:cd19752 132 EAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGWaEFSAIQQR---HSYLrprpgadfgvqrivTDE-LLDYASSRP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 166 -ITVTAYSPL--GSPDRPWAKPEDPSLLEDP-----KIKEIAAKHKKTAAQVLIRFHIQRNVIVIP--KSVTPARIVENI 235
Cdd:cd19752 208 dLTLLAYSPLlsGAYTRPDRPLPEQYDGPDSdarlaVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENL 287
|
.
gi 2462615417 236 Q 236
Cdd:cd19752 288 A 288
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-237 |
1.83e-09 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 56.86 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 14 PIVGLGTWK-------SPLGKVKEAVKVAIDAGYRHIDCAYVYQN-EHEVGEAIqekiqeKAVKREDLFIVSKSG----D 81
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL------AGLRRDDLFIATKVGthgeG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 82 DLFPKDDKGNAIggKATF-----------LDAW---------------EAMEELVDEGLVKALGVSNFSHfQIEKLLNKP 135
Cdd:cd19095 75 GRDRKDFSPAAI--RASIerslrrlgtdyIDLLqlhgpsddeltgevlETLEDLKAAGKVRYIGVSGDGE-ELEAAIASG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 136 GLKykpvTNQVechPY----LTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHK-KTAAQVL 210
Cdd:cd19095 152 VFD----VVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIGgATWAQAA 224
|
250 260
....*....|....*....|....*....
gi 2462615417 211 IRFHIQ--RNVIVIPKSVTPARIVENIQV 237
Cdd:cd19095 225 LRFVLShpGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-248 |
1.14e-08 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 54.96 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 12 KMPIVGLGTWK-----SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKI--QEKAVKREDLFIVSKSGDDLF 84
Cdd:cd19089 10 HLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRIlkRDLRPYRDELVISTKAGYGMW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 85 PkddkG-NAIGG-------------KATFLD------------------AWEAMEELVDEGlvKAL--GVSNFSHFQIEK 130
Cdd:cd19089 90 P----GpYGDGGsrkyllasldqslKRMGLDyvdifyhhrydpdtpleeTMTALADAVRSG--KALyvGISNYPGAKARR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 131 ---LLNKpgLKYKPVTNQVechPY--LTQ---EKLIQYCHSKGITVTAYSPL-----------GSPDRPWAKPEDPSLLE 191
Cdd:cd19089 164 aiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylnGIPPDSRRAAESKFLTE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 192 D-------PKIK---EIAAKHKKTAAQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFD-FKLSDEEMA 248
Cdd:cd19089 239 EaltpeklEQLRklnKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-245 |
1.93e-07 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 51.07 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 14 PIVGLGTwkSPLG---------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIQEKAV-------KREDLF 74
Cdd:cd19152 1 PKLGFGT--APLGnlyeavsdeEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREDYVistkvgrLLVPLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 75 IVSKSGDDLFPKDDKGNAIG--GKATFLDAWE-----------------------------------------AMEELVD 111
Cdd:cd19152 79 EVEPTFEPGFWNPLPFDAVFdySYDGILRSIEdslqrlglsridllsihdpdedlagaesdehfaqaikgafrALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 112 EGLVKALGV-SNFSHFqIEKLLNKPGLKYKPVTNQvechpY--LTQE---KLIQYCHSKGITVTAYSPLGS--------P 177
Cdd:cd19152 159 EGVIKAIGLgVNDWEV-ILRILEEADLDWVMLAGR-----YtlLDHSaarELLPECEKRGVKVVNAGPFNSgflaggdnF 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462615417 178 DRPWAKPEDPSLLE--DpKIKEIAAKHKKTAAQVLIRFHIQRNVI--VIPKSVTPARIVENIQVFDFKLSDE 245
Cdd:cd19152 233 DYYEYGPAPPELIArrD-RIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
97-250 |
2.80e-07 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 50.64 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 97 ATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN---KPGLKyKPVTNQvecHPY--LTQ---EKLIQYCHSKGITV 168
Cdd:cd19094 144 VSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLElaeQLGLP-RIVSIQ---NPYslLNRnfeEGLAEACHRENVGL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 169 TAYSPLG----------SPDRP--------------WAKPEDPSLLEdpKIKEIAAKHKKTAAQVLIRFHIQR----NVI 220
Cdd:cd19094 220 LAYSPLAggvltgkyldGAARPeggrlnlfpgymarYRSPQALEAVA--EYVKLARKHGLSPAQLALAWVRSRpfvtSTI 297
|
170 180 190
....*....|....*....|....*....|
gi 2462615417 221 VIPKSVtpARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19094 298 IGATTL--EQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-213 |
5.05e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 49.83 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 26 GKV--KEAVKV---AIDAGYRHIDCAYVYQNEHEV-GEAIQEKiqekavkrEDLFIVSKSGDDLFPKDDKGNAIGG---- 95
Cdd:cd19097 21 GKPseKEAKKIleyALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLPPLKEDKKEDEAAIEAsvea 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 96 -----KATFLDA----------------WEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYkpVtnQVECHPY--- 151
Cdd:cd19097 93 slkrlKVDSLDGlllhnpddllkhggklVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I--QLPFNILdqr 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615417 152 LTQEKLIQYCHSKGITVTAYSP------LGSPDRPWAKPED-PSLLEdpKIKEIAAKHKKTAAQVLIRF 213
Cdd:cd19097 169 FLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPaKPLLK--KLHELAKKLGLSPLELALGF 235
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
17-250 |
7.29e-07 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 49.35 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 17 GLGTWKSPLGKVKEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIQEKIQEKavkredLFIVSKSGddLFPKDDKG 90
Cdd:cd19145 21 GLSGDYGAPKPEEEGIALihhAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPREK------VQLATKFG--IHEIGGSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 91 NAIGGKATFL-DAWEA------------------------------MEELVDEGLVKALGVSNFSHFQIEKllnkpGLKY 139
Cdd:cd19145 93 VEVRGDPAYVrAACEAslkrldvdyidlyyqhridttvpieitmgeLKKLVEEGKIKYIGLSEASADTIRR-----AHAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 140 KPVTN-QVECHPYL--TQEKLIQYCHSKGITVTAYSPLGspdRP--WAKPEDPSLLEDP--------------------- 193
Cdd:cd19145 168 HPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---RGffAGKAKLEELLENSdvrkshprfqgenleknkvly 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 194 -KIKEIAAKHKKTAAQV-LIRFHIQRN-VIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19145 245 eRVEALAKKKGCTPAQLaLAWVLHQGEdVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-214 |
1.77e-06 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 48.32 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 15 IVGLGTWKSPLG-----KVKEAVKVAIDAGYRHIDCAYVYQN-EHE--VGEA--------IQEKI---QEKAVKREDlfi 75
Cdd:cd19075 4 ILGTMTFGSQGRfttaeAAAELLDAFLERGHTEIDTARVYPDgTSEelLGELglgergfkIDTKAnpgVGGGLSPEN--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 76 VSKSGD-----------DLF----PkdDKGNAIggKATFldawEAMEELVDEGLVKALGVSNFSHFQIEKLLN------- 133
Cdd:cd19075 81 VRKQLEtslkrlkvdkvDVFylhaP--DRSTPL--EETL----AAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 134 -KP----GLkYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLG--------------------SPDRPWA------ 182
Cdd:cd19075 153 vLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAggfltgkykysedkagggrfDPNNALGklyrdr 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462615417 183 --KPEDPSLLEdpKIKEIAAKHKKTAAQVLIR---FH 214
Cdd:cd19075 225 ywKPSYFEALE--KVEEAAEKEGISLAEAALRwlyHH 259
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
36-250 |
2.13e-06 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 47.98 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 36 IDAGYRHIDCAYVYQNEHE---VGEAIQEKiqekavkREDLFIVSKSGddLFPKDDKGNAIGG----------------K 96
Cdd:cd19080 41 VEAGGNFIDTANNYTNGTSerlLGEFIAGN-------RDRIVLATKYT--MNRRPGDPNAGGNhrknlrrsveaslrrlQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 97 ATFLD-----AWE----------AMEELVDEGLVKALGVSN--------------------FSHFQIEkllnkpglkYKP 141
Cdd:cd19080 112 TDYIDllyvhAWDfttpveevmrALDDLVRAGKVLYVGISDtpawvvarantlaelrgwspFVALQIE---------YSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 142 VTNQVEchpyltqEKLIQYCHSKGITVTAYSPLGS---------PDRPWAKPEDPSLLEDPKI-----------KEIAAK 201
Cdd:cd19080 183 LERTPE-------RELLPMARALGLGVTPWSPLGGglltgkyqrGEEGRAGEAKGVTVGFGKLternwaivdvvAAVAEE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462615417 202 HKKTAAQVLIRFHIQRNVIVIP--KSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:cd19080 256 LGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-213 |
3.21e-06 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 47.55 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 36 IDAGYRHIDCAYVYQNEHEVG---EAIQEKIQEKAvKREDLFIVSKSGDDLFPKDDKGN----AIGG---------KATF 99
Cdd:cd19082 27 VELGGNFIDTARVYGDWVERGaseRVIGEWLKSRG-NRDKVVIATKGGHPDLEDMSRSRlspeDIRAdleeslerlGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 100 LDAW---------------EAMEELVDEGLVKALGVSNFSHFQIE---KLLNKPGLkYKPVTNQV---------ECHPYL 152
Cdd:cd19082 106 IDLYflhrddpsvpvgeivDTLNELVRAGKIRAFGASNWSTERIAeanAYAKAHGL-PGFAASSPqwslarpnePPWPGP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 153 T----QEKLIQYCHSKGITVTAYSPLGS---PDRpwAKPEDPSLLEDPK-------------IKEIAAKHKKTAAQVLIR 212
Cdd:cd19082 185 TlvamDEEMRAWHEENQLPVFAYSSQARgffSKR--AAGGAEDDSELRRvyyseenferlerAKELAEEKGVSPTQIALA 262
|
.
gi 2462615417 213 F 213
Cdd:cd19082 263 Y 263
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
104-250 |
1.17e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 45.73 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 104 EAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPVTNqVECHPYLTQ---EKLIQYCHSKGITVTAYSPLG--SPd 178
Cdd:PRK10376 148 TVLAELQRQGLVRHIGLSNVTPTQVAE-----ARKIAEIVC-VQNHYNLAHradDALIDALARDGIAYVPFFPLGgfTP- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462615417 179 rpwakpedpslLEDPKIKEIAAKHKKTAAQVLIRFHIQR--NVIVIPKSVTPARIVENIQVFDFKLSDEEMATI 250
Cdd:PRK10376 221 -----------LQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
16-88 |
8.44e-03 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 36.92 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615417 16 VGLGTwkSPLG---------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavKREDLFIVSKSGDDL 83
Cdd:cd19161 3 LGLGT--AGLGnlytavsnaDADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK------PRDEFVLSTKVGRLL 74
|
....*
gi 2462615417 84 FPKDD 88
Cdd:cd19161 75 KPARE 79
|
|
| |
