|
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 ... |
10-316 |
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: 651.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSMV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 90 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEK 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 170 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2166761530 250 IRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVCALVSCASHKDYPFTDEF 316
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-299 |
1.19e-161 |
|
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: 452.61 E-value: 1.19e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKE-QVVKREDLFIVSKLWCTYHE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHL 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 166 QVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTT 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 246 AQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVC 299
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-316 |
1.69e-161 |
|
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: 452.11 E-value: 1.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 12 KMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSMVKG 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 92 ACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKIL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 172 NKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 252 FPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVCALVSCASHKDYPFTDEF 316
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
7-297 |
1.66e-142 |
|
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: 403.92 E-value: 1.66e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKS---PPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTY 83
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFN 163
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 HLQVEKILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPRIKAIAAKHN 242
Cdd:cd19108 165 RRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALAKKHK 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 243 KTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19108 245 RTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-312 |
2.65e-130 |
|
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: 373.37 E-value: 2.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTW----KSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHE 85
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHL 165
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 166 QVEKILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPRIKAIAAKHNKT 244
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166761530 245 TAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVCALVSCASHKDYPF 312
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-299 |
3.90e-130 |
|
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: 372.39 E-value: 3.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKS-PPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHE 85
Cdd:cd19116 5 LNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYfplDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHL 165
Cdd:cd19116 85 REQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS---ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 166 QVEKILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSlLEDPRIKAIAAKHNKTT 245
Cdd:cd19116 162 QINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPR-LDDPTLVAIAKKYGKTT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 246 AQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVC 299
Cdd:cd19116 239 AQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
5-297 |
2.18e-127 |
|
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: 365.58 E-value: 2.18e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 5 LVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYH 84
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 85 EKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKeYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNH 164
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 165 LQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWA-KPED-PSLLEDPRIKAIAAKHN 242
Cdd:cd19123 163 KKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLEDPVINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 243 KTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
2.89e-125 |
|
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: 358.33 E-value: 2.89e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 13 MPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLkeqvVKREDLFIVSKLWCTYHEKSMVKGA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 93 CQKTLSDLKLDYLDLYLIHWPTGFKPGkeyfpldgegnviPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEG-------------GSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 173 KPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 2166761530 253 PIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19071 214 ALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-289 |
1.32e-119 |
|
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: 345.48 E-value: 1.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 4 HLVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTY 83
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKeyfPLDGEGNVIPSDtnFVDTWEAMEELVDAGLVKAIGVSNFN 163
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVLPPD--IPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 HLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEdpsLLEDPRIKAIAAKHNK 243
Cdd:cd19125 157 VKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2166761530 244 TTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-299 |
4.89e-117 |
|
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: 339.39 E-value: 4.89e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 2 ASHLVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWC 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 82 TYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 162 FNHLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPED-----PSLLEDPRIKA 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2166761530 237 IAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVC 299
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-298 |
1.68e-113 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 328.55 E-value: 1.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 9 NGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHEKSM 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 89 VKGACQKTlsdlkldyldlylIHWPtgfkpgkeyfpldgegnvipSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVE 168
Cdd:COG0656 77 TLAAFEESlerlgldyldlylIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 169 KILNKPGlkYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKAIAAKHNKTTAQV 248
Cdd:COG0656 137 ELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2166761530 249 LIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRV 298
Cdd:COG0656 205 VLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-297 |
4.91e-101 |
|
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: 298.26 E-value: 4.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSMV 89
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 90 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEyfplDGEGNVIPSDTnfVDTWEAMEELVDAGLVKAIGVSNFNHLQVEK 169
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKKD----KGERELASSDV--TSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 170 ILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP--WAKPEDPSLLEDPRIKAIAAKHNKTTAQ 247
Cdd:cd19111 155 ILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2166761530 248 VLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-283 |
4.93e-101 |
|
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: 298.17 E-value: 4.93e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQ-VVKREDLFIVSKLWCTYHE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPL---DGEGNVIPSDTN--FVDTWEAMEELVDAGLVKAIGVS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavPTNGGEVDLDLSvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 161 NFNHLQVEKILNKPGLkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwAKPEDPSLLEDPRIKAIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2166761530 241 HNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQvfDFELSS 283
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSD 274
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
3-299 |
9.01e-100 |
|
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: 295.59 E-value: 9.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 3 SHLVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCT 82
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 83 YHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFK-PGKEYFPLDGEGNV-IPSDTNFVDTWEAMEELVDAGLVKAIGVS 160
Cdd:cd19155 82 GNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHkQDYTTDLLDIWKAMEAQVDQGLTRSIGLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 161 NFNHLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKP-------EDPSLLEDPR 233
Cdd:cd19155 162 NFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2166761530 234 IKAIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRVC 299
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-289 |
2.33e-96 |
|
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: 286.32 E-value: 2.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHEK 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLWCTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 smVKGACQKTLSDLKLDYLDLYLIHWPTGFKPG--KEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNH 164
Cdd:cd19117 84 --VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 165 LQVEKILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAIAAKHNKT 244
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2166761530 245 TAQVLIRFPIQRNLVVIPKSVTPERIAENFQVfdFELSSVDMTTL 289
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-297 |
2.32e-95 |
|
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: 284.38 E-value: 2.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEk 86
Cdd:cd19112 5 LNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSDHG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 sMVKGACQKTLSDLKLDYLDLYLIHWPTGFKP---GKEYFPLDGEGNV-IPSDTNFVDTWEAMEELVDAGLVKAIGVSNF 162
Cdd:cd19112 84 -HVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRSIGISNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 163 NHLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLG--SPDRPWAKPEDPslLEDPRIKAIAAK 240
Cdd:cd19112 163 DIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2166761530 241 HNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-292 |
1.65e-94 |
|
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: 280.67 E-value: 1.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 13 MPIVGLGTWKSPPGKVTE-AVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSMVKG 91
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 92 ACQKTLSDLKLDYLDLYLIHWptgfkPGKEYFPLDGEGNVIpsdtNFVDTWEAMEELVDAGLVKAIGVSNFN--HLQvek 169
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHW-----PGVQGLKPSDPRNAE----LRRESWRALEDLYKEGKLRAIGVSNYTvrHLE--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 170 ilnkPGLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpeDPSLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19136 149 ----ELLKYcevPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--------DLRLLEDPTVLAIAKKYGRTPA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2166761530 247 QVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSY 292
Cdd:cd19136 217 QVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
7-297 |
3.83e-90 |
|
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: 271.24 E-value: 3.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEK 86
Cdd:cd19113 5 LNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFHDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 SMVKGACQKTLSDLKLDYLDLYLIHWPTGFK--PGKEYFPLD---GEG-NVIPSDTNFVDTWEAMEELVDAGLVKAIGVS 160
Cdd:cd19113 85 KNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPGfycGDGdNFVYEDVPILDTWKALEKLVDAGKIKSIGVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 161 NFNHLQVEKILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-----DRPWAKpEDPSLLEDPRIK 235
Cdd:cd19113 165 NFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLFEHDTIK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2166761530 236 AIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19113 242 SIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
7.48e-90 |
|
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: 270.45 E-value: 7.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 1 MASHLVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 81 CTYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFK---PGKEYFP--LDGEGNVIPSDTNFVDTWEAMEELVDAGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 156 AIGVSNFNHLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGsP------DRPWAKpEDPSLL 229
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166761530 230 EDPRIKAIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-292 |
1.17e-89 |
|
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: 269.02 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLkEQVVKREDLFIVSKLWCTYHEK 86
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYHRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 smVKGACQKTLSDLKLDYLDLYLIHWPTGFKP--GKEYFPL--DGEGNVIPsDTNFVDTWEAMEELVDAGLVKAIGVSNF 162
Cdd:cd19121 85 --VELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTlpDGSRDLDW-DWNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 163 NHLQVEKILnkPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAIAAKHN 242
Cdd:cd19121 162 SIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAKKHN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2166761530 243 KTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFElsSVDMTTLLSY 292
Cdd:cd19121 232 VGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-286 |
5.31e-88 |
|
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: 263.85 E-value: 5.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHEK 86
Cdd:cd19131 4 LNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 SMVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfpldgegnviPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQ 166
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPV------------------PAQDKYVETWKALIELKKEGRVKSIGVSNFTIEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 167 VEKILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19131 142 LQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----------GLLSDPVIGEIAEKHGKTPA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2166761530 247 QVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19131 210 QVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDM 249
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-286 |
7.33e-88 |
|
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: 264.38 E-value: 7.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 14 PIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSMVKGAC 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 94 QKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 174 pgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKpedpSLLEDPRIKAIAAKHNKTTAQVLIRFP 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 2166761530 254 IQR---NLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-289 |
1.63e-85 |
|
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: 257.37 E-value: 1.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 5 LVLYNGAKMPIVGLGTWKSPPGKVTE-AVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTY 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKSMVKGACQKTLSDLKLDYLDLYLIHWPTgfkPGKeyfpldgegnvipsdtnFVDTWEAMEELVDAGLVKAIGVSNFN 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPG---KDK-----------------FIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 HLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNK 243
Cdd:cd19126 137 EHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGK 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2166761530 244 TTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19126 205 SAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAI 250
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
7-293 |
1.68e-84 |
|
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: 254.81 E-value: 1.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTE-AVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHE 85
Cdd:cd19133 3 LNNGVEMPILGFGVFQIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQDAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkeyfpldgegnvipsdtNFVDTWEAMEELVDAGLVKAIGVSNFNHL 165
Cdd:cd19133 79 YEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVSNFYPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 166 QVEKILnkPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakpEDPSLLEDPRIKAIAAKHNKTT 245
Cdd:cd19133 138 RLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE--------GRNNLFENPVLTEIAEKYGKSV 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2166761530 246 AQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYN 293
Cdd:cd19133 208 AQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
5-298 |
1.70e-84 |
|
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: 255.39 E-value: 1.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 5 LVLYNGAKMPIVGLGTWKSPPGK-VTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTY 83
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKSMVKGACQKTLSDLKLDYLDLYLIHWPtgfKPGKeyfpldgegnvipsdtnFVDTWEAMEELVDAGLVKAIGVSNFN 163
Cdd:cd19157 78 QGYDSTLKAFEASLERLGLDYLDLYLIHWP---VKGK-----------------YKETWKALEKLYKDGRVRAIGVSNFQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 HLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKAIAAKHNK 243
Cdd:cd19157 138 VHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 244 TTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRV 298
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-286 |
2.76e-84 |
|
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: 255.27 E-value: 2.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 9 NGAKMPIVGLGTWKSPPGK--VTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVK-REDLFIVSKLWCTYHE 85
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPedIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDgEGNVIPSDtnFVDTWEAMEELVDAGLVKAIGVSNFNHL 165
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIE-EEDFLPFD--IKGVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 166 QVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAkpeDPSLLEDPRIKAIAAKHNKTT 245
Cdd:cd19124 158 KLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2166761530 246 AQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDL 273
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
5.82e-83 |
|
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: 250.65 E-value: 5.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 13 MPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHEKSMVKGA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 93 CQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfpldgegnvipSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN-------------------PTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 173 KPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwAKPEdpsLLEDPRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 2166761530 253 PIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-289 |
1.28e-81 |
|
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: 248.01 E-value: 1.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 4 HLVLYNGAKMPIVGLGTWKSPpGKVTEAVKIAI-DLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCT 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 83 YHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEyfpldgegnvipSDTNFVDTWEAMEELVDAGLVKAIGVSNF 162
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN------------VKETRAETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 163 NHLQVEKILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrPWakpedpSLLEDPRIKAIAAKHN 242
Cdd:cd19135 147 LIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KG------KALEEPTVTELAKKYQ 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2166761530 243 KTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19135 215 KTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATL 261
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-276 |
1.31e-80 |
|
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: 246.60 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 9 NGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSM 88
Cdd:cd19129 2 GSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 89 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGNVIPSD-TNFVDTWEAMEELVDAGLVKAIGVSNFNHLQV 167
Cdd:cd19129 82 VKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 168 EKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwakpedPSLLEDPRIKAIAAKHNKTTAQ 247
Cdd:cd19129 162 REIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME-------PKLLEDPVITAIARRVNKTPAQ 232
|
250 260
....*....|....*....|....*....
gi 2166761530 248 VLIRFPIQRNLVVIPKSVTPERIAENFQV 276
Cdd:cd19129 233 VLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
7-297 |
2.09e-79 |
|
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: 242.42 E-value: 2.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTE-AVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHE 85
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 KSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKpgkeyfpldgegnvipsdtnFVDTWEAMEELVDAGLVKAIGVSNFNHL 165
Cdd:cd19156 79 YESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVSNFHEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 166 QVEKILNKpgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKAIAAKHNKTT 245
Cdd:cd19156 139 HLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGKSA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2166761530 246 AQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19156 207 AQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-297 |
7.38e-79 |
|
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: 242.46 E-value: 7.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTYHEKSMV 89
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 90 KGACQKTLSDLKLDYLDLYLIHWPTGFK---PGKEYFPL--DGEGNVIPSDTNFV-DTWEAMEELVDAGLVKAIGVSNFN 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLwkDKELKKFPLEQSPMqECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 hlqVEKILNKpgLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP---DRPWAKPEDPSLLEDPRIKAI 237
Cdd:cd19114 161 ---VQLILDL--LTYakiKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 238 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-289 |
2.75e-74 |
|
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: 228.68 E-value: 2.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 9 NGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYHEKSM 88
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 89 VKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeyfpldgegnviPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVE 168
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 169 KILNKPGLKYkpAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwakpeDPSLLEDPRIKAIAAKHNKTTAQV 248
Cdd:cd19140 141 EAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2166761530 249 LIRFPIQR-NLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19140 209 ALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-286 |
2.19e-73 |
|
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: 227.12 E-value: 2.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGT----WKSPPG----KVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLkeqvVKREDLFIVSKLWC 81
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 82 TyheKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGkeyfpldgegnvipsDTNFVDTWEAMEELVDAGLVKAIGVSN 161
Cdd:cd19120 77 G---IKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 162 FNHLQVEKILNKPglKYKPAVNQIECHPYLT--QEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLledpriKAIAA 239
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVL------EKIAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2166761530 240 KHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19120 211 KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEV 257
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
7-286 |
3.23e-73 |
|
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: 226.00 E-value: 3.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLkeqvVKREDLFIVSKLWCTYHEK 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSG----VPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 SMVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfpldgegnviPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQ 166
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWPN------------------PSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 167 VEKILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwakpedpsLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19132 139 LDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2166761530 247 QVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19132 208 QVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDM 247
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-286 |
1.01e-71 |
|
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: 222.67 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 5 LVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGlaiqEKLKEQVVKREDLFIVSKLWCTYH 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVG----EGIRRSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 85 EKSMVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfPLDGEgnvipsDTnfVDTWEAMEELVDAGLVKAIGVSNFNH 164
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPV---------PNDFD------RT--IQAYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 165 LQVEKILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAK--PEDPSLLEDPRIKAIAAKHN 242
Cdd:cd19127 140 EHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgpTGPGDVLQDPTITGLAEKYG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2166761530 243 KTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDM 261
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
7-273 |
8.22e-71 |
|
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: 221.22 E-value: 8.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWkSPP---GKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQVVKREDLFIVSKLWCTY 83
Cdd:cd19119 6 LNTGASIPALGLGTA-SPHedrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKsmVKGACQKTLSDLKLDYLDLYLIHWPTGFK-----PGKEYFPLDGEGNVIPSDT-NFVDTWEAMEELVDAGLVKAI 157
Cdd:cd19119 85 YDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASgDHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 158 GVSNFNHLQVEKILNKpgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAI 237
Cdd:cd19119 163 GVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVKKI 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 2166761530 238 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAEN 273
Cdd:cd19119 233 AEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSN 268
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-289 |
2.02e-70 |
|
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: 219.01 E-value: 2.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 4 HLVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTY 83
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKSMVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfpldgegnviPSDTNFVDTWEAMEELVDAGLVKAIGVSNFN 163
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPT------------------PAAGNYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 HLQVEKILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNK 243
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG----------KLLGDPPVGAIAAAHGK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2166761530 244 TTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19130 207 TPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-285 |
2.73e-67 |
|
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: 212.48 E-value: 2.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKS--PPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEKLKEQ-VVKREDLFIVSKLWCTY 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 84 HEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFPLDGEGN--VIPSD--TNFVDTWEAMEELVDAGLVKAIGV 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKLGPDGkyVILKDltENPEPTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 160 SNFNHLQVEKILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSllEDPRIKAIAA 239
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2166761530 240 KHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVfdFELSSVD 285
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDED 282
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
7-289 |
1.64e-64 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 204.54 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 7 LYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAiqekLKEQVVKREDLFIVSKLWCTYHEK 86
Cdd:PRK11565 9 LQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKA----LKEASVAREELFITTKLWNDDHKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 smVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeyfpldgegnvIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFN--H 164
Cdd:PRK11565 85 --PREALEESLKKLQLDYVDLYLMHWP------------------VPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQihH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 165 LQveKILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwakpedpSLLEDPRIKAIAAKHNKT 244
Cdd:PRK11565 145 LQ--RLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYGKT 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2166761530 245 TAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:PRK11565 213 PAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-298 |
3.29e-62 |
|
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: 198.16 E-value: 3.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 5 LVLYNGAKMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIqeklKEQVVKREDLFIVSKLWCTYH 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 85 EKSMVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeyfpldgegnvIPSDTNFVDTWEAMEELVDAGLVKAIGVSNFNH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWP------------------AGREGKYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 165 LQVEKILNKPGlkYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNKT 244
Cdd:cd19134 141 EHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG----------RLLDNPAVTAIAAAHGRT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 245 TAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWRV 298
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-287 |
2.99e-60 |
|
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: 192.57 E-value: 2.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 13 MPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQEklkeQVVKREDLFIVSKLWCTYHEKSMVKGA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 93 CQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfpldgEGNVIPSDtnfvDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPS-------------PNDEVPVE----EYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 173 KPGlKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKpedpsLLEDPRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*
gi 2166761530 253 PIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMT 287
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMA 243
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-289 |
1.48e-53 |
|
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: 176.73 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 16 VGLGTW-------KSPPGKVTEAVKIAIDLGYRHIDCAHVY---QNENEVGLAiqekLKEQVVKREDLFIVSKL------ 79
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEA----LKDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 80 WCTYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgKEYFPLDgegnvipsdtnfvDTWEAMEELVDAGLVKAIGV 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------DPDTPIE-------------ETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 160 SNFNHLQVEKILNKPglKYKPAVNQIECHPY--LTQEKLIQYCQSKGIVVTAYSPLGS-----------------PDRPW 220
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2166761530 221 AKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPIQ--RNLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
1.73e-53 |
|
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: 175.88 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWK---------SPPGKVTEAVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEklkeqvVKREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 78 KLW---CTYHEksmVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEyfpldgegnvipsdtnfvdTWEAMEELVDAGLV 154
Cdd:cd19072 75 KVSpdhLKYDD---VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEE-------------------TLRAMEELVEEGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 155 KAIGVSNFNHLQVEKILNKPGlKYKPAVNQIECHpYLTQE---KLIQYCQSKGIVVTAYSPLGSPDRPwAKPEDPSLLEd 231
Cdd:cd19072 133 RYIGVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLS-NAKGSPLLDE- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2166761530 232 prikaIAAKHNKTTAQVLIRFPIQR-NLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19072 209 -----IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
1.85e-53 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 175.98 E-value: 1.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 12 KMPIVGLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQNENEVGLAIQeklkEQVVKREDLFIVSKLWCTYHEKSMVKG 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 92 ACQKTLSDLKLDYLDLYLIHWPTgfkPGKEyfpldgegnvipsdtnfVDTWEAMEELVDA---GLVKAIGVSNFNHLQVE 168
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPS---PNDE-----------------VSVEEFMQALLEAkkqGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 169 KILNKPGlKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKpedpsLLEDPRIKAIAAKHNKTTAQV 248
Cdd:PRK11172 138 QAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2166761530 249 LIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTTLLSYNRNWR 297
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-289 |
1.79e-45 |
|
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: 155.10 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 4 HLVLYNGAKMPIVGLGTW-----KSPPGKVTEAVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEKlkeqvvkREDLFI 75
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 76 VSKLWCTYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFkpgkeyfPLDgegnvipsdtnfvDTWEAMEELVDAGLVK 155
Cdd:cd19138 75 VSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV-------PLA-------------ETVAAMEELKKEGKIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 156 AIGVSNFNHLQVEKILNKPGLKyKPAVNQIECHpyLTQE----KLIQYCQSKGIVVTAYSPLGSPDRPwakpeDPSLLED 231
Cdd:cd19138 135 AWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLEN 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2166761530 232 PRIKAIAAKHNKTTAQVLIRFPIQRNLVV-IPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19138 207 PTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-289 |
7.73e-43 |
|
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: 148.10 E-value: 7.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWK---------SPPGKVTEAVKIAIDLGYRHIDCAHVY---QNENEVGLAIQEklkeqvVKREDLFIVS 77
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 78 KLWCTYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEyfpldgegnvipsdtnfvdTWEAMEELVDAGLVKAI 157
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 158 GVSNFNHLQVEKILNKpgLKYKPAVNQIECHPY---LTQEKLIQYCQSKGIVVTAYSPLgspDRPWAKPEDpslledpRI 234
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNR-------TL 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2166761530 235 KAIAAKHNKTTAQVLIRFPIQR-NLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19137 204 EEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-289 |
6.14e-35 |
|
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: 128.50 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 12 KMPIVGLGTWK-----------SPPGKVTEAVKIAIDLGYRHIDCAHVY---QNENEVGLAIQEKlkeqvVKREDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 78 KL----WCTYHEkSMVKgACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFpldgegnvipsdtnfvdtWEAMEELVDAGL 153
Cdd:cd19093 76 KFaplpWRLTRR-SVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 154 VKAIGVSNFNHLQVEKI---LNKPGlkYKPAVNQIE---CHPYLTQEKLIQYCQSKGIVVTAYSPLG--------SPDRP 219
Cdd:cd19093 136 VRAVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 220 -----------WAKPEDPSLLEdpRIKAIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELSSVDMTT 288
Cdd:cd19093 214 ppggrrrlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAE 291
|
.
gi 2166761530 289 L 289
Cdd:cd19093 292 L 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
10-289 |
3.81e-29 |
|
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: 113.35 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWK--SPPGKVTEA-----VKIAIDLGYRHIDCAHVYQN-ENE--VGLAIQEKlkeqvvKREDLFIVSKL 79
Cdd:COG0667 10 GLKVSRLGLGTMTfgGPWGGVDEAeaiaiLDAALDAGINFFDTADVYGPgRSEelLGEALKGR------PRDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 80 WCTYHEKSMVKG--------AC---------------QktlsdlkldyldlylIHWPtgfkpgkeyfpldgegnviPSDT 136
Cdd:COG0667 84 GRRMGPGPNGRGlsrehirrAVeaslrrlgtdyidlyQ---------------LHRP-------------------DPDT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 137 NFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEchpY--LTQ---EKLIQYCQSKGIVVTAYS 211
Cdd:COG0667 130 PIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 212 PLGS---------------PDR-------PWAKPEDPSLLEdpRIKAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTP 267
Cdd:COG0667 207 PLAGglltgkyrrgatfpeGDRaatnfvqGYLTERNLALVD--ALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSP 284
|
330 340
....*....|....*....|..
gi 2166761530 268 ERIAENFQVFDFELSSVDMTTL 289
Cdd:COG0667 285 EQLEENLAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-289 |
2.34e-27 |
|
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: 108.06 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 14 PIVGLGTWKSPPGKVTE---------AVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEKlkeqvvkREDLFIVSKLWC 81
Cdd:cd19085 2 SRLGLGCWQFGGGYWWGdqddeesiaTIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 82 TYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEYFpldgegnvipsdtnfvdtwEAMEELVDAGLVKAIGVSN 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETM-------------------EALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 162 FNHLQVEKILnKPGlkyKPAVNQIECHPYLTQ-EK-LIQYCQSKGIVVTAYSPL------GSPDRPWAKPED------PS 227
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlFR 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 228 LLEDP----------RIKAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19085 212 HFEPGaeeetfealeKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-286 |
5.45e-25 |
|
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: 101.83 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWK---SPPGKVTE-----AVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEKlkeqvvkREDLFIVSK 78
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDqesieAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 79 LWCTYHEK----------SMVKgAC---------------QktlsdlkldyldlylIHWPtgfkpgkeyfplDGegnvip 133
Cdd:cd19084 74 CGLRWDGGkgvtkdlspeSIRK-EVeqslrrlqtdyidlyQ---------------IHWP------------DP------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 134 sDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKIlnkpgLKY-KPAVNQIechPY--LTQ---EKLIQYCQSKGIVV 207
Cdd:cd19084 120 -NTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 208 TAYSPLG--------------SPD---------RPWAKPEDPSLLEdpRIKAIAAKHNKTTAQVLIRFPIQRNLV--VIP 262
Cdd:cd19084 191 LPYGPLAqglltgkykkeptfPPDdrrsrfpffRGENFEKNLEIVD--KLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIV 268
|
330 340
....*....|....*....|....
gi 2166761530 263 KSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19084 269 GAKNPEQLEENAGALDWELTEEEL 292
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-286 |
2.57e-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: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 16 VGLGTW-------KSPPGKVTE-----AVKIAIDLGYRHIDCAHVY---QNENEVGLAIQEKlkeqvvkREDLFIVSK-- 78
Cdd:cd19102 4 IGLGTWaiggggwGGGWGPQDDrdsiaAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 79 -LW------CTYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkeyfpldgegnvipsDTNFVDTWEAMEELVDA 151
Cdd:cd19102 77 lLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP-------------------DEPIEEAWGALAELKEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 152 GLVKAIGVSNFNHLQVEKIlnkpgLKYKP-AVNQIechPY--LTQE---KLIQYCQSKGIVVTAYSPLGS--------PD 217
Cdd:cd19102 138 GKVRAIGVSNFSVDQMKRC-----QAIHPiASLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmtPE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 218 RPWAKPED-----------PSLLEDPRI----KAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFDFE 280
Cdd:cd19102 210 RVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLR 289
|
....*.
gi 2166761530 281 LSSVDM 286
Cdd:cd19102 290 LTPEEL 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-215 |
1.97e-20 |
|
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: 87.96 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 16 VGLGTWK-SPPGKVTEAVKI---AIDLGYRHIDCAHVY---QNENEVGLAIQEKlkeqvVKREDLFIVSKLWCTYHEKSM 88
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALldaALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGDPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 89 VKGA-----------------------CQktlsdlkldyldlylIHWPtgfkpgkeyfpldgegnviPSDTNFVDTWEAM 145
Cdd:cd06660 78 RSRLspehirrdleeslrrlgtdyidlYY---------------LHRD-------------------DPSTPVEETLEAL 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 146 EELVDAGLVKAIGVSNFNHLQVEKILN--KPGLKYKPAVNQIE---CHPYLTQEKLIQYCQSKGIVVTAYSPLGS 215
Cdd:cd06660 124 NELVREGKIRYIGVSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-282 |
9.58e-20 |
|
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: 87.23 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 17 GLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVYQN---ENEVGlaiqEKLKEQVVKREDLFIVSKlwCtyhekSMVKGAC 93
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFG----EALALNPGLREKIEIQTK--C-----GIRLGDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 94 QKTlsdlkldyldlyliHWPTGFKPGKEYFPLDGEGNVIPSDTNFVD---------------TWEAMEELVDAGLVKAIG 158
Cdd:cd19092 84 PRP--------------GRIKHYDTSKEHILASVEGSLKRLGTDYLDllllhrpdplmdpeeVAEAFDELVKSGKVRYFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 159 VSNFNHLQVEkILNKpGLKYKPAVNQIEC---HPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwAKPEDPSLLEDPRIK 235
Cdd:cd19092 150 VSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGG-----GRLFGGFDERFQRLR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 236 A----IAAKHNKTTAQV----LIRFPIQrnLVVIPKSVTPERIAENFQVFDFELS 282
Cdd:cd19092 223 AaleeLAEEYGVTIEAIalawLLRHPAR--IQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
10-282 |
5.04e-17 |
|
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: 79.18 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAkMPIVGLGTWKSPPGKvTEAVKI---AIDLGYRHIDCAHVYqnenevGLAIQEKLKEQVVK--REDLFIVSKlwctyh 84
Cdd:cd19088 7 GA-MRLTGPGIWGPPADR-EEAIAVlrrALELGVNFIDTADSY------GPDVNERLIAEALHpyPDDVVIATK------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 85 eksmvkGACQKTLSDlkldyldlyliHWPTGFKPgkEYFPLDGEGN-------VIP--------SDTNFVDTWEAMEELV 149
Cdd:cd19088 73 ------GGLVRTGPG-----------WWGPDGSP--EYLRQAVEASlrrlgldRIDlyqlhridPKVPFEEQLGALAELQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 150 DAGLVKAIGVSNFNHLQVEKILNKPGLkykpAVNQIECHPYLTQ-EKLIQYCQSKGIVVTAYSPLGSpdRPWAKPEDPsl 228
Cdd:cd19088 134 DEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQPGGL-- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2166761530 229 ledprIKAIAAKHNKTTAQVLIRFPIQR--NLVVIPKSVTPERIAENFQVFDFELS 282
Cdd:cd19088 206 -----LAEVAARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
17-282 |
1.57e-16 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 78.27 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 17 GLGTWKSPPGKVTEAVKIAIDLGYRHIDCAHVY---QNENEVGLAiqekLKEQVVKREDLFIVSKlwctyheksmvkgaC 93
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEA----LKLSPSLREKIELQTK--------------C 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 94 QKTLSDLKLDYLDLY---------------------------LIHWPTgfkpgkeyfPLdgegnvipsdTNFVDTWEAME 146
Cdd:COG4989 84 GIRLPSEARDNRVKHydtskehiiasvegslrrlgtdyldllLLHRPD---------PL----------MDPEEVAEAFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 147 ELVDAGLVKAIGVSNFNHLQVEkILNKpGLKYKPAVNQIECHPYLTQ---EKLIQYCQSKGIVVTAYSPLGSPDrpWAKP 223
Cdd:COG4989 145 ELKASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGR--LFGG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2166761530 224 EDPsllEDPRIKA----IAAKHNKTTAQVLI----RFPIqrNLVVIPKSVTPERIAENFQVFDFELS 282
Cdd:COG4989 221 FDE---QFPRLRAaldeLAEKYGVSPEAIALawllRHPA--GIQPVIGTTNPERIKAAAAALDIELT 282
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
10-291 |
1.58e-14 |
|
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: 72.69 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWK----SPPGKVTEAVKI-----AIDLGYRHIDCAHVYQN---ENEVGLAIQeKLKEQVV--------- 68
Cdd:cd19149 8 GIEASVIGLGTWAigggPWWGGSDDNESIrtihaALDLGINLIDTAPAYGFghsEEIVGKAIK-GRRDKVVlatkcglrw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 69 --KREDLFIVSKLWCTYHE--KSMVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeyfplDGEgnvipsdTNFVDTWEA 144
Cdd:cd19149 87 drEGGSFFFVRDGVTVYKNlsPESIREEVEQSLKRLGTDYIDLYQTHWQ------------DVE-------TPIEETMEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 145 MEELVDAGLVKAIGVSNFNHLQVEKILNkpglKYKPAVNQIechPY-----LTQEKLIQYCQSKGIVVTAYSPLGS---- 215
Cdd:cd19149 148 LEELKRQGKIRAIGASNVSVEQIKEYVK----AGQLDIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYSPLEQgllt 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 216 ----PDR-----------PWAKPEDPS----LLEdpRIKAIAAKHNKTTAQVLIRFPIQR--NLVVIPKSVTPERIAENF 274
Cdd:cd19149 221 gkitPDRefdagdarsgiPWFSPENREkvlaLLE--KWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQAEENA 298
|
330
....*....|....*..
gi 2166761530 275 QVFDFELSSVDMTTLLS 291
Cdd:cd19149 299 KAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
32-291 |
3.72e-14 |
|
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: 71.68 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 32 VKIAIDLGYRHIDCAHVY---QNENEVGLAIQEKLKEQVV--------KREDLFIVSklwctyHEKSMVKGACQKTLSDL 100
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEYNRNEVViatkgahkFGGDGSVLN------NSPEFLRSAVEKSLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 101 KLDYLDLYLIHWPTGFKPGKEYFpldgegnvipsdtnfvdtwEAMEELVDAGLVKAIGVSNFNhLQVEKILNKPGlkykp 180
Cdd:cd19083 113 NTDYIDLYYIHFPDGETPKAEAV-------------------GALQELKDEGKIRAIGVSNFS-LEQLKEANKDG----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 181 AVNQIEcHPY-LTQ----EKLIQYCQSKGIVVTAYSPLGS-------------PDRPWAKpeDPSLLEDP---------- 232
Cdd:cd19083 168 YVDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLASgllagkytkdtkfPDNDLRN--DKPLFKGErfsenldkvd 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2166761530 233 RIKAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFDFELSSVDMTTLLS 291
Cdd:cd19083 245 KLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-289 |
3.35e-13 |
|
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: 68.76 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 8 YNGAKMPIVGLGTW---KSPPGKVT----EAVKI---AIDLGYRHIDCAHVYQN---ENEVGLAIQEklkeqVVKREDLF 74
Cdd:cd19079 7 NSGLKVSRLCLGCMsfgDPKWRPWVldeeESRPIikrALDLGINFFDTANVYSGgasEEILGRALKE-----FAPRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 75 IVSKLWCTYHEKSMVKG--------ACQKTLSDLKLDYLDLYLIHWptgfkpgkeyfpLDgegnvipSDTNFVDTWEAME 146
Cdd:cd19079 82 IATKVYFPMGDGPNGRGlsrkhimaEVDASLKRLGTDYIDLYQIHR------------WD-------YETPIEETLEALH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 147 ELVDAGLVKAIGVSNFNHLQVEKILN---KPGLKyKPAVNQiecHPY--LTQE---KLIQYCQSKGIVVTAYSPL----- 213
Cdd:cd19079 143 DVVKSGKVRYIGASSMYAWQFAKALHlaeKNGWT-KFVSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLargrl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 214 -----GSPDRPWAKPEDPSLLED----------PRIKAIAAKHNKTTAQVLIRFPIQRNLVVIP--KSVTPERIAENFQV 276
Cdd:cd19079 219 arpwgDTTERRRSTTDTAKLKYDyfteadkeivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAA 298
|
330
....*....|...
gi 2166761530 277 FDFELSSVDMTTL 289
Cdd:cd19079 299 LDIKLSEEEIKYL 311
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
134-289 |
4.31e-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: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 134 SDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILNKPglkYKPAVNQIEC-----HPyltQEKLIQYCQSKGIVVT 208
Cdd:cd19101 117 SDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 209 AYSP----------LGSPDRPWAKPEDPSLLEDPRI-----------------KAIAAKHNKTTAQVLIRFPIQRNLV-- 259
Cdd:cd19101 191 AYGTlaggllsekyLGVPEPTGPALETRSLQKYKLMidewggwdlfqellrtlKAIADKHGVSIANVAVRWVLDQPGVag 270
|
170 180 190
....*....|....*....|....*....|
gi 2166761530 260 VIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19101 271 VIVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
140-286 |
8.53e-13 |
|
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: 67.65 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 140 DTWEAMEELVDAGLVKAIGVSNFNHLQVEKILnkpglKYKP-AVNQIECHPyLTQEKL----IQYCQSKGIVVTAYSPL- 213
Cdd:cd19077 129 ETIKALKELVKEGKIRGIGLSEVSAETIRRAH-----AVHPiAAVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLg 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 214 -----GSPDRPWAKPEDPSLLEDPR---------------IKAIAAKHNKTTAQVLIRFPIQRN---LVVIPKSVTPERI 270
Cdd:cd19077 203 rglltGRIKSLADIPEGDFRRHLDRfngenfeknlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERV 282
|
170
....*....|....*.
gi 2166761530 271 AENFQVFDFELSSVDM 286
Cdd:cd19077 283 EENLKAANVELTDEEL 298
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
9-285 |
1.12e-12 |
|
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: 67.47 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 9 NGAKMPIVGLGT-----WKSPPGKVTEAVKI---AIDLGYRHIDCAHVYQ-NENEVGlaiqEKLKEQVVKREDLFIVSKL 79
Cdd:cd19144 9 NGPSVPALGFGAmglsaFYGPPKPDEERFAVldaAFELGCTFWDTADIYGdSEELIG----RWFKQNPGKREKIFLATKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 80 ----------WCTYHEKSMVKGACQKTLSDLKLDYLDLYLIHwptgfkpgkeyfPLDGEgnvIPSDTnfvdTWEAMEELV 149
Cdd:cd19144 85 gieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH------------RVDGK---TPIEK----TVAAMAELV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 150 DAGLVKAIGVSNfnhLQVEKILNKPGLKYKPAVnQIECHPYLT-----QEKLIQYCQSKGIVVTAYSPLG---------S 215
Cdd:cd19144 146 QEGKIKHIGLSE---CSAETLRRAHAVHPIAAV-QIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGrgfltgairS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 216 PD----------RPWAKPED-PSLLE--DpRIKAIAAKHNKTTAQVLIRFPIQR--NLVVIPKSVTPERIAENFQVFDFE 280
Cdd:cd19144 222 PDdfeegdfrrmAPRFQAENfPKNLElvD-KIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEENLGALKVK 300
|
....*
gi 2166761530 281 LSSVD 285
Cdd:cd19144 301 LTEEE 305
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
140-289 |
1.13e-11 |
|
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: 64.54 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 140 DTWEAMEELVDAGLVKAIGVSNFNHLQVEKILnkpGLKYKPAVNQIEC--------HPYLTQEKLIQYCQSKGIVVTAYS 211
Cdd:cd19081 132 ETLGALNDLIRQGKVRYIGASNYSAWRLQEAL---ELSRQHGLPRYVSlqpeynlvDRESFEGELLPLCREEGIGVIPYS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 212 PLGS--------PDRPWAK----PEDPSLLEDPR-------IKAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERI 270
Cdd:cd19081 209 PLAGgfltgkyrSEADLPGstrrGEAAKRYLNERglrildaLDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQL 288
|
170
....*....|....*....
gi 2166761530 271 AENFQVFDFELSSVDMTTL 289
Cdd:cd19081 289 EDLLAAAGLRLTDEEVARL 307
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-273 |
2.06e-11 |
|
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: 63.02 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 14 PIVGLGTWKS--PPGKVTE--AVKI---AIDLGYRHIDCAHVYQN-ENEVGLAIQEklkeqvVKREDLFIVSKLWCTYhe 85
Cdd:cd19095 1 SVLGLGTSGIgrVWGVPSEaeAARLlntALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 ksmvkgacqktlsdlkldyldlylihwpTGFKPGKEYFPLDGEGNVI-------------------PSDTNFVDTWEAME 146
Cdd:cd19095 73 ----------------------------EGGRDRKDFSPAAIRASIErslrrlgtdyidllqlhgpSDDELTGEVLETLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 147 ELVDAGLVKAIGVSNFNHLqVEKILNKPGLkykpAVNQIechPY----LTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAK 222
Cdd:cd19095 125 DLKAAGKVRYIGVSGDGEE-LEAAIASGVF----DVVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRV 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 223 PEDPSLLEDPRIKAIAAKHN-KTTAQVLIRFPIQRNLV--VIPKSVTPERIAEN 273
Cdd:cd19095 197 RRRPLYADYARRPEFAAEIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
35-286 |
5.20e-11 |
|
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: 62.23 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 35 AIDLGYRHIDCAHVY-QNENE--VGLAIQEKlkeqvvkREDLFIVSKlwctyheksmvkgacqktlsdlkldyldlylih 111
Cdd:cd19076 41 ALELGVTFLDTADMYgPGTNEelLGKALKDR-------RDEVVIATK--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 112 WPTGFKPGKEYFPLDGE-GNV-----------------------IPSDTNFVDTWEAMEELVDAGLVKAIGVSNFN---- 163
Cdd:cd19076 81 FGIVRDPGSGFRGVDGRpEYVraaceaslkrlgtdvidlyyqhrVDPNVPIEETVGAMAELVEEGKVRYIGLSEASadti 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 164 ------H----LQVEkilnkpglkYKPAVNQIEchpyltqEKLIQYCQSKGIVVTAYSPL------GSPDRPWAKPEDPS 227
Cdd:cd19076 161 rrahavHpitaVQSE---------YSLWTRDIE-------DEVLPTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDF 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2166761530 228 LLEDPR---------------IKAIAAKHNKTTAQVLIRFPIQR--NLVVIPKSVTPERIAENFQVFDFELSSVDM 286
Cdd:cd19076 225 RRNNPRfqgenfdknlklvekLEAIAAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVGALDVVLTPEEL 300
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-213 |
2.34e-10 |
|
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: 60.40 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 16 VGLGTWK--------SPPGKVTEAVKIAIDLGYRHIDCAHVY---QNENEVGLAIqeklkEQVVKREDLFIVSKLWCTYH 84
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATKVGLEWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 85 EKSMVKGACQKTLSDLKLDYLDL---------YLIHWPTgfkpgkeyfpldgegnvipSDTNFVDTWEAMEELVDAGLVK 155
Cdd:cd19148 82 EGGEVVRNSSPARIRKEVEDSLRrlqtdyidlYQVHWPD-------------------PLVPIEETAEALKELLDEGKIR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2166761530 156 AIGVSNFNHLQVEKILNKPGLkykpAVNQIechPY-----LTQEKLIQYCQSKGIVVTAYSPL 213
Cdd:cd19148 143 AIGVSNFSPEQMETFRKVAPL----HTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
135-273 |
3.50e-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: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 135 DTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEK---ILNKPGLKYKPAVNQIecHPYL--------------TQEkLI 197
Cdd:cd19752 124 DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGWAEFSAIQQR--HSYLrprpgadfgvqrivTDE-LL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 198 QYCQSKG-IVVTAYSPL--GSPDRPWAKPEDPSLLEDPR-----IKAIAAKHNKTTAQVLIRFPIQRNLVVIP--KSVTP 267
Cdd:cd19752 201 DYASSRPdLTLLAYSPLlsGAYTRPDRPLPEQYDGPDSDarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTV 280
|
....*.
gi 2166761530 268 ERIAEN 273
Cdd:cd19752 281 EQLEEN 286
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-226 |
9.62e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 57.88 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWKSPPGKVTEAVKI---AIDLGYRHIDCAHVYQN-ENEVGLAIQEKlkeqvvkREDLFIVSKLWCTyhe 85
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAAIirrALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 ksMVKGA------------------CQktlsdlkldyldlylIHwptGFKPGKEYFPLDGEGNVIpsdtnfvdtwEAMEE 147
Cdd:cd19100 78 --DYEGAkrdlerslkrlgtdyidlYQ---------------LH---AVDTEEDLDQVFGPGGAL----------EALLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 148 LVDAGLVKAIGVSNFNHLQVEKILNKPG----LkykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKP 223
Cdd:cd19100 128 AKEEGKIRFIGISGHSPEVLLRALETGEfdvvL---FPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDP 204
|
...
gi 2166761530 224 EDP 226
Cdd:cd19100 205 LDP 207
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-276 |
9.83e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 57.98 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTwKSPPGKVTEAVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEklkeqvVKREDLFIVSKlwctyhek 86
Cdd:cd19105 10 GLKVSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATK-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 smvkgacqktlsdlkldyldlylIHWPTGFKPGKE-------------------YFPLDGEGnviPSDTNFVDTW-EAME 146
Cdd:cd19105 75 -----------------------ASPRLDKKDKAEllksveeslkrlqtdyidiYQLHGVDT---PEERLLNEELlEALE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 147 ELVDAGLVKAIGVS---NFNHLqVEKILNKPG-----LKYKPAvnqiecHPYLTQEKLIQYCQSKGIVVTAYSPLGS-PD 217
Cdd:cd19105 129 KLKKEGKVRFIGFSthdNMAEV-LQAAIESGWfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGgYL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2166761530 218 RPWAKPEDPSLLEDPrikaiaakhnkttAQVLIRFPIQRNLV--VIPKSVTPERIAENFQV 276
Cdd:cd19105 202 QPALLSVLKAKGFSL-------------PQAALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-273 |
2.50e-09 |
|
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: 56.72 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 16 VGLGTW--------KSPPGKVTEAVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEKlkeqvvkREDLFIVSKLWCTYH 84
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 85 EKSmvkgacqktlsdlkldyldlyliHWPTGFKP--------------GKEYfpLD------GEGNVIPSDtnfvDTWEA 144
Cdd:cd19086 79 GGP-----------------------ERPQDFSPeyireaveaslkrlGTDY--IDlyqlhnPPDEVLDND----ELFEA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 145 MEELVDAGLVKAIGVSNFNHLQVEKILNKPGLKykpAV----NQIECHPYltqEKLIQYCQSKGIVVTAYSPLGSpdrpw 220
Cdd:cd19086 130 LEKLKQEGKIRAYGVSVGDPEEALAALRRGGID---VVqviyNLLDQRPE---EELFPLAEEHGVGVIARVPLAS----- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2166761530 221 akpedpSLLEDprikaiaakhnkTTAQVLIRFPIQRNLV--VIPKSVTPERIAEN 273
Cdd:cd19086 199 ------GLLTG------------KLAQAALRFILSHPAVstVIPGARSPEQVEEN 235
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
109-282 |
8.46e-09 |
|
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: 56.03 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 109 LIHWP---TGFKPGKEYFPLDGEGNVIPsdtnFVDTWEAMEELVDAGLVKAIGVSN------FNHLQVEKILNKPglkyK 179
Cdd:cd19094 118 QLHWPdryTPLFGGGYYTEPSEEEDSVS----FEEQLEALGELVKAGKIRHIGLSNetpwgvMKFLELAEQLGLP----R 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 180 PAVNQiecHPY--LTQ---EKLIQYCQSKGIVVTAYSPLG----------SPDRpwakPEDPSLLEDPRI---------- 234
Cdd:cd19094 190 IVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAAR----PEGGRLNLFPGYmaryrspqal 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2166761530 235 ------KAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFDFELS 282
Cdd:cd19094 263 eavaeyVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLS 318
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
10-289 |
8.79e-09 |
|
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: 55.70 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGT--------WKSPPGKVTEA-----VKIAIDLGYRHIDCAHVY---QNENEVGLAIQEKlkeqvvkREDL 73
Cdd:cd19091 10 GLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 74 FIVSKLwctyhekSMVKG---------------ACQKTLSDLKLDYLDLYLIHWPTGFKPGKEyfpldgegnvipsdtnf 138
Cdd:cd19091 83 LIATKV-------RGRMGegpndvglsrhhiirAVEASLKRLGTDYIDLYQLHGFDALTPLEE----------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 139 vdTWEAMEELVDAGLVKAIGVSNFNHLQVEKIL---NKPGL--------KYKPAVNQIEchpyltQEkLIQYCQSKGIVV 207
Cdd:cd19091 139 --TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLarfvalqaYYSLLGRDLE------HE-LMPLALDQGVGL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 208 TAYSPLG--------SPDRPwaKPEDPSL---------LEDPRI-------KAIAAKHNKTTAQVLIRFPIQRNLV--VI 261
Cdd:cd19091 210 LVWSPLAggllsgkyRRGQP--APEGSRLrrtgfdfppVDRERGydvvdalREIAKETGATPAQVALAWLLSRPTVssVI 287
|
330 340
....*....|....*....|....*...
gi 2166761530 262 PKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19091 288 IGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-283 |
6.38e-08 |
|
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: 52.98 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 10 GAKMPIVGLGTWKSPPGKVT-----EAVKIAIDLGYRHIDCAHVY---QNENEVGLAIQEklkeqvVKREDLFIVSKL-W 80
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDdedakACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKVfW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 81 CTYHE--------KSMVKGaCQKTLSDLKLDYLDLYLIHwptGFKPgkeyfpldgegnvipsDTNFVDTWEAMEELVDAG 152
Cdd:cd19074 75 PTGPGpndrglsrKHIFES-IHASLKRLQLDYVDIYYCH---RYDP----------------ETPLEETVRAMDDLIRQG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 153 LVKAIGVSNFNHLQVEKILN--KPGLKYKPAVNQIECHpYLTQEK---LIQYCQSKGIVVTAYSPLGS------------ 215
Cdd:cd19074 135 KILYWGTSEWSAEQIAEAHDlaRQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQglltgkyrdgip 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 216 -PDRPWAKPEDP-----SLLEDPRI------KAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFDFEL 281
Cdd:cd19074 214 pPSRSRATDEDNrdkkrRLLTDENLekvkklKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKL 293
|
..
gi 2166761530 282 SS 283
Cdd:cd19074 294 SP 295
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-252 |
7.71e-08 |
|
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: 53.09 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 16 VGLGTWKSPPGKVT-----EAVKIAIDLGYRHIDCAHVYQN---ENEVGLAIQEKLKEQVVKREDLFIVSKL-WCTYHEK 86
Cdd:cd19099 6 LGLGTYRGDSDDETdeeyrEALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgYIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 87 SMVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK--------------------------EYFPLDGEGNVipsDTNFVD 140
Cdd:cd19099 86 EPLRPLKYLEEKLGRGLIDVADSAGLRHCISPAYledqierslkrlgldtidlyllhnpeEQLLELGEEEF---YDRLEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 141 TWEAMEELVDAGLVKAIGVSNFN----------HLQVEKIL--------NKPGLKYkpaVnQIECHPYLTQ--------- 193
Cdd:cd19099 163 AFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKV---I-QLPLNLLEPEaltekntvk 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 194 ---EKLIQYCQSKGIVVTAYSPL--GSPDRPWAKPEDPSLLEDprikaiaakhnKTTAQVLIRF 252
Cdd:cd19099 239 geaLSLLEAAKELGLGVIASRPLnqGQLLGELRLADLLALPGG-----------ATLAQRALQF 291
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-282 |
3.88e-07 |
|
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: 50.63 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 14 PIVGLGT--WKSPPGKVT-----EAVKIAIDLGYRHIDCAHVYQN-ENEVGLAIQEklkeqvVKREDLFIVSKLwCTYHE 85
Cdd:cd19090 1 SALGLGTagLGGVFGGVDddeavATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 86 ksmvkgacqktlsdlkldyldlylihWPTGFKP--------------GKEYFPL----DgegnviPSDTNFVD------T 141
Cdd:cd19090 74 --------------------------DTADYSAdrvrrsveeslerlGRDRIDLlmihD------PERVPWVDilapggA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 142 WEAMEELVDAGLVKAIGVSnfnhlqvekiLNKPGLkYKPAV--NQIEC----HPY--LTQE---KLIQYCQSKGIVVTAY 210
Cdd:cd19090 122 LEALLELKEEGLIKHIGLG----------GGPPDL-LRRAIetGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 211 SPLGS-------PDRPWAKPEDPSLLEDPR---IKAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFD 278
Cdd:cd19090 191 SPLGMgllagrpPERVRYTYRWLSPELLDRakrLYELCDEHGVPLPALALRFLLRDPRIstVLVGASSPEELEQNVAAAE 270
|
....
gi 2166761530 279 FELS 282
Cdd:cd19090 271 GPLP 274
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
134-236 |
5.37e-07 |
|
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: 50.26 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 134 SDTNFVDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILN---KPGL--------KYKPAVNQIECHpyltqekLIQYCQS 202
Cdd:cd19087 123 RDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGLlrfvseqpMYNLLKRQAELE-------ILPAARA 195
|
90 100 110
....*....|....*....|....*....|....*....
gi 2166761530 203 KGIVVTAYSPLGS-----PDRPWAKPEDPSLLEDPRIKA 236
Cdd:cd19087 196 YGLGVIPYSPLAGglltgKYGKGKRPESGRLVERARYQA 234
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-289 |
9.81e-06 |
|
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: 46.56 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 12 KMPIVGLGTWK----SPPGKVT-----------EAVKIAIDLGYRHIDCAHVYqnenevGLAIQEKLKEQVVK---REDL 73
Cdd:cd19103 3 KLPKIALGTWSwgsgGAGGDQVfgnhldedtlkAVFDKAMAAGLNLWDTAAVY------GMGASEKILGEFLKrypREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 74 FIVSKL--WCTYHEKSMVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeyfplDGEGN---VIPsdtnfvdtweameeL 148
Cdd:cd19103 77 IISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPA-----------DVERWtpeLIP--------------L 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 149 VDAGLVKAIGVSNFNHLQVEK---ILNKPGLKykpaVNQIECH---PYLTQEK--LIQYCQSKGIVVTAYSPL------G 214
Cdd:cd19103 132 LKSGKVKHVGVSNHNLAEIKRaneILAKAGVS----LSAVQNHyslLYRSSEEagILDYCKENGITFFAYMVLeqgalsG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 215 SPDRPWAKPEDPSLLED-----PRIKA-------IAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFQVFDFELS 282
Cdd:cd19103 208 KYDTKHPLPEGSGRAETynpllPQLEEltavmaeIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLT 287
|
....*..
gi 2166761530 283 SVDMTTL 289
Cdd:cd19103 288 DDEIKEL 294
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
143-278 |
1.53e-05 |
|
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: 45.62 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 143 EAMEELVDAGLVKAIGVSNFNH---LQVEKILNKPGLkYKPAVNQI---------ECHPYLT----QEKLIQYCQSKGIV 206
Cdd:cd19082 125 DTLNELVRAGKIRAFGASNWSTeriAEANAYAKAHGL-PGFAASSPqwslarpnePPWPGPTlvamDEEMRAWHEENQLP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 207 VTAYSPLGS---PDRpwAKPEDPSLLEDP-------------RIKAIAAKHNKTTAQVLIRFPIQRNLVVIP--KSVTPE 268
Cdd:cd19082 204 VFAYSSQARgffSKR--AAGGAEDDSELRrvyyseenferleRAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPE 281
|
170
....*....|
gi 2166761530 269 RIAENFQVFD 278
Cdd:cd19082 282 QLRDSLAAAD 291
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
140-274 |
2.43e-05 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; 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: 381388 [Multi-domain] Cd Length: 290 Bit Score: 45.04 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 140 DTWEAMEELVDAGLVKAIGVSNFNHLQVEKILNKPGLKykpAVNQIECHPYLTQE---KLIQYCQSKGIVVTAYSPLGS- 215
Cdd:cd19162 129 DAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVD---VVMVAGRYTLLDRRaatELLPLCAAKGVAVVAAGVFNSg 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2166761530 216 --------PDRPWAKPEDPSLLEDP-RIKAIAAKHNKTTAQVLIRFPIQRNLVVipkSV-----TPERIAENF 274
Cdd:cd19162 206 ilatddpaGDRYDYRPATPEVLARArRLAAVCRRYGVPLPAAALQFPLRHPAVA---SVvvgaaSPAELRDNL 275
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
144-283 |
4.97e-05 |
|
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: 44.14 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 144 AMEELVDAGLVKAIGVSnFNHLQV-EKILNKPGLKYKPAVNQiechpY--LTQE---KLIQYCQSKGIVVTAYSPLGS-- 215
Cdd:cd19152 152 ALEELREEGVIKAIGLG-VNDWEViLRILEEADLDWVMLAGR-----YtlLDHSaarELLPECEKRGVKVVNAGPFNSgf 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166761530 216 ------PDRPWAKPEDPSLLE--DpRIKAIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFQVFDFELSS 283
Cdd:cd19152 226 laggdnFDYYEYGPAPPELIArrD-RIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALLATEIPA 302
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-252 |
9.42e-05 |
|
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: 43.28 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 26 GKV--TEAVKI---AIDLGYRHIDCAHVYqnenevGLAiQEKLKEQVVKREDLFIVSKL-----WCTYHEKSMVKgACQK 95
Cdd:cd19097 21 GKPseKEAKKIleyALKAGINTLDTAPAY------GDS-EKVLGKFLKRLDKFKIITKLpplkeDKKEDEAAIEA-SVEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 96 TLSDLKLDYLDLYLIHWPtgfkpgkEYFPLDGEgnvipsdtnfvDTWEAMEELVDAGLVKAIGVSNFNHLQVEKILNkpg 175
Cdd:cd19097 93 SLKRLKVDSLDGLLLHNP-------DDLLKHGG-----------KLVEALLELKKEGLIRKIGVSVYSPEELEKALE--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 176 lKYKPAVNQIechPY------LTQEKLIQYCQSKGIVVTAYSP------LGSPDRPWAKPED-PSLLEdpRIKAIAAKHN 242
Cdd:cd19097 152 -SFKIDIIQL---PFnildqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPaKPLLK--KLHELAKKLG 225
|
250
....*....|
gi 2166761530 243 KTTAQVLIRF 252
Cdd:cd19097 226 LSPLELALGF 235
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
144-289 |
1.36e-04 |
|
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: 42.98 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 144 AMEELVDAGLVKAIGVSNFNHLQVEK---ILNKPGLKyKPAVNQIECHpyLTQ----EKLIQYCQSKGIVVTAYSPLGS- 215
Cdd:cd19080 135 ALDDLVRAGKVLYVGISDTPAWVVARantLAELRGWS-PFVALQIEYS--LLErtpeRELLPMARALGLGVTPWSPLGGg 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 216 -----------------PDRPWAKPEdpsllEDPR-------IKAIAAKHNKTTAQVLIRFPIQRNLVVIP--KSVTPER 269
Cdd:cd19080 212 lltgkyqrgeegrageaKGVTVGFGK-----LTERnwaivdvVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQ 286
|
170 180
....*....|....*....|
gi 2166761530 270 IAENFQVFDFELSSVDMTTL 289
Cdd:cd19080 287 LKDNLGALDLTLSPEQLARL 306
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-237 |
1.81e-04 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 42.88 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 9 NGAKMPIVGLGTW---KSPPGKVTEAVKIAIDLGYRHIDCAHVY-QNENEVGLAIQEKlkeqvvkREDLFIVSKL--WC- 81
Cdd:COG1453 9 TGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLppWVr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 82 ------TYHEKSMVKgaCQktlsdlkldyldLYLIH-------WPTGFKPGkeyfpldgegnvipsdtnfvDTWEAMEEL 148
Cdd:COG1453 82 dpedmrKDLEESLKR--LQtdy-------idLYLIHglnteedLEKVLKPG--------------------GALEALEKA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 149 VDAGLVKAIGVSNFNHLQV-EKILNkpglKYKPAVNQIECHPYLTQ----EKLIQYCQSKGIVVTAYSPLG-------SP 216
Cdd:COG1453 133 KAEGKIRHIGFSTHGSLEViKEAID----TGDFDFVQLQYNYLDQDnqagEEALEAAAEKGIGVIIMKPLKggrlanpPE 208
|
250 260
....*....|....*....|....*....
gi 2166761530 217 D--RPWAKPEDPS------LLEDPRIKAI 237
Cdd:COG1453 209 KlvELLCPPLSPAewalrfLLSHPEVTTV 237
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
140-252 |
3.84e-04 |
|
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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 41.48 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 140 DTWEAMEELVDAGLVKAIGVSNFNHLQVEKIL---NKPG--------LKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVT 208
Cdd:cd19104 142 GVADAFERLRSEGKIRFIGITGLGNPPAIRELldsGKFDavqvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVM 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2166761530 209 AYSPL------GSPDRPwakPEDPSLLEDP---------RIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19104 222 GIRVLaagaltTSLDRG---REAPPTSDSDvaidfrraaAFRALAREWGETLAQLAHRF 277
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
143-289 |
5.59e-04 |
|
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: 41.06 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 143 EAMEELVDAGLVKAIGVSNFNhlqVEKIlnKPGLKYKP--AVnQIECH-----PyltQEKLIQYCQSKGIVVTAYSPLGS 215
Cdd:cd19078 130 GTMKELIKEGKIRHWGLSEAG---VETI--RRAHAVCPvtAV-QSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 216 --------PDRPWAKPEDPSLLedPR---------------IKAIAAKHNKTTAQV-----LIRFPiqrNLVVIPKSVTP 267
Cdd:cd19078 201 gfltgkidENTKFDEGDDRASL--PRftpealeanqalvdlLKEFAEEKGATPAQIalawlLAKKP---WIVPIPGTTKL 275
|
170 180
....*....|....*....|..
gi 2166761530 268 ERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19078 276 SRLEENIGAADIELTPEELREI 297
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
17-289 |
1.93e-03 |
|
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: 39.34 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 17 GLGTWKSPPGKVTEAVKI---AIDLGYRHIDCAHVY-QNENEV--GLAIQEKLKEQVVkredlfIVSKLWCTYHEKS--- 87
Cdd:cd19145 21 GLSGDYGAPKPEEEGIALihhAFNSGVTFLDTSDIYgPNTNEVllGKALKDGPREKVQ------LATKFGIHEIGGSgve 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 88 ------MVKGACQKTLSDLKLDYLDLYLIHwptgfkpgkeyfpldgegnVIPSDTNFVDTWEAMEELVDAGLVKAIGVSn 161
Cdd:cd19145 95 vrgdpaYVRAACEASLKRLDVDYIDLYYQH-------------------RIDTTVPIEITMGELKKLVEEGKIKYIGLS- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 162 fnHLQVEKILNKPGLKYKPAVnQIECHPYL--TQEKLIQYCQSKGIVVTAYSPLGspdRP--WAKPEDPSLLED------ 231
Cdd:cd19145 155 --EASADTIRRAHAVHPITAV-QLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---RGffAGKAKLEELLENsdvrks 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2166761530 232 -PR---------------IKAIAAKHNKTTAQVLIRFPIQR--NLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:cd19145 229 hPRfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
143-289 |
2.82e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 38.80 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 143 EAMEELVDAGLVKAIGVSNFNHLQVEKilnkpGLKYKPAVNqIECHPYLTQ---EKLIQYCQSKGIVVTAYSPLG--SPd 217
Cdd:PRK10376 148 TVLAELQRQGLVRHIGLSNVTPTQVAE-----ARKIAEIVC-VQNHYNLAHradDALIDALARDGIAYVPFFPLGgfTP- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2166761530 218 rpwakpedpslLEDPRIKAIAAKHNKTTAQVLIRFPIQR--NLVVIPKSVTPERIAENFQVFDFELSSVDMTTL 289
Cdd:PRK10376 221 -----------LQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
140-240 |
4.12e-03 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; 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(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 38.30 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166761530 140 DTWEAMEELVDAGLVKAIGVSNFN-HLQVEKILNKPG-----LKYkpavnqieCHPYL---TQEKLIQYCQSKGIVVTAY 210
Cdd:cd19163 137 ETLPALQKLKEEGKVRFIGITGYPlDVLKEVLERSPVkidtvLSY--------CHYTLndtSLLELLPFFKEKGVGVINA 208
|
90 100 110
....*....|....*....|....*....|....*...
gi 2166761530 211 SPLG------SPDRPW--AKPEdpslledprIKAIAAK 240
Cdd:cd19163 209 SPLSmgllteRGPPDWhpASPE---------IKEACAK 237
|
|
| |
