|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
15-322 |
0e+00 |
|
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: 636.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTYSDPR-PVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHD 93
Cdd:cd19109 1 GNSIPIIGLGTYSEPKtTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 94 PEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNFNRR 173
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 174 QLEVILNKPGLKYKPVTNQVECHPYFTQTKLLEVSASSMtSFIVAYSPLGTCRNPLWVNVSSPPLLKDELLTSLGKKYNK 253
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHD-IVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398962 254 TQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPF 322
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-309 |
4.66e-173 |
|
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: 481.73 E-value: 4.66e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 8 HHIPLNDGNSIPIIGLGTYSdPRPVP-GKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGK 86
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYA-PEEVPkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 87 LWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLG 166
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 167 VSNFNRRQLEVILNKPGLKYKPVTNQVECHPYFTQTKLLEVSASSmTSFIVAYSPLGTCRNPLWVNVSSPPLLKDELLTS 246
Cdd:cd19108 160 VSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSK-DIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398962 247 LGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 309
Cdd:cd19108 239 LAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-326 |
8.08e-148 |
|
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: 417.97 E-value: 8.08e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19107 1 GAKMPILGLGTWKSP---PGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQ 174
Cdd:cd19107 78 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 175 LEVILNKPGLKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTCRNPlWVNVSSPPLLKDELLTSLGKKYNKT 254
Cdd:cd19107 158 IERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIV-VTAYSPLGSPDRP-WAKPEDPSLLEDPKIKEIAAKHNKT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398962 255 QAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPFHDEY 326
Cdd:cd19107 236 TAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
12-309 |
2.48e-129 |
|
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: 371.33 E-value: 2.48e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGK-VKREEIFYCGKLWST 90
Cdd:cd19106 1 LHTGQKMPLIGLGTW---KSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNF 170
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 171 NRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEvSASSMTSFIVAYSPLGTCRNPlWVNVSSPPLLKDELLTSLGKK 250
Cdd:cd19106 158 NSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIA-HCKARGLVVTAYSPLGSPDRP-WAKPDEPVLLEEPKVKALAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 398962 251 YNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 309
Cdd:cd19106 234 YNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
18-326 |
7.72e-122 |
|
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: 351.95 E-value: 7.72e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPEMV 97
Cdd:cd19110 4 IPAVGLGTW---KASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 98 RPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQLEV 177
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 178 ILNKPGLKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTcrnplwvNVSSPPLLKDELLTSLGKKYNKTQAQ 257
Cdd:cd19110 161 LLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVS-VTAYRPLGG-------SCEGVDLIDDPVIQRIAKKHGKSPAQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398962 258 IVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPFHDEY 326
Cdd:cd19110 233 ILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-309 |
5.78e-120 |
|
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: 346.96 E-value: 5.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSDPRPVPGKTfiAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLKDDEGVRQ--AVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKpgeEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSN 169
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 170 FNRRQLEVILNkpGLKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTCRNPLWVNvsSPPLLKDELLTSLGK 249
Cdd:cd19116 158 FNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIV-VMAYSPFGRLVPRGQTN--PPPRLDDPTLVAIAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 250 KYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 309
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
18-300 |
4.08e-115 |
|
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: 332.91 E-value: 4.08e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWSTDHDPEMV 97
Cdd:cd19071 1 MPLIGLGTYKLK---PEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRES----GVPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 98 RPALERTLQTLKLDYIDLYIIEMPMAFKPGEefypkdengrviyHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQLEV 177
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 178 ILNKPglKYKPVTNQVECHPYFTQTKLLEVSAS-SMTsfIVAYSPLGTCRNPLwvnvsspplLKDELLTSLGKKYNKTQA 256
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEhGIV--VQAYSPLGRGRRPL---------LDDPVLKEIAKKYGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 398962 257 QIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 300
Cdd:cd19071 208 QVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-307 |
2.18e-111 |
|
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: 325.52 E-value: 2.18e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 9 HIPLNDGNSIPIIGLGTYsDPRPVPGKTfiAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLW 88
Cdd:cd19154 3 SITLSNGVKMPLIGLGTW-QSKGAEGIT--AVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTC--RNPLWVNVSSPP--LLKDELL 244
Cdd:cd19154 160 NFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNIS-VTSYATLGSPgrANFTKSTGVSPApnLLQDPIV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398962 245 TSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 307
Cdd:cd19154 237 KAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
14-308 |
6.24e-109 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 317.38 E-value: 6.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 14 DGNSIPIIGLGTYsdprPVPGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWSTDH 92
Cdd:COG0656 1 NGVEIPALGLGTW----QLPGEEAAaAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA----SGVPREELFVTTKVWNDNH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMafkPGeefypkdengrviyhksNLCATWEALEACKDAGLVKSLGVSNFNR 172
Cdd:COG0656 73 GYDDTLAAFEESLERLGLDYLDLYLIHWPG---PG-----------------PYVETWRALEELYEEGLIRAIGVSNFDP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 173 RQLEVILNKPGlkYKPVTNQVECHPYFTQTKLLEVSAS-SMTsfIVAYSPLGtcrnplwvnvsSPPLLKDELLTSLGKKY 251
Cdd:COG0656 133 EHLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREhGIV--VEAYSPLG-----------RGKLLDDPVLAEIAEKH 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 252 NKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:COG0656 198 GKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-297 |
2.23e-108 |
|
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: 317.37 E-value: 2.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 9 HIPLNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLW 88
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEefyPKDENGRVIyhKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19125 79 CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTcRNPLWVNvssPPLLKDELLTSLG 248
Cdd:cd19125 154 NFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIH-LSAYSPLGS-PGTTWVK---KNVLKDPIVTKVA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 398962 249 KKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMK 297
Cdd:cd19125 227 EKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFA 275
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-309 |
2.63e-104 |
|
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: 307.42 E-value: 2.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 11 PLNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWST 90
Cdd:cd19123 5 PLSNGDLIPALGLGTW---KSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGeEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNF 170
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 171 NRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTC-RNPLWVNVSSPPLLKDELLTSLGK 249
Cdd:cd19123 161 SVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIH-LTAYSPLGSGdRPAAMKAEGEPVLLEDPVINKIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 250 KYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 309
Cdd:cd19123 238 KHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-302 |
3.96e-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: 270.82 E-value: 3.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAE-GKVKREEIFYCGKLWST 90
Cdd:cd19118 1 LNTGNKIPAIGLGTW---QAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPK-----DENGRVIYHKSNLCATWEALEACKDAGLVKSL 165
Cdd:cd19118 78 SHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavptNGGEVDLDLSVSLVDTWKAMVELKKTGKVKSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 166 GVSNFNRRQLEVILNKPGLkyKPVTNQVECHPYFTQTKLLEVSASSMTsFIVAYSPLGTCRnplwvnVSSPPLLKDELLT 245
Cdd:cd19118 158 GVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNI-HITAYSPLGNNL------AGLPLLVQHPEVK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 246 SLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQifDFSLTKEEMKDIEAL 302
Cdd:cd19118 229 AIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-308 |
4.53e-90 |
|
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: 270.52 E-value: 4.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19111 1 GFPMPVIGLGTYQSP---PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAFKpgeefyPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQ 174
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPCGFV------NKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 175 LEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTcrnPLWVNVSSPP----LLKDELLTSLGKK 250
Cdd:cd19111 152 INKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIV-VTAYAPLGS---PGRANQSLWPdqpdLLEDPTVLAIAKE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 398962 251 YNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19111 226 LDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-303 |
8.30e-89 |
|
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: 266.36 E-value: 8.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWS 89
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQ--IPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS----GIPREELFITTKLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMafkpgeefypkdengrviyhkSNLCATWEALEACKDAGLVKSLGVSN 169
Cdd:cd19133 75 QDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPF---------------------GDVYGAWRAMEELYKEGKIRAIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 170 FNRRQLEVILnkPGLKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTCRNPLwvnvsspplLKDELLTSLGK 249
Cdd:cd19133 134 FYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQ-IEAWGPFAEGRNNL---------FENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398962 250 KYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-307 |
8.49e-89 |
|
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: 268.24 E-value: 8.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 9 HIPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLW 88
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSS---PEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAF--KPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLG 166
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSlsKEDDSGKLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 167 VSNFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSFiVAYSPLGT-CRNPLWVNVSSPP-----LLK 240
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITV-TAYAPLGSpGAAHFSPGTGSPSgsspdLLQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 241 DELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 307
Cdd:cd19155 237 DPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
10-307 |
1.22e-85 |
|
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: 260.11 E-value: 1.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19112 3 ITLNSGHKMPVIGLGVW---RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHdpEMVRPALERTLQTLKLDYIDLYIIEMPMAFKP---GEEFYPKDENGRV-IYHKSNLCATWEALEACKDAGLVKSL 165
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 166 GVSNFnrrqlEVILNKPGLKY---KPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLG-TCRNPLWVNVSSPplLKD 241
Cdd:cd19112 158 GISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGIS-VTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 242 ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 307
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-308 |
1.60e-85 |
|
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: 259.31 E-value: 1.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 13 NDGNSIPIIGLGTYSdprPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDH 92
Cdd:cd19129 1 NGSGAIPALGFGTLI---PDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKS-NLCATWEALEACKDAGLVKSLGVSNFN 171
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 172 RRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSFIvAYSPLGtcrnplwvNVSSPPLLKDELLTSLGKKY 251
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQ-AFAPLG--------HGMEPKLLEDPVITAIARRV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 398962 252 NKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIfdFSLTKEEMKDI-EALNKNVRF 308
Cdd:cd19129 227 NKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
10-314 |
4.37e-85 |
|
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: 258.92 E-value: 4.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSDPRPVPGKTfiaVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQ---IYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK--PGEEFYPK-----DENgRVIYHKSNLCATWEALEACKDAGLV 162
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPgfycgDGD-NFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 163 KSLGVSNFNRRQLEVILNkpGLKYKPVTNQVECHPYFTQTKLLEVsASSMTSFIVAYSPLG-----TCRNPLWVNVssPP 237
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEY-AQKAGITITAYSSFGpqsfvELNQGRALNT--PT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 238 LLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMW 314
Cdd:cd19113 234 LFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDPWDW 310
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-303 |
6.38e-85 |
|
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: 256.53 E-value: 6.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWS 89
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVS---NDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMafkPGEEFYPKdengrviyhksnlcaTWEALEACKDAGLVKSLGVSN 169
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQDKYVE---------------TWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 170 FNRRQLEVILNKPGLKykPVTNQVECHPYFTQTKLLEVSAssmTSFIV--AYSPLGTCRnplwvnvssppLLKDELLTSL 247
Cdd:cd19131 137 FTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHA---KHGIQteSWSPLGQGG-----------LLSDPVIGEI 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 248 GKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:cd19131 201 AEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-302 |
8.24e-83 |
|
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: 251.80 E-value: 8.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 14 DGNSIPIIGLGTYSDPrPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVK-REEIFYCGKLWSTDH 92
Cdd:cd19124 1 SGQTMPVIGMGTASDP-PSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENgrvIYHKSNLCATWEALEACKDAGLVKSLGVSNFNR 172
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 173 RQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTCRNPlWvnvSSPPLLKDELLTSLGKKYN 252
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIH-VTAYSPLGAPGTK-W---GSNAVMESDVLKEIAAAKG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 398962 253 KTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19124 230 KTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-304 |
1.78e-82 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 251.26 E-value: 1.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIRekvAEGkVKREEIFYCGKLWSTD 91
Cdd:cd19117 8 LNTGAEIPAVGLGTW---QSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 92 H-DPEMvrpALERTLQTLKLDYIDLYIIEMPMAFKP-GEEFYPKDENG-RVIYHKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19117 81 HrRVEE---ALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILNKPGLKYKPVTNQVECHPYFTQTKLLEVSASSMTsFIVAYSPLGTcrnplwvnvSSPPLLKDELLTSLG 248
Cdd:cd19117 158 NFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGI-HATAYSPLGS---------TNAPLLKEPVIIKIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 249 KKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIfdFSLTKEEMKDIEALNK 304
Cdd:cd19117 228 KKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
12-308 |
1.55e-80 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 245.76 E-value: 1.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYSDPRpvpGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWST 90
Cdd:cd19157 4 LNNGVKMPWLGLGVFKVEE---GSEVVnAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPmafkpGEEFYpKDengrviyhksnlcaTWEALEACKDAGLVKSLGVSNF 170
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWP-----VKGKY-KE--------------TWKALEKLYKDGRVRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 171 NRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSFiVAYSPLGTCRnplwvnvssppLLKDELLTSLGKK 250
Cdd:cd19157 137 QVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQL-EAWSPLMQGQ-----------LLDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 398962 251 YNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19157 203 YNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-300 |
5.95e-80 |
|
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: 243.33 E-value: 5.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYSDPrpvpGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDPEM 96
Cdd:cd19073 1 IPALGLGTWQLR----GDDCAnAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 97 VRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLE 176
Cdd:cd19073 73 LKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEE-------------------TLGALKELKEAGKVKSIGVSNFTIELLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 177 VILNKPGLKykPVTNQVECHPYFTQTKLLEVsASSMTSFIVAYSPLG-TCrnplwvnvssppLLKDELLTSLGKKYNKTQ 255
Cdd:cd19073 134 EALDISPLP--IAVNQVEFHPFLYQAELLEY-CRENDIVITAYSPLArGE------------VLRDPVIQEIAEKYDKTP 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 398962 256 AQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 300
Cdd:cd19073 199 AQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
18-302 |
1.22e-79 |
|
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: 243.31 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYSdprpVPGKTFI--AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPE 95
Cdd:cd19136 1 MPILGLGTFR----LRGEEEVrqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 96 MVRPALERTLQTLKLDYIDLYIIEMPMAFKpgeeFYPKDENgrviyHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQL 175
Cdd:cd19136 77 KARAACLGSLERLGTDYLDLYLIHWPGVQG----LKPSDPR-----NAELRRESWRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 176 EVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTsFIVAYSPLGTcrnplwvnvSSPPLLKDELLTSLGKKYNKTQ 255
Cdd:cd19136 148 EELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGI-HLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 398962 256 AQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19136 216 AQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
12-308 |
1.24e-79 |
|
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: 245.02 E-value: 1.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYSDPRPVPGKTfiaVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTD 91
Cdd:cd19115 7 LNSGYDMPLVGFGLWKVNNDTCADQ---VYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 92 HDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK---PGEEFYP--KDENGRVIYHKSNLCATWEALEACKDAGLVKSLG 166
Cdd:cd19115 84 HDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 167 VSNFNrRQLEVILnkpgLKY---KPVTNQVECHPYFTQTKLLEVsASSMTSFIVAYSPLGtcrnPLWV-------NVSSP 236
Cdd:cd19115 164 VSNFS-AQLLMDL----LRYariRPATLQIEHHPYLTQPRLVKY-AQKEGIAVTAYSSFG----PQSFleldlpgAKDTP 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398962 237 PLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19115 234 PLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-303 |
3.70e-77 |
|
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: 236.57 E-value: 3.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSDPRPvpGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWS 89
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDG--DETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEefypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSN 169
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFID--------------------TWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 170 FNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTCRnplwvnvssppLLKDELLTSLGK 249
Cdd:cd19126 135 FQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIV-VEAWSPLGQGG-----------LLSNPVLAAIGE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398962 250 KYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:cd19126 201 KYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
19-302 |
1.39e-76 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 235.88 E-value: 1.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 19 PIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPEMVR 98
Cdd:cd19128 2 PRLGFGTYKIT---ESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 99 PALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQLEVI 178
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 179 LNKpgLKYKPVTNQVECHPYFTQTKLLEVSASSmTSFIVAYSPL-GTCRNPLWVnvssppLLKDELLTSLGKKYNKTQAQ 257
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIEN-NIHVTAYRPLgGSYGDGNLT------FLNDSELKALATKYNTTPPQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 398962 258 IVLRFDIQRGL---VVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19128 230 VIIAWHLQKWPknySVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-303 |
3.23e-76 |
|
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: 234.09 E-value: 3.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYsdprPVPGKT-FIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWST 90
Cdd:cd19132 1 LNDGTQIPAIGFGTY----PLKGDEgVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMafkPGEEFYpkdengrviyhksnlCATWEALEACKDAGLVKSLGVSNF 170
Cdd:cd19132 73 HHGYEEALRTIEESLYRLGLDYVDLYLIHWPN---PSRDLY---------------VEAWQALIEAREEGLVRSIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 171 NRRQLEVILNKPGLKykPVTNQVECHPYFTQTKLLEVSASSMtsfIV--AYSPLGTCRNplwvnvssppLLKDELLTSLG 248
Cdd:cd19132 135 LPEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHG---IVtqSWSPLGRGSG----------LLDEPVIKAIA 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398962 249 KKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:cd19132 200 EKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
12-302 |
4.12e-76 |
|
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: 234.73 E-value: 4.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGkVKREEIFYCGKLWSTD 91
Cdd:cd19121 6 LNTGASIPAVGLGTWQAK---AGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 92 HDpeMVRPALERTLQTLKLDYIDLYIIEMPMAFKP--GEEFYPKDENG-RVIYHKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19121 82 HR--RVELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGsRDLDWDWNHVDTWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILnkPGLKYKPVTNQVECHPYFTQTKLLEVSASSMTsFIVAYSPLGTcrnplwvnvSSPPLLKDELLTSLG 248
Cdd:cd19121 160 NYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGI-LIEAYSPLGS---------TGSPLISDEPVVEIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398962 249 KKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFslTKEEMKDIEAL 302
Cdd:cd19121 228 KKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-303 |
8.80e-76 |
|
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: 233.45 E-value: 8.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWS 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP---PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMafkpgeefyPKDENGRViyhksnlcATWEALEACKDAGLVKSLGVSN 169
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------PNDFDRTI--------QAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 170 FNRRQLEVILNKPGLKykPVTNQVECHPYFTQTKLLEVSASSMtsfIV--AYSPLGTCRNPLWVNVSSPP-LLKDELLTS 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLG---IVtqAWSPIGGVMRYGASGPTGPGdVLQDPTITG 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 247 LGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:cd19127 212 LAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-302 |
4.71e-75 |
|
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: 230.99 E-value: 4.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQ 174
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAE-------------------TLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 175 LE--VILNKPGLkykpVTNQVECHPYFTQTKLLEvSASSMTSFIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYN 252
Cdd:cd19140 139 LReaVELSEAPL----FTNQVEYHPYLDQRKLLD-AAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHG 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 398962 253 KTQAQIVLRFDIQR-GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19140 203 KTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-308 |
1.68e-74 |
|
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: 230.20 E-value: 1.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGT----YSDPRPVPGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWS 89
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLVdSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPemvRPALERTLQTLKLDYIDLYIIEMPMAFKPGeefypkdengrviyhKSNLCATWEALEACKDAGLVKSLGVSN 169
Cdd:cd19120 77 GIKDP---REALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 170 FNRRQLEVILNKPglKYKPVTNQVECHPYFT--QTKLLEVSASSMtsfIV--AYSPLgtcrNPLWVNVSSPpllKDELLT 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHG---IVvsAYSPL----SPLTRDAGGP---LDPVLE 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398962 246 SLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19120 207 KIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-308 |
3.39e-73 |
|
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: 227.02 E-value: 3.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYSDPRPvpGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWSTD 91
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDG--AEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 92 HDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPgeefypKDengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFN 171
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKF------KD--------------TWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 172 RRQLEVILNKpgLKYKPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGtcrnplwvnvsSPPLLKDELLTSLGKKY 251
Cdd:cd19156 137 EHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIA-VEAWSPLG-----------QGKLLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 252 NKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-303 |
4.91e-72 |
|
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: 223.63 E-value: 4.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 9 HIPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLW 88
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVP---PADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMafkPGeefypkdengrviyhKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPT---PA---------------AGNYVHTWEAMIELRAAGRTRSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILNKPGLKykPVTNQVECHPYFTQTKLLEVSASSMTSfIVAYSPLGTCRnplwvnvssppLLKDELLTSLG 248
Cdd:cd19130 136 NFLPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVK-IEAWSPLGQGK-----------LLGDPPVGAIA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398962 249 KKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:cd19130 202 AAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-302 |
2.60e-71 |
|
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: 222.20 E-value: 2.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 9 HIPLNDGNSIPIIGLGTYSdprpVPGKTFIAVKTAIDE-GYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKL 87
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSH----SGGYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 88 WSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyHKSNLCATWEALEACKDAGLVKSLGV 167
Cdd:cd19135 76 WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN------------VKETRAETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 168 SNFNRRQLEVILNKPGLKykPVTNQVECHPYFTQTKLLEVSASSMTSFiVAYSPLgtcrnplwvnvSSPPLLKDELLTSL 247
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVF-EGYCPL-----------AKGKALEEPTVTEL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398962 248 GKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19135 210 AKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
10-307 |
1.79e-70 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 220.33 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTY--SDPRPVpgktfIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKL 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWqaSNEEVI-----TAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 88 WSTDHDPemVRPALERTLQTLKLDYIDLYIIEMPMAfkpgeefypkdengrviyHKSNLCATWEALEACKDAGLVKSLGV 167
Cdd:PRK11565 78 WNDDHKR--PREALEESLKKLQLDYVDLYLMHWPVP------------------AIDHYVEAWKGMIELQKEGLIKSIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 168 SNFNRRQLEVILNKPGLKykPVTNQVECHPYFTQTKLlevSASSMTSFIV--AYSPLGTCRNplwvNVSSPPLLKDellt 245
Cdd:PRK11565 138 CNFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQL---HAWNATHKIQteSWSPLAQGGK----GVFDQKVIRD---- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398962 246 sLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 307
Cdd:PRK11565 205 -LADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-308 |
4.64e-70 |
|
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: 219.68 E-value: 4.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTYSdPRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19119 4 FKLNTGASIPALGLGTAS-PHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDHDPemVRPALERTLQTLKLDYIDLYIIEMPMAFK-----PGEEFYPKDENGRVIYHKS-NLCATWEALEACKDAGLVK 163
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASgDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 164 SLGVSNFNRRQLEVILNKpgLKYKPVTNQVECHPYFTQTKLLEVSASSMTsFIVAYSPLGTcrnplwvnvSSPPLLKDEL 243
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGI-LVTAYSPLGS---------HGAPNLKNPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 244 LTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIfdFSLTKEEMKDIE--ALNKNVRF 308
Cdd:cd19119 229 VKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDdiGEKYPVRF 293
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-308 |
1.71e-69 |
|
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: 218.58 E-value: 1.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAFK---PGEEFYPKDENGRVI---YHKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKELKkfpLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEvSASSMTSFIVAYSPLGtcrNPLWVNVSS-----PPLLKDEL 243
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLID-WAKKQGIQITAYSSFG---NAVYTKVTKhlkhfTNLLEHPV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398962 244 LTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19114 232 VKKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-308 |
1.26e-63 |
|
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: 202.39 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 10 IPLNDGNSIPIIGLGTY--SDprpvpGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKL 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGelSD-----DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 88 WSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAfkpgeefypkdengrviyHKSNLCATWEALEACKDAGLVKSLGV 167
Cdd:cd19134 74 ATPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 168 SNFNRRQLEVILNKPGlkYKPVTNQVECHPYFTQTKLLEVSASSmTSFIVAYSPLGTCRnplwvnvssppLLKDELLTSL 247
Cdd:cd19134 136 SNFTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQH-GIVTQAYSPLGVGR-----------LLDNPAVTAI 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398962 248 GKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 308
Cdd:cd19134 202 AAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
12-304 |
6.05e-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: 193.61 E-value: 6.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 12 LNDGNSIPIIGLGTYSDpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEG-KVKREEIFYCGKLWST 90
Cdd:cd19122 3 LNNGVKIPAVGFGTFAN-EGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPK-DENGRVIYHKS---NLCATWEALEACKDAGLVKSLG 166
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILKDlteNPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 167 VSNFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLEVSASSmTSFIVAYSPLGTCRNplwVNVSSPPLLKDELLTS 246
Cdd:cd19122 162 VSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSN-DILPEAYSPLGSQNQ---VPSTGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 398962 247 LGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSltkeeMKDIEALNK 304
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELS-----DEDFEAINQ 288
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-302 |
4.58e-58 |
|
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: 187.56 E-value: 4.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDPEMV 97
Cdd:cd19139 1 IPAFGLGTF---RLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 98 RPALERTLQTLKLDYIDLYIIEMPmafkpgeefypkDENGRViyhksNLCATWEALEACKDAGLVKSLGVSNFNRRQLEV 177
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIHWP------------SPNDEV-----PVEEYIGALAEAKEQGLTRHIGVSNFTIALLDE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 178 ILNKPGlKYKPVTNQVECHPYFtQTKLLEVSASSMTSFIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQ 257
Cdd:cd19139 137 AIAVVG-AGAIATNQIELSPYL-QNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQ 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 398962 258 IVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19139 204 IALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-300 |
2.47e-51 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 170.49 E-value: 2.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTY------SDPRPVPGKTFIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFYCG 85
Cdd:cd19072 1 GEEVPVLGLGTWgigggmSKDYSDDKKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 86 KLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSL 165
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEE-------------------TLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 166 GVSNFNRRQLEVILNKPGlKYKPVTNQVECHPYFT--QTKLLE-VSASSMTsfIVAYSPLG---TCRNPLwvnvssppll 239
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYNLFDReeESGLLPyCQKNGIA--IIAYSPLEkgkLSNAKG---------- 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398962 240 kDELLTSLGKKYNKTQAQIVLRFDIQR-GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 300
Cdd:cd19072 203 -SPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
21-303 |
1.20e-50 |
|
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: 169.80 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTYS----DPRPVPGKTFIAVKTAIDEGYRHIDGAYVYR---NEHEVGEAIREKvaegKVKREEIFYCGKL------ 87
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 88 WSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGV 167
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEE-------------------TWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 168 SNFNRRQLEVILNKPglKYKPVTNQVECHPYF--TQTKLLEVSASSMTSFIvAYSPLG----------------TCRNPL 229
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLI-AYSPLGgglltgkytrdpdkgpGERRRL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 230 WVNVSSPPLLKDELLTSLGKKYNKTQAQIVLRF--DIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 303
Cdd:pfam00248 215 LKKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-309 |
3.12e-48 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 162.89 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 17 SIPIIGLGTYSdprpVPGKTFIA-VKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDPE 95
Cdd:PRK11172 2 SIPAFGLGTFR----LKDQVVIDsVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 96 MVRPALERTLQTLKLDYIDLYIIEMPMafkpgeefyPKDEngrviyhkSNLCATWEALEACKDAGLVKSLGVSNFNRRQL 175
Cdd:PRK11172 74 KLIPSLKESLQKLRTDYVDLTLIHWPS---------PNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTIALM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 176 EVILNKPGlKYKPVTNQVECHPYFTQTKLLEVsASSMTSFIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQ 255
Cdd:PRK11172 137 KQAIAAVG-AENIATNQIELSPYLQNRKVVAF-AKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398962 256 AQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 309
Cdd:PRK11172 204 AQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-300 |
3.70e-39 |
|
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: 138.92 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 8 HHIPLNDGNSIPIIGLGT-YSDPRPVPGKTFI-AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIF 82
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTwYMGEDPAKRAQEIeALRAGIDLGMTLIDTAEMYgdgGSEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 83 YCGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAfkpgeefYPKDEngrviyhksnlcaTWEALEACKDAGLV 162
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-------VPLAE-------------TVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 163 KSLGVSNFNRRQLEVILNKPGLKyKPVTNQVECH-----------PYFTQTKLLevsassmtsfIVAYSPLGTCRNPlwv 231
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYNlgsrgieydllPWCREHGVP----------VMAYSPLAQGGLL--- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 232 nvsSPPLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVV-IPKSTTPERIKENFQIFDFSLTKEEMKDIE 300
Cdd:cd19138 200 ---RRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-297 |
5.82e-38 |
|
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: 135.78 E-value: 5.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGT----------YSDPRPVPGktfiAVKTAIDEGYRHIDGAYVYRNEHE---VGEAIREkvaegkVKREEI 81
Cdd:cd19137 1 GEKIPALGLGTwgiggfltpdYSRDEEMVE----LLKTAIELGYTHIDTAEMYGGGHTeelVGKAIKD------FPREDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 82 FYCGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGL 161
Cdd:cd19137 71 FIVTKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 162 VKSLGVSNFNRRQLEVILNKpgLKYKPVTNQVECHPY---FTQTKLLEVSASSMTSfIVAYSPLgtcrnplwvnvSSPPL 238
Cdd:cd19137 132 IRYIGVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGIT-VVAYSPL-----------RRGLE 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 239 LKDELLTSLGKKYNKTQAQIVLRFDIQR-GLVVIPKSTTPERIKENFQIFDFSLTKEEMK 297
Cdd:cd19137 198 KTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMK 257
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
39-300 |
3.18e-33 |
|
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: 124.26 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVAegkvkREEIFYCGKLWST--DHDPEMVRPALERTLQTLKLDYI 113
Cdd:cd19093 31 AFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATKFAPLpwRLTRRSVVKALKASLERLGLDSI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 114 DLYIIEMPmafkpgEEFYPKDengrviyhksnlCATWEALEACKDAGLVKSLGVSNFNRRQLEVI---LNKPGlkYKPVT 190
Cdd:cd19093 106 DLYQLHWP------GPWYSQI------------EALMDGLADAVEEGLVRAVGVSNYSADQLRRAhkaLKERG--VPLAS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 191 NQVE---CHPYFTQTKLLEV-SASSMTsfIVAYSPLG--------TCRNP------------LWVNVssPPLLkdELLTS 246
Cdd:cd19093 166 NQVEyslLYRDPEQNGLLPAcDELGIT--LIAYSPLAqglltgkySPENPppggrrrlfgrkNLEKV--QPLL--DALEE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398962 247 LGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 300
Cdd:cd19093 240 IAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-300 |
4.35e-31 |
|
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: 118.40 E-value: 4.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYS----DPRPVPGKTFI-AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIrekvaegKVKREEIFY---CGK 86
Cdd:cd19084 4 VSRIGLGTWAiggtWWGEVDDQESIeAIKAAIDLGINFFDTAPVYgfgHSEEILGKAL-------KGRRDDVVIatkCGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 87 LWSTDH------DPEMVRPALERTLQTLKLDYIDLYIIEMPmafkpgeefypkDengrviyHKSNLCATWEALEACKDAG 160
Cdd:cd19084 77 RWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------D-------PNTPIEETAEALEKLKKEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 161 LVKSLGVSNFNRRQLEVIlnkpgLKY-KPVTNQVechPY--FTQ---TKLLEVSASSMTSFIvAYSPLGT---------- 224
Cdd:cd19084 138 KIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVL-PYGPLAQglltgkykke 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 225 -------CRNPLwVNVSSPPLLKD----ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSL 291
Cdd:cd19084 209 ptfppddRRSRF-PFFRGENFEKNleivDKLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGALDWEL 287
|
....*....
gi 398962 292 TKEEMKDIE 300
Cdd:cd19084 288 TEEELKEID 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-302 |
1.58e-29 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 114.89 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 13 NDGNSIPIIGLGTYS---DPRPVPGKTFIA-VKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvKREEIFYCG 85
Cdd:COG0667 8 RSGLKVSRLGLGTMTfggPWGGVDEAEAIAiLDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 86 KL--------WSTDHDPEMVRPALERTLQTLKLDYIDLYII-----EMPMafkpgEEfypkdengrviyhksnlcaTWEA 152
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLhrpdpDTPI-----EE-------------------TLGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 153 LEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKYKPVTNQVEchpY--FTQT---KLLEVSASSMTSFIvAYSPL----- 222
Cdd:COG0667 138 LDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVL-AYSPLaggll 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 223 ------------GTCRNPLWVNVSSPPLLKD--ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQI 286
Cdd:COG0667 214 tgkyrrgatfpeGDRAATNFVQGYLTERNLAlvDALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAA 293
|
330
....*....|....*.
gi 398962 287 FDFSLTKEEMKDIEAL 302
Cdd:COG0667 294 ADLELSAEDLAALDAA 309
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
21-302 |
2.92e-26 |
|
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: 105.58 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGT--------YSDPRPVPGKTFiaVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvKREEIFYCGK--- 86
Cdd:cd19083 14 IGLGTnavgghnlYPNLDEEEGKDL--VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgah 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 87 LWST-----DHDPEMVRPALERTLQTLKLDYIDLYIIEMPmafkpgEEFYPKDEngrviyhksnlcaTWEALEACKDAGL 161
Cdd:cd19083 86 KFGGdgsvlNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP------DGETPKAE-------------AVGALQELKDEGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 162 VKSLGVSNFNRRQLEViLNKPGL------KYKPVTNQVECH--PYFTQTKLlevsassmtSFI----VAYSPLGTCRNPl 229
Cdd:cd19083 147 IRAIGVSNFSLEQLKE-ANKDGYvdvlqgEYNLLQREAEEDilPYCVENNI---------SFIpyfpLASGLLAGKYTK- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 230 wvNVSSPP------------------LLKDELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDF 289
Cdd:cd19083 216 --DTKFPDndlrndkplfkgerfsenLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDV 293
|
330
....*....|...
gi 398962 290 SLTKEEMKDIEAL 302
Cdd:cd19083 294 TLTEEEIAFIDAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-306 |
4.74e-26 |
|
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: 104.98 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYSdprPVPGKTFI---------AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCG 85
Cdd:cd19085 1 VSRLGLGCWQ---FGGGYWWGdqddeesiaTIHAALDAGINFFDTAEAYgdgHSEEVLGKALKGR-------RDDVVIAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 86 KLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSL 165
Cdd:cd19085 71 KVSPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEE-------------------TMEALEKLKEEGKIRAI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 166 GVSNFNRRQLEVILnKPGlkyKPVTNQVECHPYFTQ--TKLLEVSASSMTSfIVAYSPL-----------------GTCR 226
Cdd:cd19085 132 GVSNFGPAQLEEAL-DAG---RIDSNQLPYNLLWRAieYEILPFCREHGIG-VLAYSPLaqglltgkfssaedfppGDAR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 227 NPLwVNVSSPPLLKD-----ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDI 299
Cdd:cd19085 207 TRL-FRHFEPGAEEEtfealEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
....*..
gi 398962 300 EALNKNV 306
Cdd:cd19085 286 DEISDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-285 |
5.58e-23 |
|
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: 94.89 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTYSDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVaegkvKREEIFYCGKL--------W 88
Cdd:cd06660 3 LGLGTMTFGGDGDEEEAFAlLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-----NRDDVVIATKGghppggdpS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPmafkpgEEFYPKDEngrviyhksnlcaTWEALEACKDAGLVKSLGVS 168
Cdd:cd06660 78 RSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFNRRQLEVILN--KPGLKYKPVTNQV------------ECHPYFTQTKLLevsassmtsfIVAYSPLGtcRNPlwvnvs 234
Cdd:cd06660 139 NWSAERLAEALAyaKAHGLPGFAAVQPqyslldrspmeeELLDWAEENGLP----------LLAYSPLA--RGP------ 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 398962 235 sppllkdelltslgkkynktqAQIVLRFDIQRGLV--VIPKSTTPERIKENFQ 285
Cdd:cd06660 201 ---------------------AQLALAWLLSQPFVtvPIVGARSPEQLEENLA 232
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-305 |
2.43e-22 |
|
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: 95.20 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 13 NDGNSIPIIGLGT-----YSDPRPVPGKTFIAVKTAIDEGYRHIDGAYVYR-NEHEVGEAIreKVAEGKvkREEIFYCGK 86
Cdd:cd19144 8 RNGPSVPALGFGAmglsaFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWF--KQNPGK--REKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 87 L----------WSTDHDPEMVRPALERTLQTLKLDYIDLYiiempmafkpgeefYPKDENGRVIYHKsnlcaTWEALEAC 156
Cdd:cd19144 84 FgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLY--------------YQHRVDGKTPIEK-----TVAAMAEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 157 KDAGLVKSLGVSNFN----RRQLEVilnkpglkyKPVTN-QVECHPYFT-----QTKLLEvSASSMTSFIVAYSPLGtcR 226
Cdd:cd19144 145 VQEGKIKHIGLSECSaetlRRAHAV---------HPIAAvQIEYSPFSLdierpEIGVLD-TCRELGVAIVAYSPLG--R 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 227 NPLWVNVSSP------------PLLKDE----------LLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKE 282
Cdd:cd19144 213 GFLTGAIRSPddfeegdfrrmaPRFQAEnfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEE 292
|
330 340
....*....|....*....|...
gi 398962 283 NFQIFDFSLTKEEMKDIEALNKN 305
Cdd:cd19144 293 NLGALKVKLTEEEEKEIREIAEE 315
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
39-295 |
5.26e-20 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 88.28 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKvaegKVKREEIFY---CG-KLWST---------DHDPEMVRPALE 102
Cdd:COG4989 36 LIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELqtkCGiRLPSEardnrvkhyDTSKEHIIASVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 103 RTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLEViLNKp 182
Cdd:COG4989 112 GSLRRLGTDYLDLLLLHRPDPLMDPEE-------------------VAEAFDELKASGKVRHFGVSNFTPSQFEL-LQS- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 183 GLKYKPVTNQVECHPyfTQTKLLEVS--ASSMTSFIV--AYSPLGTCRnplWVNVSSPPLLK-DELLTSLGKKYNKTQAQ 257
Cdd:COG4989 171 ALDQPLVTNQIELSL--LHTDAFDDGtlDYCQLNGITpmAWSPLAGGR---LFGGFDEQFPRlRAALDELAEKYGVSPEA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 398962 258 IVLRFdIQR---GLVVIPKSTTPERIKENFQIFDFSLTKEE 295
Cdd:COG4989 246 IALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
39-295 |
1.19e-19 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 87.23 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKvaegKVKREEIFY---CG-KLWST---------DHDPEMVRPALE 102
Cdd:cd19092 29 LIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIqtkCGiRLGDDprpgrikhyDTSKEHILASVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 103 RTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLEvILNKp 182
Cdd:cd19092 105 GSLKRLGTDYLDLLLLHRPDPLMDPEE-------------------VAEAFDELVKSGKVRYFGVSNFTPSQIE-LLQS- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 183 GLKYKPVTNQVECHPYFT---------QTKLLEVSassmtsfIVAYSPLGTCRnplwvnVSSPPLLKDE----LLTSLGK 249
Cdd:cd19092 164 YLDQPLVTNQIELSLLHTeaiddgtldYCQLLDIT-------PMAWSPLGGGR------LFGGFDERFQrlraALEELAE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 398962 250 KYNKTQAQIVLRFdIQR---GLVVIPKSTTPERIKENFQIFDFSLTKEE 295
Cdd:cd19092 231 EYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-302 |
2.95e-19 |
|
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: 86.19 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFY---CGKLW------STDHDPEMVRPALERTLQ 106
Cdd:cd19102 31 AIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVatkCGLLWdeegriRRSLKPASIRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 107 TLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLEVIlnkpgLKY 186
Cdd:cd19102 104 RLGVDVIDLYQIHWPDPDEPIEE-------------------AWGALAELKEEGKVRAIGVSNFSVDQMKRC-----QAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 187 KPVT-NQVechPYF-----TQTKLLEVSASSMTSFIVaYSPLG----TCR------NPLWVN-------VSSPPLLKD-- 241
Cdd:cd19102 160 HPIAsLQP---PYSllrrgIEAEILPFCAEHGIGVIV-YSPMQsgllTGKmtpervASLPADdwrrrspFFQEPNLARnl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 242 ---ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19102 236 alvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-168 |
5.03e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 81.76 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYSDPRpVPGKTFIA-VKTAIDEGYRHIDGAYVYRNEHE-VGEAIREKvaegkvkREEIFYCGKLWStdHDPE 95
Cdd:cd19100 11 VSRLGFGGGPLGR-LSQEEAAAiIRRALDLGINYFDTAPSYGDSEEkIGKALKGR-------RDKVFLATKTGA--RDYE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398962 96 MVRPALERTLQTLKLDYIDLYIIEMPmafKPGEEFYPKDENGRVIyhksnlcatwEALEACKDAGLVKSLGVS 168
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLHAV---DTEEDLDQVFGPGGAL----------EALLEAKEEGKIRFIGIS 140
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
19-168 |
5.18e-18 |
|
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: 82.22 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 19 PIIGLGTY---SDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVYRN-EHEVGEAIREkvaegkVKREEIFYCGKL-----W 88
Cdd:cd19090 1 SALGLGTAglgGVFGGVDDDEAVAtIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPkdenGRVIyhksnlcatwEALEACKDAGLVKSLGVS 168
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGLG 140
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-292 |
1.29e-17 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 80.72 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGT------YSDPRPVPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIRE---------KVaeGKVKR 78
Cdd:cd19088 1 VSRLGYGAmrltgpGIWGPPADREEAIAVlRRALELGVNFIDTADSYgpdVNERLIAEALHPypddvviatKG--GLVRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 79 EeifycGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKD 158
Cdd:cd19088 79 G-----PGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEE-------------------QLGALAELQD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 159 AGLVKSLGVSNFNRRQLEVILNKPGLkykpVTNQVECHPYFTQT-KLLEVSASSMTSFIvAYSPLGtcrnplwvnvSSPP 237
Cdd:cd19088 135 EGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFI-PWFPLG----------GGDL 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398962 238 LLKDELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLT 292
Cdd:cd19088 200 AQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-168 |
1.61e-16 |
|
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: 77.52 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTYSDPRPVPGKT-----FIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEI---------FY 83
Cdd:cd19086 6 IGFGTWGLGGDWWGDVddaeaIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVviatkfgnrFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 84 CGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEmpmafKPGEEFYPKDEngrviyhksnlcaTWEALEACKDAGLVK 163
Cdd:cd19086 79 GGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLH-----NPPDEVLDNDE-------------LFEALEKLKQEGKIR 140
|
....*
gi 398962 164 SLGVS 168
Cdd:cd19086 141 AYGVS 145
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-301 |
5.98e-16 |
|
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: 76.93 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNS---IPIIGLGTYS---DPRPVPGKTFIAVKT---AIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIF 82
Cdd:cd19149 5 GKSgieASVIGLGTWAiggGPWWGGSDDNESIRTihaALDLGINLIDTAPAYgfgHSEEIVGKAIKGR-------RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 83 Y---CGKLW----------STDHD------PEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhk 143
Cdd:cd19149 78 LatkCGLRWdreggsfffvRDGVTvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEE-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 144 snlcaTWEALEACKDAGLVKSLGVSNFNRRQLevilnKPGLKYKPV-TNQVechPY-----FTQTKLLEVSASSMTSFIv 217
Cdd:cd19149 144 -----TMEALEELKRQGKIRAIGASNVSVEQI-----KEYVKAGQLdIIQE---KYsmldrGIEKELLPYCKKNNIAFQ- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 218 AYSPL-----------------GTCRN--PLWVNVSSPPLLK-DELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKST 275
Cdd:cd19149 210 AYSPLeqglltgkitpdrefdaGDARSgiPWFSPENREKVLAlLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGAR 289
|
330 340
....*....|....*....|....*.
gi 398962 276 TPERIKENFQIFDFSLTKEEMKDIEA 301
Cdd:cd19149 290 KPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-168 |
6.02e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 76.08 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYSDPRPVPGktfiAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFYCGKLWSTDH-- 92
Cdd:cd19105 13 VSRLGFGGGGLPRESPE----LLRRALDLGINYFDTAEGYgngNSEEIIGEALK------GLRRDKVFLATKASPRLDkk 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMafkpGEEFYPKDENGRviyhksnlcatwEALEACKDAGLVKSLGVS 168
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLHGVD----TPEERLLNEELL------------EALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
13-299 |
1.17e-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: 76.10 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 13 NDGNSIPIIGLGT------YSDPrpvPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIF 82
Cdd:cd19076 7 TQGLEVSALGLGCmgmsafYGPA---DEEESIATlHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 83 Y---CGKLWS-------TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEA 152
Cdd:cd19076 77 IatkFGIVRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEE-------------------TVGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 153 LEACKDAGLVKSLGVSNFN----RR----------QLEvilnkpglkYKPVTNQVECHPYFTqTKLLEVSassmtsfIVA 218
Cdd:cd19076 138 MAELVEEGKVRYIGLSEASadtiRRahavhpitavQSE---------YSLWTRDIEDEVLPT-CRELGIG-------FVA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 219 YSPLGtcRNPLWVNVSSPPLLKD----------------------ELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKS 274
Cdd:cd19076 201 YSPLG--RGFLTGAIKSPEDLPEddfrrnnprfqgenfdknlklvEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGT 278
|
330 340
....*....|....*....|....*
gi 398962 275 TTPERIKENFQIFDFSLTKEEMKDI 299
Cdd:cd19076 279 KRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-168 |
4.13e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 74.66 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTYS-DPRPVPGKTFI-AVKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKVAEGKVKREEIFYC---GKLwsTDH 92
Cdd:cd19099 6 LGLGTYRgDSDDETDEEYReALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVtkaGYI--PGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRP--------------------------------ALERTLQTLKLDYIDLYII---EMPMAFKPGEEFYPKDEng 137
Cdd:cd19099 84 GDEPLRPlkyleeklgrglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLhnpEEQLLELGEEEFYDRLE-- 161
|
170 180 190
....*....|....*....|....*....|.
gi 398962 138 rviyhksnlcATWEALEACKDAGLVKSLGVS 168
Cdd:cd19099 162 ----------EAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-300 |
1.10e-14 |
|
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: 73.43 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTYS---DPRPVPGKTFIAV-KTAIDEGYRHIDGAYVY------RNEHEVGEAIReKVAEgkvKREEIFYC------ 84
Cdd:cd19077 8 IGLGLMGltwRPNPTPDEEAFETmKAALDAGSNLWNGGEFYgppdphANLKLLARFFR-KYPE---YADKVVLSvkggld 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 85 GKLWSTDHDPEMVRPALERTLQTLK-LDYIDLYiiempmafkpgeefypkdENGRV-----IYHksnlcaTWEALEACKD 158
Cdd:cd19077 84 PDTLRPDGSPEAVRKSIENILRALGgTKKIDIF------------------EPARVdpnvpIEE------TIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 159 AGLVKSLGVSNFN----RRQLEVilnkpglkYKPVTNQVECHPYFTqtkllEVSASSMTSF-------IVAYSPLGtcRN 227
Cdd:cd19077 140 EGKIRGIGLSEVSaetiRRAHAV--------HPIAAVEVEYSLFSR-----EIEENGVLETcaelgipIIAYSPLG--RG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 228 PLWVNVSSPPLLKD----------------------ELLTSLGKKYNKTQAQIVLRFDIQRG---LVVIPKSTTPERIKE 282
Cdd:cd19077 205 LLTGRIKSLADIPEgdfrrhldrfngenfeknlklvDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEE 284
|
330
....*....|....*...
gi 398962 283 NFQIFDFSLTKEEMKDIE 300
Cdd:cd19077 285 NLKAANVELTDEELKEIN 302
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
19-171 |
1.38e-14 |
|
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: 72.27 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 19 PIIGLGTYS--DPRPVP--GKTFIAVKTAIDEGYRHIDGAYVY-RNEHEVGEAIREkvaegkVKREEIFYCGKLWST--- 90
Cdd:cd19095 1 SVLGLGTSGigRVWGVPseAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 91 -----DHDPEMVRPALERTLQTLKLDYIDLYIIEmpmafKPGEEfypkDENGRVIyhksnlcatwEALEACKDAGLVKSL 165
Cdd:cd19095 75 grdrkDFSPAAIRASIERSLRRLGTDYIDLLQLH-----GPSDD----ELTGEVL----------ETLEDLKAAGKVRYI 135
|
....*.
gi 398962 166 GVSNFN 171
Cdd:cd19095 136 GVSGDG 141
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-179 |
9.18e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 71.00 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 15 GNSIPIIGLGTYSDPRpVPGKTFIA-VKTAIDEGYRHIDGAYVYRN-EHEVGEAIREKvaegkvkREEIFYCGKLWSTDH 92
Cdd:COG1453 10 GLEVSVLGFGGMRLPR-KDEEEAEAlIRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLPPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMAfkpgEEFYPK--DENGrviyhksnlcaTWEALEACKDAGLVKSLGVSNF 170
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIHGLNT----EEDLEKvlKPGG-----------ALEALEKAKAEGKIRHIGFSTH 146
|
....*....
gi 398962 171 NRrqLEVIL 179
Cdd:COG1453 147 GS--LEVIK 153
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
43-302 |
1.67e-13 |
|
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: 69.90 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 43 AIDEGYRHIDGAYVY----RNEHE-VGEAIREKVAEGKVKREEIFYCGKL--------W----STDHDPEMVRPALERTL 105
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppSPETQgRTEEIIGSWLKKKGNRDKVVLATKVagpgegitWprggGTRLDRENIREAVEGSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 106 QTLKLDYIDLYIIEMPMAFKP----GEEFYPKDENGRVIYHksnlcATWEALEACKDAGLVKSLGVSN--------FNR- 172
Cdd:cd19094 107 KRLGTDYIDLYQLHWPDRYTPlfggGYYTEPSEEEDSVSFE-----EQLEALGELVKAGKIRHIGLSNetpwgvmkFLEl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 173 -RQLEVilnkPglkyKPVTNQvecHPY--FTQTK---LLEVSASSMTSFiVAYSPLG--------------TCR-----N 227
Cdd:cd19094 182 aEQLGL----P----RIVSIQ---NPYslLNRNFeegLAEACHRENVGL-LAYSPLAggvltgkyldgaarPEGgrlnlF 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398962 228 PLWVNVSSPPLLKDEL--LTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19094 250 PGYMARYRSPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
19-168 |
1.86e-13 |
|
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: 69.13 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 19 PIIGLGT----YSDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVYRN---EHEVGEAIREkvaegkVKREEIFYCGKL-WS 89
Cdd:cd19096 1 SVLGFGTmrlpESDDDSIDEEKAIEmIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398962 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAfkpgEEFYPKDENGRViyhksnlcatWEALEACKDAGLVKSLGVS 168
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNS----PEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS 139
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-302 |
7.46e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 67.74 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFYcgklwSTDHDPEM-------VRPALERTLQTL 108
Cdd:cd19103 37 VFDKAMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYII-----STKFTPQIagqsadpVADMLEGSLARL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 109 KLDYIDLYIIEMPMAFkpgEEFYPKdengrviyhksnlcatweaLEACKDAGLVKSLGVSNFNRRQLEV---ILNKPGLK 185
Cdd:cd19103 106 GTDYIDIYWIHNPADV---ERWTPE-------------------LIPLLKSGKVKHVGVSNHNLAEIKRaneILAKAGVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 186 YKPVTNQVE--------------CH----PYFTQTkLLEVSASSMTSFIVAYSPLGTCR----NPLWvnvsspPLLKD-- 241
Cdd:cd19103 164 LSAVQNHYSllyrsseeagildyCKengiTFFAYM-VLEQGALSGKYDTKHPLPEGSGRaetyNPLL------PQLEElt 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398962 242 ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 302
Cdd:cd19103 237 AVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
21-176 |
2.13e-12 |
|
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: 66.56 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTY---------SDPRPvpgktfiAVKT---AIDEGYRHIDGAYVY---RNEHEVGEAIrekvaEGKVKREEIFY-- 83
Cdd:cd19148 7 IALGTWaiggwmwggTDEKE-------AIETihkALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIat 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 84 -CGKLWSTDH------DPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEAC 156
Cdd:cd19148 75 kVGLEWDEGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEE-------------------TAEALKEL 135
|
170 180
....*....|....*....|
gi 398962 157 KDAGLVKSLGVSNFNRRQLE 176
Cdd:cd19148 136 LDEGKIRAIGVSNFSPEQME 155
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
21-300 |
1.85e-11 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 63.79 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLG----TYSDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVY---RNEHEVGEAIrekvaegKVKREEIFYCGKL-WSTD 91
Cdd:cd19078 7 IGLGcmgmSHGYGPPPDKEEMIElIRKAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFgFKID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 92 HD----------PEMVRPALERTLQTLKLDYIDLYIIempmafkpgeefypkdengrviyHKSNLCATWEAL-EACKD-- 158
Cdd:cd19078 80 GGkpgplgldsrPEHIRKAVEGSLKRLQTDYIDLYYQ-----------------------HRVDPNVPIEEVaGTMKEli 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 159 -AGLVKSLGVS----NFNRRQLEVilnkpglkyKPVTN-QVECHPYFT--QTKLLEVSASSMTSFiVAYSPLG------- 223
Cdd:cd19078 137 kEGKIRHWGLSeagvETIRRAHAV---------CPVTAvQSEYSMMWRepEKEVLPTLEELGIGF-VPFSPLGkgfltgk 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 224 ----------TCRNplWVNVSSP-------PLLkdELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENF 284
Cdd:cd19078 207 identkfdegDDRA--SLPRFTPealeanqALV--DLLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENI 282
|
330
....*....|....*.
gi 398962 285 QIFDFSLTKEEMKDIE 300
Cdd:cd19078 283 GAADIELTPEELREIE 298
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
21-300 |
2.66e-11 |
|
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: 63.37 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLG--TYSDPRPVP-------GKTFIavKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKVaegkvKREEIFYCGKLW 88
Cdd:cd19079 15 LCLGcmSFGDPKWRPwvldeeeSRPII--KRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 -STDHDPEM-------VRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAG 160
Cdd:cd19079 88 fPMGDGPNGrglsrkhIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEE-------------------TLEALHDVVKSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 161 LVKSLGVSNFNRRQLEVILN---KPGLKyKPVTNQ-----------VECHPYFTQTKLlevsassmtsFIVAYSPL---- 222
Cdd:cd19079 149 KVRYIGASSMYAWQFAKALHlaeKNGWT-KFVSMQnhynllyreeeREMIPLCEEEGI----------GVIPWSPLargr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 223 -------------GTCRNPLWVNVSSPPLLKD--ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIP--KSTTPERIKENFQ 285
Cdd:cd19079 218 larpwgdtterrrSTTDTAKLKYDYFTEADKEivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVA 297
|
330
....*....|....*
gi 398962 286 IFDFSLTKEEMKDIE 300
Cdd:cd19079 298 ALDIKLSEEEIKYLE 312
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
40-304 |
6.62e-11 |
|
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: 62.25 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 40 VKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCGKLWS-TDHDP--------EMVRpALERTLQT 107
Cdd:cd19091 45 VDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDVLIATKVRGrMGEGPndvglsrhHIIR-AVEASLKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 108 LKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLEVIL---NKPGL 184
Cdd:cd19091 117 LGTDYIDLYQLHGFDALTPLEE-------------------TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 185 KyKPVTNQVechpYFTqtkLL------EV----SASSMTsfIVAYSPLG----------------TCRNPLwVNVSSPPL 238
Cdd:cd19091 178 A-RFVALQA----YYS---LLgrdlehELmplaLDQGVG--LLVWSPLAggllsgkyrrgqpapeGSRLRR-TGFDFPPV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398962 239 LKD------ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEmkdIEALNK 304
Cdd:cd19091 247 DRErgydvvDALREIAKETGATPAQVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEE---IARLDK 317
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
21-299 |
1.58e-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: 55.13 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLG----TYSDPRPVPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVAEgKVKREEIFYC----GKLW 88
Cdd:cd19145 15 QGLGcmglSGDYGAPKPEEEGIALiHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPRE-KVQLATKFGIheigGSGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMpmafkpgeefypkdengrvIYHKSNLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19145 94 EVRGDPAYVRAACEASLKRLDVDYIDLYYQHR-------------------IDTTVPIEITMGELKKLVEEGKIKYIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 169 NFN----RRQLEVilnkpglkyKPVTN-QVEchpYFTQTKLLE----VSASSMTSFIVAYSPLGtcRNPLWvnvSSPPLL 239
Cdd:cd19145 155 EASadtiRRAHAV---------HPITAvQLE---WSLWTRDIEeeiiPTCRELGIGIVPYSPLG--RGFFA---GKAKLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 240 KD-------------------------ELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLT 292
Cdd:cd19145 218 ELlensdvrkshprfqgenleknkvlyERVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLT 297
|
....*..
gi 398962 293 KEEMKDI 299
Cdd:cd19145 298 KEDLKEI 304
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
93-304 |
1.75e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 55.25 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMafKPGEEFypkdenGRVIYHKSN------LCATWEALEACKDAGLVKSLG 166
Cdd:PRK10625 106 DRKNIREALHDSLKRLQTDYLDLYQVHWPQ--RPTNCF------GKLGYSWTDsapavsLLETLDALAEQQRAGKIRYIG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 167 VSNFN----RRQLEvILNKPGLKyKPVTNQvecHPYFTQTKLLEVSASSMTSF----IVAYSPL--GTCRNPlWVNVSSP 236
Cdd:PRK10625 178 VSNETafgvMRYLH-LAEKHDLP-RIVTIQ---NPYSLLNRSFEVGLAEVSQYegveLLAYSCLafGTLTGK-YLNGAKP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 237 PLLKDELLT------------------SLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEM 296
Cdd:PRK10625 252 AGARNTLFSrftrysgeqtqkavaayvDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSEEVL 331
|
....*...
gi 398962 297 KDIEALNK 304
Cdd:PRK10625 332 AEIEAVHQ 339
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-301 |
4.98e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 53.37 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVY-RNEHEVGEAIREKVAEGKVKREEIF---YCGKLWSTDHDPEMVRPALERTLQTLKLDYID 114
Cdd:cd19101 28 AMAAYVDAGLTTFDCADIYgPAEELIGEFRKRLRRERDAADDVQIhtkWVPDPGELTMTRAYVEAAIDRSLKRLGVDRLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 115 LYiiempmafkpgeEFYPKDengrviYHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQLEVILNKPglkYKPVTNQVe 194
Cdd:cd19101 108 LV------------QFHWWD------YSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQV- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 195 chpyftQTKLLEVSASS-MTSF-------IVAYSPLG----TCRnplWVNVSSPP--------LLKD------------- 241
Cdd:cd19101 166 ------QYSLLDRRPENgMAALcedhgikLLAYGTLAggllSEK---YLGVPEPTgpaletrsLQKYklmidewggwdlf 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398962 242 -ELLTSL---GKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEA 301
Cdd:cd19101 237 qELLRTLkaiADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
40-294 |
5.43e-08 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 53.36 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 40 VKTAIDEGYRHIDGAYVYRN---EHEVGEAIRekvaegKVKREEIFYCGKL-WSTDHDP-------EMVRPALERTLQTL 108
Cdd:cd19074 28 VRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKVfWPTGPGPndrglsrKHIFESIHASLKRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 109 KLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLE--VILNKPGLKY 186
Cdd:cd19074 102 QLDYVDIYYCHRYDPETPLEE-------------------TVRAMDDLIRQGKILYWGTSEWSAEQIAeaHDLARQFGLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 187 KPVTNQVECHpYFTQTKLLEVSASSMTSFI--VAYSPL---------------------GTCRNPLWVNvsspPLLKDEL 243
Cdd:cd19074 163 PPVVEQPQYN-MLWREIEEEVIPLCEKNGIglVVWSPLaqglltgkyrdgipppsrsraTDEDNRDKKR----RLLTDEN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 398962 244 ------LTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKE 294
Cdd:cd19074 238 lekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-170 |
4.41e-07 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 50.65 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 41 KTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCGKLW-STDHDPEM-------VRPALERTLQTLK 109
Cdd:cd19087 37 DRALDAGINFFDTADVYgggRSEEIIGRWIAGR-------RDDIVLATKVFgPMGDDPNDrglsrrhIRRAVEASLRRLQ 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398962 110 LDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNF 170
Cdd:cd19087 110 TDYIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
21-169 |
1.09e-06 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 49.47 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGTySDPRPVPGKT--FIAVKTAIDEGYRHIDGAYVYRNEHEVGEAirEKV----AEGKVKREEIFYCGK-----LWS 89
Cdd:cd19082 3 IVLGT-ADFGTRIDEEeaFALLDAFVELGGNFIDTARVYGDWVERGAS--ERVigewLKSRGNRDKVVIATKgghpdLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 90 TDH---DPEMVRPALERTLQTLKLDYIDLYII-----EMPMafkpgEEFYpkdengrviyhksnlcatwEALEACKDAGL 161
Cdd:cd19082 80 MSRsrlSPEDIRADLEESLERLGTDYIDLYFLhrddpSVPV-----GEIV-------------------DTLNELVRAGK 135
|
....*...
gi 398962 162 VKSLGVSN 169
Cdd:cd19082 136 IRAFGASN 143
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
45-223 |
2.11e-06 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 48.71 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 45 DEGYRHIDGAYVYRN-EHE--VGEAireKVAEGKVKreeIfyCGK---LWSTDHDPEMVRPALERTLQTLKLDYIDLYII 118
Cdd:cd19075 31 ERGHTEIDTARVYPDgTSEelLGEL---GLGERGFK---I--DTKanpGVGGGLSPENVRKQLETSLKRLKVDKVDVFYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 119 EMPmafkpgeefypkDENGRVIyhksnlcatwEALEACKD---AGLVKSLGVSNFNRRQLEVILN--------KP----G 183
Cdd:cd19075 103 HAP------------DRSTPLE----------ETLAAIDElykEGKFKEFGLSNYSAWEVAEIVEickengwvLPtvyqG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398962 184 LkYKPVTNQVEchpyftqTKLLEV-SASSMTsfIVAYSPLG 223
Cdd:cd19075 161 M-YNAITRQVE-------TELFPClRKLGIR--FYAYSPLA 191
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-186 |
3.65e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 47.52 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 40 VKTAIDEGYRHIDGAYVYRNEHEV-GEAIREKvaegkvkrEEIFYCGKL----WSTDHDPEMVRPALERTLQTLKLDYID 114
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398962 115 LYIIEMPMAFkpgeefypkDENGRVIyhksnlcatWEALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKY 186
Cdd:cd19097 104 GLLLHNPDDL---------LKHGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI 157
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
44-297 |
3.67e-06 |
|
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: 47.98 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 44 IDEGYRHIDGAYVY----------RNEHEVGEAIREKVaegkvKREEIFYCGKL-WSTDHD-----PEMVRPALERTLQT 107
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-----KRDRVVIATKVgFPMGPNgpglsRKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 108 LKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNRRQLEVILN---KPGL 184
Cdd:cd19081 111 LQTDYIDLYQAHWDDPATPLEE-------------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 185 KyKPVTNQVEchpY------FTQTKLLEVS-ASSMTsfIVAYSPLG--------TCRNPLWVNVSSPPLLKD-------- 241
Cdd:cd19081 172 P-RYVSLQPE---YnlvdreSFEGELLPLCrEEGIG--VIPYSPLAggfltgkyRSEADLPGSTRRGEAAKRylnerglr 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 242 --ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMK 297
Cdd:cd19081 246 ilDALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVA 305
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
18-168 |
1.64e-05 |
|
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: 45.62 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 18 IPIIGLGTYS---DPRPVPGKTFI-AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFY---CGK- 86
Cdd:cd19163 13 VSKLGFGASPlggVFGPVDEEEAIrTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLatkVGRy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 87 --LWSTDHD--PEMVRPALERTLQTLKLDYIDLYIIEMPmafkpgeEFYPKDEngRVIYHksnlcaTWEALEACKDAGLV 162
Cdd:cd19163 87 glDPDKMFDfsAERITKSVEESLKRLGLDYIDIIQVHDI-------EFAPSLD--QILNE------TLPALQKLKEEGKV 151
|
....*.
gi 398962 163 KSLGVS 168
Cdd:cd19163 152 RFIGIT 157
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
21-170 |
1.83e-05 |
|
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: 45.78 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 21 IGLGT------YsdpRPVPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIREK-----VAEGKVkreeifycG 85
Cdd:cd19161 3 LGLGTaglgnlY---TAVSNADADATlDAAWDSGIRYFDTAPMYghgLAEHRLGDFLREKprdefVLSTKV--------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 86 KLWSTDHDPEMVRP----------------------ALERTLQTLKLDYID-LYIIEMpmafkpgEEFYPKDENGRvIYH 142
Cdd:cd19161 72 RLLKPAREGSVPDPngfvdplpfeivydysydgimrSFEDSLQRLGLNRIDiLYVHDI-------GVYTHGDRKER-HHF 143
|
170 180 190
....*....|....*....|....*....|
gi 398962 143 KSNLCATWEALEACKDAGLVK--SLGVSNF 170
Cdd:cd19161 144 AQLMSGGFKALEELKKAGVIKafGLGVNEV 173
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-168 |
2.43e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 45.33 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCGKLWSTDHDPE----MVRPALERTLQTLKLD 111
Cdd:cd19104 37 AVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVEKSLKRLKRD 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 112 YIDLYIIE---MPMAFKPGEEFYPKDEngrviYHKSNlcATWEALEACKDAGLVKSLGVS 168
Cdd:cd19104 110 SVDLLQLHnriGDERDKPVGGTLSTTD-----VLGLG--GVADAFERLRSEGKIRFIGIT 162
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
20-295 |
2.66e-05 |
|
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: 44.96 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 20 IIGLGTYS-----DPRPVPgkTFIAVKTAIDEGYRHIDGAYVYRNEHEV-GEAIreKVAEGKVKREEIFYCGK-----LW 88
Cdd:cd19164 17 IFGAATFSyqyttDPESIP--PVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL--KALRDEFPRDTYFIITKvgrygPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 89 STDHDPEMVRPALERTLQTLKLDYIDL-YIIEMpmafkpgeEFYPKDEngrviyhksnlcaTWEALEAC---KDAGLVKS 164
Cdd:cd19164 93 DFDYSPEWIRASVERSLRRLHTDYLDLvYLHDV--------EFVADEE-------------VLEALKELfklKDEGKIRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 165 LGVSNFnrrQLEVILNKPGLKYKPVTNQVE-----CHPYFTQTKLLEV----SASSMTSFIVAYSPL--GTCRN---PLW 230
Cdd:cd19164 152 VGISGY---PLPVLLRLAELARTTAGRPLDavlsyCHYTLQNTTLLAYipkfLAAAGVKVVLNASPLsmGLLRSqgpPEW 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398962 231 vnVSSPPLLKD------ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPErIKENFQIFDFSLTKEE 295
Cdd:cd19164 229 --HPASPELRAaaakaaEYCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDE-LEEAVEAYWSVLAGAS 296
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
37-168 |
9.45e-05 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 43.50 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 37 FIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvKREEIFYCGKL----------WSTDHDPEM------V 97
Cdd:cd19162 22 AATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrllepgaagRPAGADRRFdfsadgI 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398962 98 RPALERTLQTLKLDYIDL-YIIEMPMAFKPGeefypkdengrviyhksnLCATWEALEACKDAGLVKSLGVS 168
Cdd:cd19162 96 RRSIEASLERLGLDRLDLvFLHDPDRHLLQA------------------LTDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
93-283 |
1.31e-03 |
|
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: 40.01 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEfypkdengrviyhksnlcaTWEALEACKDAGLVKSLGVSNFNR 172
Cdd:cd19752 93 SAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEE-------------------TLEAFNELVKAGKVRAIGASNFAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398962 173 RQLEVILN----------------------KPGLKYK---PVTNQ----VECHPYFTqtkllevsassmtsfIVAYSPLg 223
Cdd:cd19752 154 WRLERARQiarqqgwaefsaiqqrhsylrpRPGADFGvqrIVTDElldyASSRPDLT---------------LLAYSPL- 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398962 224 tcrnpLWVNVSSP--PLLKD----------ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIP--KSTTPERIKEN 283
Cdd:cd19752 218 -----LSGAYTRPdrPLPEQydgpdsdarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEEN 286
|
|
| |
