|
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 ... |
10-247 |
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: 528.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 10 KAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 90 RKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEK 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615415 170 LLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQ 238
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-247 |
5.04e-133 |
|
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: 379.04 E-value: 5.04e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 7 LSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQE-KAVKREDLFIVSKLWPTFFE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 86 RPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHF 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 166 QIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTA 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
..
gi 2462615415 246 AQ 247
Cdd:cd19106 239 AQ 240
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-247 |
9.86e-124 |
|
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: 355.38 E-value: 9.86e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 3 TFVELSTKAKMPIVGLGTWKS---PLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKL 79
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGV 159
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIA 238
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALA 240
|
....*....
gi 2462615415 239 AKHKKTAAQ 247
Cdd:cd19108 241 KKHKRTPAL 249
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-247 |
1.68e-117 |
|
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: 339.24 E-value: 1.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRK 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 AFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 172 NKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwAKPEDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQ 232
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-247 |
1.55e-113 |
|
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: 327.52 E-value: 1.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqekaVKREDLFIVSKLWPTFFERPLVRKA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPQGFKSGDDlfpkddkgnaiggKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGGS-------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615415 173 KPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQ 208
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-247 |
5.30e-108 |
|
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: 315.59 E-value: 5.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTW----KSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPL 88
Cdd:cd19109 4 IPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 89 VRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIE 168
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 169 KLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19109 164 LILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKTAAQ 243
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-247 |
1.81e-107 |
|
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: 313.58 E-value: 1.81e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 1 MATFvELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLW 80
Cdd:cd19123 1 MKTL-PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 81 PTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFK-------SGDDLFPKDDKGNAiggkatflDAWEAMEELVDEGL 153
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKkgvgfpeSGEDLLSLSPIPLE--------DTWRAMEELVDKGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 154 VKALGVSNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWA-KPED-PSLLED 231
Cdd:cd19123 152 CRHIGVSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLED 229
|
250
....*....|....*.
gi 2462615415 232 PKIKEIAAKHKKTAAQ 247
Cdd:cd19123 230 PVINKIAEKHGASPAQ 245
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-247 |
4.98e-106 |
|
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: 309.98 E-value: 4.98e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKS-PLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVR 90
Cdd:cd19116 10 EIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 91 KAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDlfpKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKL 170
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615415 171 LNkpGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSlLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19116 167 LS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPR-LDDPTLVAIAKKYGKTTAQ 240
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-247 |
3.47e-101 |
|
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: 297.33 E-value: 3.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 3 TFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPT 82
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 FFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDK-GNAIGGkatfldAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVlPPDIPS------TWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 162 FSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEdpsLLEDPKIKEIAAKH 241
Cdd:cd19125 155 FSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKL 229
|
....*.
gi 2462615415 242 KKTAAQ 247
Cdd:cd19125 230 GKTPAQ 235
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-247 |
4.88e-100 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 293.50 E-value: 4.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 11 AKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTFFERPLVR 90
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEA----IAASGVPREELFVTTKVWNDNHGYDDTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 91 KAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaigGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKL 170
Cdd:COG0656 79 AAFEESLERLGLDYLDLYLIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615415 171 LNKPGlkYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKHKKTAAQ 247
Cdd:COG0656 139 LAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQ 203
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-247 |
4.93e-96 |
|
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: 285.07 E-value: 4.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 2 ATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWP 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 82 TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 162 FSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPED-----PSLLEDPKIKE 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250
....*....|.
gi 2462615415 237 IAAKHKKTAAQ 247
Cdd:cd19154 239 IAEKHGKTPAQ 249
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-247 |
2.11e-90 |
|
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: 270.05 E-value: 2.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 7 LSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEK-AVKREDLFIVSKLWPTFFE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 86 RPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPK----DDKGN-AIGGKATFLDAWEAMEELVDEGLVKALGVS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEvDLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 161 NFSHFQIEKLLNKPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwAKPEDPSLLEDPKIKEIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
....*..
gi 2462615415 241 HKKTAAQ 247
Cdd:cd19118 234 LGKTPAQ 240
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-247 |
5.53e-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: 263.61 E-value: 5.53e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 14 PIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKAF 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 94 EKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462615415 174 pgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKpedpSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQ 229
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-247 |
2.32e-84 |
|
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: 254.73 E-value: 2.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRK 91
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 AFEKTLKDLKLSYLDVYLIHWPQGFKSgddlfpKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 171
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKIL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615415 172 NKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRP--WAKPEDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19111 157 AYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-247 |
3.01e-82 |
|
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: 250.14 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 4 FVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTF 83
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKS-GDDLFPKDDKGNAIGGKAT-FLDAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSkEDDSGKLDPTGEHKQDYTTdLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 162 FSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKP-------EDPSLLEDPKI 234
Cdd:cd19155 163 FNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250
....*....|...
gi 2462615415 235 KEIAAKHKKTAAQ 247
Cdd:cd19155 241 KAIAERHGKSPAQ 253
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-247 |
1.69e-81 |
|
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: 247.41 E-value: 1.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 7 LSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPTFFER 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDS----GVPREEIFITTKLWCTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 87 PlvRKAFEKTLKDLKLSYLDVYLIHWPQGFKSG--DDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSH 164
Cdd:cd19117 84 V--EEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 165 FQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHKKT 244
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKT 233
|
...
gi 2462615415 245 AAQ 247
Cdd:cd19117 234 PAQ 236
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-247 |
4.30e-80 |
|
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: 242.92 E-value: 4.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKspLGKVKEAVKV---AIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLV 89
Cdd:cd19136 1 MPILGLGTFR--LRGEEEVRQAvdaALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 90 RKAFEKTLKDLKLSYLDVYLIHWP--QGFKSgddlfpkDDKGNAIGGKATfldaWEAMEELVDEGLVKALGVSNFSHFQI 167
Cdd:cd19136 79 RAACLGSLERLGTDYLDLYLIHWPgvQGLKP-------SDPRNAELRRES----WRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 168 EKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpeDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19136 148 EELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--------DLRLLEDPTVLAIAKKYGRTPAQ 217
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
2-241 |
5.92e-77 |
|
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: 235.50 E-value: 5.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 2 ATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqEKAVKREDLFIVSKLWP 81
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 82 TFFERPlvRKAFEKTLKDLKLSYLDVYLIHWPQGF--KSGDDLFPKDDKGN-AIGGKATFLDAWEAMEELVDEGLVKALG 158
Cdd:cd19121 80 TYHRRV--ELCLDRSLKSLGLDYVDLYLVHWPVLLnpNGNHDLFPTLPDGSrDLDWDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 159 VSNFSHFQIEKLLnkPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIA 238
Cdd:cd19121 158 VSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIA 227
|
...
gi 2462615415 239 AKH 241
Cdd:cd19121 228 KKH 230
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-247 |
2.91e-76 |
|
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: 233.70 E-value: 2.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 11 AKMPIVGLGTWKSPLGK--VKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVK-REDLFIVSKLWPTFFERP 87
Cdd:cd19124 3 QTMPVIGMGTASDPPSPedIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 88 LVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSG--------DDLFPKDDKGnaiggkatfldAWEAMEELVDEGLVKALGV 159
Cdd:cd19124 83 LVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGkfsfpieeEDFLPFDIKG-----------VWEAMEECQRLGLTKAIGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAkpeDPSLLEDPKIKEIAA 239
Cdd:cd19124 152 SNFSCKKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKEIAA 226
|
....*...
gi 2462615415 240 KHKKTAAQ 247
Cdd:cd19124 227 AKGKTVAQ 234
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-247 |
3.33e-74 |
|
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: 229.64 E-value: 3.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFF 84
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFK--SGDDLFPKD----DKGNAIGGKATFLDAWEAMEELVDEGLVKALG 158
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPGfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 159 VSNFSHFQIEKLLNkpGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-----DRPWAKpEDPSLLEDPK 233
Cdd:cd19113 163 VSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLFEHDT 239
|
250
....*....|....
gi 2462615415 234 IKEIAAKHKKTAAQ 247
Cdd:cd19113 240 IKSIAAKHNKTPAQ 253
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-247 |
5.99e-74 |
|
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: 228.50 E-value: 5.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKA 92
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKA-TFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 171
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 172 NKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19129 166 EAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME-------PKLLEDPVITAIARRVNKTPAQ 232
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-247 |
5.43e-73 |
|
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: 226.53 E-value: 5.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 1 MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 81 PTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDL--FP---KDDKGNAIGGKATFLDAWEAMEELVDEGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAvrYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 156 ALGVSNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGsP------DRPWAKpEDPSLL 229
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250
....*....|....*...
gi 2462615415 230 EDPKIKEIAAKHKKTAAQ 247
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQ 254
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-247 |
1.09e-72 |
|
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: 223.30 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPTFFERPLVRKA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPQgfksgddlfPKDDKGNAIGgkatfldaweAMEELVDEGLVKALGVSNFSHFQIEKLLN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN---------PTVPLEETLG----------ALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615415 173 KPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLgspdrpwAKPEdpsLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19073 138 ISPL--PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQ 200
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-247 |
1.88e-72 |
|
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: 223.42 E-value: 1.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 4 FVELSTKAKMPIVGLGTWKSPLGK-VKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqekaVKREDLFIVSKLWPT 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG----IPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 --FFERPLvrKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaigGKATFLDAWEAMEELVDEGLVKALGVS 160
Cdd:cd19157 77 dqGYDSTL--KAFEASLERLGLDYLDLYLIHWP--------------------VKGKYKETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 161 NFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAK 240
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEK 202
|
....*..
gi 2462615415 241 HKKTAAQ 247
Cdd:cd19157 203 YNKSVAQ 209
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-241 |
3.89e-72 |
|
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: 223.53 E-value: 3.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWkSP---LGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWP 81
Cdd:cd19119 4 FKLNTGASIPALGLGTA-SPhedRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 82 TFFERplVRKAFEKTLKDLKLSYLDVYLIHWPQGFK-----SGDDLFPKDDKGNAIGGKAT-FLDAWEAMEELVDEGLVK 155
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASGdHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 156 ALGVSNFSHFQIEKLLNKpgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIK 235
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVK 230
|
....*.
gi 2462615415 236 EIAAKH 241
Cdd:cd19119 231 KIAEKY 236
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-247 |
5.41e-72 |
|
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: 221.93 E-value: 5.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLG-KVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPTF 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES----GVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaigGKATFLDAWEAMEELVDEGLVKALGVSNFS 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWP--------------------GKDKFIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 164 HFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpedPSLLEDPKIKEIAAKHKK 243
Cdd:cd19126 137 EHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQ----------GGLLSNPVLAAIGEKYGK 204
|
....
gi 2462615415 244 TAAQ 247
Cdd:cd19126 205 SAAQ 208
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-247 |
1.55e-71 |
|
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: 222.75 E-value: 1.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTff 84
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFK-SG---DDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVS 160
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKhTGvgtTGSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 161 NFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLG--SPDRPWAKPEDPslLEDPKIKEIA 238
Cdd:cd19112 161 NYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDLA 236
|
....*....
gi 2462615415 239 AKHKKTAAQ 247
Cdd:cd19112 237 KKYGKSAAQ 245
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-247 |
1.69e-71 |
|
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: 220.71 E-value: 1.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTFF 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKA----IRASGVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfksgddlfPKDDKgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSH 164
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPV---------PAQDK---------YVETWKALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 165 FQIEKLLNKPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpedPSLLEDPKIKEIAAKHKKT 244
Cdd:cd19131 140 EHLQRLIDETGV--VPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQ----------GGLLSDPVIGEIAEKHGKT 207
|
...
gi 2462615415 245 AAQ 247
Cdd:cd19131 208 PAQ 210
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-247 |
2.01e-69 |
|
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: 215.65 E-value: 2.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 4 FVELSTKAKMPIVGLGTWKSPlGKVKEAVKVAI-DAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPT 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKES----GVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 FFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDlfpkddkgnaigGKATFLDAWEAMEELVDEGLVKALGVSNF 162
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN------------VKETRAETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 163 SHFQIEKLLNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrPWakpedpSLLEDPKIKEIAAKHK 242
Cdd:cd19135 147 LIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KG------KALEEPTVTELAKKYQ 214
|
....*
gi 2462615415 243 KTAAQ 247
Cdd:cd19135 215 KTPAQ 219
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-247 |
2.36e-69 |
|
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: 215.13 E-value: 2.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWK-SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIqekaVKREDLFIVSKLWPTF 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGfksgddlfpkDDKGnaiggkatfldAWEAMEELVDEGLVKALGVSNFS 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 164 HFQIEKLLnkPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpEDPSLLEDPKIKEIAAKHKK 243
Cdd:cd19133 136 PDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE--------GRNNLFENPVLTEIAEKYGK 205
|
....
gi 2462615415 244 TAAQ 247
Cdd:cd19133 206 SVAQ 209
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-247 |
3.61e-68 |
|
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: 212.76 E-value: 3.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLGKVKE-AVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPT- 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 -FFERPLvrKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaigGKATFLDAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19156 77 qGYESTL--AAFEESLEKLGLDYVDLYLIHWP--------------------VKGKFKDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 162 FSHFQIEKLLNKpgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKH 241
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKY 202
|
....*.
gi 2462615415 242 KKTAAQ 247
Cdd:cd19156 203 GKSAAQ 208
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-247 |
6.44e-67 |
|
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: 209.40 E-value: 6.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGT----WKSPLG----KVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTF 83
Cdd:cd19120 3 KIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEA----LKESGVPREDLFITTKVSPGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 ferPLVRKAFEKTLKDLKLSYLDVYLIHwpqgfksgddlFPKDDKgnaiGGKATFLDAWEAMEELVDEGLVKALGVSNFS 163
Cdd:cd19120 79 ---KDPREALRKSLAKLGVDYVDLYLIH-----------SPFFAK----EGGPTLAEAWAELEALKDAGLVRSIGVSNFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 164 HFQIEKLLNKPglKYKPVTNQVECHPYLT--QEKLIQYCHSKGITVTAYSPLGspdrPWAKPEDPSLleDPKIKEIAAKH 241
Cdd:cd19120 141 IEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLS----PLTRDAGGPL--DPVLEKIAEKY 212
|
....*.
gi 2462615415 242 KKTAAQ 247
Cdd:cd19120 213 GVTPAQ 218
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-247 |
6.62e-66 |
|
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: 206.34 E-value: 6.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 11 AKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTFFERPLVR 90
Cdd:cd19140 6 VRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 91 KAFEKTLKDLKLSYLDVYLIHWPQgfksgddlfPKDDKGNAIGgkatfldaweAMEELVDEGLVKALGVSNFSHFQIEKL 170
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWPN---------KDVPLAETLG----------ALNEAQEAGLARHIGVSNFTVALLREA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615415 171 LNKPGLKYkpVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwakpeDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19140 143 VELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPAQ 207
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-247 |
4.03e-64 |
|
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: 203.56 E-value: 4.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRK 91
Cdd:cd19114 3 KMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHVRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 AFEKTLKDLKLSYLDVYLIHWP--QGFKSGDDLFPkddKGNAIGGKATF-------LDAWEAMEELVDEGLVKALGVSNF 162
Cdd:cd19114 83 AFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENYP---FLWKDKELKKFpleqspmQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 163 SHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP---DRPWAKPEDPSLLEDPKIKEIAA 239
Cdd:cd19114 160 NVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLAD 237
|
....*...
gi 2462615415 240 KHKKTAAQ 247
Cdd:cd19114 238 KHKRDTGQ 245
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-247 |
2.54e-63 |
|
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: 199.80 E-value: 2.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPTFFERPLVRK 91
Cdd:cd19132 6 QIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRS----GVPREELFVTTKLPGRHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 AFEKTLKDLKLSYLDVYLIHWPQgfksgddlfPKDDKgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLL 171
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWPN---------PSRDL---------YVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 172 NKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedpsLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19132 144 DETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQ 208
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-247 |
1.16e-60 |
|
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: 194.38 E-value: 1.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 7 LSTKAKMPIVGLGTWKS--PLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEK-AVKREDLFIVSKLWPTF 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPK-DDKGNAIGGKATFLD---AWEAMEELVDEGLVKALGV 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILKDLTENpepTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEKLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSllEDPKIKEIAA 239
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAE 238
|
....*...
gi 2462615415 240 KHKKTAAQ 247
Cdd:cd19122 239 KGGYSLAQ 246
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-247 |
1.61e-60 |
|
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: 193.01 E-value: 1.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPTFF 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfksgddlfpKDDKGNAIggkatflDAWEAMEELVDEGLVKALGVSNFSH 164
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPV----------PNDFDRTI-------QAYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 165 FQIEKLLNKPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAK--PEDPSLLEDPKIKEIAAKHK 242
Cdd:cd19127 140 EHLERLIDATTV--VPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgpTGPGDVLQDPTITGLAEKYG 217
|
....*
gi 2462615415 243 KTAAQ 247
Cdd:cd19127 218 KTPAQ 222
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-247 |
2.74e-56 |
|
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: 182.04 E-value: 2.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 10 KAKMPIVGLGTWK------SPLGKVKEAVKV---AIDAGYRHIDCAYVYQN---EHEVGEAIqekiqeKAVKREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmsKDYSDDKKAIEAlryAIELGINLIDTAEMYGGghaEELVGKAI------KGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 78 KLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPkddkgnaiggkatFLDAWEAMEELVDEGLVKAL 157
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP------NPSIP-------------IEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 158 GVSNFSHFQIEKLLNKPGlKYKPVTNQVECHpYLTQE---KLIQYCHSKGITVTAYSPLGSPDRPWAKPedpslleDPKI 234
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------SPLL 206
|
250
....*....|...
gi 2462615415 235 KEIAAKHKKTAAQ 247
Cdd:cd19072 207 DEIAKKYGKTPAQ 219
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-247 |
5.88e-55 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 178.32 E-value: 5.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKiqekAVKREDLFIVSKLWPTFFERPLVRKA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPqgfkSGDDLFPKDDkgnaiggkatFLdawEAMEELVDEGLVKALGVSNFSHFQIEKLLN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP----SPNDEVPVEE----------YI---GALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615415 173 KPGlKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQ 203
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-247 |
2.70e-54 |
|
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: 177.89 E-value: 2.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWKSPLG-------KVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekAVKREDLFIVSKL------ 79
Cdd:pfam00248 1 IGLGTWQLGGGwgpiskeEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlFPKDDkgnaiggkatFLDAWEAMEELVDEGLVKALGV 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP---------DPDTP----------IEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEKLLNKPglKYKPVTNQVECHPY--LTQEKLIQYCHSKGITVTAYSPLGS-----------------PDRPW 220
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRRLL 215
|
250 260
....*....|....*....|....*..
gi 2462615415 221 AKPEDPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQ 242
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-247 |
4.41e-53 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 174.11 E-value: 4.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 3 TFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPT 82
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKA----LKEASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 FFERPlvRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlFPKDDkgnaiggkaTFLDAWEAMEELVDEGLVKALGVSNF 162
Cdd:PRK11565 81 DHKRP--REALEESLKKLQLDYVDLYLMHWP---------VPAID---------HYVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 163 SHFQIEKLLNKPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedpSLLEDPKIKEIAAKHK 242
Cdd:PRK11565 141 QIHHLQRLIDETGV--TPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYG 210
|
....*
gi 2462615415 243 KTAAQ 247
Cdd:PRK11565 211 KTPAQ 215
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
13-247 |
1.30e-51 |
|
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: 169.71 E-value: 1.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTFFERPLVRKA 92
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAA----IAASGIPRDELFVTTKLWNDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN 172
Cdd:cd19130 86 FAESLAKLGLDQVDLYLVHWP------------------TPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615415 173 KPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpedPSLLEDPKIKEIAAKHKKTAAQ 247
Cdd:cd19130 148 ATGV--VPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ----------GKLLGDPPVGAIAAAHGKTPAQ 210
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-247 |
1.82e-50 |
|
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: 167.04 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTW-----KSPLGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 77 SKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaigGKATFLDAWEAMEELVDEGLVKA 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR--------------------GGVPLAETVAAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 157 LGVSNFSHFQIEKLLNKPGLKyKPVTNQVECHpyLTQE----KLIQYCHSKGITVTAYSPLGSPDRPwakpeDPSLLEDP 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLENP 207
|
250
....*....|....*
gi 2462615415 233 KIKEIAAKHKKTAAQ 247
Cdd:cd19138 208 TLKEIAARHGATPAQ 222
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-247 |
3.14e-47 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 158.65 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTFFERPLVRK 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 AFEKTLKDLKLSYLDVYLIHWPqgfkSGDDLFPKDdkgnaiggkatfldawEAMEELVD---EGLVKALGVSNFSHFQIE 168
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWP----SPNDEVSVE----------------EFMQALLEakkQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615415 169 KLLNKPGlKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHKKTAAQ 247
Cdd:PRK11172 138 QAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQ 205
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-266 |
2.46e-45 |
|
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: 153.86 E-value: 2.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 5 VELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAiqekIQEKAVKREDLFIVSKLWPTFF 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRA----IAASGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkddkgnaIGGKATFLDAWEAMEELVDEGLVKALGVSNFSH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWP------------------AGREGKYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 165 FQIEKLLNKPGlkYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpedPSLLEDPKIKEIAAKHKKT 244
Cdd:cd19134 141 EHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGV----------GRLLDNPAVTAIAAAHGRT 208
|
250 260 270
....*....|....*....|....*....|
gi 2462615415 245 AA--------QEGSLELSGSlMSPFRIGSD 266
Cdd:cd19134 209 PAqvllrwslQLGNVVISRS-SNPERIASN 237
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-247 |
2.04e-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: 148.87 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWK---------SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHE---VGEAIqekiqeKAVKREDLFIVSKL 79
Cdd:cd19137 3 KIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGGGHTeelVGKAI------KDFPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfksgddlfpkddkgNAIGGKATFldawEAMEELVDEGLVKALGV 159
Cdd:cd19137 77 WPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN---------------PNIPLEETL----SAMAEGVRQGLIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEKLLNKpgLKYKPVTNQVECHPY---LTQEKLIQYCHSKGITVTAYSPLgspDRPWAKPEDpslledpKIKE 236
Cdd:cd19137 138 SNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNR-------TLEE 205
|
250
....*....|.
gi 2462615415 237 IAAKHKKTAAQ 247
Cdd:cd19137 206 IAKNYGKTIAQ 216
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-247 |
2.87e-40 |
|
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: 141.60 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWK---------SPLGK--VKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekaVKREDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgyGEYGDedLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 78 KLWPTF--FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFpkddkgnaiggkatfldaWEAMEELVDEGLVK 155
Cdd:cd19093 76 KFAPLPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 156 ALGVSNFSHFQIE---KLLNKPGlkYKPVTNQVE---CHPYLTQEKLIQYCHSKGITVTAYSPLG--------SPDRP-- 219
Cdd:cd19093 138 AVGVSNYSADQLRrahKALKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPpp 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462615415 220 ---------WAKPEDPSLLEdpKIKEIAAKHKKTAAQ 247
Cdd:cd19093 216 ggrrrlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQ 250
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-247 |
3.71e-37 |
|
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: 133.77 E-value: 3.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWksPLGKV------KEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIqekiqeKAVKREDLFIVSKLWPTF 83
Cdd:COG0667 16 LGLGTM--TFGGPwggvdeAEAIAIldaALDAGINFFDTADVYgpgRSEELLGEAL------KGRPRDDVVIATKVGRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FERPL--------VRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPKDDkgnaiggkatfldAWEAMEELVDEGLVK 155
Cdd:COG0667 88 GPGPNgrglsrehIRRAVEASLRRLGTDYIDLYQLHRP------DPDTPIEE-------------TLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 156 ALGVSNFSHFQIEKLLNKPGLKYKPVTNQVEchpY--LTQ---EKLIQYCHSKGITVTAYSPLGS--------------- 215
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGglltgkyrrgatfpe 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462615415 216 PDR-------PWAKPEDPSLLEdpKIKEIAAKHKKTAAQ 247
Cdd:COG0667 226 GDRaatnfvqGYLTERNLALVD--ALRAIAAEHGVTPAQ 262
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-215 |
1.45e-35 |
|
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: 127.63 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWK-SPLGKVKEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekaVKREDLFIVSKLWPTFFERPL 88
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALldaALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGDPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 89 --------VRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPKDDkgnaiggkatfldAWEAMEELVDEGLVKALGVS 160
Cdd:cd06660 78 rsrlspehIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 161 NFSHFQIEKLLN--KPGLKYKPVTNQVE---CHPYLTQEKLIQYCHSKGITVTAYSPLGS 215
Cdd:cd06660 139 NWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-247 |
2.70e-34 |
|
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: 125.78 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 14 PIVGLGTW----KSPLGKVKE-----AVKVAIDAGYRHIDCAYVYQNEHE---VGEAIQEKiqekavkREDLFIVSKLWP 81
Cdd:cd19085 2 SRLGLGCWqfggGYWWGDQDDeesiaTIHAALDAGINFFDTAEAYGDGHSeevLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 82 TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfKSGDDLfpkddkgnaiggKATFldawEAMEELVDEGLVKALGVSN 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP---SSDVPL------------EETM----EALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 162 FSHFQIEKLLnKPGlkyKPVTNQVECHPYLTQ-EK-LIQYCHSKGITVTAYSPL------GSPDRPWAKPED------PS 227
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlFR 211
|
250 260 270
....*....|....*....|....*....|
gi 2462615415 228 LLEDP----------KIKEIAAKHKKTAAQ 247
Cdd:cd19085 212 HFEPGaeeetfealeKLKEIADELGVTMAQ 241
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-247 |
6.92e-34 |
|
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: 124.95 E-value: 6.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWksPLG----------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIVSK 78
Cdd:cd19084 3 KVSRIGLGTW--AIGgtwwgevddqESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 79 ---LW--PTFFERPL----VRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPKDDkgnaiggkatfldAWEAMEELV 149
Cdd:cd19084 74 cglRWdgGKGVTKDLspesIRKEVEQSLRRLQTDYIDLYQIHWP------DPNTPIEE-------------TAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 150 DEGLVKALGVSNFSHFQIEKLlnkpgLKY-KPVTNQVechPY--LTQ---EKLIQYCHSKGITVTAYSPLG--------- 214
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAqglltgkyk 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462615415 215 -----SPD---------RPWAKPEDPSLLEdpKIKEIAAKHKKTAAQ 247
Cdd:cd19084 207 keptfPPDdrrsrfpffRGENFEKNLEIVD--KLKEIAEKYGKSLAQ 251
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-247 |
1.20e-29 |
|
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: 113.42 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 17 GLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekAVKREDLFIVSK--LWPTFFERPL--- 88
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgIRLGDDPRPGrik 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 89 --------VRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFpkddkgnaiggkatflDAWE---AMEELVDEGLVKAL 157
Cdd:cd19092 91 hydtskehILASVEGSLKRLGTDYLDLLLLHRP------DPLM----------------DPEEvaeAFDELVKSGKVRYF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 158 GVSNFSHFQIEkLLNKpGLKYKPVTNQVEC---HPYLTQEKLIQYCHSKGITVTAYSPLG-----SPDRpwakPEDPSLL 229
Cdd:cd19092 149 GVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGggrlfGGFD----ERFQRLR 222
|
250
....*....|....*...
gi 2462615415 230 EdpKIKEIAAKHKKTAAQ 247
Cdd:cd19092 223 A--ALEELAEEYGVTIEA 238
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
17-247 |
4.77e-29 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 112.17 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 17 GLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekAVKREDLFIVSK----LWPTFFERPL- 88
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEALKLS----PSLREKIELQTKcgirLPSEARDNRVk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 89 --------VRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDdlfpkddkgnaiggkaTFLDAWE---AMEELVDEGLVKAL 157
Cdd:COG4989 98 hydtskehIIASVEGSLRRLGTDYLDLLLLHRP------D----------------PLMDPEEvaeAFDELKASGKVRHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 158 GVSNFSHFQIEkLLNKpGLKYKPVTNQVECHPYLTQ---EKLIQYCHSKGITVTAYSPLGSPDrpWAKPEDPSLLE-DPK 233
Cdd:COG4989 156 GVSNFTPSQFE-LLQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGR--LFGGFDEQFPRlRAA 231
|
250
....*....|....
gi 2462615415 234 IKEIAAKHKKTAAQ 247
Cdd:COG4989 232 LDELAEKYGVSPEA 245
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-232 |
1.19e-25 |
|
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: 101.89 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 9 TKAKMPIVGLGTWKSPlGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIqekiqeKAVKREDLFIVSKLWPTFFE 85
Cdd:cd19105 9 TGLKVSRLGFGGGGLP-RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEAL------KGLRRDKVFLATKASPRLDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 86 RPL--VRKAFEKTLKDLKLSYLDVYLIHwpqgfksGDDlFPKDDKGNaiggkatflDAW-EAMEELVDEGLVKALGVSnf 162
Cdd:cd19105 82 KDKaeLLKSVEESLKRLQTDYIDIYQLH-------GVD-TPEERLLN---------EELlEALEKLKKEGKVRFIGFS-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 163 SHFQIEKLLN---KPG------LKYKPVtnqvecHPYLTQEKLIQYCHSKGITVTAYSPLGS-PDRPWAKPEDPSLLEDP 232
Cdd:cd19105 143 THDNMAEVLQaaiESGwfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGgYLQPALLSVLKAKGFSL 216
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-226 |
7.14e-25 |
|
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: 99.48 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 8 STKAKMPIVGLGTWksPLGKV--KEAVKV---AIDAGYRHIDCAYVYQNEHE-VGEAIQEKiqekavkREDLFIVSKLWP 81
Cdd:cd19100 6 RTGLKVSRLGFGGG--PLGRLsqEEAAAIirrALDLGINYFDTAPSYGDSEEkIGKALKGR-------RDKVFLATKTGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 82 TffERPLVRKAFEKTLKDLKLSYLDVYLIHwpqGFKSGDDLFPKDDKGNAIggkatfldawEAMEELVDEGLVKALGVSN 161
Cdd:cd19100 77 R--DYEGAKRDLERSLKRLGTDYIDLYQLH---AVDTEEDLDQVFGPGGAL----------EALLEAKEEGKIRFIGISG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615415 162 FSHFQIEKLLNKPglkykPV------TNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDP 226
Cdd:cd19100 142 HSPEVLLRALETG-----EFdvvlfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-215 |
4.73e-24 |
|
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: 97.16 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWksPLG----------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekavkREDLFIVSKLWPT 82
Cdd:cd19086 6 IGFGTW--GLGgdwwgdvddaEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 FFERPL---------VRKAFEKTLKDLKLSYLDVYLIH-WPqgfksgDDLFPKDdkgnaiggkatflDAWEAMEELVDEG 152
Cdd:cd19086 77 FDGGPErpqdfspeyIREAVEASLKRLGTDYIDLYQLHnPP------DEVLDND-------------ELFEALEKLKQEG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615415 153 LVKALGVSNFSHFQIEKLLNKPGLK-----YkpvtNQVECHPYltqEKLIQYCHSKGITVTAYSPLGS 215
Cdd:cd19086 138 KIRAYGVSVGDPEEALAALRRGGIDvvqviY----NLLDQRPE---EELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-247 |
5.12e-24 |
|
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: 98.51 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWksPLG--------------KVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavkREDLFIVSK 78
Cdd:cd19102 4 IGLGTW--AIGgggwgggwgpqddrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 79 ---LW-----PTFFERP-LVRKAFEKTLKDLKLSYLDVYLIHWPQgfksgddlfPKDDkgnaiggkatFLDAWEAMEELV 149
Cdd:cd19102 75 cglLWdeegrIRRSLKPaSIRAECEASLRRLGVDVIDLYQIHWPD---------PDEP----------IEEAWGALAELK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 150 DEGLVKALGVSNFSHFQIEKLlnkpgLKYKPVT-NQVechPY--LTQE---KLIQYCHSKGITVTAYSPLGS-------- 215
Cdd:cd19102 136 EEGKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmt 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462615415 216 PDRPWAKPED-----------PSLLEDPKI----KEIAAKHKKTAAQ 247
Cdd:cd19102 208 PERVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQ 254
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-214 |
7.54e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 99.12 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEAVKV---AIDAGYRHIDCAYVY-QNEHEVGEAIQEKiqekavkREDLFIVSKLWPTFFERP 87
Cdd:COG1453 12 EVSVLGFGGMRLPRKDEEEAEALirrAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVRDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 88 LVRKAFEKTLKDLKLSYLDVYLIH-------WPQGFKSGddlfpkddkgnaiggkatflDAWEAMEELVDEGLVKALGVS 160
Cdd:COG1453 85 DMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPG--------------------GALEALEKAKAEGKIRHIGFS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 161 nfSHFQ---IEKLLNkpglkykpvTNQVEC---------HPYLTQEKLIQYCHSKGITVTAYSPLG 214
Cdd:COG1453 145 --THGSlevIKEAID---------TGDFDFvqlqynyldQDNQAGEEALEAAAEKGIGVIIMKPLK 199
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-247 |
5.65e-23 |
|
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: 95.95 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 29 KEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavKREDLFIVSKLWPTFF--------ERPLVRKAFEKTL 97
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFGgdgsvlnnSPEFLRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 98 KDLKLSYLDVYLIHWPqgfksgDDLFPKDDkgnAIGgkatfldaweAMEELVDEGLVKALGVSNFSHFQIeKLLNKPGLk 177
Cdd:cd19083 110 KRLNTDYIDLYYIHFP------DGETPKAE---AVG----------ALQELKDEGKIRAIGVSNFSLEQL-KEANKDGY- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 178 ykpvTNQVEcHPY-LTQ----EKLIQYCHSKGITVTAYSPLGS-------------PDRPWAKpeDPSLLEDP------- 232
Cdd:cd19083 169 ----VDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLASgllagkytkdtkfPDNDLRN--DKPLFKGErfsenld 241
|
250
....*....|....*...
gi 2462615415 233 ---KIKEIAAKHKKTAAQ 247
Cdd:cd19083 242 kvdKLKSIADEKGVTVAH 259
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
19-247 |
7.95e-22 |
|
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: 92.65 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 19 GTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIqekavKREDLFIVSKLWPTFFERP----LVRK 91
Cdd:cd19079 28 RPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFPMGDGPngrgLSRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 ----AFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPkddkgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQI 167
Cdd:cd19079 103 himaEVDASLKRLGTDYIDLYQIHRW------DYETP-------------IEETLEALHDVVKSGKVRYIGASSMYAWQF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 168 EKLLN---KPGLKyKPVTNQvecHPY--LTQE---KLIQYCHSKGITVTAYSPL----------GSPDRPWAKPEDPSLL 229
Cdd:cd19079 164 AKALHlaeKNGWT-KFVSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLargrlarpwgDTTERRRSTTDTAKLK 239
|
250 260
....*....|....*....|....*...
gi 2462615415 230 ED----------PKIKEIAAKHKKTAAQ 247
Cdd:cd19079 240 YDyfteadkeivDRVEEVAKERGVSMAQ 267
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-213 |
4.88e-21 |
|
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: 90.34 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWKSPLGKV-----KEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEkiqekaVKREDLFIVSKL-WPT---F 83
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKVfWPTgpgP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FERPLVRK----AFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPKDDkgnaiggkaTFldawEAMEELVDEGLVKALGV 159
Cdd:cd19074 81 NDRGLSRKhifeSIHASLKRLQLDYVDIYYCHRY------DPETPLEE---------TV----RAMDDLIRQGKILYWGT 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEK---LLNKPGLkYKPVTNQVECHpYLTQEK---LIQYCHSKGITVTAYSPL 213
Cdd:cd19074 142 SEWSAEQIAEahdLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPL 199
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-213 |
6.69e-21 |
|
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: 90.06 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWKspLG-------KVKEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekaVKREDLFIVSKLWPT 82
Cdd:cd19148 7 IALGTWA--IGgwmwggtDEKEAIETihkALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 FFERPLV---------RKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPkddkgnaiggkatFLDAWEAMEELVDEGL 153
Cdd:cd19148 80 WDEGGEVvrnsspariRKEVEDSLRRLQTDYIDLYQVHWP------DPLVP-------------IEETAEALKELLDEGK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 154 VKALGVSNFSHFQIEKLlnkpgLKYKPV-TNQVechPY-----LTQEKLIQYCHSKGITVTAYSPL 213
Cdd:cd19148 141 IRAIGVSNFSPEQMETF-----RKVAPLhTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
27-214 |
8.68e-21 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 88.77 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 27 KVKEAVKVAIDAGYRHIDCAYVY---QNEHEVGEAIqekiqeKAVKREDLFIVSKLWPTFFERPL-VRKAFEKTLKDLKL 102
Cdd:cd19096 22 KAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEAL------KEGPREKFYLATKLPPWSVKSAEdFRRILEESLKRLGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 103 SYLDVYLIHWPqgfkSGDDLFPKDDKGnaiggkatflDAWEAMEELVDEGLVKALGVSnfSHFQ---IEKLLNkpglkyk 179
Cdd:cd19096 96 DYIDFYLLHGL----NSPEWLEKARKG----------GLLEFLEKAKKEGLIRHIGFS--FHDSpelLKEILD------- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462615415 180 pvTNQVEC----HPYLTQE-----KLIQYCHSKGITVTAYSPLG 214
Cdd:cd19096 153 --SYDFDFvqlqYNYLDQEnqagrPGIEYAAKKGMGVIIMEPLK 194
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-247 |
1.34e-19 |
|
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: 86.56 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTW---------KSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHevgeaiQEKIQEKAVK--REDLFIVSK---LWP 81
Cdd:cd19149 14 IGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFGH------SEEIVGKAIKgrRDKVVLATKcglRWD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 82 T-----FFERPLV-----------RKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPkddkgnaIGgkatflDAWEAM 145
Cdd:cd19149 88 ReggsfFFVRDGVtvyknlspesiREEVEQSLKRLGTDYIDLYQTHWQ------DVETP-------IE------ETMEAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 146 EELVDEGLVKALGVSNFSHFQIEKLLNKPGL-----KYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLGS----- 215
Cdd:cd19149 149 EELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLEQglltg 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462615415 216 ---PDR-----------PWAKPEDPS----LLEdpKIKEIAAKHKKTAAQ 247
Cdd:cd19149 222 kitPDRefdagdarsgiPWFSPENREkvlaLLE--KWKPLCEKYGCTLAQ 269
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-247 |
1.92e-19 |
|
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: 85.35 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWKSPLGKvKEAVKV---AIDAGYRHIDCAYVYqnehevGEAIQEKIQEKAVK--REDLFIVSKL-------- 79
Cdd:cd19088 9 MRLTGPGIWGPPADR-EEAIAVlrrALELGVNFIDTADSY------GPDVNERLIAEALHpyPDDVVIATKGglvrtgpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 -WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkDDKGnaiggkaTFLDAWEAMEELVDEGLVKALG 158
Cdd:cd19088 82 wWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------------DPKV-------PFEEQLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 159 VSNFSHFQIEKLLNKPGLkykpVTNQVECHPYLTQ-EKLIQYCHSKGITVTAYSPLGSpdRPWAKPEdpslledPKIKEI 237
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQPG-------GLLAEV 209
|
250
....*....|
gi 2462615415 238 AAKHKKTAAQ 247
Cdd:cd19088 210 AARLGATPAQ 219
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-241 |
4.74e-19 |
|
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: 84.53 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 14 PIVGLGTwkSPLGKVK---------EAVKVAIDAGYRHIDCAYVYQN-EHEVGEAIQEkiqekaVKREDLFIVSKL---- 79
Cdd:cd19090 1 SALGLGT--AGLGGVFggvdddeavATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 -WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfksgddlFPKDDKGNAIGGkatfldAWEAMEELVDEGLVKALG 158
Cdd:cd19090 73 eDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPE--------RVPWVDILAPGG------ALEALLELKEEGLIKHIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 159 VSNFSHFQIEKLLNkpglkykpvTNQVEC----HPY--LTQE---KLIQYCHSKGITVTAYSPLGS-------PDRPWAK 222
Cdd:cd19090 139 LGGGPPDLLRRAIE---------TGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGMgllagrpPERVRYT 209
|
250 260
....*....|....*....|..
gi 2462615415 223 PEDPSLLEDP---KIKEIAAKH 241
Cdd:cd19090 210 YRWLSPELLDrakRLYELCDEH 231
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-238 |
1.00e-18 |
|
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: 84.29 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTWKSPLGK-----VKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIQEKAVKREDLFIVSK--------- 78
Cdd:cd19099 6 LGLGTYRGDSDDetdeeYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 79 ------LWPTFFERPLV------------------RKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKgnaigg 134
Cdd:cd19099 86 eplrplKYLEEKLGRGLidvadsaglrhcispaylEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEFYDR------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 135 katFLDAWEAMEELVDEGLVKALGVS----------NFSHFQIEKLL--------NKPGLKYkpVtnQVECHPYLTQ--- 193
Cdd:cd19099 160 ---LEEAFEALEEAVAEGKIRYYGIStwdgfrappaLPGHLSLEKLVaaaeevggDNHHFKV--I--QLPLNLLEPEalt 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 194 ---------EKLIQYCHSKGITVTAYSPL--GSPDRPWAKPEDPSLLEDPKIKEIA 238
Cdd:cd19099 233 ekntvkgeaLSLLEAAKELGLGVIASRPLnqGQLLGELRLADLLALPGGATLAQRA 288
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-247 |
3.30e-18 |
|
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: 82.19 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 17 GLGTW--------KSPLGKV--KEAVKV---AIDAGYRHIDCAYVYQNEHEV-GEAIQEKiqekavkrEDLFIVSKL--- 79
Cdd:cd19097 4 ALGTAqfgldygiANKSGKPseKEAKKIleyALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLppl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 -WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPKDDKgnaiggkatfldAWEAMEELVDEGLVKALG 158
Cdd:cd19097 76 kEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNP------DDLLKHGGK------------LVEALLELKKEGLIRKIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 159 VSNFSHFQIEKLLNKPGLKYkpVtnQVechPY------LTQEKLIQYCHSKGITVTAYSP------LGSPDRPWAKPED- 225
Cdd:cd19097 138 VSVYSPEELEKALESFKIDI--I--QL---PFnildqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPa 210
|
250 260
....*....|....*....|..
gi 2462615415 226 PSLLEdpKIKEIAAKHKKTAAQ 247
Cdd:cd19097 211 KPLLK--KLHELAKKLGLSPLE 230
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-251 |
4.62e-17 |
|
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: 78.43 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 14 PIVGLGTWK-------SPLGKVKEAVKVAIDAGYRHIDCAYVYQN-EHEVGEAIqekiqeKAVKREDLFIVSKLWPTF-- 83
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL------AGLRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 ------FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFpkddkgnaiggkatfldawEAMEELVDEGLVKAL 157
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVL-------------------ETLEDLKAAGKVRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 158 GVSNFSHfQIEKLLNKPGLKykpvTNQVechPY----LTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPK 233
Cdd:cd19095 136 GVSGDGE-ELEAAIASGVFD----VVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYAR 207
|
250
....*....|....*...
gi 2462615415 234 IKEIAAKHKKTAAQEGSL 251
Cdd:cd19095 208 RPEFAAEIGGATWAQAAL 225
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
35-249 |
1.01e-16 |
|
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: 78.38 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 35 AIDAGYRHIDCAYVYQN---EHEVGEAIQEkiqekavKREDLFIVSKlwptFFERP------------LVRKAFEKTLKD 99
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATK----VFGPMgddpndrglsrrHIRRAVEASLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 100 LKLSYLDVYLIHwpqgfksgddlfpkddkgnAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLN---KPGL 176
Cdd:cd19087 108 LQTDYIDLYQMH-------------------HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 177 --------KYKPVTNQVECHpyltqekLIQYCHSKGITVTAYSPLGS-----PDRPWAKPEDPSLLED---------PKI 234
Cdd:cd19087 169 lrfvseqpMYNLLKRQAELE-------ILPAARAYGLGVIPYSPLAGglltgKYGKGKRPESGRLVERaryqaryglEEY 241
|
250
....*....|....*
gi 2462615415 235 KEIAAKHKKTAAQEG 249
Cdd:cd19087 242 RDIAERFEALAAEAG 256
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-247 |
1.33e-16 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 78.42 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGT--------WKSPLGKV--KEA---VKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavkREDLFI 75
Cdd:cd19091 12 KVSELALGTmtfgggggFFGAWGGVdqEEAdrlVDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 76 VSKlwpTFF-------ERPLVR----KAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPkddkgnaiggkatFLDAWEA 144
Cdd:cd19091 85 ATK---VRGrmgegpnDVGLSRhhiiRAVEASLKRLGTDYIDLYQLHGF------DALTP-------------LEETLRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 145 MEELVDEGLVKALGVSNFSHFQIEKLL---NKPGLKyKPVTNQVechpYLT------QEKLIQYCHSKGITVTAYSPLG- 214
Cdd:cd19091 143 LDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAg 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462615415 215 -------SPDRPWAK------------PEDPSLLED--PKIKEIAAKHKKTAAQ 247
Cdd:cd19091 218 gllsgkyRRGQPAPEgsrlrrtgfdfpPVDRERGYDvvDALREIAKETGATPAQ 271
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
16-214 |
8.45e-16 |
|
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: 76.06 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGT--WKSPLGKvKEAVK---VAIDAGYRHIDCAYVY---QNEHEVGEAiqEKI----QEKAVKREDLFIVSKL---- 79
Cdd:cd19094 4 ICLGTmtWGEQNTE-AEAHEqldYAFDEGVNFIDTAEMYpvpPSPETQGRT--EEIigswLKKKGNRDKVVLATKVagpg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 ----WP----TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQ----GFKSGDDLFPKDDkgnaiGGKATFLDAWEAMEE 147
Cdd:cd19094 81 egitWPrgggTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytpLFGGGYYTEPSEE-----EDSVSFEEQLEALGE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615415 148 LVDEGLVKALGVSNFSHFQIEKLLN---KPGLKyKPVTNQvecHPY--LTQ---EKLIQYCHSKGITVTAYSPLG 214
Cdd:cd19094 156 LVKAGKIRHIGLSNETPWGVMKFLElaeQLGLP-RIVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLA 226
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-247 |
1.59e-15 |
|
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: 75.06 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWK--SPL-------------GKVKEAVKVAIDAGYRHIDCAYVYqnehevGEAIQEKIQE---KAVKREDL 73
Cdd:cd19103 3 KLPKIALGTWSwgSGGaggdqvfgnhldeDTLKAVFDKAMAAGLNLWDTAAVY------GMGASEKILGeflKRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 74 FIVSKLWPTF---FERPlVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDlfpkddkgnaiggkatfLDAW-EAMEELV 149
Cdd:cd19103 77 IISTKFTPQIagqSADP-VADMLEGSLARLGTDYIDIYWIHNP------AD-----------------VERWtPELIPLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 150 DEGLVKALGVSNFSHFQIEK---LLNKPGLKYKPVTNqvecH---PYLTQEK--LIQYCHSKGITVTAYSPL------GS 215
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN----HyslLYRSSEEagILDYCKENGITFFAYMVLeqgalsGK 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462615415 216 PDRPWAKPEDPSLLED-----PKI-------KEIAAKHKKTAAQ 247
Cdd:cd19103 209 YDTKHPLPEGSGRAETynpllPQLeeltavmAEIGAKHGASIAQ 252
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
36-247 |
2.21e-15 |
|
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: 74.56 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 36 IDAGYRHIDCAYVY---QNEHEVGEAiqEKI----QEKAVKREDLFIVSKL-WPTFFERP-----LVRKAFEKTLKDLKL 102
Cdd:cd19081 36 VDAGGNFIDTADVYsawVPGNAGGES--ETIigrwLKSRGKRDRVVIATKVgFPMGPNGPglsrkHIRRAVEASLRRLQT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 103 SYLDVYLIHWPqgfksgDDLFPKDDkgnaiggkaTFldawEAMEELVDEGLVKALGVSNFSHFQIEKLLN---KPGLKyK 179
Cdd:cd19081 114 DYIDLYQAHWD------DPATPLEE---------TL----GALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-R 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 180 PVTNQVEchpY------LTQEKLIQYCHSKGITVTAYSPLGS--------PDRPWAK----PEDPSLLEDPK-------I 234
Cdd:cd19081 174 YVSLQPE---YnlvdreSFEGELLPLCREEGIGVIPYSPLAGgfltgkyrSEADLPGstrrGEAAKRYLNERglrildaL 250
|
250
....*....|...
gi 2462615415 235 KEIAAKHKKTAAQ 247
Cdd:cd19081 251 DEVAAEHGATPAQ 263
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
35-247 |
3.45e-15 |
|
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: 74.17 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 35 AIDAGYRHIDCAYVYQ---NEHEVGEAIQEKiqekavkREDLFIVSKLWPTFFERPL----------VRKAFEKTLKDLK 101
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKFGIVRDPGSGfrgvdgrpeyVRAACEASLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 102 LSYLDVYLIHWPqgfksgDDLFPKDDkgnaiggkatfldAWEAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPV 181
Cdd:cd19076 114 TDVIDLYYQHRV------DPNVPIEE-------------TVGAMAELVEEGKVRYIGLSEASADTIRR-----AHAVHPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 182 TN-QVECHPYLT--QEKLIQYCHSKGITVTAYSPL------GSPDRPWAKPEDPSLLEDP---------------KIKEI 237
Cdd:cd19076 170 TAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDFRRNNPrfqgenfdknlklveKLEAI 249
|
250
....*....|
gi 2462615415 238 AAKHKKTAAQ 247
Cdd:cd19076 250 AAEKGCTPAQ 259
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-215 |
1.22e-14 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 72.59 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 15 IVGLGTWKSPLG-----KVKEAVKVAIDAGYRHIDCAYVYQNehevGEAiqEKI--QEKAVKREdlFIVSKLWPTFFERP 87
Cdd:cd19075 4 ILGTMTFGSQGRfttaeAAAELLDAFLERGHTEIDTARVYPD----GTS--EELlgELGLGERG--FKIDTKANPGVGGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 88 L----VRKAFEKTLKDLKLSYLDVYLIHWPqgfksgddlfpkdDKGNAIggKATFldawEAMEELVDEGLVKALGVSNFS 163
Cdd:cd19075 76 LspenVRKQLETSLKRLKVDKVDVFYLHAP-------------DRSTPL--EETL----AAIDELYKEGKFKEFGLSNYS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462615415 164 HFQIEKLLN--------KP----GLkYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLGS 215
Cdd:cd19075 137 AWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
35-271 |
9.12e-13 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 67.47 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 35 AIDAGYRHIDCAYVYQ-NEHEVGEAIQEKIQekavKREDLFIVSKL----------WPTFFERPLVRKAFEKTLKDLKLS 103
Cdd:cd19144 43 AFELGCTFWDTADIYGdSEELIGRWFKQNPG----KREKIFLATKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 104 YLDVYLIHwpqgfksgddlfpkddkgnAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPVTN 183
Cdd:cd19144 119 YIDLYYQH-------------------RVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRR-----AHAVHPIAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 184 -QVECHPYLT-----QEKLIQYCHSKGITVTAYSPLG---------SPD----------RPWAKPED-PSLLE--DpKIK 235
Cdd:cd19144 175 vQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGrgfltgairSPDdfeegdfrrmAPRFQAENfPKNLElvD-KIK 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462615415 236 EIAAKHKKTAAQegsLELSGSLMSpfriGSDPFPYP 271
Cdd:cd19144 254 AIAKKKNVTAGQ---LTLAWLLAQ----GDDIIPIP 282
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-261 |
9.68e-13 |
|
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: 66.81 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 36 IDAGYRHIDCAYVYQNEHEVG---EAIQEKIQEKAvKREDLFIVSK--------LWPTFFERPLVRKAFEKTLKDLKLSY 104
Cdd:cd19082 27 VELGGNFIDTARVYGDWVERGaseRVIGEWLKSRG-NRDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 105 LDVYLIHwpqgfksgddlfpKDDKGNAIGGkatFLDaweAMEELVDEGLVKALGVSNFSHFQIE---KLLNKPGLkYKPV 181
Cdd:cd19082 106 IDLYFLH-------------RDDPSVPVGE---IVD---TLNELVRAGKIRAFGASNWSTERIAeanAYAKAHGL-PGFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 182 TNQV---------ECHPYLT----QEKLIQYCHSKGITVTAYSPLGS---PDRpwAKPEDPSLLEDPK------------ 233
Cdd:cd19082 166 ASSPqwslarpnePPWPGPTlvamDEEMRAWHEENQLPVFAYSSQARgffSKR--AAGGAEDDSELRRvyyseenferle 243
|
250 260
....*....|....*....|....*....
gi 2462615415 234 -IKEIAAKHKKTAAQegsLELSGSLMSPF 261
Cdd:cd19082 244 rAKELAEEKGVSPTQ---IALAYVLNQPF 269
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-249 |
1.09e-12 |
|
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: 66.91 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 31 AVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavkREDLFIVSKLWPTFFERP----LVRKAFEKTLKDLKLS 103
Cdd:cd19104 37 AVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVEKSLKRLKRD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 104 YLDVYLIH--------WPQGFKSG--DDLFPKDdkgnaiggkatfldAWEAMEELVDEGLVKALGVS------------- 160
Cdd:cd19104 110 SVDLLQLHnrigderdKPVGGTLSttDVLGLGG--------------VADAFERLRSEGKIRFIGITglgnppairelld 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 161 --NFSHFQIE-KLLNKP-GLKYKPVtnqvecHPYLTQEKLIQYCHSKGITVTAYSPL------GSPDRPwakPEDPSLLE 230
Cdd:cd19104 176 sgKFDAVQVYyNLLNPSaAEARPRG------WSAQDYGGIIDAAAEHGVGVMGIRVLaagaltTSLDRG---REAPPTSD 246
|
250 260
....*....|....*....|.
gi 2462615415 231 DPKIKEI--AAKHKKTAAQEG 249
Cdd:cd19104 247 SDVAIDFrrAAAFRALAREWG 267
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
29-215 |
3.00e-12 |
|
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: 65.72 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 29 KEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIqekiqekAVKREDLFIVSKLWPTFFE----------RP-LVRK 91
Cdd:cd19078 25 EEMIELirkAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFGFKIDGgkpgplgldsRPeHIRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 92 AFEKTLKDLKLSYLDVYLIHwpqgfksgddlfpKDDKGNAIGGKAtfldawEAMEELVDEGLVKALGVSNFSHFQIEKll 171
Cdd:cd19078 98 AVEGSLKRLQTDYIDLYYQH-------------RVDPNVPIEEVA------GTMKELIKEGKIRHWGLSEAGVETIRR-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462615415 172 nkpGLKYKPVTN-QVECH-----PyltQEKLIQYCHSKGITVTAYSPLGS 215
Cdd:cd19078 157 ---AHAVCPVTAvQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGK 200
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-247 |
1.03e-11 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 64.20 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWK-----SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKI--QEKAVKREDLFIVSK----LW 80
Cdd:cd19089 10 HLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRIlkRDLRPYRDELVISTKagygMW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 81 P----TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPKDdkgnaiggkatflDAWEAMEELVDEGlvKA 156
Cdd:cd19089 90 PgpygDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRY------DPDTPLE-------------ETMTALADAVRSG--KA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 157 L--GVSNFSHFQIEK---LLNKpgLKYKPVTNQVechPY--LTQ---EKLIQYCHSKGITVTAYSPL-----------GS 215
Cdd:cd19089 149 LyvGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylnGI 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462615415 216 PDRPWAKPEDPSLLED-------PKIK---EIAAKHKKTAAQ 247
Cdd:cd19089 224 PPDSRRAAESKFLTEEaltpeklEQLRklnKIAAKRGQSLAQ 265
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-247 |
1.12e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 63.89 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 36 IDAGYRHIDCAYVY----------QNEHEVGEAIQEKIQekavkREDLFIVSKL---------WPTFFE---RPLVRKAF 93
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-----RDDVVIATKVgagprdpdgGPESPEglsAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 94 EKTLKDLKLSYLDVYLIHwpqgfksgddlfpKDDKGNAIGgkatflDAWEAMEELVDEGLVKALGVSNFSHFQIEK---L 170
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAH-------------VDDRDTPLE------ETLEAFNELVKAGKVRAIGASNFAAWRLERarqI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 171 LNKPGL-KYKPVTNQvecHPYL--------------TQEkLIQYCHSKG-ITVTAYSPL--GSPDRPWAKPEDPSLLEDP 232
Cdd:cd19752 163 ARQQGWaEFSAIQQR---HSYLrprpgadfgvqrivTDE-LLDYASSRPdLTLLAYSPLlsGAYTRPDRPLPEQYDGPDS 238
|
250 260
....*....|....*....|
gi 2462615415 233 -----KIKEIAAKHKKTAAQ 247
Cdd:cd19752 239 darlaVLEEVAGELGATPNQ 258
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-228 |
1.28e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 63.77 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 13 MPIVGLGTWK--------SPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHE-VGEAIqEKIQEKAVKREDLFIVSKLWPTF 83
Cdd:cd19101 2 ISRVINGMWQlsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFR-KRLRRERDAADDVQIHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 84 FE----RPLVRKAFEKTLKDLKLSYLDVYLIHWpqgfksGDDlfpkDDKGnaiggkatFLDAWEAMEELVDEGLVKALGV 159
Cdd:cd19101 81 GEltmtRAYVEAAIDRSLKRLGVDRLDLVQFHW------WDY----SDPG--------YLDAAKHLAELQEEGKIRHLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 160 SNFSHFQIEKLLNKPglkYKPVTNQVEC-----HPyltQEKLIQYCHSKGITVTAYSP----------LGSPDRPWAKPE 224
Cdd:cd19101 143 TNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGTlaggllsekyLGVPEPTGPALE 216
|
....
gi 2462615415 225 DPSL 228
Cdd:cd19101 217 TRSL 220
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
12-250 |
2.48e-10 |
|
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: 59.87 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTwkSPLGKV------KEAVKV---AIDAGYRHIDCAYVYqnehevGEAIQEKIQEKA---VKREDLFIVSK- 78
Cdd:cd19163 12 KVSKLGFGA--SPLGGVfgpvdeEEAIRTvheALDSGINYIDTAPWY------GQGRSETVLGKAlkgIPRDSYYLATKv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 79 -----LWPTFF----ERplVRKAFEKTLKDLKLSYLDVYLIHWPQgFKSGDDLfpkddkgnaiggkaTFLDAWEAMEELV 149
Cdd:cd19163 84 gryglDPDKMFdfsaER--ITKSVEESLKRLGLDYIDIIQVHDIE-FAPSLDQ--------------ILNETLPALQKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 150 DEGLVKALGVSNFSHFQIEKLLNKpglkykpVTNQVE-----CHPYL---TQEKLIQYCHSKGITVTAYSPLG------S 215
Cdd:cd19163 147 EEGKVRFIGITGYPLDVLKEVLER-------SPVKIDtvlsyCHYTLndtSLLELLPFFKEKGVGVINASPLSmgllteR 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462615415 216 PDRPW--AKPEdpslledpkIKEIAAKHKKTAAQEGS 250
Cdd:cd19163 220 GPPDWhpASPE---------IKEACAKAAAYCKSRGV 247
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-215 |
1.25e-09 |
|
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: 57.75 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 14 PIVGLGTwkSPLGKVKE--------AVKVAIDAGYRHIDCAYVY---QNEHEVGEAIQEKiqekavKREDLFIVSKL--- 79
Cdd:cd19162 1 PRLGLGA--ASLGNLARagedeaaaTLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 80 -------WPTFFERPL------VRKAFEKTLKDLKLSYLDVYLIHwpqgfksgdDLFPKDDKgnAIGgkatflDAWEAME 146
Cdd:cd19162 73 lepgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLH---------DPDRHLLQ--ALT------DAFPALE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462615415 147 ELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTNQvecHPYLTQE---KLIQYCHSKGITVTAYSPLGS 215
Cdd:cd19162 136 ELRAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVFNS 204
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-246 |
2.82e-09 |
|
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: 56.85 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 14 PIVGLGTwkSPLG---------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIQEKAV-------KREDLF 74
Cdd:cd19152 1 PKLGFGT--APLGnlyeavsdeEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREDYVistkvgrLLVPLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 75 IVSKLWPTFFERPL------------VRKAFEKTLKDLKLSYLDVYLIHWPqgfkSGDDLFPKDDKGNAIGGKatflDAW 142
Cdd:cd19152 79 EVEPTFEPGFWNPLpfdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDP----DEDLAGAESDEHFAQAIK----GAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 143 EAMEELVDEGLVKALGV-SNFSHFqIEKLLNKPGLKYKPVTNQvechpY--LTQE---KLIQYCHSKGITVTAYSPLGS- 215
Cdd:cd19152 151 RALEELREEGVIKAIGLgVNDWEV-ILRILEEADLDWVMLAGR-----YtlLDHSaarELLPECEKRGVKVVNAGPFNSg 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462615415 216 -------PDRPWAKPEDPSLLE--DpKIKEIAAKHK---KTAA 246
Cdd:cd19152 225 flaggdnFDYYEYGPAPPELIArrD-RIEALCEQHGvslAAAA 266
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-213 |
4.91e-09 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 56.32 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKSPLGKVKEA-----VKVAIDAGYRHIDCAYVYQN---EHEVGeAIqekIQEKAVKREDLFIVSKL-WPT 82
Cdd:cd19142 12 RVSNVGLGTWSTFSTAISEEqaeeiVTLAYENGINYFDTSDAFTSgqaETELG-RI---LKKKGWKRSSYIVSTKIyWSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 83 F-FERPLVRK----AFEKTLKDLKLSYLDVYLIHwpqgfkSGDDLFPKDdkgnaiggkatflDAWEAMEELVDEGLVKAL 157
Cdd:cd19142 88 GsEERGLSRKhiieSVRASLRRLQLDYIDIVIIH------KADPMCPME-------------EVVRAMSYLIDNGLIMYW 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 158 GVSNFSH------FQIEKLLNKPglkyKPVTNQVECHPyLTQEKLIQYC----HSKGITVTAYSPL 213
Cdd:cd19142 149 GTSRWSPveimeaFSIARQFNCP----TPICEQSEYHM-FCREKMELYMpelyNKVGVGLITWSPL 209
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
17-247 |
2.33e-08 |
|
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: 53.98 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 17 GLGTWKSPLGKVKEAVKV---AIDAGYRHIDCAYVY---QNEHEVGEAIQEKIQEK---AVKReDLFIVSKLWPTFFERP 87
Cdd:cd19145 21 GLSGDYGAPKPEEEGIALihhAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPREKvqlATKF-GIHEIGGSGVEVRGDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 88 -LVRKAFEKTLKDLKLSYLDVYLIHwpqgfkSGDDLFPKDDkgnAIGgkatfldaweAMEELVDEGLVKALGVSNFSHFQ 166
Cdd:cd19145 100 aYVRAACEASLKRLDVDYIDLYYQH------RIDTTVPIEI---TMG----------ELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 167 IEKllnkpGLKYKPVTN-QVECHPYL--TQEKLIQYCHSKGITVTAYSPLGspdRP--WAKPEDPSLLEDP--------- 232
Cdd:cd19145 161 IRR-----AHAVHPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---RGffAGKAKLEELLENSdvrkshprf 232
|
250 260
....*....|....*....|....*...
gi 2462615415 233 -------------KIKEIAAKHKKTAAQ 247
Cdd:cd19145 233 qgenleknkvlyeRVEALAKKKGCTPAQ 260
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
35-214 |
4.92e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 53.32 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 35 AIDAGYRHIDCAYVYQ----------NEHEVGEAIQekiqeKAVKREDLFIVSKL-WPT-----------FFERPLVRKA 92
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvpprpetqglTETYIGNWLA-----KRGSREKLIIASKVsGPSrnndkgirpnqALDRKNIREA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPQ---------GFKSGDDlfpkddkgnaiGGKATFLDAWEAMEELVDEGLVKALGVSNFS 163
Cdd:PRK10625 114 LHDSLKRLQTDYLDLYQVHWPQrptncfgklGYSWTDS-----------APAVSLLETLDALAEQQRAGKIRYIGVSNET 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615415 164 HFQIEKLL---NKPGLKyKPVTNQvecHPYLTQEK-----LIQYCHSKGITVTAYSPLG 214
Cdd:PRK10625 183 AFGVMRYLhlaEKHDLP-RIVTIQ---NPYSLLNRsfevgLAEVSQYEGVELLAYSCLA 237
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
28-215 |
1.36e-07 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. 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: 381369 [Multi-domain] Cd Length: 319 Bit Score: 51.83 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 28 VKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKiqekAVKREDLFIVSKLwptFF--------ERPLVRK----A 92
Cdd:cd19143 33 AKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL----GWPRSDYVVSTKI---FWggggpppnDRGLSRKhiveG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 93 FEKTLKDLKLSYLDVYLIHWPqgfksgDDLFPkddkgnaiggkatFLDAWEAMEELVDEGLVKALGVSNFSHFQIEK--- 169
Cdd:cd19143 106 TKASLKRLQLDYVDLVFCHRP------DPATP-------------IEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEahe 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462615415 170 LLNKPGLkYKPVTNQVECHpYLTQEKL-IQY---CHSKGITVTAYSPLGS 215
Cdd:cd19143 167 IADRLGL-IPPVMEQPQYN-LFHRERVeVEYaplYEKYGLGTTTWSPLAS 214
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
30-160 |
1.35e-06 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; 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: 381390 [Multi-domain] Cd Length: 298 Bit Score: 48.81 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 30 EAVKVAIDAGYRHIDCAYVYQNEHEV-GEAIQekIQEKAVKREDLFIVSK-----LWPTFFERPLVRKAFEKTLKDLKLS 103
Cdd:cd19164 38 DIVRRALELGIRAFDTSPYYGPSEIIlGRALK--ALRDEFPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTD 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 104 YLDVYLIHwpqgfksgDDLFPKDDkgnaiggkatflDAWEAMEELV---DEGLVKALGVS 160
Cdd:cd19164 116 YLDLVYLH--------DVEFVADE------------EVLEALKELFklkDEGKIRNVGIS 155
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
143-247 |
1.42e-06 |
|
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: 48.77 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 143 EAMEELVDEGLVKALGVSNFSHFQIEKllnkpGLKYKPVT-NQVECHPyLTQEKL----IQYCHSKGITVTAYSPL---- 213
Cdd:cd19077 132 KALKELVKEGKIRGIGLSEVSAETIRR-----AHAVHPIAaVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLgrgl 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462615415 214 --GSPDRPWAKPEDPSLLEDP---------------KIKEIAAKHKKTAAQ 247
Cdd:cd19077 206 ltGRIKSLADIPEGDFRRHLDrfngenfeknlklvdALQELAEKKGCTPAQ 256
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
16-162 |
2.03e-06 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 48.09 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 16 VGLGTwkSPLG---------KVKEAVKVAIDAGYRHIDCAYVYQN---EHEVGEAIQEKIQEKAV-----------KRED 72
Cdd:cd19161 3 LGLGT--AGLGnlytavsnaDADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEFVlstkvgrllkpAREG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 73 lfivSKLWPTFFERPL------------VRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGkatfld 140
Cdd:cd19161 81 ----SVPDPNGFVDPLpfeivydysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERHHFAQLMSGG------ 150
|
170 180
....*....|....*....|....
gi 2462615415 141 aWEAMEELVDEGLVKA--LGVSNF 162
Cdd:cd19161 151 -FKALEELKKAGVIKAfgLGVNEV 173
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
36-215 |
1.22e-05 |
|
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: 46.06 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 36 IDAGYRHIDCAYVYQNEHE---VGEAIQEKiqekavkREDLFIVSKLwpTFFERP------------LVRkAFEKTLKDL 100
Cdd:cd19080 41 VEAGGNFIDTANNYTNGTSerlLGEFIAGN-------RDRIVLATKY--TMNRRPgdpnaggnhrknLRR-SVEASLRRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 101 KLSYLDVYLIHWPQGFKSGDDLFpkddkgnaiggkatfldawEAMEELVDEGLVKALGVSN------------------- 161
Cdd:cd19080 111 QTDYIDLLYVHAWDFTTPVEEVM-------------------RALDDLVRAGKVLYVGISDtpawvvarantlaelrgws 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462615415 162 -FSHFQIEkllnkpglkYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLGS 215
Cdd:cd19080 172 pFVALQIE---------YSLLERTPE-------RELLPMARALGLGVTPWSPLGG 210
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
12-213 |
1.27e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 46.14 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 12 KMPIVGLGTWKS-----PLGKVKEAVKVAIDAGYRHIDCAYVY-----QNEHEVGEAIQEKIqekAVKREDLFIVSK--- 78
Cdd:PRK09912 24 RLPALSLGLWHNfghvnALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDF---AAYRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 79 -LWPTFF----ERPLVRKAFEKTLKDLKLSYLDVYLIHwpqgfkSGDDLFPKDDKGNAIGgkatfldaweameELVDEGL 153
Cdd:PRK09912 101 dMWPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSH------RVDENTPMEETASALA-------------HAVQSGK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615415 154 VKALGVSNFSHFQIEK---LLNK---PGLKYKPVTNQVecHPYLTQEKLIQYCHSKGITVTAYSPL 213
Cdd:PRK09912 162 ALYVGISSYSPERTQKmveLLREwkiPLLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPL 225
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
9-252 |
1.35e-05 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) 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(+). 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: 381379 [Multi-domain] Cd Length: 294 Bit Score: 45.60 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 9 TKAKMPIVGLGTwkSPLGKV----------KEAVKVAIDAGYRHIDCAYVYQNEhevgeaIQEKIQEKAVK-----REDL 73
Cdd:cd19153 8 ALGNVSPVGLGT--AALGGVygdgleqdeaVAIVAEAFAAGINHFDTSPYYGAE------SSEAVLGKALAalqvpRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 74 FIVSKLW----PTF-FERPLVRKAFEKTLKDLKLSYLDVYLIHwpqgfksgDDLFPKDDKgnaiggkaTFLDAWEAMEEL 148
Cdd:cd19153 80 TVATKVGryrdSEFdYSAERVRASVATSLERLHTTYLDVVYLH--------DIEFVDYDT--------LVDEALPALRTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615415 149 VDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTnQVECH------------PYLTQEKLIQYCHSKGITVTAYSPLGSP 216
Cdd:cd19153 144 KDEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAV-LSYCHltlqdarlesdaPGLVRGAGPHVINASPLSMGLLTSQGPP 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462615415 217 drPWaKPEDPSLLEDPKikeIAAKHkkTAAQEGSLE 252
Cdd:cd19153 223 --PW-HPASGELRHYAA---AADAV--CASVEASLP 250
|
|
| |
