|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
15-322 |
0e+00 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 680.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHV 94
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRR 174
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 175 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLKDALLNSLGKRYNKT 254
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 255 AAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPF 322
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-309 |
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: 522.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 8 HRIPLSDGNSIPIIGLGTYSePKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGK 87
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYA-PEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 88 LWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLG 167
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 168 VSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLKDALLNSL 247
Cdd:cd19108 160 VSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174695 248 GKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFV 309
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-326 |
1.17e-147 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 417.59 E-value: 1.17e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYsepKSTPkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHV 94
Cdd:cd19107 1 GAKMPILGLGTW---KSPP-GQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRR 174
Cdd:cd19107 77 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 175 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPiWVNVSSPPLLKDALLNSLGKRYNKT 254
Cdd:cd19107 157 QIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP-WAKPEDPSLLEDPKIKEIAAKHNKT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174695 255 AAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY 326
Cdd:cd19107 236 TAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
12-309 |
1.88e-138 |
|
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: 394.44 E-value: 1.88e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYsepKSTPkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGK-VRREDIFYCGKLWA 90
Cdd:cd19106 1 LHTGQKMPLIGLGTW---KSKP-GQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 91 TNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSN 170
Cdd:cd19106 77 TKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 171 FNRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPiWVNVSSPPLLKDALLNSLGKR 250
Cdd:cd19106 157 FNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRP-WAKPDEPVLLEEPKVKALAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5174695 251 YNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFV 309
Cdd:cd19106 234 YNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
18-326 |
1.17e-126 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 364.28 E-value: 1.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYsepKSTPkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEM 97
Cdd:cd19110 4 IPAVGLGTW---KASP-GEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 98 VRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLE 177
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 178 LILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIwvnvsspPLLKDALLNSLGKRYNKTAAQ 257
Cdd:cd19110 160 RLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGV-------DLIDDPVIQRIAKKHGKSPAQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174695 258 IVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY 326
Cdd:cd19110 233 ILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-309 |
2.66e-125 |
|
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: 360.44 E-value: 2.66e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 9 RIPLSDGNSIPIIGLGTYsepKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKL 88
Cdd:cd19116 2 TIKLNDGNEIPAIALGTW---KLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKpgdEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGV 168
Cdd:cd19116 79 WNSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILNkpGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGT-----SRNPiwvnvssPPLLKDAL 243
Cdd:cd19116 156 SNFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRlvprgQTNP-------PPRLDDPT 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5174695 244 LNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFV 309
Cdd:cd19116 227 LVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
18-300 |
2.47e-124 |
|
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: 356.41 E-value: 2.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYSepksTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIaegkVRREDIFYCGKLWATNHVPEM 97
Cdd:cd19071 1 MPLIGLGTYK----LKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 98 VRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDeiyprdengkwlyHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLE 177
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 178 LILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPiwvnvssppLLKDALLNSLGKRYNKTAAQ 257
Cdd:cd19071 140 ELLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 5174695 258 IVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE 300
Cdd:cd19071 209 VLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
10-307 |
8.30e-121 |
|
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: 349.40 E-value: 8.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYsepKSTPKgACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLW 89
Cdd:cd19154 4 ITLSNGVKMPLIGLGTW---QSKGA-EGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGT--SRNPIWVNVSSPP--LLKDALLN 245
Cdd:cd19154 160 NFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgRANFTKSTGVSPApnLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174695 246 SLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVR 307
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
14-308 |
1.27e-119 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 344.73 E-value: 1.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 14 DGNSIPIIGLGTYsepKSTPKgACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKLWATNH 93
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGE-EAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA----SGVPREELFVTTKVWNDNH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 94 VPEMVRPTLERTLRVLQLDYVDLYIIEVPMafkPGDeiyprdengkwlyhksnLCATWEAMEACKDAGLVKSLGVSNFNR 173
Cdd:COG0656 73 GYDDTLAAFEESLERLGLDYLDLYLIHWPG---PGP-----------------YVETWRALEELYEEGLIRAIGVSNFDP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 174 RQLELILNKPGlkHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGKRYNK 253
Cdd:COG0656 133 EHLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGK 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 254 TAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:COG0656 200 TPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-309 |
5.91e-113 |
|
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: 329.37 E-value: 5.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 11 PLSDGNSIPIIGLGTYsepKSTPkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWA 90
Cdd:cd19123 5 PLSNGDLIPALGLGTW---KSKP-GEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 91 TNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGdEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSN 170
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 171 FNRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGT-SRNPIWVNVSSPPLLKDALLNSLGK 249
Cdd:cd19123 160 FSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFV 309
Cdd:cd19123 238 KHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-297 |
1.61e-108 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 317.75 E-value: 1.61e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 11 PLSDGNSIPIIGLGTY-SEPkstpkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLW 89
Cdd:cd19125 4 KLNTGAKIPAVGLGTWqADP-----GVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDEngkwlYHKSNLCATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19125 79 CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEE-----VLPPDIPSTWKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLkhKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGtSRNPIWVNvssPPLLKDALLNSLGK 249
Cdd:cd19125 154 NFSVKKLEDLLAVARV--PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLG-SPGTTWVK---KNVLKDPIVTKVAE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMK 297
Cdd:cd19125 228 KLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFA 275
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-302 |
1.13e-97 |
|
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: 290.08 E-value: 1.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTY-SEPkstpkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAE-GKVRREDIFYCGKLW 89
Cdd:cd19118 1 LNTGNKIPAIGLGTWqAEP-----GEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPR-----DENGKWLYHKSNLCATWEAMEACKDAGLVK 164
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavptNGGEVDLDLSVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 165 SLGVSNFNRRQLELILNKPGLkhKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnVSSPPLLKDALL 244
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 245 NSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQifDFSLTEEEMKDIEAL 302
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-308 |
4.52e-97 |
|
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: 288.63 E-value: 4.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYSEPKSTpkgaCATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHV 94
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEE----VRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKpgdeiyPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRR 174
Cdd:cd19111 77 FKDTEKSLEKSLENLKLPYVDLYLIHHPCGFV------NKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 175 QLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTsrnPIWVNVSSPP----LLKDALLNSLGKR 250
Cdd:cd19111 151 QINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGS---PGRANQSLWPdqpdLLEDPTVLAIAKE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 251 YNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:cd19111 226 LDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-307 |
6.67e-97 |
|
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: 289.04 E-value: 6.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSEPKSTpkgaCATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLW 89
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEE----IETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFK-PGDEIYPRDENGKWLY-HKSNLCATWEAMEACKDAGLVKSLG 167
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQdYTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 168 VSNFNRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGT-SRNPIWVNVSSPP-----LLKD 241
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpGAAHFSPGTGSPSgsspdLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5174695 242 ALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVR 307
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-303 |
2.73e-91 |
|
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: 272.53 E-value: 2.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYsepKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKiaegKVRREDIFYCGKLW 89
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS----GIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMafkpGDeiyprdengkwlYHksnlcATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPF----GD------------VY-----GAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQL-ELILNKpglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIwvnvsspplLKDALLNSLG 248
Cdd:cd19133 133 NFYPDRLvDLILHN---EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNL---------FENPVLTEIA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 249 KRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:cd19133 201 EKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-302 |
4.26e-91 |
|
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: 272.99 E-value: 4.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 14 DGNSIPIIGLGTYSEPKStPKGACATSVKvAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVR-REDIFYCGKLWATN 92
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS-PEDIKAAVLE-AIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 93 HVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENgkwLYHKSNLCATWEAMEACKDAGLVKSLGVSNFN 172
Cdd:cd19124 79 AHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 173 RRQLELIL---NKPglkhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPiWvnvSSPPLLKDALLNSLGK 249
Cdd:cd19124 156 CKKLQELLsfaTIP-----PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-W---GSNAVMESDVLKEIAA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19124 227 AKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
10-307 |
9.49e-91 |
|
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: 273.21 E-value: 9.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSepksTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLW 89
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWR----MEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHvpEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKP---GDEIYPRDENGKW-LYHKSNLCATWEAMEACKDAGLVKS 165
Cdd:cd19112 79 NSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 166 LGVSNFnrrqlELILNKPGL---KHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLG-TSRNPIWVNVSSPplLKD 241
Cdd:cd19112 157 IGISNY-----DIFLTRDCLaysKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5174695 242 ALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVR 307
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
10-314 |
6.83e-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: 268.55 E-value: 6.83e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSEPKSTpkgaCATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLW 89
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNAT----AADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFK--PGDEIYPR-----DENgKWLYHKSNLCATWEAMEACKDAGL 162
Cdd:cd19113 79 NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPgfycgDGD-NFVYEDVPILDTWKALEKLVDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 163 VKSLGVSNFNRRQLELILNkpGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTS-----RNPIWVNVssPP 237
Cdd:cd19113 158 IKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRALNT--PT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5174695 238 LLKDALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMW 314
Cdd:cd19113 234 LFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDPWDW 310
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-308 |
9.15e-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: 267.79 E-value: 9.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 13 SDGNSIPIIGLGTYSEPKSTPKGAcatsVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATN 92
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNA----VKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 93 HVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKS-NLCATWEAMEACKDAGLVKSLGVSNF 171
Cdd:cd19129 77 HRPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 172 NRRQLELILNKPGLkhKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSrnpiwvnvSSPPLLKDALLNSLGKRY 251
Cdd:cd19129 157 SLEKLREIFEAARI--KPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHG--------MEPKLLEDPVITAIARRV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 252 NKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIfdFSLTEEEMKDI-EALNKNVRF 308
Cdd:cd19129 227 NKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-300 |
2.12e-88 |
|
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: 264.90 E-value: 2.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYSEPKSTpkgaCATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIrekiAEGKVRREDIFYCGKLWATNHVPEM 97
Cdd:cd19073 1 IPALGLGTWQLRGDD----CANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 98 VRPTLERTLRVLQLDYVDLYIIEVPmafkpGDEIYPRDengkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLE 177
Cdd:cd19073 73 LKKSVDRSLEKLGTDYVDLLLIHWP-----NPTVPLEE--------------TLGALKELKEAGKVKSIGVSNFTIELLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 178 LILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGKRYNKTAAQ 257
Cdd:cd19073 134 EALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE-----------VLRDPVIQEIAEKYDKTPAQ 200
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 5174695 258 IVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE 300
Cdd:cd19073 201 VALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-308 |
2.20e-88 |
|
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: 265.64 E-value: 2.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGT----YSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKiaegKVRREDIFYCGKLW- 89
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEmvrpTLERTLRVLQLDYVDLYIIEVPMAFKPGDEiyprdengkwlyhksNLCATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19120 77 GIKDPRE----ALRKSLAKLGVDYVDLYLIHSPFFAKEGGP---------------TLAEAWAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPglKHKPVSNQVECHPYFT--QPKLLKFCQQHDIVITAYSPLgtsrNPIWVNVSSPpllKDALLNSL 247
Cdd:cd19120 138 NFRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPL----SPLTRDAGGP---LDPVLEKI 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174695 248 GKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:cd19120 209 AEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
18-302 |
2.79e-88 |
|
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: 265.26 E-value: 2.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYsepKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEM 97
Cdd:cd19136 1 MPILGLGTF---RLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 98 VRPTLERTLRVLQLDYVDLYIIEVPMA--FKPGDEIyprdengkwlyHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQ 175
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGVqgLKPSDPR-----------NAELRRESWRALEDLYKEGKLRAIGVSNYTVRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 176 LELILNKPGLkhKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTsrnpiwvnvSSPPLLKDALLNSLGKRYNKTA 255
Cdd:cd19136 147 LEELLKYCEV--PPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 5174695 256 AQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19136 216 AQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
19-302 |
1.95e-86 |
|
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: 260.92 E-value: 1.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 19 PIIGLGTYSEPKSTPKgacaTSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMV 98
Cdd:cd19128 2 PRLGFGTYKITESESK----EAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 99 RPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLEL 178
Cdd:cd19128 78 KEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 179 ILNKpgLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTS-RNPIWVnvssppLLKDALLNSLGKRYNKTAAQ 257
Cdd:cd19128 158 LLNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSyGDGNLT------FLNDSELKALATKYNTTPPQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 5174695 258 IVLRFNIQR---GVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19128 230 VIIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-308 |
4.96e-86 |
|
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: 261.20 E-value: 4.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 6 ASHRIPLSDGNSIPIIGLGTYSEPKSTpkgaCATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYC 85
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDT----CADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 86 GKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEI--YP---RDENGKWLYHKSNLCATWEAMEACKDA 160
Cdd:cd19115 77 SKLWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAvrYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 161 GLVKSLGVSNFNrRQLELILNKPGlKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLG-TSRNPIWVN--VSSPP 237
Cdd:cd19115 157 GLARSIGVSNFS-AQLLMDLLRYA-RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpQSFLELDLPgaKDTPP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174695 238 LLKDALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:cd19115 235 LFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-303 |
7.41e-86 |
|
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: 258.84 E-value: 7.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYsepKSTPKGAcATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKLW 89
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEA-ASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMafkPGDEIYprdengkwlyhksnlCATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19131 74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQDKY---------------VETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGK 249
Cdd:cd19131 136 NFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAE 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:cd19131 203 KHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-303 |
1.41e-83 |
|
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: 252.96 E-value: 1.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYSEpkstpKG-ACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKLWA 90
Cdd:cd19132 1 LNDGTQIPAIGFGTYPL-----KGdEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 91 TNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMafkpgdeiyPRdeNGKWLyhksnlcATWEAMEACKDAGLVKSLGVSN 170
Cdd:cd19132 72 RHHGYEEALRTIEESLYRLGLDYVDLYLIHWPN---------PS--RDLYV-------EAWQALIEAREEGLVRSIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 171 FNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNpiwvnvssppLLKDALLNSLGKR 250
Cdd:cd19132 134 FLPEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5174695 251 YNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:cd19132 202 HGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-304 |
2.24e-83 |
|
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: 253.57 E-value: 2.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYsepKSTPkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIRekiAEGkVRREDIFYCGKLWAT 91
Cdd:cd19117 8 LNTGAEIPAVGLGTW---QSKP-NEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLWCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 92 NHvpEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPG--DEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19117 80 WH--RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTsrnpiwvnvSSPPLLKDALLNSLGK 249
Cdd:cd19117 158 NFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS---------TNAPLLKEPVIIKIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIfdFSLTEEEMKDIEALNK 304
Cdd:cd19117 229 KHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
12-308 |
3.19e-83 |
|
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: 252.31 E-value: 3.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYSEPKSTpkgACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKLWAT 91
Cdd:cd19157 4 LNNGVKMPWLGLGVFKVEEGS---EVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 92 NHVPEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgdeiyprdenGKWLYHKsnlcaTWEAMEACKDAGLVKSLGVSNF 171
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWP---------------VKGKYKE-----TWKALEKLYKDGRVRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 172 NRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGKRY 251
Cdd:cd19157 137 QVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEKY 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 5174695 252 NKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:cd19157 204 NKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-302 |
5.07e-83 |
|
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: 251.41 E-value: 5.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYsepKSTPkGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIrekiAEGKVRREDIFYCGKLWATNHV 94
Cdd:cd19140 5 GVRIPALGLGTY---PLTG-EECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYII-----EVPMAfkpgdeiyprdengkwlyhksnlcATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19140 77 PDDFLASVEESLRKLRTDYVDLLLLhwpnkDVPLA------------------------ETLGALNEAQEAGLARHIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKHkpVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGK 249
Cdd:cd19140 133 NFTVALLREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGR 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5174695 250 RYNKTAAQIVLRFNIQR-GVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19140 200 KHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-308 |
9.77e-82 |
|
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: 248.59 E-value: 9.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYSepksTPKGACA-TSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKiaegKVRREDIFYCGKLWA 90
Cdd:cd19156 3 LANGVEMPRLGLGVWR----VQDGAEAeNAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 91 TNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDeiyprdengkwlyhksnlcaTWEAMEACKDAGLVKSLGVSN 170
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKD--------------------TWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 171 FNRRQLELILNKpgLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGKR 250
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 251 YNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
12-302 |
2.20e-81 |
|
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: 248.21 E-value: 2.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYSEPKSTPKGACATsvkvAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGkVRREDIFYCGKLWAT 91
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAH----ALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 92 NHvpEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKP--GDEIYPRDENGKW-LYHKSNLCATWEAMEACKDAGLVKSLGV 168
Cdd:cd19121 81 YH--RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRdLDWDWNHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILnkPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTsrnpiwvnvSSPPLLKDALLNSLG 248
Cdd:cd19121 159 SNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS---------TGSPLISDEPVVEIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5174695 249 KRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFslTEEEMKDIEAL 302
Cdd:cd19121 228 KKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-303 |
4.08e-80 |
|
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: 244.27 E-value: 4.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSepksTPKG-ACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKL 88
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQ----TPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAfkpgdeiyprdenGKWLyhksnlcATWEAMEACKDAGLVKSLGV 168
Cdd:cd19126 73 WNDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK-------------DKFI-------DTWKALEKLYASGKVKAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILnkpglKH---KPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLN 245
Cdd:cd19126 133 SNFQEHHLEELL-----AHadvVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 246 SLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:cd19126 197 AIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-314 |
3.40e-76 |
|
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: 235.91 E-value: 3.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYsepKSTPKgACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHV 94
Cdd:cd19114 1 GDKMPLVGFGTA---KIKAN-ETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGD--EIYP----RDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGV 168
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaENYPflwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNrrqLELILN-KPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGtsrNPIWVNVSS-----PPLLKDA 242
Cdd:cd19114 157 ANFN---VQLILDlLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFG---NAVYTKVTKhlkhfTNLLEHP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174695 243 LLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMW 314
Cdd:cd19114 231 VVKKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVVY 302
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-308 |
2.22e-75 |
|
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: 233.54 E-value: 2.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSEPKStpKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLW 89
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHED--RAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHvpEMVRPTLERTLRVLQLDYVDLYIIEVPMAFK-----PGDEIYPRDENGKWLYHKS-NLCATWEAMEACKDAGLV 163
Cdd:cd19119 82 PTFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASgDHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 164 KSLGVSNFNRRQLELILNKpgLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIwvnvsspplLKDAL 243
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPN---------LKNPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5174695 244 LNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIfdFSLTEEEMKDIE--ALNKNVRF 308
Cdd:cd19119 229 VKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDdiGEKYPVRF 293
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-303 |
3.03e-75 |
|
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: 232.30 E-value: 3.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSepksTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKiaegKVRREDIFYCGKLW 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ----TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIyprdengkwlyhksnlcATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19127 73 ISDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTI-----------------QAYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPP-LLKDALLNSLG 248
Cdd:cd19127 136 NFTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGdVLQDPTITGLA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 249 KRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:cd19127 214 EKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-302 |
4.00e-75 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 231.83 E-value: 4.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTysepkSTPKGACATSVKVAI-DTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKL 88
Cdd:cd19135 5 VRLSNGVEMPILGLGT-----SHSGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIyprdengkwlyhKSNLCATWEAMEACKDAGLVKSLGV 168
Cdd:cd19135 76 WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNV------------KETRAETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSrnpiwvnvsspPLLKDALLNSLG 248
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKG-----------KALEEPTVTELA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5174695 249 KRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19135 211 KKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-303 |
3.66e-70 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 219.01 E-value: 3.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 9 RIPLSDGNSIPIIGLGTYSEPKSTPKGACATsvkvAIDTGYRHIDGAYIYQNEHEVGEAIrekiAEGKVRREDIFYCGKL 88
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVAT----ALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMafkPGdeiyprdengkwlyhKSNLCATWEAMEACKDAGLVKSLGV 168
Cdd:cd19130 73 WNDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPT---PA---------------AGNYVHTWEAMIELRAAGRTRSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLG 248
Cdd:cd19130 135 SNFLPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 249 KRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:cd19130 202 AAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-302 |
3.59e-69 |
|
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: 216.07 E-value: 3.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYSEpkstpKG-ACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIrekiAEGKVRREDIFYCGKLWATNHVPE 96
Cdd:cd19139 1 IPAFGLGTFRL-----KDdVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 97 MVRPTLERTLRVLQLDYVDLYIIEVPmafKPGDEIyprdengkwlyhksNLCATWEAMEACKDAGLVKSLGVSNFNRRQL 176
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWP---SPNDEV--------------PVEEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 177 ELILNKPGlKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGKRYNKTAA 256
Cdd:cd19139 135 DEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5174695 257 QIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19139 203 QIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
10-307 |
1.13e-65 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 208.00 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYsepKSTPKGAcATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREkiaeGKVRREDIFYCGKLW 89
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVW---QASNEEV-ITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHvpEMVRPTLERTLRVLQLDYVDLYIIEVPMAfkpgdeiyprdengkwlyHKSNLCATWEAMEACKDAGLVKSLGVS 169
Cdd:PRK11565 79 NDDH--KRPREALEESLKKLQLDYVDLYLMHWPVP------------------AIDHYVEAWKGMIELQKEGLIKSIGVC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNpiwvNVSSPPLLKDallnsLGK 249
Cdd:PRK11565 139 NFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK----GVFDQKVIRD-----LAD 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVR 307
Cdd:PRK11565 208 KYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
12-304 |
1.79e-64 |
|
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: 205.55 E-value: 1.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 12 LSDGNSIPIIGLGTYSEPKStpKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEG-KVRREDIFYCGKLWA 90
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGA--KGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 91 TNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPR-DENGKWLYHKS---NLCATWEAMEACKDAGLVKSL 166
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILKDlteNPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 167 GVSNFNRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGtSRNPiwVNVSSPPLLKDALLNS 246
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLG-SQNQ--VPSTGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 247 LGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSlteeeMKDIEALNK 304
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELS-----DEDFEAINQ 288
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-308 |
4.82e-64 |
|
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: 203.55 E-value: 4.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 10 IPLSDGNSIPIIGLGTYSEPKSTPKGacatSVKVAIDTGYRHIDGAYIYQNEHEVGEAIrekiAEGKVRREDIFYCGKLW 89
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAER----SVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAfkpgdeiyprdENGKWLyhksnlcATWEAMEACKDAGLVKSLGVS 169
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGK 249
Cdd:cd19134 137 NFTAEHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAA 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRF 308
Cdd:cd19134 204 AHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-300 |
4.72e-60 |
|
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: 193.21 E-value: 4.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTY------SEPKSTPKGAcATSVKVAIDTGYRHIDGAYIYQN---EHEVGEAIRekiaegKVRREDIFYC 85
Cdd:cd19072 1 GEEVPVLGLGTWgigggmSKDYSDDKKA-IEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 86 GKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEvpmafkpgdeiyprdengkWLYHKSNLCATWEAMEACKDAGLVKS 165
Cdd:cd19072 74 TKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIH-------------------WPNPSIPIEETLRAMEELVEEGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 166 LGVSNFNRRQLELILNKPGlKHKPVSNQVECHPYFTQP--KLLKFCQQHDIVITAYSPLGTSRnpiwVNVSSPPllkdAL 243
Cdd:cd19072 135 IGVSNFSLEELEEAQSYLK-KGPIVANQVEYNLFDREEesGLLPYCQKNGIAIIAYSPLEKGK----LSNAKGS----PL 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5174695 244 LNSLGKRYNKTAAQIVLRFNIQR-GVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE 300
Cdd:cd19072 206 LDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-309 |
2.91e-57 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 186.00 E-value: 2.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 17 SIPIIGLGTYSEpkstpKG-ACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIrekiAEGKVRREDIFYCGKLWATNHVP 95
Cdd:PRK11172 2 SIPAFGLGTFRL-----KDqVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 96 EMVRPTLERTLRVLQLDYVDLYIIEVPmafKPGDEIyprdengkwlyhksnlcATWEAMEACKDA---GLVKSLGVSNFN 172
Cdd:PRK11172 73 DKLIPSLKESLQKLRTDYVDLTLIHWP---SPNDEV-----------------SVEEFMQALLEAkkqGLTREIGISNFT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 173 RRQLELILNKPGlKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRnpiwvnvssppLLKDALLNSLGKRYN 252
Cdd:PRK11172 133 IALMKQAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 5174695 253 KTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFV 309
Cdd:PRK11172 201 ATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
21-303 |
4.32e-56 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 183.67 E-value: 4.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLGTYS---EPKSTPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKiaegKVRREDIFYCGKL------ 88
Cdd:pfam00248 1 IGLGTWQlggGWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGV 168
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------DPDTPIEE-------------TWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILNKPglKHKPVSNQVECHPYF--TQPKLLKFCQQHDIVITAYSPLG----------------TSRNPIW 230
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpGERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 231 VNVSSPPLLKDALLNSLGKRYNKTAAQIVLRF--NIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALN 303
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-300 |
3.62e-49 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 165.11 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 8 HRIPLSDGNSIPIIGLGTY--SEPKSTPKgACATSVKVAIDTGYRHIDGAYIYQN---EHEVGEAIREkiaegkvRREDI 82
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWymGEDPAKRA-QEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 83 FYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAfkpgdeiYPRDEngkwlyhksnlcaTWEAMEACKDAGL 162
Cdd:cd19138 73 FLVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-------VPLAE-------------TVAAMEELKKEGK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 163 VKSLGVSNFNRRQLELILNKPGlKHKPVSNQVECH-----PYFTqpkLLKFCQQHDIVITAYSPLGTSRNPiwvnvsSPP 237
Cdd:cd19138 133 IRAWGVSNFDTDDMEELWAVPG-GGNCAANQVLYNlgsrgIEYD---LLPWCREHGVPVMAYSPLAQGGLL------RRG 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174695 238 LLKDALLNSLGKRYNKTAAQIVLRFNI-QRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE 300
Cdd:cd19138 203 LLENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-297 |
4.23e-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: 164.67 E-value: 4.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGT-----YSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHE---VGEAIREkiaegkVRREDIFYCG 86
Cdd:cd19137 1 GEKIPALGLGTwgiggFLTPDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTeelVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 87 KLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEiyprdengkwlyhksnlcaTWEAMEACKDAGLVKSL 166
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 167 GVSNFNRRQLELILNKpgLKHKPVSNQVECHPYFTQPK---LLKFCQQHDIVITAYSPLGTSrnpiwvnvsspPLLKDAL 243
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEDRDPErdgLLEYCQKNGITVVAYSPLRRG-----------LEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 244 LNSLGKRYNKTAAQIVLRFNIQR-GVVVIPKSFNLERIKENFQIFDFSLTEEEMK 297
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMK 257
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
18-300 |
1.50e-37 |
|
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: 135.43 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYS-------EPKSTPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKIAegkvrREDIFYCGK 87
Cdd:cd19093 2 VSPLGLGTWQwgdrlwwGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 88 LWAT--NHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDeiyprdengkwlyhksnlCATWEAMEACKDAGLVKS 165
Cdd:cd19093 77 FAPLpwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQI------------------EALMDGLADAVEEGLVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 166 LGVSNFNRRQLELI---LNKPGlkHKPVSNQVE---CHPYFTQPKLLKFCQQHDIVITAYSPLG--------TSRNP--- 228
Cdd:cd19093 139 VGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPppg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 229 ---------IWVNVssPPLLkdALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDI 299
Cdd:cd19093 217 grrrlfgrkNLEKV--QPLL--DALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
.
gi 5174695 300 E 300
Cdd:cd19093 293 D 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
15-302 |
7.21e-35 |
|
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: 129.14 E-value: 7.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYS---EPKSTPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKiaegkvRREDIFYCGKL 88
Cdd:COG0667 10 GLKVSRLGLGTMTfggPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 --------WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDA 160
Cdd:COG0667 84 grrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------DPDTPIEE-------------TLGALDELVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 161 GLVKSLGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQP--KLLKFCQQHDIVITAYSPLG--------------- 223
Cdd:COG0667 145 GKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSLLDRSAeeELLPAARELGVGVLAYSPLAgglltgkyrrgatfp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 224 -TSR-NPIWVNVSSPPLLKDAL--LNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEMK 297
Cdd:COG0667 225 eGDRaATNFVQGYLTERNLALVdaLRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAEDLA 304
|
....*
gi 5174695 298 DIEAL 302
Cdd:COG0667 305 ALDAA 309
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-306 |
3.14e-33 |
|
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: 124.24 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGT------YSEPKSTPKGACATsVKVAIDTGYRHIDGAYIYQNEHE---VGEAIREkiaegkvRREDIFYCGKL 88
Cdd:cd19085 1 VSRLGLGCwqfgggYWWGDQDDEESIAT-IHAALDAGINFFDTAEAYGDGHSeevLGKALKG-------RRDDVVIATKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 WATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEiyprdengkwlyhksnlcaTWEAMEACKDAGLVKSLGV 168
Cdd:cd19085 73 SPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEE-------------------TMEALEKLKEEGKIRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 169 SNFNRRQLELILnKPGlkhKPVSNQVECHPYFTQPK--LLKFCQQHDIVITAYSPLGT-------------------SRN 227
Cdd:cd19085 134 SNFGPAQLEEAL-DAG---RIDSNQLPYNLLWRAIEyeILPFCREHGIGVLAYSPLAQglltgkfssaedfppgdarTRL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 228 ------PIWVNVSspPLLKdaLLNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEMKDI 299
Cdd:cd19085 210 frhfepGAEEETF--EALE--KLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
....*..
gi 5174695 300 EALNKNV 306
Cdd:cd19085 286 DEISDPL 292
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-300 |
5.25e-33 |
|
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: 123.40 E-value: 5.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYSEpKSTPKGACATS-----VKVAIDTGYRHIDGAYIYQN---EHEVGEAIrekiaegKVRREDIFY---CG 86
Cdd:cd19084 4 VSRIGLGTWAI-GGTWWGEVDDQesieaIKAAIDLGINFFDTAPVYGFghsEEILGKAL-------KGRRDDVVIatkCG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 87 KLWATNHV------PEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDA 160
Cdd:cd19084 76 LRWDGGKGvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWP------DPNTPIEE-------------TAEALEKLKKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 161 GLVKSLGVSNFNRRQLELILNkpglKHKPVSNQVECHPYFTQP--KLLKFCQQHDIVITAYSPLGT-------SRNPIWV 231
Cdd:cd19084 137 GKIRYIGVSNFSVEQLEEARK----YGPIVSLQPPYSMLEREIeeELLPYCRENGIGVLPYGPLAQglltgkyKKEPTFP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 232 -------NVS-SPPLLKDAL-----LNSLGKRYNKTAAQIVLRFNIQR-GV-VVIPKSFNLERIKENFQIFDFSLTEEEM 296
Cdd:cd19084 213 pddrrsrFPFfRGENFEKNLeivdkLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWELTEEEL 292
|
....
gi 5174695 297 KDIE 300
Cdd:cd19084 293 KEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-285 |
3.61e-26 |
|
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: 103.75 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKiaegkVRREDIFYCGKLWATNHV--- 94
Cdd:cd06660 3 LGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 -----PEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVS 169
Cdd:cd06660 78 rsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 NFNRRQLELILNKPGLKHK--PVSNQVE---CHPYFTQPKLLKFCQQHDIVITAYSPLGtsRNPiwvnvssppllkdall 244
Cdd:cd06660 139 NWSAERLAEALAYAKAHGLpgFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA--RGP---------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 5174695 245 nslgkrynktaAQIVLRF--NIQRGVVVIPKSFNLERIKENFQ 285
Cdd:cd06660 201 -----------AQLALAWllSQPFVTVPIVGARSPEQLEENLA 232
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
9-295 |
8.23e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 104.46 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 9 RIPLS-DGNSIPIIGLGTY--SEPKSTPKGAcATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKiaegKVRREDI 82
Cdd:COG4989 3 RIKLGaSGLSVSRIVLGCMrlGEWDLSPAEA-AALIEAALELGITTFDHADIYggyTCEALFGEALKLS----PSLREKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 83 FY---CGKLWATNHVPEMV----------RPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIyprdengkwlyhksnlcA 149
Cdd:COG4989 78 ELqtkCGIRLPSEARDNRVkhydtskehiIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEV-----------------A 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 150 twEAMEACKDAGLVKSLGVSNFNRRQLELiLNKpGLKHKPVSNQVECHPYFTQP---KLLKFCQQHDIVITAYSPLGTSR 226
Cdd:COG4989 141 --EAFDELKASGKVRHFGVSNFTPSQFEL-LQS-ALDQPLVTNQIELSLLHTDAfddGTLDYCQLNGITPMAWSPLAGGR 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5174695 227 npiWVNVSSPPLLK-DALLNSLGKRYNKTAAQIVLRFnIQR---GVVVIPKSFNLERIKENFQIFDFSLTEEE 295
Cdd:COG4989 217 ---LFGGFDEQFPRlRAALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
36-295 |
5.62e-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: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 36 ACATSVKVAIDTGYRHIDGAYIYQN---EHEVGEAIREKiaegKVRREDIFY---CG-KLWATNHV---------PEMVR 99
Cdd:cd19092 25 ELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIqtkCGiRLGDDPRPgrikhydtsKEHIL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 100 PTLERTLRVLQLDYVDLYIIEVPMAFKPGDEiyprdengkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLELi 179
Cdd:cd19092 101 ASVEGSLKRLGTDYLDLLLLHRPDPLMDPEE-------------------VAEAFDELVKSGKVRYFGVSNFTPSQIEL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 180 LNKpGLKHKPVSNQVECHPYFTQP---KLLKFCQQHDIVITAYSPLGTSRnpiwvnVSSPPLLKD----ALLNSLGKRYN 252
Cdd:cd19092 161 LQS-YLDQPLVTNQIELSLLHTEAiddGTLDYCQLLDITPMAWSPLGGGR------LFGGFDERFqrlrAALEELAEEYG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5174695 253 KTAAQIVLRFnIQR---GVVVIPKSFNLERIKENFQIFDFSLTEEE 295
Cdd:cd19092 234 VTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-302 |
1.73e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 98.13 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 44 AIDTGYRHIDGAYIY---QNEHEVGEAIREkiaegkvRREDIFY---CGKLW-----ATNHV-PEMVRPTLERTLRVLQL 111
Cdd:cd19102 35 ALDLGINWIDTAAVYglgHSEEVVGRALKG-------LRDRPIVatkCGLLWdeegrIRRSLkPASIRAECEASLRRLGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 112 DYVDLYIIEVPmafkpgdeiyPRDENgkwlyhksnLCATWEAMEACKDAGLVKSLGVSNFNRRQLELIL-------NKPG 184
Cdd:cd19102 108 DVIDLYQIHWP----------DPDEP---------IEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQaihpiasLQPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 185 --LKHKPVSNQVechpyftqpklLKFCQQHDIVITAYSPLGT----------SRNPIWVN-------VSSPPLLKDAL-- 243
Cdd:cd19102 169 ysLLRRGIEAEI-----------LPFCAEHGIGVIVYSPMQSglltgkmtpeRVASLPADdwrrrspFFQEPNLARNLal 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174695 244 ---LNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19102 238 vdaLRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
41-302 |
2.13e-22 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 95.18 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 41 VKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKiaegkvRREDIfycgkLWAT-------------NHVPEMVRPTLER 104
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEV-----VIATkgahkfggdgsvlNNSPEFLRSAVEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 105 TLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLELiLNKPG 184
Cdd:cd19083 108 SLKRLNTDYIDLYYIHFP------DGETPKAE-------------AVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 185 L------KHKPVSNQVECHpyftqpkLLKFCQQHDIVITAYSPLG-----------TSRNPIWVNVSSPPLLKDAL---- 243
Cdd:cd19083 168 YvdvlqgEYNLLQREAEED-------ILPYCVENNISFIPYFPLAsgllagkytkdTKFPDNDLRNDKPLFKGERFsenl 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5174695 244 -----LNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19083 241 dkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
14-305 |
7.05e-22 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 94.05 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 14 DGNSIPIIGLGT------YSEPKstPKGACATSVKVAIDTGYRHIDGAYIYQ-NEHEVGEAIreKIAEGKvrREDIFYCG 86
Cdd:cd19144 9 NGPSVPALGFGAmglsafYGPPK--PDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWF--KQNPGK--REKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 87 KL----------WATNHVPEMVRPTLERTLRVLQLDYVDLYiievpmafkpgdeiYPRDENGKWLYHKsnlcaTWEAMEA 156
Cdd:cd19144 83 KFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLY--------------YQHRVDGKTPIEK-----TVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 157 CKDAGLVKSLGVSNFNRRQLelilnKPGLKHKPVSN-QVECHPYFT-----QPKLLKFCQQHDIVITAYSPLG------- 223
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETL-----RRAHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGrgfltga 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 224 -TSRN---PIWVNVSSPPLLKDAL---------LNSLGKRYNKTAAQIVLRFNIQRG--VVVIPKSFNLERIKENFQIFD 288
Cdd:cd19144 219 iRSPDdfeEGDFRRMAPRFQAENFpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALK 298
|
330
....*....|....*..
gi 5174695 289 FSLTEEEMKDIEALNKN 305
Cdd:cd19144 299 VKLTEEEEKEIREIAEE 315
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
22-292 |
6.55e-21 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 89.97 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 22 GLGTYSEPKstPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIRE-----KIAE--GKVRREDifycgKLWAT 91
Cdd:cd19088 13 GPGIWGPPA--DREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPypddvVIATkgGLVRTGP-----GWWGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 92 NHVPEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNF 171
Cdd:cd19088 86 DGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------DPKVPFEE-------------QLGALAELQDEGLIRHIGLSNV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 172 NRRQLELILNKPGLkhkpVSNQVECHPYFTQP-KLLKFCQQHDIVITAYSPLGtsrnpiwvnvSSPPLLKDALLNSLGKR 250
Cdd:cd19088 147 TVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLG----------GGDLAQPGGLLAEVAAR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 5174695 251 YNKTAAQIVLRFNIQRG--VVVIPKSFNLERIKENFQIFDFSLT 292
Cdd:cd19088 213 LGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-301 |
2.52e-19 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 86.56 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNS---IPIIGLGTY-----SEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHE---VGEAIREkiaegkvRREDIF 83
Cdd:cd19149 5 GKSgieASVIGLGTWaigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSeeiVGKAIKG-------RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 84 Y---CGKLW---ATNHV-------------PEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEiyprdengkwlyhk 144
Cdd:cd19149 78 LatkCGLRWdreGGSFFfvrdgvtvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEE-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 145 snlcaTWEAMEACKDAGLVKSLGVSNFNRRQLelilnKPGLKHKPVS-NQVechPY-----FTQPKLLKFCQQHDIVITA 218
Cdd:cd19149 144 -----TMEALEELKRQGKIRAIGASNVSVEQI-----KEYVKAGQLDiIQE---KYsmldrGIEKELLPYCKKNNIAFQA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 219 YSPL-----------------GTSRNPI-WVNVSSPPLLKDAL--LNSLGKRYNKTAAQIVLRFNIQRG--VVVIPKSFN 276
Cdd:cd19149 211 YSPLeqglltgkitpdrefdaGDARSGIpWFSPENREKVLALLekWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARK 290
|
330 340
....*....|....*....|....*
gi 5174695 277 LERIKENFQIFDFSLTEEEMKDIEA 301
Cdd:cd19149 291 PEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-223 |
2.17e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 82.53 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYSEPKSTPKGACATsVKVAIDTGYRHIDGAYIYQNEHE-VGEAIREkiaegkvRREDIFYCGKLWATNhvPE 96
Cdd:cd19100 11 VSRLGFGGGPLGRLSQEEAAAI-IRRALDLGINYFDTAPSYGDSEEkIGKALKG-------RRDKVFLATKTGARD--YE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 97 MVRPTLERTLRVLQLDYVDLYII-EVPmafKPGDEIYPRDENGkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQ 175
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLhAVD---TEEDLDQVFGPGG-----------ALEALLEAKEEGKIRFIGISGHSPEV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5174695 176 LELILNKPGLK--HKPVsNQVECHPYFTQPKLLKFCQQHDIVITAYSPLG 223
Cdd:cd19100 147 LLRALETGEFDvvLFPI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLA 195
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-300 |
2.47e-16 |
|
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: 78.05 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLG----TYSEPKSTPKGACATsVKVAIDTGYRHIDGAYIY------QNEHEVGEAIReKIAEgkvRREDIFYCGK--- 87
Cdd:cd19077 8 IGLGlmglTWRPNPTPDEEAFET-MKAALDAGSNLWNGGEFYgppdphANLKLLARFFR-KYPE---YADKVVLSVKggl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 88 --LWATNHV-PEMVRPTLERTLRVL-QLDYVDLYiieVPMAFKPGDEIYprdengkwlyhksnlcATWEAMEACKDAGLV 163
Cdd:cd19077 83 dpDTLRPDGsPEAVRKSIENILRALgGTKKIDIF---EPARVDPNVPIE----------------ETIKALKELVKEGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 164 KSLGVSNFN----RRQLELilnkpglkHKPVSNQVECHPYFTQPK---LLKFCQQHDIVITAYSPLG--------TSRNP 228
Cdd:cd19077 144 RGIGLSEVSaetiRRAHAV--------HPIAAVEVEYSLFSREIEengVLETCAELGIPIIAYSPLGrglltgriKSLAD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 229 I---WVNVSSPPLLKDAL---------LNSLGKRYNKTAAQIVLRFNIQRG---VVVIPKSFNLERIKENFQIFDFSLTE 293
Cdd:cd19077 216 IpegDFRRHLDRFNGENFeknlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTD 295
|
....*..
gi 5174695 294 EEMKDIE 300
Cdd:cd19077 296 EELKEIN 302
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-301 |
3.65e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 77.63 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 45 IDTGYRHIDGAYIYQNEHE-VGEAIREKIAEGKVRREDIF---YC---GKLWATNHVpemVRPTLERTLRVLQLDYVDLy 117
Cdd:cd19101 33 VDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIhtkWVpdpGELTMTRAY---VEAAIDRSLKRLGVDRLDL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 118 iieVPMAFkpgdeiyprdengkWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELILNKPGlkhKPVSNQVECH 197
Cdd:cd19101 109 ---VQFHW--------------WDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGV---PIVSNQVQYS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 198 PYFTQP--KLLKFCQQHDIVITAYSPLG----TSRnpiWVNVSSPP-------------LLKDA------------LLNS 246
Cdd:cd19101 169 LLDRRPenGMAALCEDHGIKLLAYGTLAggllSEK---YLGVPEPTgpaletrslqkykLMIDEwggwdlfqellrTLKA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 5174695 247 LGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEMKDIEA 301
Cdd:cd19101 246 IADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
21-302 |
4.33e-16 |
|
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: 77.35 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLGTYSEP-----KSTPKGACATSVKvAIDTGYRHIDGAYIY---QNEHEVGEAIREKiaeGKvrREDIFY---CGKLW 89
Cdd:cd19148 7 IALGTWAIGgwmwgGTDEKEAIETIHK-ALDLGINLIDTAPVYgfgLSEEIVGKALKEY---GK--RDRVVIatkVGLEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 90 ATNHV------PEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLV 163
Cdd:cd19148 81 DEGGEvvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWP------DPLVPIEE-------------TAEALKELLDEGKI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 164 KSLGVSNFNRRQLELIlnkpgLKHKPVS-NQVechPY--FTQ---PKLLKFCQQHDIVITAYSPL--GTSRNPIWVNVSS 235
Cdd:cd19148 142 RAIGVSNFSPEQMETF-----RKVAPLHtVQP---PYnlFEReieKDVLPYARKHNIVTLAYGALcrGLLSGKMTKDTKF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 236 PPllkDAL---------------------LNSLGK-RYNKTAAQIVLRFNIQRGVVVIP-----KSFNLERIKEnfqIFD 288
Cdd:cd19148 214 EG---DDLrrtdpkfqeprfsqylaaveeLDKLAQeRYGKSVIHLAVRWLLDQPGVSIAlwgarKPEQLDAVDE---VFG 287
|
330
....*....|....
gi 5174695 289 FSLTEEEMKDIEAL 302
Cdd:cd19148 288 WSLNDEDMKEIDAI 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-302 |
1.04e-15 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 76.78 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 15 GNSIPIIGLGTYSEPKSTPKGACATsVKVAIDTGYRHIDGAYIY-QNEHEVGEAIREkiaegkvRREDIFYCGKLWATNH 93
Cdd:COG1453 10 GLEVSVLGFGGMRLPRKDEEEAEAL-IRRAIDNGINYIDTARGYgDSEEFLGKALKG-------PRDKVILATKLPPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 94 VPEMVRPTLERTLRVLQLDYVDLYIIEvpmafkpgdeiYPRDENG-KWLYHKSNLcatWEAMEACKDAGLVKSLGVSNFN 172
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIH-----------GLNTEEDlEKVLKPGGA---LEALEKAKAEGKIRHIGFSTHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 173 RRQ-LELILNkpglkhkpvSNQVEC-----HPYFTQP----KLLKFCQQHDIVITAYSPL--GTSRNPiwvnvssPPLLK 240
Cdd:COG1453 148 SLEvIKEAID---------TGDFDFvqlqyNYLDQDNqageEALEAAAEKGIGVIIMKPLkgGRLANP-------PEKLV 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5174695 241 DALlnslgkRYNKTAAQIVLRF--NIQRGVVVIPKSFNLERIKENFQIFD--FSLTEEEMKDIEAL 302
Cdd:COG1453 212 ELL------CPPLSPAEWALRFllSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
41-300 |
2.01e-15 |
|
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: 75.31 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 41 VKVAIDTGYRHIDGAYIYQN---EHEVGEAIREKIaegkvRREDIFYCGKLWA-TNHVPEM-------VRPTLERTLRVL 109
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFpMGDGPNGrglsrkhIMAEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 110 QLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLELILN---KPGLk 186
Cdd:cd19079 116 GTDYIDLYQIHRW------DYETPIEE-------------TLEALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKNGW- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 187 HKPVSNQvechPYFT------QPKLLKFCQQHDIVITAYSPL-----------------GTSRNPIWVNVSSPPLLKDAL 243
Cdd:cd19079 176 TKFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLargrlarpwgdtterrrSTTDTAKLKYDYFTEADKEIV 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174695 244 --LNSLGKRYNKTAAQIVLRFNIQRGVVVIP-----KsfnLERIKENFQIFDFSLTEEEMKDIE 300
Cdd:cd19079 252 drVEEVAKERGVSMAQVALAWLLSKPGVTAPivgatK---LEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-169 |
3.21e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 74.16 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 18 IPIIGLGTYSEPkstpkGACATSVKVAIDTGYRHIDGAYIYQN---EHEVGEAIRekiaegKVRREDIFYCGKLWAT--N 92
Cdd:cd19105 13 VSRLGFGGGGLP-----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPRldK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5174695 93 HVPEMVRPTLERTLRVLQLDYVDLYIIevpMAFKPGDEIYprdENGKWLyhksnlcatwEAMEACKDAGLVKSLGVS 169
Cdd:cd19105 82 KDKAELLKSVEESLKRLQTDYIDIYQL---HGVDTPEERL---LNEELL----------EALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
19-294 |
3.44e-15 |
|
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: 74.51 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 19 PIIGLGTY---SEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQN-EHEVGEAIREKIAEG-----KV--RREDIFYCGk 87
Cdd:cd19090 1 SALGLGTAglgGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAELPREPlvlstKVgrLPEDTADYS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 88 lwatnhvPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRdengkwlyhksnlcATWEAMEACKDAGLVKSLG 167
Cdd:cd19090 80 -------ADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPG--------------GALEALLELKEEGLIKHIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 168 VSNfnrRQLELilnkpglkHKPV--SNQVEC---HPYFT---QP---KLLKFCQQHDIVITAYSPLG----TSRNPIWVN 232
Cdd:cd19090 139 LGG---GPPDL--------LRRAieTGDFDVvltANRYTlldQSaadELLPAAARHGVGVINASPLGmgllAGRPPERVR 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174695 233 VSSPPLLKDAL-----LNSLGKRYNKTAAQIVLRFNIQ----RGVVVIPKsfNLERIKENFQIFDFSLTEE 294
Cdd:cd19090 208 YTYRWLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-283 |
5.85e-15 |
|
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: 72.90 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLGTYS-----EPKSTPKGACATsVKVAIDTGYRHIDGAYIYQN---EHEVGEAIREkiaegkvRREDI---------F 83
Cdd:cd19086 6 IGFGTWGlggdwWGDVDDAEAIRA-LRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVviatkfgnrF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 84 YCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLV 163
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPP-----DEVLDNDE-------------LFEALEKLKQEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 164 KSLGVSNFNRRQLELILNKPGLkhkpVSNQVECHPYFTQP--KLLKFCQQHDIVITAYSPL--Gtsrnpiwvnvssppll 239
Cdd:cd19086 140 RAYGVSVGDPEEALAALRRGGI----DVVQVIYNLLDQRPeeELFPLAEEHGVGVIARVPLasG---------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5174695 240 kdaLLNslGKrynktAAQIVLRFNIQRGVV--VIPKSFNLERIKEN 283
Cdd:cd19086 200 ---LLT--GK-----LAQAALRFILSHPAVstVIPGARSPEQVEEN 235
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-302 |
1.31e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 73.14 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 44 AIDTGYRHIDGAYIY---QNEHEVGEAIRekiaegKVRREDIFYCGKL------WATNHVPEMvrptLERTLRVLQLDYV 114
Cdd:cd19103 41 AMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYIISTKFtpqiagQSADPVADM----LEGSLARLGTDYI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 115 DLYIIEVPMAFKpgdeiyprdengKWLYHKSNLcatweameacKDAGLVKSLGVSNFNRRQLEL---ILNKPGLKHKPVS 191
Cdd:cd19103 111 DIYWIHNPADVE------------RWTPELIPL----------LKSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 192 NQVE-CHPYFTQPKLLKFCQQHDIVITAYS-----------------PLGTSR----NPIWvnvsspPLLKD--ALLNSL 247
Cdd:cd19103 169 NHYSlLYRSSEEAGILDYCKENGITFFAYMvleqgalsgkydtkhplPEGSGRaetyNPLL------PQLEEltAVMAEI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 248 GKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEAL 302
Cdd:cd19103 243 GAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
21-300 |
3.63e-14 |
|
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: 71.88 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLG------TYSEPKSTPKgacatSVKV---AIDTGYRHIDGAYIY---QNEHEVGEAIrekiaegKVRREDIFYCGKL 88
Cdd:cd19078 7 IGLGcmgmshGYGPPPDKEE-----MIELirkAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 89 W-----------ATNHVPEMVRPTLERTLRVLQLDYVDLYII-----EVPMAfkpgdeiyprdengkwlyhksnlcATWE 152
Cdd:cd19078 75 GfkidggkpgplGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQhrvdpNVPIE------------------------EVAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 153 AMEACKDAGLVKSLGVS----NFNRRqlelilnkpglKHK--PVSN-QVECHPYFTQP--KLLKFCQQHDIVITAYSPLG 223
Cdd:cd19078 131 TMKELIKEGKIRHWGLSeagvETIRR-----------AHAvcPVTAvQSEYSMMWREPekEVLPTLEELGIGFVPFSPLG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 224 -----------TSRNPIWVNVSSPPLLKDA---------LLNSLGKRYNKTAAQIVLRFNIQRG--VVVIPKSFNLERIK 281
Cdd:cd19078 200 kgfltgkidenTKFDEGDDRASLPRFTPEAleanqalvdLLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLE 279
|
330
....*....|....*....
gi 5174695 282 ENFQIFDFSLTEEEMKDIE 300
Cdd:cd19078 280 ENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-268 |
2.14e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 69.65 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 21 IGLGTYSEPKSTPKGACA-TSVKVAIDTGYRHIDGAYIYQN---EHEVGEAIREKIAEGKVRREDIFYC---GKLwaTNH 93
Cdd:cd19099 6 LGLGTYRGDSDDETDEEYrEALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVtkaGYI--PGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 94 VPEMVRPT--------------------------------LERTLRVLQLDYVDLYII---EVPMAFKPGDEIYPRDEng 138
Cdd:cd19099 84 GDEPLRPLkyleeklgrglidvadsaglrhcispayledqIERSLKRLGLDTIDLYLLhnpEEQLLELGEEEFYDRLE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 139 kwlyhksnlcATWEAMEACKDAGLVKSLGVSNFN------------------RRQLELILNKPGLKHkpVsnQVECHPYF 200
Cdd:cd19099 162 ----------EAFEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKV--I--QLPLNLLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 201 TQ------------PKLLKFCQQHDIVITAYSPLGtsrnpiwvnvsSPPLLKDALLNSLG-KRYNKTAAQIVLRFNI-QR 266
Cdd:cd19099 228 PEaltekntvkgeaLSLLEAAKELGLGVIASRPLN-----------QGQLLGELRLADLLaLPGGATLAQRALQFARsTP 296
|
..
gi 5174695 267 GV 268
Cdd:cd19099 297 GV 298
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
19-283 |
5.16e-13 |
|
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: 67.65 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 19 PIIGLGTySEPKSTP----KGACATSVKVAIDTGYRHIDGAYIYQN-EHEVGEAIREkiaegkVRREDIFYCGKLWATN- 92
Cdd:cd19095 1 SVLGLGT-SGIGRVWgvpsEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 93 -------HVPEMVRPTLERTLRVLQLDYVDLYIIEvpmafKPGDEiyprDENGKWLyhksnlcatwEAMEACKDAGLVKS 165
Cdd:cd19095 74 ggrdrkdFSPAAIRASIERSLRRLGTDYIDLLQLH-----GPSDD----ELTGEVL----------ETLEDLKAAGKVRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 166 LGVSNFNrrqlelilnkPGLKHKPVSNQVEC--HPY----FTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLL 239
Cdd:cd19095 135 IGVSGDG----------EELEAAIASGVFDVvqLPYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYAD 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5174695 240 KDALLNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKEN 283
Cdd:cd19095 205 YARRPEFAAEIGGATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
43-302 |
1.89e-12 |
|
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: 66.82 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 43 VAIDTGYRHIDGAYIY---QNEHEVGEAirEKIA----EGKVRREDIFYCGKL--------W----ATNHVPEMVRPTLE 103
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvpPSPETQGRT--EEIIgswlKKKGNRDKVVLATKVagpgegitWprggGTRLDRENIREAVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 104 RTLRVLQLDYVDLYIIE-----VPMAFKPGDEIYPRDENgkwlyhKSNLCATWEAMEACKDAGLVKSLGVSN-------- 170
Cdd:cd19094 104 GSLKRLGTDYIDLYQLHwpdryTPLFGGGYYTEPSEEED------SVSFEEQLEALGELVKAGKIRHIGLSNetpwgvmk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 171 FNR--RQLELilnkPglkhKPVSNQvecHPYftqpKLL--KF-------CQQHDIVITAYSPLG---------------- 223
Cdd:cd19094 178 FLElaEQLGL----P----RIVSIQ---NPY----SLLnrNFeeglaeaCHRENVGLLAYSPLAggvltgkyldgaarpe 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 224 TSR---NPIWVNVSSPPLLKDAL--LNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEM 296
Cdd:cd19094 243 GGRlnlFPGYMARYRSPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELL 322
|
....*.
gi 5174695 297 KDIEAL 302
Cdd:cd19094 323 AEIDAV 328
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
41-304 |
4.68e-12 |
|
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: 65.71 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 41 VKVAIDTGYRHIDGAYIY---QNEHEVGEAIREkiaegkvRREDIFYCGK--LWATN----------HVPEMVRPTLERt 105
Cdd:cd19091 45 VDIALDAGINFFDTADVYsegESEEILGKALKG-------RRDDVLIATKvrGRMGEgpndvglsrhHIIRAVEASLKR- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 106 lrvLQLDYVDLYIIEVPMAFKPGDEiyprdengkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLELIL---NK 182
Cdd:cd19091 117 ---LGTDYIDLYQLHGFDALTPLEE-------------------TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 183 PGLKhKPVSNQVechpYFT------QPKLLKFCQQHDIVITAYSPLGTSR--------NPI-------WVNVSSPPLLKD 241
Cdd:cd19091 175 RGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAGGLlsgkyrrgQPApegsrlrRTGFDFPPVDRE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174695 242 AL------LNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEmkdIEALNK 304
Cdd:cd19091 250 RGydvvdaLREIAKETGATPAQVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEE---IARLDK 317
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
19-288 |
1.66e-11 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 63.35 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 19 PIIGLGT----YSEPKSTPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREkiaegkVRREDIFYCGKL-WA 90
Cdd:cd19096 1 SVLGFGTmrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 91 TNHVPEMVRPTLERTLRVLQLDYVDLYII------EVPMAFKPGDeiyprdengkwlyhksnlcaTWEAMEACKDAGLVK 164
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLhglnspEWLEKARKGG--------------------LLEFLEKAKKEGLIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 165 SLGVS------NFNRrqlelILNkpglkhkpvSNQVEC----HPYFTQP-----KLLKFCQQHDIVITAYSPLGTSRNPi 229
Cdd:cd19096 135 HIGFSfhdspeLLKE-----ILD---------SYDFDFvqlqYNYLDQEnqagrPGIEYAAKKGMGVIIMEPLKGGGLA- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174695 230 wvnvSSPPLLKDALlnslgKRYNKTAAQIVLRFNI-QRGVVVIPKSF-NLERIKENFQIFD 288
Cdd:cd19096 200 ----NNPPEALAIL-----CGAPLSPAEWALRFLLsHPEVTTVLSGMsTPEQLDENIAAAD 251
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
41-222 |
2.64e-11 |
|
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: 63.38 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 41 VKVAIDTGYRHIDGAYIY---QNEHEVGEAIRekiaegKVRREDIFYCGKL-WAT-----------NHVPEMVRPTLERt 105
Cdd:cd19074 28 VRKAYDLGINFFDTADVYaagQAEEVLGKALK------GWPRESYVISTKVfWPTgpgpndrglsrKHIFESIHASLKR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 106 lrvLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLE--LILNKP 183
Cdd:cd19074 101 ---LQLDYVDIYYCHRY------DPETPLEE-------------TVRAMDDLIRQGKILYWGTSEWSAEQIAeaHDLARQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5174695 184 GLKHKPVSNQVECHPYFTQ--PKLLKFCQQHDIVITAYSPL 222
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREieEEVIPLCEKNGIGLVVWSPL 199
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
95-297 |
4.33e-10 |
|
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: 59.92 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYIIEVPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRR 174
Cdd:cd19081 97 RKHIRRAVEASLRRLQTDYIDLYQAHWD------DPATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAW 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 175 QLELILN---KPGLKhKPVSNQVEchpY------FTQPKLLKFCQQHDIVITAYSPLG--------TSRNPIWVNVSSPP 237
Cdd:cd19081 158 RLQEALElsrQHGLP-RYVSLQPE---YnlvdreSFEGELLPLCREEGIGVIPYSPLAggfltgkyRSEADLPGSTRRGE 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174695 238 LLKD----------ALLNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDFSLTEEEMK 297
Cdd:cd19081 234 AAKRylnerglrilDALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVA 305
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
52-300 |
4.69e-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: 56.46 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 52 IDGAYIYQNEHE---VGEAI---REKIA-----EGKVRREDIFYCGklwatNHVPEMVRpTLERTLRVLQLDYVDLYIIE 120
Cdd:cd19080 48 IDTANNYTNGTSerlLGEFIagnRDRIVlatkyTMNRRPGDPNAGG-----NHRKNLRR-SVEASLRRLQTDYIDLLYVH 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 121 VPmafkpgDEIYPRDE----------NGKWLYHK-SNLCAtWEAMEAckdAGLVKSLGVSNFNRRQLELILNKPGLKHKp 189
Cdd:cd19080 122 AW------DFTTPVEEvmralddlvrAGKVLYVGiSDTPA-WVVARA---NTLAELRGWSPFVALQIEYSLLERTPERE- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 190 vsnqvechpyftqpkLLKFCQQHDIVITAYSPLG--------------TSRNPIWVNVSSPPL------LKDALLnSLGK 249
Cdd:cd19080 191 ---------------LLPMARALGLGVTPWSPLGgglltgkyqrgeegRAGEAKGVTVGFGKLternwaIVDVVA-AVAE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5174695 250 RYNKTAAQIVLRFNIQRGVVVIP--KSFNLERIKENFQIFDFSLTEEEMKDIE 300
Cdd:cd19080 255 ELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
48-223 |
2.96e-08 |
|
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: 54.10 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 48 GYRHIDGAYIYQN-EHE--VGEAIRE----KIAEgKVRredifycgKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIE 120
Cdd:cd19075 33 GHTEIDTARVYPDgTSEelLGELGLGergfKIDT-KAN--------PGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 121 VPmafkpgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLELILN--------KP----GLkHK 188
Cdd:cd19075 104 AP------DRSTPLEE-------------TLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwvLPtvyqGM-YN 163
|
170 180 190
....*....|....*....|....*....|....*
gi 5174695 189 PVSNQVEchpyftqPKLLKFCQQHDIVITAYSPLG 223
Cdd:cd19075 164 AITRQVE-------TELFPCLRKLGIRFYAYSPLA 191
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
44-223 |
9.66e-08 |
|
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: 52.57 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 44 AIDTGYRHIDGAYIYQN---EHEVGEAIREkiaegkvRREDIFYCGKLWA-TNHVPEM-------VRPTLERTLRVLQLD 112
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVFGpMGDDPNDrglsrrhIRRAVEASLRRLQTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 113 YVDLYIIEVPMAFKPGDEiyprdengkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNF-------------NRRQLELI 179
Cdd:cd19087 112 YIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRGLLRFV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5174695 180 LnkpglkHKPVSNQVECHPyftQPKLLKFCQQHDIVITAYSPLG 223
Cdd:cd19087 173 S------EQPMYNLLKRQA---ELEILPAARAYGLGVIPYSPLA 207
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-302 |
1.15e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 52.65 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 30 KSTPKGACATsVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKIAE----GKVRREDIfycgklwATNHVPEMVRPTL 102
Cdd:cd19104 28 RTTREEQIAA-VRRALDLGINFFDTAPSYgdgKSEENLGRALKGLPAGpyitTKVRLDPD-------DLGDIGGQIERSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 103 ERTLRVLQLDYVDLYIIE---VPMAFKPGDEIYPRDEngkWLYhksnLCATWEAMEACKDAGLVKSLGVS---------- 169
Cdd:cd19104 100 EKSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSTTD---VLG----LGGVADAFERLRSEGKIRFIGITglgnppaire 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 170 -----NFNRRQLELILNKPGLKHKPVSNqvecHPYFTQPKLLKFCQQHDIVITAYSP-----LGTS--RNPIWVNVSSPP 237
Cdd:cd19104 173 lldsgKFDAVQVYYNLLNPSAAEARPRG----WSAQDYGGIIDAAAEHGVGVMGIRVlaagaLTTSldRGREAPPTSDSD 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174695 238 LLKD----ALLNSLGKRYNKTAAQIVLRFNI-QRGVV-VIPKSFNLERIKENFQIFDF-SLTEEEMKDIEAL 302
Cdd:cd19104 249 VAIDfrraAAFRALAREWGETLAQLAHRFALsNPGVStVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
9-299 |
1.66e-07 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 52.05 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 9 RIPL-SDGNSIPIIGLG------TYSEPKstPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKIAEgKVR 78
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGcmglsgDYGAPK--PEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPRE-KVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 79 REDIFYCGKLWATNHV----PEMVRPTLERTLRVLQLDYVDLYII-----EVPMafkpgdEIyprdengkwlyhksnlca 149
Cdd:cd19145 79 LATKFGIHEIGGSGVEvrgdPAYVRAACEASLKRLDVDYIDLYYQhridtTVPI------EI------------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 150 TWEAMEACKDAGLVKSLGVSNFN----RR----------QLELILnkpglkhkpVSNQVEchpyftqPKLLKFCQQHDIV 215
Cdd:cd19145 135 TMGELKKLVEEGKIKYIGLSEASadtiRRahavhpitavQLEWSL---------WTRDIE-------EEIIPTCRELGIG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 216 ITAYSPLGT---SRNPIWVNVSSPPLLKDAL-----------------LNSLGKRYNKTAAQIVLRFNIQRG--VVVIPK 273
Cdd:cd19145 199 IVPYSPLGRgffAGKAKLEELLENSDVRKSHprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPG 278
|
330 340
....*....|....*....|....*.
gi 5174695 274 SFNLERIKENFQIFDFSLTEEEMKDI 299
Cdd:cd19145 279 TTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
95-272 |
2.79e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 48.10 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 95 PEMVRPTLERTLRVLQLDYVDLYIIEVpmafkpGDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRR 174
Cdd:cd19752 94 AETIEQEIDKSLRRLGTDYIDLYYAHV------DDRDTPLEE-------------TLEAFNELVKAGKVRAIGASNFAAW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 175 QLEL---ILNKPGLkHKPVSNQVEcHPYFtQPK--------------LLKFCQQH-DIVITAYSPL--GTSRNPiWVNVS 234
Cdd:cd19752 155 RLERarqIARQQGW-AEFSAIQQR-HSYL-RPRpgadfgvqrivtdeLLDYASSRpDLTLLAYSPLlsGAYTRP-DRPLP 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5174695 235 SPPLLKD-----ALLNSLGKRYNKTAAQIVLRFNIQRGVVVIP 272
Cdd:cd19752 231 EQYDGPDsdarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
52-170 |
5.64e-06 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 47.16 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 52 IDGAYIYQNEHEVG---EAIREKIAEGKVRrEDIFYCGK-------LWATNHV-PEMVRPTLERTLRVLQLDYVDLYII- 119
Cdd:cd19082 34 IDTARVYGDWVERGaseRVIGEWLKSRGNR-DKVVIATKgghpdleDMSRSRLsPEDIRADLEESLERLGTDYIDLYFLh 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 5174695 120 ----EVPMafkpgDEIYprdengkwlyhksnlcatwEAMEACKDAGLVKSLGVSN 170
Cdd:cd19082 113 rddpSVPV-----GEIV-------------------DTLNELVRAGKIRAFGASN 143
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
41-301 |
5.84e-06 |
|
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: 47.21 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 41 VKVAIDTGYRHIDGAYIYQN---EHEVGEAIREkiaeGKVRRED------IFYCGKLWATN-------HVPEMVRPTLER 104
Cdd:cd19143 37 MKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDyvvstkIFWGGGGPPPNdrglsrkHIVEGTKASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 105 tlrvLQLDYVDLYiievpMAFKPgDEIYPRDEngkwlyhksnlcaTWEAMEACKDAGLVKSLGVSNFNRRQLE---LILN 181
Cdd:cd19143 113 ----LQLDYVDLV-----FCHRP-DPATPIEE-------------TVRAMNDLIDQGKAFYWGTSEWSAQQIEeahEIAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 182 KPGLkHKPVSNQVECHpYFTQPKL----LKFCQQHDIVITAYSPLGT--------------SR----NPIWVNVSSPPLL 239
Cdd:cd19143 170 RLGL-IPPVMEQPQYN-LFHRERVeveyAPLYEKYGLGTTTWSPLASglltgkynngipegSRlalpGYEWLKDRKEELG 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174695 240 KDAL-----LNSLGKRYNKTAAQIVLRFNIQRGVV--VIPKSFNLERIKENFQIFDF--SLTEEEMKDIEA 301
Cdd:cd19143 248 QEKIekvrkLKPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVlpKLTPEVMEKIEA 318
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
20-291 |
3.71e-05 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 44.58 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 20 IIGLGTYSEPKSTPKGACATS--VKVAIDTGYRHIDGAYIYQNEHEV-GEAIreKIAEGKVRREDIFYCGK-----LWAT 91
Cdd:cd19164 17 IFGAATFSYQYTTDPESIPPVdiVRRALELGIRAFDTSPYYGPSEIIlGRAL--KALRDEFPRDTYFIITKvgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 92 NHVPEMVRPTLERTLRVLQLDYVDL-YIIEVpmAFKPGDEIyprdengkwlyhksnlcatWEAMEAC---KDAGLVKSLG 167
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLvYLHDV--EFVADEEV-------------------LEALKELfklKDEGKIRNVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 168 VSNFnrrQLELILNKPGLKHKPVSNQVE-----CHPYFTQPKLLKF------CQQHDIVITAySPLG----TSRN-PIWv 231
Cdd:cd19164 154 ISGY---PLPVLLRLAELARTTAGRPLDavlsyCHYTLQNTTLLAYipkflaAAGVKVVLNA-SPLSmgllRSQGpPEW- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5174695 232 nVSSPPLLKDA------LLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSfNLERIKENFQIFDFSL 291
Cdd:cd19164 229 -HPASPELRAAaakaaeYCQAKGTDLADVALRYALREWGGEGPTVVGCS-NVDELEEAVEAYWSVL 292
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-262 |
4.16e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 44.44 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 44 AIDTGYRHIDGAYIYQNEHEV-GEAIrekiaegkVRREDIFYCGKLWATNHVPEMVRP----TLERTLRVLQLDYVDLYI 118
Cdd:cd19097 35 ALKAGINTLDTAPAYGDSEKVlGKFL--------KRLDKFKIITKLPPLKEDKKEDEAaieaSVEASLKRLKVDSLDGLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 119 IEvpmafkpgdeiyprdeNGKWLYHKSNlcATWEAMEACKDAGLVKSLGVSNFNRRQLELILNKPGLKHkpVsnQVECHP 198
Cdd:cd19097 107 LH----------------NPDDLLKHGG--KLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I--QLPFNI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174695 199 Y---FTQPKLLKFCQQHDIVITAYSPL--G-----TSRNPIWVNVSSPPLLKdalLNSLGKRYNKTAAQIVLRF 262
Cdd:cd19097 165 LdqrFLKSGLLAKLKKKGIEIHARSVFlqGlllmePDKLPAKFAPAKPLLKK---LHELAKKLGLSPLELALGF 235
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
19-169 |
2.20e-03 |
|
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: 39.26 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 19 PIIGLGTYS--EPKSTPKGACATSVKVAIDTGYRHIDGAYIY---QNEHEVGEAIREKIAEG-----KVRR-----EDIF 83
Cdd:cd19162 1 PRLGLGAASlgNLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARHPRAEyvvstKVGRllepgAAGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174695 84 YCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLyiievpmafkpgdeIYPRDENGKWLyhkSNLCATWEAMEACKDAGLV 163
Cdd:cd19162 81 PAGADRRFDFSADGIRRSIEASLERLGLDRLDL--------------VFLHDPDRHLL---QALTDAFPALEELRAEGVV 143
|
....*.
gi 5174695 164 KSLGVS 169
Cdd:cd19162 144 GAIGVG 149
|
|
| |
