|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
9-308 |
0e+00 |
|
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: 646.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 9 HSVRLNDGPFMPVLGFGTYAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKL 88
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 89 WATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGV 168
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 169 SNFNHKLLELILNKPGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQWVDPDCPHLLEEPILKSIA 248
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 249 KKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRY 300
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
16-322 |
6.96e-171 |
|
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: 476.60 E-value: 6.96e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 16 GPFMPVLGFGTYA-PDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFR 94
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 95 AELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVSNFNHK 174
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 175 LLELILNKPGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQWVDPDCPHLLEEPILKSIAKKHSGS 254
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 255 PGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYDKLQFAANHPYFPF 322
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
19-326 |
3.85e-137 |
|
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: 391.01 E-value: 3.85e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19107 4 MPILGLGTW---KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqWVDPDCPHLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP-WAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 259 ALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYDKLQFAANHPYFPFSEEY 326
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
13-308 |
5.67e-126 |
|
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: 362.47 E-value: 5.67e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 13 LNDGPFMPVLGFGTYapdhtpKS---QAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKI-ADGTVKREEIFYTIKL 88
Cdd:cd19106 1 LHTGQKMPLIGLGTW------KSkpgQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 89 WATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGV 168
Cdd:cd19106 75 WNTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 169 SNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQrDPQWVDPDCPHLLEEPILKSIA 248
Cdd:cd19106 155 SNFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSP-DRPWAKPDEPVLLEEPKVKALA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 249 KKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19106 232 KKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-308 |
7.30e-123 |
|
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: 354.28 E-value: 7.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYApDHTPKSqAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLW 89
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK-LKDDEG-VRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKEllpKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNkpGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQ-RDPQWVDPDcphLLEEPILKSIA 248
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLvPRGQTNPPP---RLDDPTLVAIA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 249 KKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19116 232 KKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
19-300 |
1.91e-120 |
|
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: 346.39 E-value: 1.91e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIadgtVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPFAMKPGKEllpkdasgeiileTVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGS-------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqwvdpdcphLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2091808387 259 ALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19071 210 LLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
19-326 |
6.88e-118 |
|
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: 341.94 E-value: 6.88e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19110 4 IPAVGLGTW---KASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQwvdpdcpHLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19110 161 LLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGV-------DLIDDPVIQRIAKKHGKSPAQI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 259 ALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYDKLQFAANHPYFPFSEEY 326
Cdd:cd19110 234 LIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
15-308 |
1.39e-116 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 337.03 E-value: 1.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 15 DGPFMPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWATFFR 94
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 95 AELVHPALERSLKKLGPDYVDLFIIHVPFamkPGKellpkdasgeiiletveLCDTWEALEKCKEAGLTRSIGVSNFNHK 174
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPG---PGP-----------------YVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 175 LLELILNKPGlkYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSqrdpqwvdpdcPHLLEEPILKSIAKKHSGS 254
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGR-----------GKLLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2091808387 255 PGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-307 |
2.35e-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: 2.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 8 SHSVRLNDGPFMPVLGFGTYapdhtpKSQAAE---ATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFY 84
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTW------QSKGAEgitAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 85 TIKLWATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTR 164
Cdd:cd19154 75 TTKLWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 165 SIGVSNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS------QRDPQWVDPdcPHL 238
Cdd:cd19154 155 AIGVSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranfTKSTGVSPA--PNL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 239 LEEPILKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLR 307
Cdd:cd19154 231 LQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
10-308 |
3.00e-111 |
|
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: 325.13 E-value: 3.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLW 89
Cdd:cd19123 3 TLPLSNGDLIPALGLGTW---KSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGkelLPKDASGE--IILETVELCDTWEALEKCKEAGLTRSIG 167
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG---VGFPESGEdlLSLSPIPLEDTWRAMEELVDKGLCRHIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 168 VSNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-QRDPQWVDPDCPHLLEEPILKS 246
Cdd:cd19123 157 VSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2091808387 247 IAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19123 235 IAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
15-302 |
1.31e-100 |
|
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: 297.26 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 15 DGPFMPVLGFGTyAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVK-REEIFYTIKLWATFF 93
Cdd:cd19124 1 SGQTMPVIGMGT-ASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 94 RAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDAsgEIILEtVELCDTWEALEKCKEAGLTRSIGVSNFNH 173
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEE--EDFLP-FDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 174 KLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqWVDPDcphLLEEPILKSIAKKHSG 253
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-WGSNA---VMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2091808387 254 SPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
13-302 |
4.61e-100 |
|
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: 296.18 E-value: 4.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 13 LNDGPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATF 92
Cdd:cd19125 5 LNTGAKIPAVGLGTWQAD---PGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 FRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGkellpKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVSNFN 172
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKG-----AHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 173 HKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqWVDPDcphLLEEPILKSIAKKHS 252
Cdd:cd19125 157 VKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTT-WVKKN---VLKDPIVTKVAEKLG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2091808387 253 GSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19125 231 KTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-307 |
3.02e-94 |
|
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: 282.11 E-value: 3.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLW 89
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKpGKEL--LPKDASGEIILE-TVELCDTWEALEKCKEAGLTRSI 166
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSL-SKEDdsGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 167 GVSNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS----QRDPQWVDP--DCPHLLE 240
Cdd:cd19155 159 GLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaaHFSPGTGSPsgSSPDLLQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2091808387 241 EPILKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLR 307
Cdd:cd19155 237 DPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
19-308 |
2.91e-92 |
|
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: 276.30 E-value: 2.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19111 4 MPVIGLGTY---QSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPFAMKpgkellPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFV------NKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-QRDPQWVDPDCPHLLEEPILKSIAKKHSGSPGQ 257
Cdd:cd19111 155 ILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 258 VALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
14-309 |
1.31e-89 |
|
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: 269.71 E-value: 1.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 14 NDGPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFF 93
Cdd:cd19129 1 NGSGAIPALGFGTLIPD---PSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 94 RAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILET-VELCDTWEALEKCKEAGLTRSIGVSNFN 172
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 173 HKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQwvdpdcphLLEEPILKSIAKKHS 252
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPK--------LLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 253 GSPGQVALRYQLQRGVVVLAKSFSQERIKENfqiFDFELTPED-MKAI-DGLNRNLRYD 309
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPEDaMREInEGIKTRYRFN 283
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-303 |
1.38e-89 |
|
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: 268.47 E-value: 1.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLW 89
Cdd:cd19131 1 TITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKpGKELlpkdasgeiiletvelcDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19131 74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQ-DKYV-----------------ETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAK 249
Cdd:cd19131 136 NFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAE 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLN 303
Cdd:cd19131 203 KHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
19-300 |
2.46e-89 |
|
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: 267.21 E-value: 2.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYAPDHtpkSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19073 1 IPALGLGTWQLRG---DDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkdasgeiiLETVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWP-------------------NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGsQRDpqwvdpdcphLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19073 135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2091808387 259 ALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
11-303 |
2.70e-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: 267.52 E-value: 2.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 11 VRLNDGPFMPVLGFGTYapDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWA 90
Cdd:cd19133 1 VTLNNGVEMPILGFGVF--QIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 TFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGkellpkdasgeiiletvelcdTWEALEKCKEAGLTRSIGVSN 170
Cdd:cd19133 75 QDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVYG---------------------AWRAMEELYKEGKIRAIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FN-HKLLELILNKpglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcPHLLEEPILKSIAK 249
Cdd:cd19133 134 FYpDRLVDLILHN---EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR---------NNLFENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLN 303
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
13-302 |
4.19e-89 |
|
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: 268.12 E-value: 4.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 13 LNDGPFMPVLGFGTY--APDhtpksQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIAD-GTVKREEIFYTIKLW 89
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPG-----EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDAS----GEIILET-VELCDTWEALEKCKEAGLTR 164
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVptngGEVDLDLsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 165 SIGVSNFNHKLLELILNKPGLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQwvdpdcPHLLEEPIL 244
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAGL------PLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 245 KSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQifDFELTPEDMKAIDGL 302
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-304 |
7.18e-89 |
|
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: 267.44 E-value: 7.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 8 SHSVRLNDGPFMPVLGFGTY--APDhtpksQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYT 85
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWqsKPN-----EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 86 IKLWATFFRAelVHPALERSLKKLGPDYVDLFIIHVPFAMKPG--KELLPKDASGEIILETVELCDTWEALEKCKEAGLT 163
Cdd:cd19117 74 TKLWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 164 RSIGVSNFNHKLLELILNKPGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqwvdpdcphLLEEPI 243
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP---------LLKEPV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 244 LKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIfdFELTPEDMKAIDGLNR 304
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
10-309 |
9.77e-89 |
|
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: 268.16 E-value: 9.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLW 89
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLD---NATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMK--PGKELLPKD----ASGEIILETVELCDTWEALEKCKEAGLT 163
Cdd:cd19113 79 NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPGfycgDGDNFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 164 RSIGVSNFNHKLLELILNkpGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQWVDP---DCPHLLE 240
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQGralNTPTLFE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 241 EPILKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYD 309
Cdd:cd19113 237 HDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFN 305
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
10-302 |
1.11e-87 |
|
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: 264.39 E-value: 1.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGtVKREEIFYTIKLW 89
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQAK---AGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAelVHPALERSLKKLGPDYVDLFIIHVPFAMKP--GKELLPKDASGE-IILETVELCDTWEALEKCKEAGLTRSI 166
Cdd:cd19121 79 STYHRR--VELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSrDLDWDWNHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 167 GVSNFNHKLLELILnkPGLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqwvdpdcphLLEEPILKS 246
Cdd:cd19121 157 GVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP---------LISDEPVVE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2091808387 247 IAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFelTPEDMKAIDGL 302
Cdd:cd19121 226 IAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
11-303 |
1.38e-87 |
|
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: 263.14 E-value: 1.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 11 VRLNDGPFMPVLGFGTY-APDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLW 89
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFqTPD---GDETERAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkdASGEIIletvelcDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWP-------------GKDKFI-------DTWKALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFN-HKLLELILNKpglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQrdpqwvdpdcpHLLEEPILKSIA 248
Cdd:cd19126 134 NFQeHHLEELLAHA---DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG-----------GLLSNPVLAAIG 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2091808387 249 KKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLN 303
Cdd:cd19126 200 EKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
19-302 |
2.02e-87 |
|
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: 262.58 E-value: 2.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYAPDHtpkSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19140 8 IPALGLGTYPLTG---EECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPfamkpgkellPKDasgeiiletVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVALLRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPGLKYkpTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19140 142 AVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2091808387 259 ALRYQLQR-GVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19140 209 ALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-308 |
6.91e-87 |
|
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: 261.94 E-value: 6.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYAPDHTpkSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEkiadGTVKREEIFYTIKLW 89
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEG--SEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamKPGKELlpkdasgeiiletvelcDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWP---VKGKYK-----------------ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAK 249
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
16-300 |
1.42e-86 |
|
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: 261.01 E-value: 1.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 16 GPFMPVLGFGT-----YAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWA 90
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 tffRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKellpkdasgeiiletVELCDTWEALEKCKEAGLTRSIGVSN 170
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGG---------------PTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FNHKLLELILNKPglKYKPTCNQVECHPYLN--QSKLLEFCKSKDIVLVAYSALGsqrdPQWVDPDCPhllEEPILKSIA 248
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLS----PLTRDAGGP---LDPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2091808387 249 KKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
19-302 |
2.04e-85 |
|
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: 257.95 E-value: 2.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYAPDHTPksQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELV 98
Cdd:cd19136 1 MPILGLGTFRLRGEE--EVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHVPfamkpGKELLPKDASGEIILETvelcDTWEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19136 79 RAACLGSLERLGTDYLDLYLIHWP-----GVQGLKPSDPRNAELRR----ESWRALEDLYKEGKLRAIGVSNYTVRHLEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcPHLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19136 150 LLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD---------LRLLEDPTVLAIAKKYGRTPAQV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2091808387 259 ALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19136 219 LLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
11-308 |
2.19e-85 |
|
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: 258.22 E-value: 2.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 11 VRLNDGPFMPVLGFGTY-APDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLW 89
Cdd:cd19156 1 VKLANGVEMPRLGLGVWrVQD---GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKpgkellpkdasgeiiletveLCDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19156 74 NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFN-HKLLELILNkpgLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQrdpqwvdpdcpHLLEEPILKSIA 248
Cdd:cd19156 134 NFHeHHLEELLKS---CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQG-----------KLLSNPVLKAIG 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 249 KKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19156 200 KKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-310 |
5.29e-85 |
|
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: 258.50 E-value: 5.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 8 SHSVRLNDGPFMPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIK 87
Cdd:cd19115 2 SPTVKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 88 LWATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMK---PGKELLP--KDASGEIILETVELCDTWEALEKCKEAGL 162
Cdd:cd19115 79 LWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 163 TRSIGVSNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPQWVDP---DCPHLL 239
Cdd:cd19115 159 ARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPgakDTPPLF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 240 EEPILKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYDK 310
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNN 307
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
20-302 |
3.23e-83 |
|
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: 252.83 E-value: 3.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELVH 99
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 100 PALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEIILETVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLELI 179
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 180 LNKpgLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSAL-GSQRDPQWVdpdcphLLEEPILKSIAKKHSGSPGQV 258
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLgGSYGDGNLT------FLNDSELKALATKYNTTPPQV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2091808387 259 ALRYQLQR---GVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19128 231 IIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
10-309 |
1.90e-82 |
|
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: 252.02 E-value: 1.90e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLW 89
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRME---PGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATffRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPKDASGEI----ILETVELCDTWEALEKCKEAGLTRS 165
Cdd:cd19112 79 NS--DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDgvldIDVTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 166 IGVSNFnhkllELILNKPGLKY---KPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALG-SQRDPQWVDPDCPhlLEE 241
Cdd:cd19112 157 IGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 242 PILKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYD 309
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTN 297
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
13-304 |
9.67e-82 |
|
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: 248.34 E-value: 9.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 13 LNDGPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWATF 92
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLK---GDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAV----RRSGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 FRAELVHPALERSLKKLGPDYVDLFIIHVPfamKPGKELLpkdasgeiiletVElcdTWEALEKCKEAGLTRSIGVSNFN 172
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWP---NPSRDLY------------VE---AWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 173 HKLLELILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDpqwvdpdcphLLEEPILKSIAKKHS 252
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2091808387 253 GSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNR 304
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-304 |
4.50e-81 |
|
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: 248.18 E-value: 4.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYAPdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLW 89
Cdd:cd19119 3 SFKLNTGASIPALGLGTASP-HEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAelVHPALERSLKKLGPDYVDLFIIHVPFAMK-----PGKELLPKDASGEIIL-ETVELCDTWEALEKCKEAGLT 163
Cdd:cd19119 82 PTFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 164 RSIGVSNFNHKLLELILNKpgLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDPqwvdpdcphLLEEPI 243
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 244 LKSIAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIfdFELTPEDMKAIDGLNR 304
Cdd:cd19119 229 VKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
16-311 |
2.64e-77 |
|
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: 238.61 E-value: 2.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 16 GPFMPVLGFGTYAPDhtpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRA 95
Cdd:cd19114 1 GDKMPLVGFGTAKIK---ANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 96 ELVHPALERSLKKLGPDYVDLFIIHVPFAMK---PGKELLPKDASGEII---LETVELCDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKELKkfpLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQ---RDPQWVDPDCPhLLEEPILKS 246
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTN-LLEHPVVKK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2091808387 247 IAKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRYDKL 311
Cdd:cd19114 235 LADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDP 299
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
11-303 |
4.18e-77 |
|
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: 236.92 E-value: 4.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 11 VRLNDGPFMPVLGFGTYApdhTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKiadgTVKREEIFYTIKLWA 90
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 TFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkelLPKDASGEIiletvelcDTWEALEKCKEAGLTRSIGVSN 170
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWP---------VPNDFDRTI--------QAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FNHKLLELILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-QRDPQWVDPDCPHLLEEPILKSIAK 249
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvMRYGASGPTGPGDVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLN 303
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-302 |
4.88e-76 |
|
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: 234.14 E-value: 4.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 11 VRLNDGPFMPVLGFGTyapDHTpKSQAAEATKVAI-DVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLW 89
Cdd:cd19135 5 VRLSNGVEMPILGLGT---SHS-GGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKEllpkdaSGEIILETvelcdtWEALEKCKEAGLTRSIGVS 169
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN------VKETRAET------WRALEELYDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAK 249
Cdd:cd19135 145 NFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19135 212 KYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
19-302 |
3.40e-71 |
|
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: 221.07 E-value: 3.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTY--APDHTPKSqaaeaTKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWATFFRAE 96
Cdd:cd19139 1 IPAFGLGTFrlKDDVVIDS-----VRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 97 LVHPALERSLKKLGPDYVDLFIIHVPfamkpgkelLPKDAsgeiiletVELCDTWEALEKCKEAGLTRSIGVSNFNHKLL 176
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWP---------SPNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 177 ELILNKPGlKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAKKHSGSPG 256
Cdd:cd19139 135 DEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2091808387 257 QVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19139 203 QIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-308 |
1.47e-70 |
|
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: 220.11 E-value: 1.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYAPDHTPKSQAAEAtkvAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLW 89
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSA---ALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPfAMKPGKELlpkdasgeiiletvelcDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWP-AGREGKYV-----------------DSWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPGlkYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAK 249
Cdd:cd19134 137 NFTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAA 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLRY 308
Cdd:cd19134 204 AHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-303 |
1.56e-69 |
|
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: 217.09 E-value: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 10 SVRLNDGPFMPVLGFGTYapdHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLW 89
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkelLPkdASGEIIletvelcDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWP---------TP--AAGNYV-------HTWEAMIELRAAGRTRSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAK 249
Cdd:cd19130 136 NFLPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2091808387 250 KHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLN 303
Cdd:cd19130 203 AHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
22-303 |
5.60e-66 |
|
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: 209.09 E-value: 5.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 22 LGFGTYA----PDHTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiADGTVKREEIFYTIKL------ 88
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 89 WATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFamkpgkellpkdasgeiilETVELCDTWEALEKCKEAGLTRSIGV 168
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPD-------------------PDTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 169 SNFNHKLLELILNKPglKYKPTCNQVECHPY--LNQSKLLEFCKSKDIVLVAYSALGS----------------QRDPQW 230
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2091808387 231 VDPDCPHLLEEPILKSIAKKHSGSPGQVALRY--QLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLN 303
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
13-300 |
5.11e-65 |
|
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: 206.70 E-value: 5.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 13 LNDGPFMPVLGFGTYAPDHTpKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADG-TVKREEIFYTIKLWAT 91
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGA-KGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 92 FFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPK-DASGE-IILE--TVELCDTWEALEKCKEAGLTRSIG 167
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKyVILKdlTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 168 VSNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDpqwVDPDCPHLLEEPILKSI 247
Cdd:cd19122 162 VSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNEV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2091808387 248 AKKHSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIfdFELTPEDMKAID 300
Cdd:cd19122 237 AEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAIN 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
19-307 |
6.46e-64 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 202.95 E-value: 6.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYapdhTPKSQAAEAT-KVAIDVGFRHIDSAYLYQNEEEVGQAIwekiADGTVKREEIFYTIKLWATFFRAEL 97
Cdd:PRK11172 3 IPAFGLGTF----RLKDQVVIDSvKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 98 VHPALERSLKKLGPDYVDLFIIHVPfamKPGKEllpkdasgeiiletVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLE 177
Cdd:PRK11172 75 LIPSLKESLQKLRTDYVDLTLIHWP---SPNDE--------------VSVEEFMQALLEAKKQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 178 LILNKPGLKYKPTcNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLLEEPILKSIAKKHSGSPGQ 257
Cdd:PRK11172 138 QAIAAVGAENIAT-NQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2091808387 258 VALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLR 307
Cdd:PRK11172 206 VILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
19-300 |
2.54e-61 |
|
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: 196.30 E-value: 2.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYA------PDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIwekiadGTVKREEIFYTIKLW 89
Cdd:cd19072 4 VPVLGLGTWGigggmsKDYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI------KGFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamKPgkellpkdasgeiileTVELCDTWEALEKCKEAGLTRSIGVS 169
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP---NP----------------SIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKPGlKYKPTCNQVECHpYLNQ---SKLLEFCKSKDIVLVAYSALGsQRDPQWVDPDcphlleePILKS 246
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDReeeSGLLPYCQKNGIAIIAYSPLE-KGKLSNAKGS-------PLLDE 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2091808387 247 IAKKHSGSPGQVALRYQLQR-GVVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
11-307 |
6.20e-60 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 193.37 E-value: 6.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 11 VRLNDGPFMPVLGFGTYAPDHTpksQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEkiadGTVKREEIFYTIKLWA 90
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNE---EVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 TffRAELVHPALERSLKKLGPDYVDLFIIHVPFAmkpgkellPKDasgeiiletvELCDTWEALEKCKEAGLTRSIGVSN 170
Cdd:PRK11565 80 D--DHKRPREALEESLKKLQLDYVDLYLMHWPVP--------AID----------HYVEAWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FNHKLLELILNKPGLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSQRDpqwvdpdcpHLLEEPILKSIAKK 250
Cdd:PRK11565 140 FQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK---------GVFDQKVIRDLADK 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2091808387 251 HSGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGLNRNLR 307
Cdd:PRK11565 209 YGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-300 |
1.79e-51 |
|
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: 170.89 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 9 HSVRLNDGPFMPVLGFGTY--APDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIWEKiadgtvkREEIF 83
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWymGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 84 YTIKLWATFFRAELVHPALERSLKKLGPDYVDLFIIH----VPFAmkpgkellpkdasgeiilETVelcdtwEALEKCKE 159
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHwrggVPLA------------------ETV------AAMEELKK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 160 AGLTRSIGVSNFNHKLLELILNKPGLKyKPTCNQVECHpyLNQS----KLLEFCKSKDIVLVAYSALGSQRDPQwvdpdc 235
Cdd:cd19138 130 EGKIRAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLR------ 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2091808387 236 PHLLEEPILKSIAKKHSGSPGQVALRYQL-QRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19138 201 RGLLENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
16-300 |
2.59e-49 |
|
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: 165.44 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 16 GPFMPVLGFGTYA------PDHTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIWEkiadgtVKREEIFYTI 86
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 87 KLWATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKEllpkdasgeiiletvelcdTWEALEKCKEAGLTRSI 166
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 167 GVSNFNHKLLELILNKpgLKYKPTCNQVECHPY---LNQSKLLEFCKSKDIVLVAYSALgsqrdpqwvdpDCPHLLEEPI 243
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 244 LKSIAKKHSGSPGQVALRYQLQR-GVVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
16-300 |
4.45e-38 |
|
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: 136.89 E-value: 4.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 16 GPFMPVLGFGTYA-----PDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIWEK-----IAD--GTVKRE 80
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGRrddvvIATkcGLRWDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 81 EIFYTIKLWATFFRAELvhpalERSLKKLGPDYVDLFIIHVPFamkpgkellpkdasgeiilETVELCDTWEALEKCKEA 160
Cdd:cd19084 81 GKGVTKDLSPESIRKEV-----EQSLRRLQTDYIDLYQIHWPD-------------------PNTPIEETAEALEKLKKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 161 GLTRSIGVSNFNHKLLELIlnkpgLKY-KPTCNQVechPY--LNQ---SKLLEFCKSKDIVLVAYSALGS-------QRD 227
Cdd:cd19084 137 GKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAQglltgkyKKE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 228 PQWVDPDCPH---------------LLEEpiLKSIAKKHSGSPGQVALRYQLQR-GV-VVLAKSFSQERIKENFQIFDFE 290
Cdd:cd19084 209 PTFPPDDRRSrfpffrgenfeknleIVDK--LKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWE 286
|
330
....*....|
gi 2091808387 291 LTPEDMKAID 300
Cdd:cd19084 287 LTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
20-300 |
8.96e-38 |
|
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: 136.20 E-value: 8.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYA---------PDHTPKsQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiaDGTVKREEIFYTIK 87
Cdd:cd19093 3 SPLGLGTWQwgdrlwwgyGEYGDE-DLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFL-----KELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 88 LWATFFRA--ELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGkellpkdasgeiiletveLCDTWEALEKCKEAGLTRS 165
Cdd:cd19093 77 FAPLPWRLtrRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ------------------IEALMDGLADAVEEGLVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 166 IGVSNFNHKLLELI---LNKPGlkYKPTCNQVE---CHPYLNQSKLLEFCKSKDIVLVAYSALG---------------- 223
Cdd:cd19093 139 VGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenpppg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 224 ---SQRDPQWVDPDCPhLLEEpiLKSIAKKHSGSPGQVALRYQLQRGVVVL--AKSFSQERikENFQIFDFELTPEDMKA 298
Cdd:cd19093 217 grrRLFGRKNLEKVQP-LLDA--LEEIAEKYGKTPAQVALNWLIAKGVVPIpgAKNAEQAE--ENAGALGWRLSEEEVAE 291
|
..
gi 2091808387 299 ID 300
Cdd:cd19093 292 LD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
14-300 |
7.97e-36 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 131.45 E-value: 7.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 14 NDGPFMPVLGFGT----YAPDHTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiadGTVKREEIFYTI 86
Cdd:COG0667 8 RSGLKVSRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEAL------KGRPRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 87 KL--------WATFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkDASgeiiletVELCDTWEALEKCK 158
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLGALDELV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 159 EAGLTRSIGVSNFNHKLLELILNKPGLKYKPTCNQVEchpY--LNQS---KLLEFCKSKDIVLVAYSAL----------- 222
Cdd:COG0667 143 REGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLagglltgkyrr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 223 ------GSQRDPQWVDPDCPHLLEEPI--LKSIAKKHSGSPGQVALRYQLQRGVVVL----AKSFSQerIKENFQIFDFE 290
Cdd:COG0667 220 gatfpeGDRAATNFVQGYLTERNLALVdaLRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARSPEQ--LEENLAAADLE 297
|
330
....*....|
gi 2091808387 291 LTPEDMKAID 300
Cdd:COG0667 298 LSAEDLAALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
20-306 |
1.93e-35 |
|
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: 130.01 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYA--PDHTPKSQ---AAEAT-KVAIDVGFRHIDSAYLYQN---EEEVGQAIwEKiadgtvKREEIFYTIKLWA 90
Cdd:cd19085 2 SRLGLGCWQfgGGYWWGDQddeESIATiHAALDAGINFFDTAEAYGDghsEEVLGKAL-KG------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 TFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLpkdasgeiiletvelcdtwEALEKCKEAGLTRSIGVSN 170
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETM-------------------EALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FNHKLLELILnKPGlkyKPTCNQVechPY--LNQSK---LLEFCKSKDIVLVAYSALGS-------QRDPQWVDPDC--- 235
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQL---PYnlLWRAIeyeILPFCREHGIGVLAYSPLAQglltgkfSSAEDFPPGDArtr 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 236 -PHLLEEPI----------LKSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19085 209 lFRHFEPGAeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
....
gi 2091808387 303 NRNL 306
Cdd:cd19085 289 SDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
20-285 |
8.35e-29 |
|
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: 110.69 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYA-PDHTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiaDGTVKREEIFYTIKLWATFFR- 94
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWL-----KGRGNRDDVVIATKGGHPPGGd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 95 -------AELVHPALERSLKKLGPDYVDLFIIHVPFAMKPgkellpkdasgeiiletVElcDTWEALEKCKEAGLTRSIG 167
Cdd:cd06660 76 psrsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTP-----------------VE--ETLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 168 VSNFNHKLLELILN--KPGLKYKPTCNQVE---CHPYLNQSKLLEFCKSKDIVLVAYSALGsqrdpqwvdpdcphlleep 242
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2091808387 243 ilksiakkhsGSPGQVALRYQLQR--GVVVLAKSFSQERIKENFQ 285
Cdd:cd06660 198 ----------RGPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
14-299 |
1.23e-28 |
|
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: 112.54 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 14 NDGPFMPVLGFGT------YAPdHTPKSQAAEATKVAIDVGFRHIDSAYLYQ-NEEEVGQaiWEKIADGtvKREEIFYTI 86
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGP-PKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGR--WFKQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 87 KL----------WATFFRAELVHPALERSLKKLGPDYVDLFIIHvpfamkpgkellpkDASGEIILETvelcdTWEALEK 156
Cdd:cd19144 83 KFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH--------------RVDGKTPIEK-----TVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 157 CKEAGLTRSIGVSNFNHKLLelilnKPGLKYKP-TCNQVECHPYL-----NQSKLLEFCKSKDIVLVAYSAL------GS 224
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETL-----RRAHAVHPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLgrgfltGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 225 QRDPQWVDPD-----CPHLLEEPI---------LKSIAKKHSGSPGQVALRYQLQRG--VVVLAKSFSQERIKENFQIFD 288
Cdd:cd19144 219 IRSPDDFEEGdfrrmAPRFQAENFpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALK 298
|
330
....*....|.
gi 2091808387 289 FELTPEDMKAI 299
Cdd:cd19144 299 VKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-302 |
1.81e-26 |
|
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: 106.22 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFGTYA-----------PDHTPKSQAAeaTKVAIDVGFRHIDSAYLY---QNEEEVGQAIWEKiadgtvkREEIFYTI 86
Cdd:cd19102 3 TIGLGTWAiggggwgggwgPQDDRDSIAA--IRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 87 K---LWA------TFFRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkdasgeiiLETVELCDTWEALEKC 157
Cdd:cd19102 74 KcglLWDeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWP-------------------DPDEPIEEAWGALAEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 158 KEAGLTRSIGVSNFNHKLLELILNKPGLKYkptcNQVechPY--LN---QSKLLEFCKSKDIVLVAYSALGS-----QRD 227
Cdd:cd19102 135 KEEGKVRAIGVSNFSVDQMKRCQAIHPIAS----LQP---PYslLRrgiEAEILPFCAEHGIGVIVYSPMQSglltgKMT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 228 PQWVDPDCPH-------LLEEP----------ILKSIAKKHSGSPGQVALRYQLQR----GVVVLAKSFSQerIKENFQI 286
Cdd:cd19102 208 PERVASLPADdwrrrspFFQEPnlarnlalvdALRPIAERHGRTVAQLAIAWVLRRpevtSAIVGARRPDQ--IDETVGA 285
|
330
....*....|....*.
gi 2091808387 287 FDFELTPEDMKAIDGL 302
Cdd:cd19102 286 ADLRLTPEELAEIEAL 301
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
20-294 |
6.44e-25 |
|
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: 101.48 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTY----APDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEE-VGQAIwekiadGTVKREEIFYTIKL-----W 89
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDSEErLGLAL------AELPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 ATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKELLPkdasGEIIletvelcdtwEALEKCKEAGLTRSIGVS 169
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELILNKpglkykptcNQVEC----HPY--LNQS---KLLEFCKSKDIVLVAYSALG----SQRDPQWVDPDCP 236
Cdd:cd19090 141 GGPPDLLRRAIET---------GDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYR 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2091808387 237 HLLEEPI-----LKSIAKKHSGSPGQVALRYQLQ----RGVVVLAKsfSQERIKENFQIFDFELTPE 294
Cdd:cd19090 212 WLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
22-302 |
1.08e-24 |
|
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: 101.34 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 22 LGFGT-YAPDHTPKSQAAEAT-----KVAIDVGFRHIDSAYLY---QNEEEVGQAIWEKiadgtvKREEIFYTIKlWATF 92
Cdd:cd19083 14 IGLGTnAVGGHNLYPNLDEEEgkdlvREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATK-GAHK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 F---------RAELVHPALERSLKKLGPDYVDLFIIHvpfamKPGKELLPKDASGeiiletvelcdtweALEKCKEAGLT 163
Cdd:cd19083 87 FggdgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIH-----FPDGETPKAEAVG--------------ALQELKDEGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 164 RSIGVSNFNHKLLELiLNKPGlkykptcnQVEC--HPY--LNQ---SKLLEFCKSKDIVLV-----AYSALGSQRDPQWV 231
Cdd:cd19083 148 RAIGVSNFSLEQLKE-ANKDG--------YVDVlqGEYnlLQReaeEDILPYCVENNISFIpyfplASGLLAGKYTKDTK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 232 DPDC------PHLLEEPI---------LKSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKENFQIFDFELTPE 294
Cdd:cd19083 219 FPDNdlrndkPLFKGERFsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEE 298
|
....*...
gi 2091808387 295 DMKAIDGL 302
Cdd:cd19083 299 EIAFIDAL 306
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-295 |
4.88e-24 |
|
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: 99.17 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFGTYAPDHTPKSQAAEATKVAIDVGFRHIDSA--Y-LYQNEEEVGQAIWEKiadgTVKREEIFYT----IKLWATFF 93
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHAdiYgGGKCEELFGEALALN----PGLREKIEIQtkcgIRLGDDPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 94 RAELVH---------PALERSLKKLGPDYVDLFIIHVPfamkpgkellpkDAsgeiiletveLCDTWE---ALEKCKEAG 161
Cdd:cd19092 86 PGRIKHydtskehilASVEGSLKRLGTDYLDLLLLHRP------------DP----------LMDPEEvaeAFDELVKSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 162 LTRSIGVSNFNHKLLELiLNKpGLKYKPTCNQVEC---HPYLNQSKLLEFCKSKDIVLVAYSALGSQR--DPQwvDPDCP 236
Cdd:cd19092 144 KVRYFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRlfGGF--DERFQ 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2091808387 237 HLLEEpiLKSIAKKHSGSPGQVALRYQLQ---RGVVVLAkSFSQERIKENFQIFDFELTPED 295
Cdd:cd19092 220 RLRAA--LEELAEEYGVTIEAIALAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-300 |
6.79e-23 |
|
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: 96.51 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 31 HTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEE-VGQAIWEKIADGTVKREEIFYTiKlWATFFRAELVHPA-----LER 104
Cdd:cd19101 19 IRDEDAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHT-K-WVPDPGELTMTRAyveaaIDR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 105 SLKKLGPDYVDLFIIHVpfamkpgkellpKDASGEIILETVElcdtweALEKCKEAGLTRSIGVSNFNHKLLELILNKPg 184
Cdd:cd19101 97 SLKRLGVDRLDLVQFHW------------WDYSDPGYLDAAK------HLAELQEEGKIRHLGLTNFDTERLREILDAG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 185 lkYKPTCNQVEcHPYLNQ---SKLLEFCKSKDIVLVAYSALGS---------QRDPQWVDPDCP---------------- 236
Cdd:cd19101 158 --VPIVSNQVQ-YSLLDRrpeNGMAALCEDHGIKLLAYGTLAGgllsekylgVPEPTGPALETRslqkyklmidewggwd 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 237 ---HLLEEpiLKSIAKKHSGSPGQVALRYQLQR----GVVVLAKSfsQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19101 235 lfqELLRT--LKAIADKHGVSIANVAVRWVLDQpgvaGVIVGARN--SEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-272 |
4.83e-21 |
|
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: 89.85 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN-EEEVGQAIwekiADgtvKREEIFYTIKLWATffRAELV 98
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKAL----KG---RRDKVFLATKTGAR--DYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 99 HPALERSLKKLGPDYVDLFIIHvpfAMKPGKELLPKDASGEIIletvelcdtwEALEKCKEAGLTRSIGVSNFNHKLLEL 178
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH---AVDTEEDLDQVFGPGGAL----------EALLEAKEEGKIRFIGISGHSPEVLLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 179 ILNKPglkykptcnqvechpylnqskllEFckskDIVLVAYSALGSQRDPQwvdpdcphllEEPIL-------------K 245
Cdd:cd19100 150 ALETG-----------------------EF----DVVLFPINPAGDHIDSF----------REELLplarekgvgviamK 192
|
250 260 270
....*....|....*....|....*....|.
gi 2091808387 246 SIAKKHSGSPGQV----ALRYQLQRGVVVLA 272
Cdd:cd19100 193 VLAGGRLLSGDPLdpeqALRYALSLPPVDVV 223
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-286 |
6.78e-21 |
|
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: 89.95 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTYAPDhtpkSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIwekiadGTVKREEIFYTIKLWA---TF 92
Cdd:cd19105 13 VSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEAL------KGLRRDKVFLATKASPrldKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 FRAELVhPALERSLKKLGPDYVDLFIIHvpfAMKPGKELLpkdASGEIIletvelcdtwEALEKCKEAGLTRSIGVS--- 169
Cdd:cd19105 83 DKAELL-KSVEESLKRLQTDYIDIYQLH---GVDTPEERL---LNEELL----------EALEKLKKEGKVRFIGFSthd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFNHKLLELIlnKPG------LKYkptcNqvechpYLNQS----KLLEFCKSKDIVLVAYSALGSqrdpqwvdpdcphLL 239
Cdd:cd19105 146 NMAEVLQAAI--ESGwfdvimVAY----N------FLNQPaeleEALAAAAEKGIGVVAMKTLAG-------------GY 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 240 EEPILKSIAKKHSGSPGQVALRYQLQR----GVVVLAKSFSQerIKENFQI 286
Cdd:cd19105 201 LQPALLSVLKAKGFSLPQAALKWVLSNprvdTVVPGMRNFAE--LEENLAA 249
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
14-300 |
8.74e-21 |
|
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: 90.75 E-value: 8.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 14 NDGPFMPVLGFGT-------YAPDHTPKSQAAEAT---KVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiadgTVKRE 80
Cdd:cd19091 8 RSGLKVSELALGTmtfggggGFFGAWGGVDQEEADrlvDIALDAGINFFDTADVYsegESEEILGKAL-------KGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 81 EIFYTIKlwaTFFR---------AELVH--PALERSLKKLGPDYVDLFIIHVPFAMKPgkellpkdasgeiILETVelcd 149
Cdd:cd19091 81 DVLIATK---VRGRmgegpndvgLSRHHiiRAVEASLKRLGTDYIDLYQLHGFDALTP-------------LEETL---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 150 twEALEKCKEAGLTRSIGVSNFN----HKLLElILNKPGLKyKPTCNQVechpYLN------QSKLLEFCKSKDIVLVAY 219
Cdd:cd19091 141 --RALDDLVRQGKVRYIGVSNFSawqiMKALG-ISERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 220 SALG--------------------SQRDPQWVDPDCPHL---LEEpiLKSIAKKHSGSPGQVALRYQLQR----GVVVLA 272
Cdd:cd19091 213 SPLAggllsgkyrrgqpapegsrlRRTGFDFPPVDRERGydvVDA--LREIAKETGATPAQVALAWLLSRptvsSVIIGA 290
|
330 340
....*....|....*....|....*...
gi 2091808387 273 KsfSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19091 291 R--NEEQLEDNLGAAGLSLTPEEIARLD 316
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
19-307 |
4.81e-20 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 89.49 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTyapDHTPKSQAAEATKV---AIDVGFRHIDSAYLYQNEEE-VGQAIwEKIadgtvkREEIFYTIKLWATFFR 94
Cdd:COG1453 13 VSVLGFGG---MRLPRKDEEEAEALirrAIDNGINYIDTARGYGDSEEfLGKAL-KGP------RDKVILATKLPPWVRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 95 AELVHPALERSLKKLGPDYVDLFIIHvpfAMKpGKELLPKD-ASGEIiletvelcdtWEALEKCKEAGLTRSIGVSnfNH 173
Cdd:COG1453 83 PEDMRKDLEESLKRLQTDYIDLYLIH---GLN-TEEDLEKVlKPGGA----------LEALEKAKAEGKIRHIGFS--TH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 174 KLLELILnkpglkykptcNQVECHP---------YLNQS-----KLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcphLL 239
Cdd:COG1453 147 GSLEVIK-----------EAIDTGDfdfvqlqynYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LA 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2091808387 240 EEPI-LKSIAKKHSgSPGQVALRYQLQR-GVVVL---AKSFSQerIKENFQIFD-FE-LTPEDMKAIDGLNRNLR 307
Cdd:COG1453 205 NPPEkLVELLCPPL-SPAEWALRFLLSHpEVTTVlsgMSTPEQ--LDENLKTADnLEpLTEEELAILERLAEELG 276
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
34-295 |
7.74e-20 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 87.90 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 34 KSQAAEATKVAIDVGFRHIDSA--Y-LYQNEEEVGQAIwekiADGTVKREEIFYT----IKLWATF---------FRAEL 97
Cdd:COG4989 30 PAEAAALIEAALELGITTFDHAdiYgGYTCEALFGEAL----KLSPSLREKIELQtkcgIRLPSEArdnrvkhydTSKEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 98 VHPALERSLKKLGPDYVDLFIIHVPFAMkpgkellpkdasgeiiletVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLE 177
Cdd:COG4989 106 IIASVEGSLRRLGTDYLDLLLLHRPDPL-------------------MDPEEVAEAFDELKASGKVRHFGVSNFTPSQFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 178 LiLNKpGLKYKPTCNQVECHPyLNQSKL----LEFCKSKDIVLVAYSALGSQR--DPQwvDPDCPHLLEEpiLKSIAKKH 251
Cdd:COG4989 167 L-LQS-ALDQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRlfGGF--DEQFPRLRAA--LDELAEKY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2091808387 252 SGSPGQVALRYqLQR---GVVVLAKSFSQERIKENFQIFDFELTPED 295
Cdd:COG4989 240 GVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
20-179 |
2.00e-19 |
|
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: 85.75 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYAP-DHTPKSQAAEATKV---AIDVGFRHIDSAYLYQNEEEV-GQAIwekiadGTVKREEIFYTIKLWATF-- 92
Cdd:cd19095 1 SVLGLGTSGIgRVWGVPSEAEAARLlntALDLGINLIDTAPAYGRSEERlGRAL------AGLRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 ------FRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkelLPKDASGEIIletvelcdtwEALEKCKEAGLTRSI 166
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGP---------SDDELTGEVL----------ETLEDLKAAGKVRYI 135
|
170
....*....|...
gi 2091808387 167 GVSNFNHKLLELI 179
Cdd:cd19095 136 GVSGDGEELEAAI 148
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
19-294 |
2.92e-19 |
|
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: 86.07 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFGTyAP-----DHTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIWekiadgTVKREEIF------- 83
Cdd:cd19163 13 VSKLGFGA-SPlggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYlatkvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 84 YTIKLWATF-FRAELVHPALERSLKKLGPDYVDLFIIH-VPFAmkpgkellpkdASGEIILEtvelcDTWEALEKCKEAG 161
Cdd:cd19163 86 YGLDPDKMFdFSAERITKSVEESLKRLGLDYIDIIQVHdIEFA-----------PSLDQILN-----ETLPALQKLKEEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 162 LTRSIGVSNFNHKLLELILNKPglKYKPTCNQVECHPYLNQSKLLE---FCKSKDIVLVAYSALG----SQRDPQ-Wvdp 233
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVLERS--PVKIDTVLSYCHYTLNDTSLLEllpFFKEKGVGVINASPLSmgllTERGPPdW--- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 234 dcpHLLEEPILKSIAK--KHSGSPG----QVALRYQLQ--RGVVVLAKSFSQERIKENFQIFDFELTPE 294
Cdd:cd19163 225 ---HPASPEIKEACAKaaAYCKSRGvdisKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
42-300 |
1.95e-18 |
|
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: 84.17 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 42 KVAIDVGFRHIDSAYLYQN---EEEVGQAIWEKIadgtvKREEIFYTIKLwatFFRAEL-----------VHPALERSLK 107
Cdd:cd19079 42 KRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKV---YFPMGDgpngrglsrkhIMAEVDASLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 108 KLGPDYVDLFIIHVPFAMKPgkellpkdasgeiILETVelcdtwEALEKCKEAGLTRSIGVSNFN----HKLLELILNKP 183
Cdd:cd19079 114 RLGTDYIDLYQIHRWDYETP-------------IEETL------EALHDVVKSGKVRYIGASSMYawqfAKALHLAEKNG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 184 GLKYkptcnqVECHPYLN------QSKLLEFCKSKDIVLVAYSAL------GSQRDPQ---WVDPDCPHLLE-------E 241
Cdd:cd19079 175 WTKF------VSMQNHYNllyreeEREMIPLCEEEGIGVIPWSPLargrlaRPWGDTTerrRSTTDTAKLKYdyfteadK 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2091808387 242 PIL---KSIAKKHSGSPGQVALRYQLQRGVVV-----LAKSfsqERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19079 249 EIVdrvEEVAKERGVSMAQVALAWLLSKPGVTapivgATKL---EHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-285 |
2.50e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 83.91 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 22 LGFGTY--APDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIWEKIADGTVKREEIFYTIKL-------- 88
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 89 ----WATFFRAELV----------------HPA-----LERSLKKLGPDYVDLFIIHVPFAMKPgkellpkDASGEIILE 143
Cdd:cd19099 86 eplrPLKYLEEKLGrglidvadsaglrhciSPAyledqIERSLKRLGLDTIDLYLLHNPEEQLL-------ELGEEEFYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 144 TVElcDTWEALEKCKEAGLTRSIGVSNFN----------HKLLELIL--------NKPGLKYKptcnQVECHPYLNQS-- 203
Cdd:cd19099 159 RLE--EAFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKVI----QLPLNLLEPEAlt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 204 ----------KLLEFCKSKDIVLVAYSALGSQRDPQWVDPdcPHLLEEPILKSIAkkhsgspgQVALRYQL-QRGV-VVL 271
Cdd:cd19099 233 ekntvkgealSLLEAAKELGLGVIASRPLNQGQLLGELRL--ADLLALPGGATLA--------QRALQFARsTPGVdSAL 302
|
330
....*....|....
gi 2091808387 272 AKSFSQERIKENFQ 285
Cdd:cd19099 303 VGMRRPEHVDENLA 316
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
34-300 |
5.42e-18 |
|
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: 83.00 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 34 KSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAiwEKIA----DGTVKREEIFYTIK-----LWATFFR------- 94
Cdd:cd19094 17 EAEAHEQLDYAFDEGVNFIDTAEMYpvpPSPETQGRT--EEIIgswlKKKGNRDKVVLATKvagpgEGITWPRgggtrld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 95 AELVHPALERSLKKLGPDYVDLFIIH-----VPFAMKPGKELLPKDASGEIILETVelcdtwEALEKCKEAGLTRSIGVS 169
Cdd:cd19094 95 RENIREAVEGSLKRLGTDYIDLYQLHwpdryTPLFGGGYYTEPSEEEDSVSFEEQL------EALGELVKAGKIRHIGLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 170 NFN----HKLLEL--ILNKPglkyKPTCNQvecHPY--LNQSK---LLEFCKSKDIVLVAYSAL------GSQRDPQWVD 232
Cdd:cd19094 169 NETpwgvMKFLELaeQLGLP----RIVSIQ---NPYslLNRNFeegLAEACHRENVGLLAYSPLaggvltGKYLDGAARP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 233 PDCPHLL-------------EEPI--LKSIAKKHSGSPGQVALRYQLQR----GVVVLAKSFSQerIKENFQIFDFELTP 293
Cdd:cd19094 242 EGGRLNLfpgymaryrspqaLEAVaeYVKLARKHGLSPAQLALAWVRSRpfvtSTIIGATTLEQ--LKENIDAFDVPLSD 319
|
....*..
gi 2091808387 294 EDMKAID 300
Cdd:cd19094 320 ELLAEID 326
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-299 |
1.45e-16 |
|
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: 78.80 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 14 NDGPFMPVLGFGT------YAPdhtPKSQAAEAT-KVAIDVGFRHIDSAYLYQ---NEEEVGQAIWEKiadgtvkREEIF 83
Cdd:cd19076 7 TQGLEVSALGLGCmgmsafYGP---ADEEESIATlHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 84 YTIKLWATFF----------RAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkDAsgeiileTVELCDTWEA 153
Cdd:cd19076 77 IATKFGIVRDpgsgfrgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRV------------DP-------NVPIEETVGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 154 LEKCKEAGLTRSIGVSNFN----------HKLLELilnkpGLKYKPTCNQVECHpylnqskLLEFCKSKDIVLVAYSALG 223
Cdd:cd19076 138 MAELVEEGKVRYIGLSEASadtirrahavHPITAV-----QSEYSLWTRDIEDE-------VLPTCRELGIGFVAYSPLG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 224 -------------------SQRDPQWVDPDCPH---LLEEpiLKSIAKKHSGSPGQVALRYQLQRG--VVVLAKSFSQER 279
Cdd:cd19076 206 rgfltgaikspedlpeddfRRNNPRFQGENFDKnlkLVEK--LEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKY 283
|
330 340
....*....|....*....|
gi 2091808387 280 IKENFQIFDFELTPEDMKAI 299
Cdd:cd19076 284 LEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
20-300 |
1.57e-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: 78.85 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYA------PDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAI----------------WEkIAD 74
Cdd:cd19149 12 SVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIkgrrdkvvlatkcglrWD-REG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 75 GTVKREEIFYTIKLWAtffRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkdaSGEIILEtvelcDTWEAL 154
Cdd:cd19149 91 GSFFFVRDGVTVYKNL---SPESIREEVEQSLKRLGTDYIDLYQTHWQ--------------DVETPIE-----ETMEAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 155 EKCKEAGLTRSIGVSNFN-------HKLLELILNKPglKYKPTCNQVEchpylnqSKLLEFCKSKDIVLVAYSAL----- 222
Cdd:cd19149 149 EELKRQGKIRAIGASNVSveqikeyVKAGQLDIIQE--KYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLeqgll 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 223 -------------GSQRDPQWVDPD----CPHLLEEpiLKSIAKKHSGSPGQVALRYQLQRG--VVVLAKSFSQERIKEN 283
Cdd:cd19149 220 tgkitpdrefdagDARSGIPWFSPEnrekVLALLEK--WKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEEN 297
|
330
....*....|....*..
gi 2091808387 284 FQIFDFELTPEDMKAID 300
Cdd:cd19149 298 AKAGDIRLSAEDIATMR 314
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-283 |
6.36e-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: 75.59 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFGTYA------PDHTPKsQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIWEKiadgtvkREEI--------- 82
Cdd:cd19086 5 EIGFGTWGlggdwwGDVDDA-EAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVviatkfgnr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 83 FYTIKLWATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAmkpgkELLPKDasgeiiletvelcDTWEALEKCKEAGL 162
Cdd:cd19086 77 FDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPD-----EVLDND-------------ELFEALEKLKQEGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 163 TRSIGVS-NFNHKLLELILNkpglkykPTCNQVEcHPY--LNQS---KLLEFCKSKDIVLVAysalgsqRDPqwvdpdcp 236
Cdd:cd19086 139 IRAYGVSvGDPEEALAALRR-------GGIDVVQ-VIYnlLDQRpeeELFPLAEEHGVGVIA-------RVP-------- 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 237 hlLEEPILksiakkhSGSPGQVALRYQLQR---GVVVL-AKSFSQerIKEN 283
Cdd:cd19086 196 --LASGLL-------TGKLAQAALRFILSHpavSTVIPgARSPEQ--VEEN 235
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
36-300 |
1.46e-15 |
|
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: 75.81 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 36 QAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIWEKiadgtVKREEIFYTIKL---W---ATFFR---AELVHPALE 103
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVgleWdegGEVVRnssPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 104 RSLKKLGPDYVDLFIIHVPFAMKPGKEllpkdasgeiiletvelcdTWEALEKCKEAGLTRSIGVSNFNHKLLELilnkp 183
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPLVPIEE-------------------TAEALKELLDEGKIRAIGVSNFSPEQMET----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 184 glkYKPTCNQVECHPYLN------QSKLLEFCKSKDIVLVAYSAL------GSQR-------------DPQWVDPDCPHL 238
Cdd:cd19148 157 ---FRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrgllsGKMTkdtkfegddlrrtDPKFQEPRFSQY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 239 L---EEpiLKSIAKKHSG-SPGQVALRYQLQRG--VVVLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19148 234 LaavEE--LDKLAQERYGkSVIHLAVRWLLDQPgvSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
101-300 |
4.49e-15 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 74.56 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 101 ALERSLKKLGPDYVDLFIIHVPfamkpgkellpkDasgeiilETVELCDTWEALEKCKEAGLTRSIGVSNFNHKLLELIL 180
Cdd:cd19081 103 AVEASLRRLQTDYIDLYQAHWD------------D-------PATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 181 N---KPGL-KY---KPTCNQVECHPYlnQSKLLEFCKSKDIVLVAYSAL----------------GSQRDPQWVD----P 233
Cdd:cd19081 164 ElsrQHGLpRYvslQPEYNLVDRESF--EGELLPLCREEGIGVIPYSPLaggfltgkyrseadlpGSTRRGEAAKrylnE 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2091808387 234 DCPHLLEEpiLKSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19081 242 RGLRILDA--LDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
15-300 |
6.46e-15 |
|
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: 73.81 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 15 DGPFMPVLGFG----TYAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYqneeevgqaiwekiadGTvkrEEIFYTIKLWA 90
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFY----------------GP---PDPHANLKLLA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 TFFRAElvhpalerslkklgPDYVDLFIIHVPFAMKPGkeLLPKDASGEIILETVELC---------------------- 148
Cdd:cd19077 62 RFFRKY--------------PEYADKVVLSVKGGLDPD--TLRPDGSPEAVRKSIENIlralggtkkidifeparvdpnv 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 149 ---DTWEALEKCKEAGLTRSIGVSNFNHkllELIlnKPGLKYKP-TCNQVECHPYLN---QSKLLEFCKSKDIVLVAYSA 221
Cdd:cd19077 126 pieETIKALKELVKEGKIRGIGLSEVSA---ETI--RRAHAVHPiAAVEVEYSLFSReieENGVLETCAELGIPIIAYSP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 222 L------GSQRDPQWVDPDCPH----------------LLEEpiLKSIAKKHSGSPGQVAL---RYQLQRGVVVLAKSFS 276
Cdd:cd19077 201 LgrglltGRIKSLADIPEGDFRrhldrfngenfeknlkLVDA--LQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTT 278
|
330 340
....*....|....*....|....
gi 2091808387 277 QERIKENFQIFDFELTPEDMKAID 300
Cdd:cd19077 279 LERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
20-288 |
8.35e-14 |
|
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: 69.90 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGT----YAPDHTPKSQAAEAT-KVAIDVGFRHIDSAYLY---QNEEEVGQAIWEkiadgtVKREEIFYTIKL-WA 90
Cdd:cd19096 1 SVLGFGTmrlpESDDDSIDEEKAIEMiRYAIDAGINYFDTAYGYgggKSEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 91 TFFRAELVHPALERSLKKLGPDYVDLFIIHvpfAMkpgkellpkdaSGEIILETVELCDTWEALEKCKEAGLTRSIGVSn 170
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH---GL-----------NSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FnH---KLLELILNkpglKYKPTCNQVECHpYLNQ-----SKLLEFCKSKDIVLVAYSALGSQRdpqwvdpdcpHLLEEP 242
Cdd:cd19096 140 F-HdspELLKEILD----SYDFDFVQLQYN-YLDQenqagRPGIEYAAKKGMGVIIMEPLKGGG----------LANNPP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2091808387 243 ILKSIAKKHSGSPGQVALRYQL-QRGV-VVL--AKSFSQerIKENFQIFD 288
Cdd:cd19096 204 EALAILCGAPLSPAEWALRFLLsHPEVtTVLsgMSTPEQ--LDENIAAAD 251
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
95-283 |
6.04e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 68.13 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 95 AELVHPALERSLKKLGPDYVDLFIIHVPFAMKPgkellpkdasgeiiletveLCDTWEALEKCKEAGLTRSIGVSNFNHK 174
Cdd:cd19752 94 AETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTP-------------------LEETLEAFNELVKAGKVRAIGASNFAAW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 175 LLEL---ILNKPGLKyKPTCNQVEcHPYL---------NQS----KLLEFCKS-KDIVLVAYSAL--GSQRDP------Q 229
Cdd:cd19752 155 RLERarqIARQQGWA-EFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLlsGAYTRPdrplpeQ 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2091808387 230 WVDPDCPHLLEepILKSIAKKHSGSPGQVALRYQLQR--GVVVLAKSFSQERIKEN 283
Cdd:cd19752 233 YDGPDSDARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIPLLGASTVEQLEEN 286
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-302 |
3.33e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 65.82 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 44 AIDVGFRHIDSAYLYqneeevGQAIWEKIAdGTV----KREEIFYTIKL--WATFFRAELVHPALERSLKKLGPDYVDLF 117
Cdd:cd19103 41 AMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 118 IIHvpfamkpgkelLPKDASGeiilETVELCDTwealekcKEAGLTRSIGVSNFNH---KLLELILNKPGLKYKptcnQV 194
Cdd:cd19103 114 WIH-----------NPADVER----WTPELIPL-------LKSGKVKHVGVSNHNLaeiKRANEILAKAGVSLS----AV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 195 ECHPYL-----NQSKLLEFCKSKDIVLVAYSAL-----------------GSQRdPQWVDPDCPHLLE-EPILKSIAKKH 251
Cdd:cd19103 168 QNHYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGR-AETYNPLLPQLEElTAVMAEIGAKH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 252 SGSPGQVALRYQLQRGVVVLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:cd19103 247 GASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
21-294 |
5.90e-12 |
|
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: 65.31 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFGTYAPD--HTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiadGTVKREEIFYTIKL-WAT--- 91
Cdd:cd19074 6 ELSLGTWLTFggQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKAL------KGWPRESYVISTKVfWPTgpg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 92 -----FFRAELVHpALERSLKKLGPDYVDLFIIHVPFAMKPgkellpkdasgeiILETVelcdtwEALEKCKEAGLTRSI 166
Cdd:cd19074 80 pndrgLSRKHIFE-SIHASLKRLQLDYVDIYYCHRYDPETP-------------LEETV------RAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 167 GVSNFNHKLLE--LILNKPGLKYKPTCNQVECHpYLNQSK---LLEFCKSKDIVLVAYSAL------------------G 223
Cdd:cd19074 140 GTSEWSAEQIAeaHDLARQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsrS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2091808387 224 SQRDPQWVDPDCPHLLEEPI-----LKSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKENFQIFDFELTPE 294
Cdd:cd19074 219 RATDEDNRDKKRRLLTDENLekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
20-265 |
8.24e-12 |
|
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: 64.88 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGT-YAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVG---QAIWEKIAdGTVKREEIF--------YTIK 87
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGaseRVIGEWLK-SRGNRDKVViatkgghpDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 88 LWATFFRAELVHPALERSLKKLGPDYVDLFIIH-----VPFamkpgkellpkdasGEIIletvelcdtwEALEKCKEAGL 162
Cdd:cd19082 80 MSRSRLSPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV--------------GEIV----------DTLNELVRAGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 163 TRSIGVSNFNHK-LLELI--LNKPGLkYKPTCNQV---------ECHP-----YLNQSkLLEFCKSKDIVLVAYSALG-- 223
Cdd:cd19082 136 IRAFGASNWSTErIAEANayAKAHGL-PGFAASSPqwslarpnePPWPgptlvAMDEE-MRAWHEENQLPVFAYSSQArg 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2091808387 224 --SQRDPQWVDP--------DCPHLLEE-PILKSIAKKHSGSPGQVALRYQLQ 265
Cdd:cd19082 214 ffSKRAAGGAEDdselrrvyYSEENFERlERAKELAEEKGVSPTQIALAYVLN 266
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-288 |
3.65e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 59.46 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 32 TPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEV-GQAIwekiadgtVKREEIFYTIKL----WATFFRAELVHPALERSL 106
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDSEKVlGKFL--------KRLDKFKIITKLpplkEDKKEDEAAIEASVEASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 107 KKLGPDYVDLFIIHVPfamkpgkELLPKDASgeiiletvelcDTWEALEKCKEAGLTRSIGVSNFNHKLLELILNkpglK 186
Cdd:cd19097 95 KRLKVDSLDGLLLHNP-------DDLLKHGG-----------KLVEALLELKKEGLIRKIGVSVYSPEELEKALE----S 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 187 YKPTCNQVECHPY---LNQSKLLEFCKSKDIVLVAYSAL--G-----SQRDPQWVDPDCPHLLEepiLKSIAKKHSGSPG 256
Cdd:cd19097 153 FKIDIIQLPFNILdqrFLKSGLLAKLKKKGIEIHARSVFlqGlllmePDKLPAKFAPAKPLLKK---LHELAKKLGLSPL 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 2091808387 257 QVALRYQLQR----GVVVLAKSFSQerIKENFQIFD 288
Cdd:cd19097 230 ELALGFVLSLpeidKIVVGVDSLEQ--LKEIIAAFK 263
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-302 |
3.94e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 59.97 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 44 AIDVGFRHIDSAYLY---QNEEEVGQAIWEKiadgtvkREEIFYTIKLWATFFRAELVHPALER----SLKKLGPDYVDL 116
Cdd:cd19104 41 ALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGDIGGQIERsvekSLKRLKRDSVDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 117 FIIHVPFAMKPGKELLPKdasgeiiLETVELC---DTWEALEKCKEAGLTRSIGVSNFNHK--LLELI------------ 179
Cdd:cd19104 114 LQLHNRIGDERDKPVGGT-------LSTTDVLglgGVADAFERLRSEGKIRFIGITGLGNPpaIRELLdsgkfdavqvyy 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 180 --LNKP-GLKYKPTcnqvecHPYLNQSKLLEFCKSKDIVLVAYSAL------GSQRDPQWVDPDCPHLLEEPI-----LK 245
Cdd:cd19104 187 nlLNPSaAEARPRG------WSAQDYGGIIDAAAEHGVGVMGIRVLaagaltTSLDRGREAPPTSDSDVAIDFrraaaFR 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 246 SIAKKHSGSPGQVALRYQL-QRGV--VVLAKSfSQERIKENFQIFDF-ELTPEDMKAIDGL 302
Cdd:cd19104 261 ALAREWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
21-224 |
1.67e-09 |
|
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: 57.95 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLG---FGTYAPDHTPkSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQA--------IWEKIADGTVKReeifyti 86
Cdd:cd19075 4 ILGtmtFGSQGRFTTA-EAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELglgergfkIDTKANPGVGGG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 87 klwatfFRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgkellpkDasgeiilETVELCDTWEALEKCKEAGLTRSI 166
Cdd:cd19075 76 ------LSPENVRKQLETSLKRLKVDKVDVFYLHAP------------D-------RSTPLEETLAAIDELYKEGKFKEF 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 167 GVSNFNHKLLELILN--------KP----GLkYKPTCNQVEchpylnqSKLLEFCKSKDIVLVAYSALGS 224
Cdd:cd19075 131 GLSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
101-308 |
5.03e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 56.79 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 101 ALERSLKKLGPDYVDLFIIHVPfamkpgkeLLPKDASGEIILE------TVELCDTWEALEKCKEAGLTRSIGVSNFN-- 172
Cdd:PRK10625 113 ALHDSLKRLQTDYLDLYQVHWP--------QRPTNCFGKLGYSwtdsapAVSLLETLDALAEQQRAGKIRYIGVSNETaf 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 173 --HKLLELIlNKPGLkykPTCNQVEcHPY--LNQS---KLLEFCKSKDIVLVAYSAL-----------GSQ--------- 225
Cdd:PRK10625 185 gvMRYLHLA-EKHDL---PRIVTIQ-NPYslLNRSfevGLAEVSQYEGVELLAYSCLafgtltgkylnGAKpagarntlf 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 226 -RDPQWVDPDCPHLLEEPIlkSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKENFQIFDFELTPEDMKAIDGL 302
Cdd:PRK10625 260 sRFTRYSGEQTQKAVAAYV--DIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAV 337
|
....*.
gi 2091808387 303 NRNLRY 308
Cdd:PRK10625 338 HQVYTY 343
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
22-300 |
6.41e-09 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 56.07 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 22 LGFGTYAPDHTPKSQAAEATKVA---IDVGFRHIDSAYLYQN---EEEVGqaiwEKIADgtvKREEIFYTIKLwaTFF-- 93
Cdd:cd19080 15 LGTMTFGTEWGWGADREEARAMFdayVEAGGNFIDTANNYTNgtsERLLG----EFIAG---NRDRIVLATKY--TMNrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 94 ----------RAELVHpALERSLKKLGPDYVDLFIIHVPFAMKPGKELLpkdasgeiiletvelcdtwEALEKCKEAGLT 163
Cdd:cd19080 86 pgdpnaggnhRKNLRR-SVEASLRRLQTDYIDLLYVHAWDFTTPVEEVM-------------------RALDDLVRAGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 164 RSIGVSNFnhkllelilnkPGLkYKPTCN--------------QVEcHPYLNQS---KLLEFCKSKDIVLVAYSALGS-- 224
Cdd:cd19080 146 LYVGISDT-----------PAW-VVARANtlaelrgwspfvalQIE-YSLLERTperELLPMARALGLGVTPWSPLGGgl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 225 --------------QRDPQWVDPdcPHLLEEPI-----LKSIAKKHSGSPGQVALRYQLQR--GVVVLAKSFSQERIKEN 283
Cdd:cd19080 213 ltgkyqrgeegragEAKGVTVGF--GKLTERNWaivdvVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDN 290
|
330
....*....|....*..
gi 2091808387 284 FQIFDFELTPEDMKAID 300
Cdd:cd19080 291 LGALDLTLSPEQLARLD 307
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
22-300 |
6.44e-09 |
|
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: 56.09 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 22 LGFG------TYAPDHTpKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiadgTVKREEIFYTIKLWATF 92
Cdd:cd19078 7 IGLGcmgmshGYGPPPD-KEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFGFKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 F-----------RAELVHPALERSLKKLGPDYVDLFIIH-----VPfamkpgkellpkdasgeiiLETVElcdtwEALEK 156
Cdd:cd19078 79 DggkpgplgldsRPEHIRKAVEGSLKRLQTDYIDLYYQHrvdpnVP-------------------IEEVA-----GTMKE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 157 CKEAGLTRSIGVSNFN-------HKLLELilnkpglkykpTCNQVECH-----PylnQSKLLEFCKSKDIVLVAYSALGS 224
Cdd:cd19078 135 LIKEGKIRHWGLSEAGvetirraHAVCPV-----------TAVQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 225 -----------------------QRDPQWVDPDCPhLLEepILKSIAKKHSGSPGQVALRYQLQRG--VVVLAKSFSQER 279
Cdd:cd19078 201 gfltgkidentkfdegddraslpRFTPEALEANQA-LVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSR 277
|
330 340
....*....|....*....|.
gi 2091808387 280 IKENFQIFDFELTPEDMKAID 300
Cdd:cd19078 278 LEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
21-299 |
9.53e-09 |
|
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: 55.52 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFG------TYAPDhTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIWEKIadgtvkREEIFYTIKLWAT 91
Cdd:cd19145 14 AQGLGcmglsgDYGAP-KPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 92 FFRA---------ELVHPALERSLKKLGPDYVDLFIIHVpfamkpgkellpkdasgeiILETVELCDTWEALEKCKEAGL 162
Cdd:cd19145 87 EIGGsgvevrgdpAYVRAACEASLKRLDVDYIDLYYQHR-------------------IDTTVPIEITMGELKKLVEEGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 163 TRSIGVSNFNHKllelILNKPGLKYKPTCNQVECHPYLN--QSKLLEFCKSKDIVLVAYSALGS---------------- 224
Cdd:cd19145 148 IKYIGLSEASAD----TIRRAHAVHPITAVQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLGRgffagkakleellens 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 225 ---QRDPQWVDPDCPH---LLEEpiLKSIAKKHSGSPGQVALRYQLQRG--VVVLAKSFSQERIKENFQIFDFELTPEDM 296
Cdd:cd19145 224 dvrKSHPRFQGENLEKnkvLYER--VEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDL 301
|
...
gi 2091808387 297 KAI 299
Cdd:cd19145 302 KEI 304
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
19-300 |
2.24e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 55.00 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 19 MPVLGFG---TYAPDHTPKSQAAEATKvAIDVGFRHIDSAYLY-----QNEEEVGQAIWEKIAdgtVKREEIFYTIK--- 87
Cdd:PRK09912 25 LPALSLGlwhNFGHVNALESQRAILRK-AFDLGITHFDLANNYgpppgSAEENFGRLLREDFA---AYRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 88 -LWATFF-----RAELVhPALERSLKKLGPDYVDLFIIHVpfamkpgkellpkdasgeiILETVELCDTWEALEKCKEAG 161
Cdd:PRK09912 101 dMWPGPYgsggsRKYLL-ASLDQSLKRMGLEYVDIFYSHR-------------------VDENTPMEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 162 LTRSIGVSNFN----HKLLELI--LNKPGLKYKPTCNQVecHPYLNQSKLLEFCKSKDIVLVAYSALGS----------- 224
Cdd:PRK09912 161 KALYVGISSYSpertQKMVELLreWKIPLLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQglltgkylngi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 225 ------QRDPQWVDPDCPHLLEEPILKSI------AKKHSGSPGQVALRYQL--QRGVVVLAKSFSQERIKENFQIF-DF 289
Cdd:PRK09912 239 pqdsrmHREGNKVRGLTPKMLTEANLNSLrllnemAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALnNL 318
|
330
....*....|.
gi 2091808387 290 ELTPEDMKAID 300
Cdd:PRK09912 319 TFSTEELAQID 329
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
33-288 |
2.93e-08 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 54.08 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 33 PKSQAAEAT-KVAIDVGFRHIDSAYLYQN---EEEVGQAIwekiADGTVKREEIFYTIKLW----ATF-FRAELVHPALE 103
Cdd:cd19153 30 LEQDEAVAIvAEAFAAGINHFDTSPYYGAessEAVLGKAL----AALQVPRSSYTVATKVGryrdSEFdYSAERVRASVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 104 RSLKKLGPDYVDLFIIHvpfamkpGKELLPKDasgEIILETVelcdtwEALEKCKEAGLTRSIGVSNFNHKLLELILNK- 182
Cdd:cd19153 106 TSLERLHTTYLDVVYLH-------DIEFVDYD---TLVDEAL------PALRTLKDEGVIKRIGIAGYPLDTLTRATRRc 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 183 -PGlkyKPTCNQVECHPYLNQSKLLE----FCKSKDIVLVAYSALG-----SQRDPQWvDPdCPHLLEEpiLKSIAKKHS 252
Cdd:cd19153 170 sPG---SLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmglltSQGPPPW-HP-ASGELRH--YAAAADAVC 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2091808387 253 GSPG----QVALRYQLQRGVVV---LAKSFSQERIKENFQIFD 288
Cdd:cd19153 243 ASVEaslpDLALQYSLAAHAGVgtvLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
23-283 |
5.48e-08 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 53.42 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 23 GFGtyapDHTPKSQAAEATKVAIDVGFRHIDSAYLY-----QNEEEVGQAIWEkiaDGTVKREEIFYTIK----LWATFF 93
Cdd:cd19089 21 NFG----DYTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVISTKagygMWPGPY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 94 -----RAELVHpALERSLKKLGPDYVDLFIIHVPfamkpgkellpkDAsgEIILEtvelcDTWEALEKCKEAGLTRSIGV 168
Cdd:cd19089 94 gdggsRKYLLA-SLDQSLKRMGLDYVDIFYHHRY------------DP--DTPLE-----ETMTALADAVRSGKALYVGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 169 SNFNHKLLEL---ILNKpgLKYKPTCNQVechPY--LNQS---KLLEFCKSKDIVLVAYSAL---------------GSQ 225
Cdd:cd19089 154 SNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRWaedGLLEVLEEAGIGFIAFSPLaqglltdkylngippDSR 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2091808387 226 RDPQWVDPDCPHLLEEPI-----LKSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKEN 283
Cdd:cd19089 229 RAAESKFLTEEALTPEKLeqlrkLNKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDN 293
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
21-278 |
6.53e-08 |
|
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: 53.05 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFGTYAP---DHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEV-GQAIwEKIADGtVKREEIFYTIK-----LWAT 91
Cdd:cd19164 17 IFGAATFSYqytTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRDE-FPRDTYFIITKvgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 92 FFRAELVHPALERSLKKLGPDYVDLFIIH-VPFamkpgkellpkdASGEIILETVelcdtwEALEKCKEAGLTRSIGVSN 170
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLVYLHdVEF------------VADEEVLEAL------KELFKLKDEGKIRNVGISG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 171 FNHKLL----ELILNKPG------LKYkptcnqveCHPYLNQSKLLEF-----CKSKDIVLVAYSALG-----SQRDPQW 230
Cdd:cd19164 157 YPLPVLlrlaELARTTAGrpldavLSY--------CHYTLQNTTLLAYipkflAAAGVKVVLNASPLSmgllrSQGPPEW 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2091808387 231 vDPdCPHLLEEPILKSIA--KKHSGSPGQVALRYQLQ----RGVVVLAKSFSQE 278
Cdd:cd19164 229 -HP-ASPELRAAAAKAAEycQAKGTDLADVALRYALRewggEGPTVVGCSNVDE 280
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
20-294 |
9.51e-08 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 52.61 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGT------YAPdhTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQA----------IWEKI-------A 73
Cdd:cd19152 1 PKLGFGTaplgnlYEA--VSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAAlrelgredyvISTKVgrllvplQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 74 DGTVKREEIF-YTIKLWATF-FRAELVHPALERSLKKLGPDYVDLFIIHVPfamkpgKELLPKDASGEIILETVElcDTW 151
Cdd:cd19152 79 EVEPTFEPGFwNPLPFDAVFdYSYDGILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDEHFAQAIK--GAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 152 EALEKCKEAGLTRSIGV-SNFNHKLLELILNKpglkyKPTCNQVECHpY--LNQSKLLEF---CKSKDIVLV---AYSA- 221
Cdd:cd19152 151 RALEELREEGVIKAIGLgVNDWEVILRILEEA-----DLDWVMLAGR-YtlLDHSAARELlpeCEKRGVKVVnagPFNSg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 222 --LGSQRDPQWVDPDCPhllEEPI-----LKSIAKKHSGSPGQVALRYQLQRGVV--VLAKSFSQERIKENFQIFDFELT 292
Cdd:cd19152 225 flAGGDNFDYYEYGPAP---PELIarrdrIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALLATEIP 301
|
..
gi 2091808387 293 PE 294
Cdd:cd19152 302 AA 303
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
35-223 |
1.24e-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: 52.19 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 35 SQAAEAT-----KVAIDVGFRHIDSAYLYQN---EEEVGQAIWEKiadgtvkREEIFYTIKLwatFFR-----------A 95
Cdd:cd19087 25 GRTDEETsfaimDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKV---FGPmgddpndrglsR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 96 ELVHPALERSLKKLGPDYVDLFIIHVPFAMKPGKEllpkdasgeiiletvelcdTWEALEKCKEAGLTRSIGVSNF---- 171
Cdd:cd19087 95 RHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNFaawq 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 172 ---------NHKLLELILNKPglKYKPTCNQVECHpylnqskLLEFCKSKDIVLVAYSALG 223
Cdd:cd19087 156 iakaqgiaaRRGLLRFVSEQP--MYNLLKRQAELE-------ILPAARAYGLGVIPYSPLA 207
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
20-169 |
1.84e-07 |
|
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: 51.59 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTYA---PDHTPKSQAAEATKVAIDVGFRHIDSAYLY---QNEEEVGQAIwekiadGTVKREEIFYTIKLWATF- 92
Cdd:cd19162 1 PRLGLGAASlgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAAL------ARHPRAEYVVSTKVGRLLe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 93 ---------------FRAELVHPALERSLKKLGPDYVDLFIIHVPfamkPGKELLPkdasgeiiletveLCDTWEALEKC 157
Cdd:cd19162 75 pgaagrpagadrrfdFSADGIRRSIEASLERLGLDRLDLVFLHDP----DRHLLQA-------------LTDAFPALEEL 137
|
170
....*....|..
gi 2091808387 158 KEAGLTRSIGVS 169
Cdd:cd19162 138 RAEGVVGAIGVG 149
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
21-283 |
9.96e-07 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.78 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFG------TYAPdhTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIwekiADGTVKREEIFYTIKLW-- 89
Cdd:PLN02587 13 SVGFGasplgsVFGP--VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKAL----KALGIPREKYVVSTKCGry 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 90 -ATF-FRAELVHPALERSLKKLGPDYVDLFIIH-VPFAmkpgkellpkdASGEIILETVElcdtweALEKCKEAGLTRSI 166
Cdd:PLN02587 87 gEGFdFSAERVTKSVDESLARLQLDYVDILHCHdIEFG-----------SLDQIVNETIP------ALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 167 GVSNFNHKLLELILNK--PG-----LKYkptcnqveCHPYLNQSKLLE---FCKSKDIVLVAYSALG-----SQRDPQWv 231
Cdd:PLN02587 150 GITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASPLAmglltENGPPEW- 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2091808387 232 DPDCPHlleepiLKSI---AKKHSGSPGQ----VALRYQL--QRGVVVLAKSFSQERIKEN 283
Cdd:PLN02587 221 HPAPPE------LKSAcaaAATHCKEKGKniskLALQYSLsnKDISTTLVGMNSVQQVEEN 275
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
21-122 |
1.94e-04 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 42.58 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 21 VLGFG---TYApDHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIwekiADGTVKREEIFYTIKLwatFF- 93
Cdd:cd19143 15 ALSFGswvTFG-NQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAI----KELGWPRSDYVVSTKI---FWg 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2091808387 94 ------------RAELVHpALERSLKKLGPDYVDLFIIHVP 122
Cdd:cd19143 87 gggpppndrglsRKHIVE-GTKASLKRLQLDYVDLVFCHRP 126
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
20-167 |
1.36e-03 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 40.00 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 20 PVLGFGTyAP-----DHTPKSQAAEATKVAIDVGFRHIDSAYLYQN---EEEVGQAIWEKIADGTV---KREEIFYTIKL 88
Cdd:cd19161 1 SELGLGT-AGlgnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEFVlstKVGRLLKPARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091808387 89 WATFFRAELVHP----------------ALERSLKKLGPDYVDLFIIHVPFAMKPGKELlpkdasgeIILETVELCDT-W 151
Cdd:cd19161 80 GSVPDPNGFVDPlpfeivydysydgimrSFEDSLQRLGLNRIDILYVHDIGVYTHGDRK--------ERHHFAQLMSGgF 151
|
170
....*....|....*.
gi 2091808387 152 EALEKCKEAGLTRSIG 167
Cdd:cd19161 152 KALEELKKAGVIKAFG 167
|
|
| |
