|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-308 |
0e+00 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 678.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 6 HCVKLNDGHFIPALGFGTYKPKEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 166 SNFNHKQLERLLNKPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPVLLDDPILCDVA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230802 246 KKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLSA 308
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-319 |
4.15e-150 |
|
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: 423.83 E-value: 4.15e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTY-KPKEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCFR 91
Cdd:cd19109 1 GNSIPIIGLGTYsEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 92 TEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHK 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 172 QLERLLNKPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPVLLDDPILCDVAKKNKRS 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 252 PALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLSAEFLADHPEYPF 319
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-305 |
3.38e-127 |
|
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: 365.07 E-value: 3.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 7 CVKLNDGHFIPALGFGTYKPKevpKSKSLEAA-HLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKL 85
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLK---DDEGVRQAvKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDEsplDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGV 165
Cdd:cd19116 79 WNSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS---ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 166 SNFNHKQLERLLNkpGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtqRYKEWVDQNSPVLLDDPILCDVA 245
Cdd:cd19116 156 SNFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFG--RLVPRGQTNPPPRLDDPTLVAIA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 246 KKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19116 232 KKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-323 |
6.88e-127 |
|
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: 364.82 E-value: 6.88e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKPkevPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCFRTEMV 95
Cdd:cd19107 4 MPILGLGTWKS---PPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 96 RPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLER 175
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 176 LLNKPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRyKEWVDQNSPVLLDDPILCDVAKKNKRSPALI 255
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPD-RPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 256 ALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLSAEFLADHPEYPFSEEY 323
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-297 |
6.72e-116 |
|
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: 334.84 E-value: 6.72e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIkagvVKRKDMFITTKLWCSCFRTEMV 95
Cdd:cd19071 1 MPLIGLGTYK---LKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 96 RPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLER 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVP-------------GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 176 LLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKewvdqnspvLLDDPILCDVAKKNKRSPALI 255
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148230802 256 ALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19071 210 LLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-323 |
2.31e-114 |
|
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: 333.08 E-value: 2.31e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYK--PKEVPkskslEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCFRTE 93
Cdd:cd19110 4 IPAVGLGTWKasPGEVT-----EAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 94 MVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 174 ERLLNKPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQryKEWVDqnspvLLDDPILCDVAKKNKRSPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGS--CEGVD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 254 LIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLSAEFLADHPEYPFSEEY 323
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-305 |
2.67e-111 |
|
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: 325.11 E-value: 2.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 10 LNDGHFIPALGFGTYK--PKEVPkskslEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAG-VVKRKDMFITTKLW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWKskPGQVK-----AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRyKEWVDQNSPVLLDDPILCDVAK 246
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPD-RPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 247 KNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-305 |
2.12e-108 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 316.23 E-value: 2.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 12 DGHFIPALGFGTYK--PKEVpksksLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQskiKAGVvKRKDMFITTKLWCSC 89
Cdd:COG0656 1 NGVEIPALGLGTWQlpGEEA-----AAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASGV-PREELFVTTKVWNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 90 FRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldtVDFCDTWEMLEKCKDAGLVKSIGVSNFN 169
Cdd:COG0656 72 HGYDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 170 HKQLERLLNKPGlkYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKKNK 249
Cdd:COG0656 132 PEHLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHG 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 148230802 250 RSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:COG0656 199 KTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-306 |
1.10e-107 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 315.89 E-value: 1.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKPKevpKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWC 87
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVdesPLDEKGKFL--LDTVDFCDTWEMLEKCKDAGLVKSIGV 165
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV---GFPESGEDLlsLSPIPLEDTWRAMEELVDKGLCRHIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 166 SNFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGT-QRYKEWVDQNSPVLLDDPILCDV 244
Cdd:cd19123 158 SNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230802 245 AKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYL 306
Cdd:cd19123 236 AEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
7-304 |
1.16e-106 |
|
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: 313.58 E-value: 1.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 7 CVKLNDGHFIPALGFGTYKPKEVpksKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLW 86
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWQSKGA---EGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALG----TQRYKEWVDQNSPVLLDDPILC 242
Cdd:cd19154 160 NFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspgrANFTKSTGVSPAPNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230802 243 DVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFR 304
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
7-299 |
2.14e-101 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 299.26 E-value: 2.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 7 CVKLNDGHFIPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLW 86
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTWQ---ADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKssvDESPLDEKGKFLldTVDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19125 79 CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLK---KGAHMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRyKEWVDQNspvLLDDPILCDVAK 246
Cdd:cd19125 154 NFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPG-TTWVKKN---VLKDPIVTKVAE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148230802 247 KNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19125 228 KLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-299 |
2.14e-96 |
|
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: 286.47 E-value: 2.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 12 DGHFIPALGFGTYKPKEVPKsKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVK-RKDMFITTKLWCSCF 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 91 RTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLdEKGKFLldTVDFCDTWEMLEKCKDAGLVKSIGVSNFNH 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPI-EEEDFL--PFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 171 KQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKeWvdqNSPVLLDDPILCDVAKKNKR 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-W---GSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 148230802 251 SPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-304 |
2.71e-92 |
|
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: 277.10 E-value: 2.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 5 LHCVKLNDGHFIPALGFGTYK--PKEVPKsksleAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFIT 82
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQssPEEIET-----AVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 83 TKLWCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDES-PLDEKGKFLLD-TVDFCDTWEMLEKCKDAGLV 160
Cdd:cd19155 76 TKLPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSgKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 161 KSIGVSNFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQ-RYKEWVDQNSPV----- 234
Cdd:cd19155 156 RSIGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPgAAHFSPGTGSPSgsspd 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 235 LLDDPILCDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFR 304
Cdd:cd19155 234 LLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-305 |
1.29e-86 |
|
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: 261.66 E-value: 1.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTY--KPKEVpksksLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCF 90
Cdd:cd19111 1 GFPMPVIGLGTYqsPPEEV-----RAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 91 RTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDespldekGKFLLDT-VDFCDTWEMLEKCKDAGLVKSIGVSNFN 169
Cdd:cd19111 76 EFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKD-------KGERELAsSDVTSVWRAMEALVSEGKVKSIGLSNFN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 170 HKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAY---GALGTQRYKEWVDQnsPVLLDDPILCDVAK 246
Cdd:cd19111 149 PRQINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYaplGSPGRANQSLWPDQ--PDLLEDPTVLAIAK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 247 KNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19111 225 ELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-303 |
4.66e-86 |
|
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: 260.12 E-value: 4.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 2 SSKLHcvKLNDGHFIPALGFGTYKPKEVPKSKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFI 81
Cdd:cd19117 2 SSKTF--KLNTGAEIPAVGLGTWQSKPNEVAKAVEAA---LKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 82 TTKLWCSCFRTemVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTV--DFCDTWEMLEKCKDAGL 159
Cdd:cd19117 73 TTKLWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPdwDFIKTWELMQKLPATGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 160 VKSIGVSNFNHKQLERLLNKPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTqrykewvdQNSPvLLDDP 239
Cdd:cd19117 151 VKAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS--------TNAP-LLKEP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148230802 240 ILCDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEfqLSPEDMKTLDGLNKNF 303
Cdd:cd19117 222 VIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHKEY 283
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-299 |
1.83e-84 |
|
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: 256.18 E-value: 1.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 10 LNDGHFIPALGFGTY--KPKEVPKsksleAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIK-AGVVKRKDMFITTKLW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEVGA-----AVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKeEPGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPL----DEKGKFLLDT-VDFCDTWEMLEKCKDAGLVK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEVDLDLsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 162 SIGVSNFNHKQLERLLNKPGLkyKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdQNSPVLLDDPIL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 242 CDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEfqLSPEDMKTLDGL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-305 |
7.77e-83 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 252.79 E-value: 7.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYK-PKEVPKSKSLEAahlaIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLW 86
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRmEPGEIKELILNA----IKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CScfRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIK-SSVD--ESPLDEKGKFLLD-TVDFCDTWEMLEKCKDAGLVKS 162
Cdd:cd19112 79 NS--DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKhTGVGttGSALGEDGVLDIDvTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 163 IGVSNFnhkqlERLLNKPGLKY---KPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALG-TQRYKEWVDQNSPvlLDD 238
Cdd:cd19112 157 IGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148230802 239 PILCDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-297 |
3.15e-82 |
|
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: 249.84 E-value: 3.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGT----YKPKEVPKSKSL-EAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWC 87
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLvDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 scfRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSvdespldekgkflldTVDFCDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQLERLLNKPglKYKPVCNQVECHLYLN--QSKLLDYCKSKDIVLVAYGALGTQrykeWVDQNSPVlldDPILCDVA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPL----TRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 148230802 246 KKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
3.21e-82 |
|
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: 249.11 E-value: 3.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKPKEvpkSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQskiKAGVvKRKDMFITTKLWCSCFRTEMV 95
Cdd:cd19073 1 IPALGLGTWQLRG---DDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA---ESGV-PREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 96 RPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLER 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 176 LLNKPGLkyKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKKNKRSPALI 255
Cdd:cd19073 135 ALDISPL--PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE-----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148230802 256 ALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-300 |
1.70e-81 |
|
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: 247.67 E-value: 1.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYkpkEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWC 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldEKGKFLldtvdfcDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVP-----------AQDKYV-------ETWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQLERLLNKPGLkyKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKK 247
Cdd:cd19131 137 FTIEHLQRLIDETGV--VPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEK 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148230802 248 NKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:cd19131 204 HGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-300 |
2.11e-81 |
|
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: 247.10 E-value: 2.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYkpkEVPKSKSLEAAHL-AIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECERAVLeAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldtvDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLnkPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKewvdqnspvLLDDPILCDVAK 246
Cdd:cd19133 133 NFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148230802 247 KNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-305 |
5.26e-80 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 244.22 E-value: 5.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 7 CVKLNDGHFIPALGFGTYKPKEvpKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLW 86
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSvdespldekgkflldtvdfcDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYK--------------------ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAK 246
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 247 KNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-305 |
4.14e-79 |
|
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: 243.51 E-value: 4.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWC 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWK---LDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSsvdeSPLDEK----------GKFLLDTVDFCDTWEMLEKCKDA 157
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKF----VPIEEKyppgfycgdgDNFVYEDVPILDTWKALEKLVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 158 GLVKSIGVSNFNHKQLERLLNkpGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEwVDQ----NSP 233
Cdd:cd19113 156 GKIKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVE-LNQgralNTP 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230802 234 VLLDDPILCDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19113 233 TLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
1.84e-78 |
|
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: 240.23 E-value: 1.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKPKEVPK-SKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCFRTEM 94
Cdd:cd19136 1 MPILGLGTFRLRGEEEvRQAVDAA---LKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 95 VRPALEKSLKNLQLDYVDLFLIHYPVPIKssvdESPLDEKGKFLLDtvdfcDTWEMLEKCKDAGLVKSIGVSNFNHKQLE 174
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGVQG----LKPSDPRNAELRR-----ESWRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 175 RLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYkewvdqnspVLLDDPILCDVAKKNKRSPAL 254
Cdd:cd19136 149 ELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDL---------RLLEDPTVLAIAKKYGRTPAQ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 148230802 255 IALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19136 218 VLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-300 |
3.92e-78 |
|
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: 240.29 E-value: 3.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 19 LGFGTY----KPKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagVVKRKDMFITTKL------ 85
Cdd:pfam00248 1 IGLGTWqlggGWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldTVDFCDTWEMLEKCKDAGLVKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 166 SNFNHKQLERLLNKPglKYKPVCNQVECHLY--LNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPV--------- 234
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKgpgerrrll 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148230802 235 -------LLDDPILCDVAKKNKRSPALIALRYLFQ--RGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:pfam00248 216 kkgtplnLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-300 |
4.42e-77 |
|
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: 236.40 E-value: 4.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 10 LNDGHFIPALGFGTYKPKEVPKSKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIQSkikAGVvKRKDMFITTKLWCSC 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAA---LQAGYRLLDTAFNYENEGAVGEAVRR---SGV-PREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 90 FRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldEKGKFLldtvdfcDTWEMLEKCKDAGLVKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPNP-----------SRDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 170 HKQLERLLNKPGLKykPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtqRYKEwvdqnspvLLDDPILCDVAKKNK 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG--RGSG--------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148230802 250 RSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-299 |
1.46e-76 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 235.30 E-value: 1.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 7 CVKLNDGHFIPALGFGT-----YkpkevpkskSLEAAHLAI-DVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMF 80
Cdd:cd19135 4 TVRLSNGVEMPILGLGTshsggY---------SHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 81 ITTKLWCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEkgkflldtvdfcDTWEMLEKCKDAGLV 160
Cdd:cd19135 71 LTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRA------------ETWRALEELYDEGLC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 161 KSIGVSNFNHKQLERLLNKPGLKykPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYkewvdqnspvlLDDPI 240
Cdd:cd19135 139 RAIGVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKA-----------LEEPT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 241 LCDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19135 206 VTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-305 |
2.78e-76 |
|
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: 235.81 E-value: 2.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 11 NDGHFIPALGFGTYKPKevpKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCF 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPD---PSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 91 RTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDT-VDFCDTWEMLEKCKDAGLVKSIGVSNFN 169
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 170 HKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtqrykewvDQNSPVLLDDPILCDVAKKNK 249
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG--------HGMEPKLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 250 RSPALIALRYLFQRGVVPLAQSFKENEMRENlqvFEFQLSPED-MKTL-DGLNKNFRY 305
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPEDaMREInEGIKTRYRF 282
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
5.57e-76 |
|
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: 233.48 E-value: 5.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKPKEvpKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWC 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPD--GDETERAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKssvdespldekgkflldtvdFCDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK--------------------FIDTWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKK 247
Cdd:cd19126 135 FQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148230802 248 NKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
6.18e-76 |
|
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: 233.30 E-value: 6.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTYKPKEVPKSKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIQskiKAGVvKRKDMFITTKLWCSCFRT 92
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHA---LELGYRHIDTAQMYGNEAQVGEAIA---ASGV-PRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 93 EMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQ 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWPNK-------------------DVPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 173 LERLLNKPGLKYkpVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKKNKRSP 252
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 148230802 253 ALIALRYLFQR-GVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-299 |
1.43e-74 |
|
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: 230.88 E-value: 1.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 9 KLNDGHFIPALGFGTY--KPKEVPKsksleAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIkAGVVKRKDMFITTKLW 86
Cdd:cd19121 5 KLNTGASIPAVGLGTWqaKAGEVKA-----AVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTemVRPALEKSLKNLQLDYVDLFLIHYPVPI--KSSVDESPLDEKGKFLLD-TVDFCDTWEMLEKCKDAGLVKSI 163
Cdd:cd19121 79 STYHRR--VELCLDRSLKSLGLDYVDLYLVHWPVLLnpNGNHDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 164 GVSNFNHKQLERLLnkPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTqrykewvdQNSPVLLDDPILcD 243
Cdd:cd19121 157 GVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDEPVV-E 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 148230802 244 VAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFqlSPEDMKTLDGL 299
Cdd:cd19121 226 IAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-305 |
4.80e-73 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 228.07 E-value: 4.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWC 87
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWK---VNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKsSVDES---P---LDEKGKFLLDTVDFCDTWEMLEKCKDAGLVK 161
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALK-YVDPAvryPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 162 SIGVSNFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQN---SPVLLDD 238
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPGakdTPPLFEH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148230802 239 PILCDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19115 239 DVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-297 |
1.10e-71 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 223.91 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKPKEvPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWc 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRpALEKSLKNLQLDYVDLFLIHYPVPIKSSVDES-----PLDEKGKFLL-DTVDFCDTWEMLEKCKDAGLVK 161
Cdd:cd19119 82 PTFYDEVER-SLDESLKALGLDYVDLLLVHWPVCFEKDSDDSgkpftPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 162 SIGVSNFNHKQLERLLNKpgLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKewvdqnspvLLDDPIL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 148230802 242 CDVAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVfeFQLSPEDMKTLD 297
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLD 283
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-300 |
2.34e-71 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 222.28 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYkpkEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWC 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVF---QTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGI----RRSGVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldtVDFCDT---WEMLEKCKDAGLVKSIG 164
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVP--------------------NDFDRTiqaYKALEKLLAEGRVRAIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 165 VSNFNHKQLERLLNKPGLKykPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALG-TQRYKEWVDQNSPVLLDDPILCD 243
Cdd:cd19127 134 VSNFTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgVMRYGASGPTGPGDVLQDPTITG 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 148230802 244 VAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:cd19127 212 LAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-299 |
3.79e-71 |
|
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: 222.01 E-value: 3.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCFRTEMVR 96
Cdd:cd19128 2 PRLGFGTYK---ITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 97 PALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESPLDEKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLERL 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 177 LNKpgLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtQRYkewvDQNSPVLLDDPILCDVAKKNKRSPALIA 256
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG-GSY----GDGNLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 148230802 257 LRYLFQR-----GVVPLAQSFKenEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19128 232 IAWHLQKwpknySVIPKSANKS--RCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-305 |
1.43e-70 |
|
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: 220.08 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKPKEvpKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWC 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVpikssvdespldeKGKFLldtvdfcDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPV-------------KGKFK-------DTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQLERLLNKpgLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKK 247
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 248 NKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-305 |
7.51e-70 |
|
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: 219.35 E-value: 7.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAGVVKRKDMFITTKLWCSCFRT 92
Cdd:cd19114 1 GDKMPLVGFGTAK---IKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 93 EMVRPALEKSLKNLQLDYVDLFLIHYPVPIK---SSVDESPLD---EKGKFLLDTVDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWkdkELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPV--LLDDPILCDV 244
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148230802 245 AKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-300 |
1.17e-66 |
|
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: 209.77 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 10 LNDGHFIPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWCSC 89
Cdd:cd19130 4 LNDGNSIPQLGYGVFK---VPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 90 FRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSsvdespldekgkflldtvDFCDTWEMLEKCKDAGLVKSIGVSNFN 169
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG------------------NYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 170 HKQLERLLNKPGLkyKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtqrykewvdQNSpvLLDDPILCDVAKKNK 249
Cdd:cd19130 139 PPHLERIVAATGV--VPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLG---------QGK--LLGDPPVGAIAAAHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148230802 250 RSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-299 |
2.24e-64 |
|
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: 203.74 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKPKEVPKSKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIQskikAGVVKRKDMFITTKLWCSCFRTEMV 95
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTA---LELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 96 RPALEKSLKNLQLDYVDLFLIHYPVPikssVDESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLER 175
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIHWPSP----NDEVPVEE-------------YIGALAEAKEQGLTRHIGVSNFTIALLDE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 176 LLNKPGlKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKKNKRSPALI 255
Cdd:cd19139 137 AIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQI 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 148230802 256 ALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19139 205 ALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-297 |
9.00e-62 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 197.99 E-value: 9.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSkikAGVvKRKDMFITTKLWC 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQ---ASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE---ASV-AREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 ScfRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKssvdespldekgkfllDTvdFCDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:PRK11565 80 D--DHKRPREALEESLKKLQLDYVDLYLMHWPVPAI----------------DH--YVEAWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQLERLLNKPGLkyKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtqrykewvdQNSPVLLDDPILCDVAKK 247
Cdd:PRK11565 140 FQIHHLQRLIDETGV--TPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLA---------QGGKGVFDQKVIRDLADK 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148230802 248 NKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPED---MKTLD 297
Cdd:PRK11565 209 YGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDElgeIAKLD 261
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-297 |
6.18e-61 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 195.14 E-value: 6.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYK---PKEVPKS---KSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSkikagvVKRKDMFITTKLW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDYSddkKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIkssvdespldekgkflldtVDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPS-------------------IPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLNKPGlKYKPVCNQVECHLYLN--QSKLLDYCKSKDIVLVAYGALGTQRYKewvdqnspVLLDDPILCDV 244
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKLS--------NAKGSPLLDEI 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148230802 245 AKKNKRSPALIALRYLFQR-GVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19072 210 AKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-301 |
1.04e-60 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 195.53 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 9 KLNDGHFIPALGFGTYKpKEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIGQAIQSKIKAG-VVKRKDMFITTKLWC 87
Cdd:cd19122 2 TLNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSVDESP-LDEKGKFLLD---TVDFCDTWEMLEKCKDAGLVKSI 163
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPkLGPDGKYVILkdlTENPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 164 GVSNFNHKQLERLLNKPglKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYkewVDQNSPVLLDDPILCD 243
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 244 VAKKNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEfqLSPEDMKTLDGLNK 301
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-305 |
2.47e-60 |
|
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: 193.92 E-value: 2.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKLNDGHFIPALGFGTYKPKEVPKSKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIqskiKAGVVKRKDMFITTKLWC 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAA---LEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 88 SCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldEKGKFLldtvdfcDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVSN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQLERLLNKPGlkYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCDVAKK 247
Cdd:cd19134 138 FTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 248 NKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRY 305
Cdd:cd19134 205 HGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-312 |
1.58e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 179.06 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKPKEVPKSKSLEAAhlaIDVGYRHIDTASAYQVEEEIGQAIQskiKAGVvKRKDMFITTKLWCSCFRTEMV 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTA---LELGYRAIDTAQIYDNEAAVGQAIA---ESGV-PRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 96 RPALEKSLKNLQLDYVDLFLIHYPVPikssVDESPLDEkgkFLldtvdfcdtwEMLEKCKDAGLVKSIGVSNFNHKQLER 175
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWPSP----NDEVSVEE---FM----------QALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 176 LLNKPGlKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGtqrYKEwvdqnspvLLDDPILCDVAKKNKRSPALI 255
Cdd:PRK11172 139 AIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA---YGK--------VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 256 ALRYLFQRG--VVPlaQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLSAEFLA 312
Cdd:PRK11172 207 ILAWAMQLGysVIP--SSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSPEGLA 263
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-297 |
8.96e-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: 163.90 E-value: 8.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTYK------PKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSkikagvVKRKDMFITT 83
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 84 KLWCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP------NIPLEE-------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 164 GVSNFNHKQLERLLNKpgLKYKPVCNQVECHLY---LNQSKLLDYCKSKDIVLVAYGAL--GTQRYKEWVDQnspvlldd 238
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLrrGLEKTNRTLEE-------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 239 pilcdVAKKNKRSPALIALRYLFQR-GVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19137 206 -----IAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-297 |
2.86e-48 |
|
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: 162.80 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 6 HCVKLNDGHFIPALGFGTYKPKEVPKS--KSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKraQEIEALRAGIDLGMTLIDTAEMYgdgGSEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 81 ITTKLWCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpikSSVdesPLDEkgkflldtvdfcdTWEMLEKCKDAGLV 160
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR----GGV---PLAE-------------TVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 161 KSIGVSNFNHKQLERLLNKPGLKyKPVCNQVECHLylnQSK-----LLDYCKSKDIVLVAYGALGTQRykewvdQNSPVL 235
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYNL---GSRgieydLLPWCREHGVPVMAYSPLAQGG------LLRRGL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230802 236 LDDPILCDVAKKNKRSPALIALRYLF-QRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19138 204 LENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-297 |
1.28e-41 |
|
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: 146.86 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT----YKPKEVPKSKSLEAAHLAIDVGYRHIDTASAYQV---EEEIGQAIQSKikagvvKRKDMFITTKL--- 85
Cdd:COG0667 13 VSRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPgrsEELLGEALKGR------PRDDVVIATKVgrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 -----WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLV 160
Cdd:COG0667 87 mgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDP------DTPIEE-------------TLGALDELVREGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 161 KSIGVSNFNHKQLERLLNKPGLKYKPVCNQVECHLyLNQS---KLLDYCKSKDIVLVAYGALG----TQRYKE------- 226
Cdd:COG0667 148 RYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSL-LDRSaeeELLPAARELGVGVLAYSPLAggllTGKYRRgatfpeg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 227 ---WVDQNSPVLLDDPI-----LCDVAKKNKRSPALIALRYLFQRGVV--PLAQSFKENEMRENLQVFEFQLSPEDMKTL 296
Cdd:COG0667 227 draATNFVQGYLTERNLalvdaLRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAEDLAAL 306
|
.
gi 148230802 297 D 297
Cdd:COG0667 307 D 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
1.84e-41 |
|
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: 145.75 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGT-----YKPKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTK 84
Cdd:cd19084 1 DLKVSRIGLGTwaiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYgfgHSEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 85 ---LW------CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldTVDFCDTWEMLEKCK 155
Cdd:cd19084 74 cglRWdggkgvTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDP-------------------NTPIEETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 156 DAGLVKSIGVSNFNHKQLERLlnkpgLKY-KPVCNQVECHLyLNQ---SKLLDYCKSKDIVLVAYGALG----TQRYKEw 227
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQPPYSM-LEReieEELLPYCRENGIGVLPYGPLAqgllTGKYKK- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 228 vdqnSPVLLDDPI---------------------LCDVAKKNKRSPALIALRYLFQR-GV-VPLAQSFKENEMRENLQVF 284
Cdd:cd19084 208 ----EPTFPPDDRrsrfpffrgenfeknleivdkLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGAL 283
|
330
....*....|...
gi 148230802 285 EFQLSPEDMKTLD 297
Cdd:cd19084 284 DWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-303 |
1.74e-40 |
|
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: 143.11 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT------YKPKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTKLW 86
Cdd:cd19085 1 VSRLGLGCwqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALKGR-------RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldTVDFCDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS-------------------DVPLEETMEALEKLKEEGKIRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 NFNHKQLERLLnKPGlkyKPVCNQVECHLyLNQSK---LLDYCKSKDIVLVAYGALG----TQRYKEwVDQNSP------ 233
Cdd:cd19085 135 NFGPAQLEEAL-DAG---RIDSNQLPYNL-LWRAIeyeILPFCREHGIGVLAYSPLAqgllTGKFSS-AEDFPPgdartr 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 234 -VLLDDPI-----------LCDVAKKNKRSPALIALRYLFQRGVV--PLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19085 209 lFRHFEPGaeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
....
gi 148230802 300 NKNF 303
Cdd:cd19085 289 SDPL 292
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-297 |
2.08e-40 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 143.14 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT-------------YKPKEVpksksLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQskikaGVVKRKDM 79
Cdd:cd19093 2 VSPLGLGTwqwgdrlwwgygeYGDEDL-----QAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 80 FITTK---LWCSCFRTEMVRpALEKSLKNLQLDYVDLFLIHYPVPIKSSVDEspldekgkflldtvdfcdTWEMLEKCKD 156
Cdd:cd19093 72 VIATKfapLPWRLTRRSVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQIEA------------------LMDGLADAVE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 157 AGLVKSIGVSNFNHKQLER---LLNKPGlkYKPVCNQVECHL---YLNQSKLLDYCKSKDIVLVAY-----GAL------ 219
Cdd:cd19093 133 EGLVRAVGVSNYSADQLRRahkALKERG--VPLASNQVEYSLlyrDPEQNGLLPACDELGITLIAYsplaqGLLtgkysp 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 220 --------GTQRYKEWVDQNSPVLLddpILCDVAKKNKRSPALIALRYLFQRGVVPL--AQSFKenEMRENLQVFEFQLS 289
Cdd:cd19093 211 enpppggrRRLFGRKNLEKVQPLLD---ALEEIAEKYGKTPAQVALNWLIAKGVVPIpgAKNAE--QAEENAGALGWRLS 285
|
....*...
gi 148230802 290 PEDMKTLD 297
Cdd:cd19093 286 EEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-282 |
6.73e-34 |
|
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: 124.17 E-value: 6.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTYK-PKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIqskikAGVVKRKDMFITTKL------- 85
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWL-----KGRGNRDDVVIATKGghppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 -WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpikssvDES-PLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSI 163
Cdd:cd06660 76 pSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD-------DPStPVEE-------------TLEALNELVREGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 164 GVSNFNHKQLERLLN--KPGLKYKPVCNQVECHLYLNQ---SKLLDYCKSKDIVLVAYGALGtqrykewvdqnspvlldd 238
Cdd:cd06660 136 GVSNWSAERLAEALAyaKAHGLPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLA------------------ 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148230802 239 pilcdvakknkRSPALIALRYLFQR--GVVPLAQSFKENEMRENLQ 282
Cdd:cd06660 198 -----------RGPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-310 |
3.89e-28 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 111.83 E-value: 3.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKPKEVPKSKSLEAAHLAIDVGYRHIDTASAY-QVEEEIGQAIQSKikagvvkRKDMFITTKL--WCSCFRT 92
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLppWVRDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 93 emVRPALEKSLKNLQLDYVDLFLIHYpvpIKSSVD-ESPLDEKGkflldtvdfcdTWEMLEKCKDAGLVKSIGVSnfNHK 171
Cdd:COG1453 86 --MRKDLEESLKRLQTDYIDLYLIHG---LNTEEDlEKVLKPGG-----------ALEALEKAKAEGKIRHIGFS--THG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 172 QLERLlnKPGLKYKP--VCNqveCHL-YLNQS-----KLLDYCKSKDIVLVAYGALGTQRykewvdqnspvLLDDPILCD 243
Cdd:COG1453 148 SLEVI--KEAIDTGDfdFVQ---LQYnYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LANPPEKLV 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148230802 244 VAKKNKRSPALIALRYLFQR-GV-VPLAQSFKENEMRENLQVFE--FQLSPEDMKTLDGLNKNFRYLSAEF 310
Cdd:COG1453 212 ELLCPPLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERLAEELGELLKDF 282
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-180 |
2.60e-27 |
|
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: 106.80 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTYKPKEVPKSKSLEAAHLAIDVGYRHIDTASAY-QVEEEIGQAIQSKikagvvkRKDMFITTKlwcSCFR 91
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYgDSEEKIGKALKGR-------RDKVFLATK---TGAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 92 T-EMVRPALEKSLKNLQLDYVDLFLIHYpvpIKSSVD-ESPLDEKGkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFN 169
Cdd:cd19100 78 DyEGAKRDLERSLKRLGTDYIDLYQLHA---VDTEEDlDQVFGPGG-----------ALEALLEAKEEGKIRFIGISGHS 143
|
170
....*....|.
gi 148230802 170 HKQLERLLNKP 180
Cdd:cd19100 144 PEVLLRALETG 154
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-289 |
1.16e-26 |
|
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: 105.38 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT---------YKPKevPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKiKAGVVkrkdmfITT 83
Cdd:cd19088 1 VSRLGYGAmrltgpgiwGPPA--DREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPY-PDDVV------IAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 84 KL---------WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldTVDFCDTWEMLEKC 154
Cdd:cd19088 72 KGglvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDP-------------------KVPFEEQLGALAEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 155 KDAGLVKSIGVSNFNHKQLERLLNKPGLkykpVCNQVECHLYLNQS-KLLDYCKSKDIVLVAYGALGTqrykewvdqnSP 233
Cdd:cd19088 133 QDEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGG----------GD 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 234 VLLDDPILCDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEMRENLQVFEFQLS 289
Cdd:cd19088 199 LAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-291 |
4.21e-26 |
|
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: 104.56 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTY----KPKEVPKSKSLEAAHLAIDVGYRHIDTASAY-QVEEEIGQAIQSkikagvVKRKDMFITTKlwCSCFR 91
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYgDSEERLGLALAE------LPREPLVLSTK--VGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 92 T-------EMVRPALEKSLKNLQLDYVDLFLIHYP--VPIKSSVDESPldekgkflldtvdfcdTWEMLEKCKDAGLVKS 162
Cdd:cd19090 73 EdtadysaDRVRRSVEESLERLGRDRIDLLMIHDPerVPWVDILAPGG----------------ALEALLELKEEGLIKH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 163 IGVSNFNHKQLERLLNKpglkykpvcNQVECHL----Y--LNQS---KLLDYCKSKDIVLVAYGALG----TQRYKEWVD 229
Cdd:cd19090 137 IGLGGGPPDLLRRAIET---------GDFDVVLtanrYtlLDQSaadELLPAAARHGVGVINASPLGmgllAGRPPERVR 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230802 230 qNSPVLLDDPI------LCDVAKKNKRSPALIALRYLFQ----RGVVPLAQSfKEnEMRENLQVFEFQLSPE 291
Cdd:cd19090 208 -YTYRWLSPELldrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGASS-PE-ELEQNVAAAEGPLPEE 276
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
35-292 |
8.17e-26 |
|
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: 104.18 E-value: 8.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 35 LEAAHLAIDVGYRHIDTA---SAYQVEEEIGQAIqskiKAGVVKRKDMFITTKlwCSCFRTEMVRP-------------- 97
Cdd:cd19092 27 LSLIEAALELGITTFDHAdiyGGGKCEELFGEAL----ALNPGLREKIEIQTK--CGIRLGDDPRPgrikhydtskehil 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 98 -ALEKSLKNLQLDYVDLFLIHYPVPikssvdespldekgkflldtvdFCDTWEM---LEKCKDAGLVKSIGVSNFNHKQL 173
Cdd:cd19092 101 aSVEGSLKRLGTDYLDLLLLHRPDP----------------------LMDPEEVaeaFDELVKSGKVRYFGVSNFTPSQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 174 ErLLNKpGLKYKPVCNQVEC---HLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPVLLDdpILCDVAKKNKR 250
Cdd:cd19092 159 E-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA--ALEELAEEYGV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 148230802 251 SPALIALRYLFQR--GVVPLAQSFKENEMRENLQVFEFQLSPED 292
Cdd:cd19092 235 TIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
1.48e-25 |
|
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: 102.70 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTYKPKEVPKSKSLEAA----HLAIDVGYRHIDTASAY-QVEEEIGQAIQSkikagvVKRKDMFITTKLWCSC-- 89
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAEAarllNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 90 ------FRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpikssvdeSPLDEKGkflldtvdfcDTWEMLEKCKDAGLVKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGP---------SDDELTG----------EVLETLEDLKAAGKVRYI 135
|
....*.
gi 148230802 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
39-292 |
1.51e-25 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 103.69 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 39 HLAIDVGYRHIDTASAY---QVEEEIGQAIqskiKAGVVKRKDMFITTKlwcsC-----------------FRTEMVRPA 98
Cdd:COG4989 38 EAALELGITTFDHADIYggyTCEALFGEAL----KLSPSLREKIELQTK----CgirlpseardnrvkhydTSKEHIIAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 99 LEKSLKNLQLDYVDLFLIHYPvpikssvdeSPLdekgkflldtVDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLErLLN 178
Cdd:COG4989 110 VEGSLRRLGTDYLDLLLLHRP---------DPL----------MDPEEVAEAFDELKASGKVRHFGVSNFTPSQFE-LLQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 179 KpGLKYKPVCNQVECHLyLNQSKL----LDYCKSKDIVLVAYGALGTQRYKEWVDQNSPVLLDdpILCDVAKKNKRSPAL 254
Cdd:COG4989 170 S-ALDQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVSPEA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148230802 255 IALRYLFQR--GVVPLAQSFKENEMRENLQVFEFQLSPED 292
Cdd:COG4989 246 IALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-299 |
6.24e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 101.98 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT---------YKPKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITT 83
Cdd:cd19102 1 LTTIGLGTwaiggggwgGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 84 K---LW------CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKC 154
Cdd:cd19102 74 KcglLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP------DEPIEE-------------AWGALAEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 155 KDAGLVKSIGVSNFNHKQLERLL-------NKPGlkYKPVCNQVEchlylnqSKLLDYCKSKDIVLVAYGALG----TQR 223
Cdd:cd19102 135 KEEGKVRAIGVSNFSVDQMKRCQaihpiasLQPP--YSLLRRGIE-------AEILPFCAEHGIGVIVYSPMQsgllTGK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 224 Y-KEWV--------DQNSPV-----------LLDdpILCDVAKKNKRSPALIALRYLFQR----GVVPLAQSfkENEMRE 279
Cdd:cd19102 206 MtPERVaslpaddwRRRSPFfqepnlarnlaLVD--ALRPIAERHGRTVAQLAIAWVLRRpevtSAIVGARR--PDQIDE 281
|
330 340
....*....|....*....|
gi 148230802 280 NLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19102 282 TVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
39-299 |
9.34e-24 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 98.65 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 39 HLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvKRKDMFITTKlWCSCF---------RTEMVRPALEKSLKNL 106
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATK-GAHKFggdgsvlnnSPEFLRSAVEKSLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 107 QLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLERlLNKPGLkykp 186
Cdd:cd19083 113 NTDYIDLYYIHFPDG------ETPKAE-------------AVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGY---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 187 vCNQVE-CHLYLNQ---SKLLDYCKSKDIVLVAYGALG----TQRYkewvDQNSpVLLDDPI------------------ 240
Cdd:cd19083 169 -VDVLQgEYNLLQReaeEDILPYCVENNISFIPYFPLAsgllAGKY----TKDT-KFPDNDLrndkplfkgerfsenldk 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148230802 241 ---LCDVAKKNKRSPALIALRYLFQR----GVVPLAQsfKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19083 243 vdkLKSIADEKGVTVAHLALAWYLTRpaidVVIPGAK--RAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-283 |
7.45e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 94.96 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 13 GHFIPALGFGTYkpkeVPKSKSLEAAHLAIDVGYRHIDTASAYQV---EEEIGQAIQSkikagvVKRKDMFITTKLWCS- 88
Cdd:cd19105 10 GLKVSRLGFGGG----GLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKASPRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 89 -CFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPIKSSV-DESPLDEkgkflldtvdfcdtwemLEKCKDAGLVKSIGVS 166
Cdd:cd19105 80 dKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLlNEELLEA-----------------LEKLKKEGKVRFIGFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 --NFNHKQLERLLNKPG-----LKYkpvcNqvechlYLNQS----KLLDYCKSKDIVLVAYGALGTQRYKEWVDQnspvl 235
Cdd:cd19105 143 thDNMAEVLQAAIESGWfdvimVAY----N------FLNQPaeleEALAAAAEKGIGVVAMKTLAGGYLQPALLS----- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 148230802 236 lddpilcdVAKKNKRSPALIALRYLFQR----GVVPLAQSFKenEMRENLQV 283
Cdd:cd19105 208 --------VLKAKGFSLPQAALKWVLSNprvdTVVPGMRNFA--ELEENLAA 249
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-219 |
1.57e-22 |
|
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: 94.08 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTY-----KPKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTKL-- 85
Cdd:cd19086 3 VSEIGFGTWglggdWWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFgn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 -------WCSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpiksSVDESPLDEkgkflldtvdfcdTWEMLEKCKDAG 158
Cdd:cd19086 76 rfdggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNP-----PDEVLDNDE-------------LFEALEKLKQEG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 159 LVKSIGVSNFNHKQLERLLNKPGLkykpVCNQVECHLyLNQS---KLLDYCKSKDI-VLV----AYGAL 219
Cdd:cd19086 138 KIRAYGVSVGDPEEALAALRRGGI----DVVQVIYNL-LDQRpeeELFPLAEEHGVgVIArvplASGLL 201
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-297 |
9.30e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 93.04 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 31 KSKSLEAAHLAIDVGYRHIDTASAY-QVEEEIGQAIqSKIKAGVVKRKDMFITTKLWCSCFRTEM----VRPALEKSLKN 105
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYgPAEELIGEFR-KRLRRERDAADDVQIHTKWVPDPGELTMtrayVEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 106 LQLDYVDLFLIH---YPVPikssvdespldekgkflldtvDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLNKPgl 182
Cdd:cd19101 101 LGVDRLDLVQFHwwdYSDP---------------------GYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 183 kYKPVCNQVECHLyLNQ---SKLLDYCKSKDIVLVAYGALG----TQRykeWVDQNSP--VLLDDPILC----------- 242
Cdd:cd19101 158 -VPIVSNQVQYSL-LDRrpeNGMAALCEDHGIKLLAYGTLAggllSEK---YLGVPEPtgPALETRSLQkyklmidewgg 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148230802 243 ------------DVAKKNKRSPALIALRYLFQR----GVVPLAQSfkENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19101 233 wdlfqellrtlkAIADKHGVSIANVAVRWVLDQpgvaGVIVGARN--SEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
2.14e-21 |
|
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: 92.28 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 42 IDVGYRHIDTASAYQV----------EEEIGQAIQSKikagvVKRKDMFITTKLwcscfRTEM-----------VRPALE 100
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSR-----GKRDRVVIATKV-----GFPMgpngpglsrkhIRRAVE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 101 KSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLN-- 178
Cdd:cd19081 106 ASLRRLQTDYIDLYQAHWDDP------ATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALEls 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 179 -KPGLKyKPVCNQVECHLYLNQS---KLLDYCKSKDIVLVAYGALG----TQRYK------------EWVDQnspvLLDD 238
Cdd:cd19081 167 rQHGLP-RYVSLQPEYNLVDRESfegELLPLCREEGIGVIPYSPLAggflTGKYRseadlpgstrrgEAAKR----YLNE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148230802 239 P------ILCDVAKKNKRSPALIALRYLFQRGVV--PLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19081 242 RglrildALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-297 |
3.35e-21 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 91.60 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 33 KSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIqskikAGVVKRKDMFITTKL---W------CSCFRTEMVRPALE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATKVgleWdeggevVRNSSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 101 KSLKNLQLDYVDLFLIHYPVPIkssvdeSPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLNKP 180
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPL------VPIEE-------------TAEALKELLDEGKIRAIGVSNFSPEQMETFRKVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 181 GLK-YKPVCNQVECHLylnQSKLLDYCKSKDIVLVAYGAL------GT------------------------QRYKEWVD 229
Cdd:cd19148 162 PLHtVQPPYNLFEREI---EKDVLPYARKHNIVTLAYGALcrgllsGKmtkdtkfegddlrrtdpkfqeprfSQYLAAVE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230802 230 QnspvllddpiLCDVAKKN--KRSPALiALRYLFQRGVVPLA--QSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19148 239 E----------LDKLAQERygKSVIHL-AVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-297 |
1.73e-20 |
|
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: 89.98 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 11 NDGHFIPALGFG--TYKPKEVPKSK----SLEAAH----LAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRK 77
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGAwggvDQEEADrlvdIALDAGINFFDTADVYsegESEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 78 DMFITTKLWcscFRTE------------MVRpALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfc 145
Cdd:cd19091 81 DVLIATKVR---GRMGegpndvglsrhhIIR-AVEASLKRLGTDYIDLYQLHGFDA------LTPLEE------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 146 dTWEMLEKCKDAGLVKSIGVSNFNHKQLERLL---NKPGLKyKPVCNQVECHLyLNQS---KLLDYCKSKDIVLVAYGAL 219
Cdd:cd19091 139 -TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQAYYSL-LGRDlehELMPLALDQGVGLLVWSPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 220 G----TQRYKewVDQNSP-----------------VLLDDPI--LCDVAKKNKRSPALIALRYLFQRGVVP--LAQSFKE 274
Cdd:cd19091 216 AggllSGKYR--RGQPAPegsrlrrtgfdfppvdrERGYDVVdaLREIAKETGATPAQVALAWLLSRPTVSsvIIGARNE 293
|
330 340
....*....|....*....|...
gi 148230802 275 NEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19091 294 EQLEDNLGAAGLSLTPEEIARLD 316
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-166 |
5.50e-20 |
|
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: 88.53 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 18 ALGFGTYK--PKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKIKAGVVKRKDMFITTK-------- 84
Cdd:cd19099 5 SLGLGTYRgdSDDETDEEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELIEKGGIKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 85 -------LW------------------CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpikssvdESPLDEKG-KFL 138
Cdd:cd19099 85 deplrplKYleeklgrglidvadsaglRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNP--------EEQLLELGeEEF 156
|
170 180
....*....|....*....|....*...
gi 148230802 139 LDTVDfcDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19099 157 YDRLE--EAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-303 |
1.60e-19 |
|
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: 87.50 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 11 NDGHFIPALGFGT------YKPKEvPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEIgqaIQSKIKAGVVKRKDMFITTK 84
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYGDSEEL---IGRWFKQNPGKREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 85 -----------LWCSCfRTEMVRPALEKSLKNLQLDYVDLFLIHY---PVPIKSSVDEspldekgkflldtvdfcdtwem 150
Cdd:cd19144 84 fgieknvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQHRvdgKTPIEKTVAA---------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 151 LEKCKDAGLVKSIGVSNFNHKQLERL-----LNKPGLKYKPVCNQVEchlyLNQSKLLDYCKSKDIVLVAYGALG----T 221
Cdd:cd19144 141 MAELVQEGKIKHIGLSECSAETLRRAhavhpIAAVQIEYSPFSLDIE----RPEIGVLDTCRELGVAIVAYSPLGrgflT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 222 QRYKEWVD---------------QNSPVLLD--DPIlCDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEMRENLQ 282
Cdd:cd19144 217 GAIRSPDDfeegdfrrmaprfqaENFPKNLElvDKI-KAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLG 295
|
330 340
....*....|....*....|.
gi 148230802 283 VFEFQLSPEDMKTLDGLNKNF 303
Cdd:cd19144 296 ALKVKLTEEEEKEIREIAEEA 316
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-260 |
2.36e-19 |
|
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: 85.69 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTYK-PKEVPKSKSLEAA----HLAIDVGYRHIDTASAY---QVEEEIGQAIqskiKAGvvKRKDMFITTKL--W 86
Cdd:cd19096 1 SVLGFGTMRlPESDDDSIDEEKAiemiRYAIDAGINYFDTAYGYgggKSEEILGEAL----KEG--PREKFYLATKLppW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMvRPALEKSLKNLQLDYVDLFLIHypvpiksSVDESPLDEKGKflldtvDFcDTWEMLEKCKDAGLVKSIGVS 166
Cdd:cd19096 75 SVKSAEDF-RRILEESLKRLGVDYIDFYLLH-------GLNSPEWLEKAR------KG-GLLEFLEKAKKEGLIRHIGFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 167 nFnH---KQLERLLNkpglkykpvCNQVEC---HL-YLNQ-----SKLLDYCKSKDIVLVAYGALGTQRykewvdqnspv 234
Cdd:cd19096 140 -F-HdspELLKEILD---------SYDFDFvqlQYnYLDQenqagRPGIEYAAKKGMGVIIMEPLKGGG----------- 197
|
250 260
....*....|....*....|....*..
gi 148230802 235 LLDDP-ILCDVAKKNKRSPALIALRYL 260
Cdd:cd19096 198 LANNPpEALAILCGAPLSPAEWALRFL 224
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-297 |
4.94e-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: 85.79 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYK------PKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTKlw 86
Cdd:cd19149 11 ASVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR-------RDKVVLATK-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CS---------------------CFRTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfc 145
Cdd:cd19149 82 CGlrwdreggsfffvrdgvtvykNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDV------ETPIEE------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 146 dTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLNkpglkykpvCNQVEchlyLNQSK-----------LLDYCKSKDIVLV 214
Cdd:cd19149 144 -TMEALEELKRQGKIRAIGASNVSVEQIKEYVK---------AGQLD----IIQEKysmldrgiekeLLPYCKKNNIAFQ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 215 AYGAL-----------------GTQRY-KEWVDQNS--PVL-LDDPILcDVAKKNKRSPALIALRYLFQRG--VVPLAQS 271
Cdd:cd19149 210 AYSPLeqglltgkitpdrefdaGDARSgIPWFSPENreKVLaLLEKWK-PLCEKYGCTLAQLVIAWTLAQPgiTSALCGA 288
|
330 340
....*....|....*....|....*.
gi 148230802 272 FKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19149 289 RKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-299 |
9.52e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 85.01 E-value: 9.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 34 SLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTKLWCSCFRTE----MVRPALEKSLKNL 106
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 107 QLDYVDLFLIHYPVpikssVDESPLDEKGKFLLDTVDFCD-TWEMLEKCKDAGLVKSIGVSNFNHKQLERLLNKPGlkyK 185
Cdd:cd19104 107 KRDSVDLLQLHNRI-----GDERDKPVGGTLSTTDVLGLGgVADAFERLRSEGKIRFIGITGLGNPPAIRELLDSG---K 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 186 PVCNQVECHLyLNQS---------------KLLDYCKSKD-----IVLVAYGALGT--QRYKEWVD-QNSPVLLD---DP 239
Cdd:cd19104 179 FDAVQVYYNL-LNPSaaearprgwsaqdygGIIDAAAEHGvgvmgIRVLAAGALTTslDRGREAPPtSDSDVAIDfrrAA 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230802 240 ILCDVAKKNKRSPALIALRY-LFQRGVVPLAQSFKE-NEMRENLQVFEF-QLSPEDMKTLDGL 299
Cdd:cd19104 258 AFRALAREWGETLAQLAHRFaLSNPGVSTVLVGVKNrEELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
40-297 |
3.17e-18 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 83.77 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 40 LAIDVGYRHIDTASAYQV----------EEEIGQAIQSKikagvVKRKDMFITTKL--------WC----SCFRTEMVRP 97
Cdd:cd19094 26 YAFDEGVNFIDTAEMYPVppspetqgrtEEIIGSWLKKK-----GNRDKVVLATKVagpgegitWPrgggTRLDRENIRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 98 ALEKSLKNLQLDYVDLFLIHYP---VPIKSSVDESPLDEKGkfllDTVDFCDTWEMLEKCKDAGLVKSIGVSN------- 167
Cdd:cd19094 101 AVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE----DSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvm 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 -FNHkqLERLLNKPglkyKPVCNQVECHLyLNQSK---LLDYCKSKDIVLVAYGALG----TQRYKEWVDQNSPVLLDD- 238
Cdd:cd19094 177 kFLE--LAEQLGLP----RIVSIQNPYSL-LNRNFeegLAEACHRENVGLLAYSPLAggvlTGKYLDGAARPEGGRLNLf 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 239 ---------PI-------LCDVAKKNKRSPALIALRYLFQR--------GVVPLAQsfkeneMRENLQVFEFQLSPEDMK 294
Cdd:cd19094 250 pgymaryrsPQaleavaeYVKLARKHGLSPAQLALAWVRSRpfvtstiiGATTLEQ------LKENIDAFDVPLSDELLA 323
|
...
gi 148230802 295 TLD 297
Cdd:cd19094 324 EID 326
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
18-297 |
7.00e-18 |
|
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: 82.28 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 18 ALGFG------TYKPkevPKSK--SLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTKlw 86
Cdd:cd19078 6 AIGLGcmgmshGYGP---PPDKeeMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 cscF----------------RTEMVRPALEKSLKNLQLDYVDLFLIHYP---VPIKssvdespldekgkflldtvdfcDT 147
Cdd:cd19078 74 ---FgfkidggkpgplgldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVdpnVPIE----------------------EV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 148 WEMLEKCKDAGLVKSIGVSNFNHKQLERllnkpGLKYKPVCN-QVECHLYLN--QSKLLDYCKSKDIVLVAYGALG---- 220
Cdd:cd19078 129 AGTMKELIKEGKIRHWGLSEAGVETIRR-----AHAVCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGkgfl 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 221 -------------------TQRYKEWVDQNSPvLLDdpILCDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEMRE 279
Cdd:cd19078 204 tgkidentkfdegddraslPRFTPEALEANQA-LVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEE 280
|
330
....*....|....*...
gi 148230802 280 NLQVFEFQLSPEDMKTLD 297
Cdd:cd19078 281 NIGAADIELTPEELREIE 298
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
41-297 |
1.00e-17 |
|
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: 81.86 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 41 AIDVGYRHIDTASAYQ--VEEEI-GQAIQskikaGVVKRKDMFITTKLwcsCFRT-----------EMVRPALEKSLKNL 106
Cdd:cd19079 44 ALDLGINFFDTANVYSggASEEIlGRALK-----EFAPRDEVVIATKV---YFPMgdgpngrglsrKHIMAEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 107 QLDYVDLFLIH---YPVPIKssvdespldekgkflldtvdfcDTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLN---KP 180
Cdd:cd19079 116 GTDYIDLYQIHrwdYETPIE----------------------ETLEALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 181 GLKyKPVCNQvechLYLN------QSKLLDYCKSKDIVLVAY---------GALGTQRYKEWVDQNSPVL-------LDD 238
Cdd:cd19079 174 GWT-KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWsplargrlaRPWGDTTERRRSTTDTAKLkydyfteADK 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148230802 239 PILCDV---AKKNKRSPALIALRYLFQRGVV--PLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19079 249 EIVDRVeevAKERGVSMAQVALAWLLSKPGVtaPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-262 |
1.06e-17 |
|
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: 81.42 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 40 LAIDVGYRHIDTASAY-QVEEEIGQAIQSKikagvvkrKDMFITTKL----WCSCFRTEMVRPALEKSLKNLQLDYVDLF 114
Cdd:cd19097 34 YALKAGINTLDTAPAYgDSEKVLGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 115 LIHypvpikssvDESPLDEKGKFLldtvdfcdtWEMLEKCKDAGLVKSIGVSNFNHKQLERLLNKPGLKYkpVcnQVECH 194
Cdd:cd19097 106 LLH---------NPDDLLKHGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I--QLPFN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 195 LY---LNQSKLLDYCKSKDIVLVA-----YGALgTQRYKEWVDQNSPV--LLDdpILCDVAKKNKRSPALIALRYLFQ 262
Cdd:cd19097 164 ILdqrFLKSGLLAKLKKKGIEIHArsvflQGLL-LMEPDKLPAKFAPAkpLLK--KLHELAKKLGLSPLELALGFVLS 238
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
19-291 |
5.50e-17 |
|
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: 79.56 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 19 LGFGTYKP--KEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSkikagvVKRKDMFITTKLwcsCFRT- 92
Cdd:cd19074 7 LSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKV---FWPTg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 93 ----------EMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldTVDFCDTwemlekCKDAGLVKS 162
Cdd:cd19074 78 pgpndrglsrKHIFESIHASLKRLQLDYVDIYYCHRYDP------ETPLEE-------TVRAMDD------LIRQGKILY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 163 IGVSNFNHKQLE---RLLNKPGLkYKPVCNQVECHLyLNQSK---LLDYCKSKDIVLVAYGALG----TQRYKEWV---- 228
Cdd:cd19074 139 WGTSEWSAEQIAeahDLARQFGL-IPPVVEQPQYNM-LWREIeeeVIPLCEKNGIGLVVWSPLAqgllTGKYRDGIppps 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 229 -----DQNSPVLLDDPI----------LCDVAKKNKRSPALIALRYLFQRGVV--PLAQSFKENEMRENLQVFEFQLSPE 291
Cdd:cd19074 217 rsratDEDNRDKKRRLLtdenlekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-220 |
7.43e-17 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 79.13 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT------YKPkeVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSkikagvVKRKDMFITTKlw 86
Cdd:cd19163 13 VSKLGFGAsplggvFGP--VDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALKG------IPRDSYYLATK-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 csC------------FRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpikssvdespldEKGKfLLDTVdFCDTWEMLEKC 154
Cdd:cd19163 83 --VgrygldpdkmfdFSAERITKSVEESLKRLGLDYIDIIQVHDI-------------EFAP-SLDQI-LNETLPALQKL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148230802 155 KDAGLVKSIGVSNFNHKQLERLLNKPG------LKYkpvcnqveCHLYLNQS---KLLDYCKSKDIVLVAYGALG 220
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVLERSPvkidtvLSY--------CHYTLNDTsllELLPFFKEKGVGVINASPLS 212
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-299 |
4.04e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 77.37 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 41 AIDVGYRHIDTASAYqveeeiGQAIQSKIKAGVVK---RKDMFITTKL--WCSCFRTEMVRPALEKSLKNLQLDYVDLFL 115
Cdd:cd19103 41 AMAAGLNLWDTAAVY------GMGASEKILGEFLKrypREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 116 IHYPVPIKssvdespldekgKFLLDTVDfcdtwemLEKckdAGLVKSIGVSNFNHKQLER---LLNKPGLKYKPVCNqve 192
Cdd:cd19103 115 IHNPADVE------------RWTPELIP-------LLK---SGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 193 cH---LYLN--QSKLLDYCKSKDIVLVAY-----GAL------------GTQRYKEWvdqnSPVL--LDD--PILCDVAK 246
Cdd:cd19103 170 -HyslLYRSseEAGILDYCKENGITFFAYmvleqGALsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAEIGA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148230802 247 KNKRSPALIALRYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19103 245 KHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
16-296 |
4.67e-16 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 77.26 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT------YKPKevPKSKSLEAAHLAIDVGYRHIDTASAYQV---EEEIGQAIQSKikagvvkRKDMFITTK-- 84
Cdd:cd19076 12 VSALGLGCmgmsafYGPA--DEEESIATLHRALELGVTFLDTADMYGPgtnEELLGKALKDR-------RDEVVIATKfg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 85 -LWC--SCFRT-----EMVRPALEKSLKNLQLDYVDLFLIHYP---VPIKssvdespldekgkflldtvdfcDTWEMLEK 153
Cdd:cd19076 83 iVRDpgSGFRGvdgrpEYVRAACEASLKRLGTDVIDLYYQHRVdpnVPIE----------------------ETVGAMAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 154 CKDAGLVKSIGVSNFNHKQLERllnkpGLKYKPVCN-QVECHLYLN--QSKLLDYCKSKDIVLVAYGALG---------- 220
Cdd:cd19076 141 LVEEGKVRYIGLSEASADTIRR-----AHAVHPITAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLGrgfltgaiks 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 221 ------------TQRY-KEWVDQNSPVLldDPILcDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEMRENLQVFE 285
Cdd:cd19076 216 pedlpeddfrrnNPRFqGENFDKNLKLV--EKLE-AIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALD 292
|
330
....*....|.
gi 148230802 286 FQLSPEDMKTL 296
Cdd:cd19076 293 VVLTPEELAEI 303
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
49-282 |
4.39e-15 |
|
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: 74.13 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 49 IDTASAYQV-------EEEIGQAIQSKIKagvvkRKDMFITTK--------LWCSCFRTEMVRPALEKSLKNLQLDYVDL 113
Cdd:cd19082 34 IDTARVYGDwvergasERVIGEWLKSRGN-----RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDYIDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 114 FLIHYPvpikssvDES-PLDEkgkfLLDTvdfcdtwemLEKCKDAGLVKSIGVSNFNHkqlERLL---------NKPGlk 183
Cdd:cd19082 109 YFLHRD-------DPSvPVGE----IVDT---------LNELVRAGKIRAFGASNWST---ERIAeanayakahGLPG-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 184 ykPVCNQV--------------ECHLYLNQSkLLDYCKSKDIVLVAYGALG----TQRYKEWVDQNSPVL--LDDPI--- 240
Cdd:cd19082 164 --FAASSPqwslarpneppwpgPTLVAMDEE-MRAWHEENQLPVFAYSSQArgffSKRAAGGAEDDSELRrvYYSEEnfe 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 148230802 241 ----LCDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEMRENLQ 282
Cdd:cd19082 241 rlerAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLRDSLA 288
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
8-296 |
1.08e-12 |
|
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: 67.46 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 8 VKL-NDGHFIPALGFG------TYKPkEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKIkagvvkRK 77
Cdd:cd19145 3 VKLgSQGLEVSAQGLGcmglsgDYGA-PKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------RE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 78 DMFITTKLWCSCFRT---------EMVRPALEKSLKNLQLDYVDLFLIH---YPVPIKSSVDEspldekgkflldtvdfc 145
Cdd:cd19145 76 KVQLATKFGIHEIGGsgvevrgdpAYVRAACEASLKRLDVDYIDLYYQHridTTVPIEITMGE----------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 146 dtwemLEKCKDAGLVKSIGVSNFNHKQLERllnkpGLKYKPVCN-QVECHLYLN--QSKLLDYCKSKDIVLVAYGALGT- 221
Cdd:cd19145 139 -----LKKLVEEGKIKYIGLSEASADTIRR-----AHAVHPITAvQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLGRg 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 222 ---------------------QRYK-EWVDQNSpVLLDDpiLCDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEM 277
Cdd:cd19145 209 ffagkakleellensdvrkshPRFQgENLEKNK-VLYER--VEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNL 285
|
330
....*....|....*....
gi 148230802 278 RENLQVFEFQLSPEDMKTL 296
Cdd:cd19145 286 NQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-260 |
2.03e-12 |
|
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: 66.43 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTYKPKEVPKSKSLEAAHLAIDV----GYRHIDTASAY---QVEEEIGQAIQSKikAGVVkrkdmfITTK---LW 86
Cdd:cd19075 1 PKIILGTMTFGSQGRFTTAEAAAELLDAflerGHTEIDTARVYpdgTSEELLGELGLGE--RGFK------IDTKanpGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 CSCFRTEMVRPALEKSLKNLQLDYVDLFLIHYPvpikssvDES-PLDEkgkflldTVDFCDTwemLEKckdAGLVKSIGV 165
Cdd:cd19075 73 GGGLSPENVRKQLETSLKRLKVDKVDVFYLHAP-------DRStPLEE-------TLAAIDE---LYK---EGKFKEFGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 166 SNFNHKQLERLLN--------KP----GLkYKPVCNQVEchlylnqSKLLDYCKSKDIVLVAYGALG----TQRYKEWVD 229
Cdd:cd19075 133 SNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAggflTGKYKYSED 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 148230802 230 QNSPVLLDDP---------------------ILCDVAKKNKRSPALIALRYL 260
Cdd:cd19075 205 KAGGGRFDPNnalgklyrdrywkpsyfealeKVEEAAEKEGISLAEAALRWL 256
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-299 |
2.63e-12 |
|
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: 66.44 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 41 AIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvkRKDMFITTKLwcsCFRT-----------EMVRPALEKSLKNL 106
Cdd:cd19087 39 ALDAGINFFDTADVYgggRSEEIIGRWIAGR-------RDDIVLATKV---FGPMgddpndrglsrRHIRRAVEASLRRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 107 QLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLN---KPGL- 182
Cdd:cd19087 109 QTDYIDLYQMHHFDR------DTPLEE-------------TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGLl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 183 -------KYKPVCNQVECHlylnqskLLDYCKSKDIVLVAYGALG----TQRY-------------------KEWVDQNS 232
Cdd:cd19087 170 rfvseqpMYNLLKRQAELE-------ILPAARAYGLGVIPYSPLAggllTGKYgkgkrpesgrlveraryqaRYGLEEYR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 233 PVLLDdpiLCDVAKKNKRSPALIALRYLFQRGVV--PLAQSFKENEMRENLQVFEFQLSPEDMKTLDGL 299
Cdd:cd19087 243 DIAER---FEALAAEAGLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-219 |
4.79e-12 |
|
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: 65.46 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGTY---KPKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagvvKRKDMFITTKL----- 85
Cdd:cd19162 1 PRLGLGAAslgNLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 86 ---WCSCFRTEM--------VRPALEKSLKNLQLDYVDLFLIHYPvpikssvdesplDEKgkfLLDTVDfcDTWEMLEKC 154
Cdd:cd19162 75 pgaAGRPAGADRrfdfsadgIRRSIEASLERLGLDRLDLVFLHDP------------DRH---LLQALT--DAFPALEEL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148230802 155 KDAGLVKSIGVSNFNHKQLERLLNKPGLKYKPVCNQvecHLYLNQS---KLLDYCKSKDIVLVAYGAL 219
Cdd:cd19162 138 RAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVF 202
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
16-266 |
4.85e-12 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 65.36 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPAL------GFGTYKPKEVPKSKSLEAahlaIDVGYRHIDTASAY-----QVEEEIGQAIQSKIKAgvvKRKDMFITTK 84
Cdd:cd19089 11 LPAIslglwhNFGDYTSPEEARELLRTA----FDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVISTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 85 L-----------WCScfRTEMVRpALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEKGKFLLDTVdfcdtwemlek 153
Cdd:cd19089 84 AgygmwpgpygdGGS--RKYLLA-SLDQSLKRMGLDYVDIFYHHRYDP------DTPLEETMTALADAV----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 154 ckDAGLVKSIGVSNFNHKQLER---LLNKpgLKYKPVCNQVECHLyLNQS---KLLDYCKSKDIVLVAYGALG----TQR 223
Cdd:cd19089 144 --RSGKALYVGISNYPGAKARRaiaLLRE--LGVPLIIHQPRYSL-LDRWaedGLLEVLEEAGIGFIAFSPLAqgllTDK 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148230802 224 YKEWVDQNSPVLLDDPILCD----------------VAKKNKRSPALIALRYLFQRGVV 266
Cdd:cd19089 219 YLNGIPPDSRRAAESKFLTEealtpekleqlrklnkIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-297 |
9.95e-12 |
|
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: 64.57 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 20 GFG----TYKPKEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEE------IGQAIQ------SKIKAGVvkrKDMFITT 83
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPhanlklLARFFRkypeyaDKVVLSV---KGGLDPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 84 KLWCSCfRTEMVRPALEKSLKNL-QLDYVDLFlihypVPikSSVDES-PLDEkgkflldtvdfcdTWEMLEKCKDAGLVK 161
Cdd:cd19077 86 TLRPDG-SPEAVRKSIENILRALgGTKKIDIF-----EP--ARVDPNvPIEE-------------TIKALKELVKEGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 162 SIGVSNFNHKQLERllnkpGLKYKPV-CNQVECHLYLN---QSKLLDYCKSKDIVLVAYGALG----TQRYK-------- 225
Cdd:cd19077 145 GIGLSEVSAETIRR-----AHAVHPIaAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGrgllTGRIKsladipeg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 226 -----------EWVDQNSPvLLDDpiLCDVAKKNKRSPALIAL---RYLFQRGVVPLAQSFKENEMRENLQVFEFQLSPE 291
Cdd:cd19077 220 dfrrhldrfngENFEKNLK-LVDA--LQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDE 296
|
....*.
gi 148230802 292 DMKTLD 297
Cdd:cd19077 297 ELKEIN 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
49-297 |
4.87e-11 |
|
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: 62.62 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 49 IDTASAYQ---VEEEIGQAIQSKikagvvkRKDMFITTKL----------WCSCFRTEMVRpALEKSLKNLQLDYVDLFL 115
Cdd:cd19080 48 IDTANNYTngtSERLLGEFIAGN-------RDRIVLATKYtmnrrpgdpnAGGNHRKNLRR-SVEASLRRLQTDYIDLLY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 116 IHYPvpikssvDE-SPLDEkgkfLLDTVDfcdtwemlekckD---AGLVKSIGVSNF------------NHKQLERllnk 179
Cdd:cd19080 120 VHAW-------DFtTPVEE----VMRALD------------DlvrAGKVLYVGISDTpawvvarantlaELRGWSP---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 180 pglkykPVCNQVECHLyLNQS---KLLDYCKSKDIVLVAYGALG-------------TQRYKEWVDQNSPVLLDD----- 238
Cdd:cd19080 173 ------FVALQIEYSL-LERTperELLPMARALGLGVTPWSPLGgglltgkyqrgeeGRAGEAKGVTVGFGKLTErnwai 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230802 239 -PILCDVAKKNKRSPALIALRYLFQR--GVVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19080 246 vDVVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
41-300 |
2.33e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 60.37 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 41 AIDVGYRHIDTASAYqveeeiGQAIQSKI--KAGVVKRKDMFITTKL---------WCSCFRTEMVRPALEKSLKNLQLD 109
Cdd:PRK10376 49 AVALGVNHIDTSDFY------GPHVTNQLirEALHPYPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLGLD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 110 YVDL------FLIHYPVPikSSVDEsPLdekgkflldtvdfcdtwEMLEKCKDAGLVKSIGVSNFNHKQLERllnkpGLK 183
Cdd:PRK10376 123 VLDVvnlrlmGDGHGPAE--GSIEE-PL-----------------TVLAELQRQGLVRHIGLSNVTPTQVAE-----ARK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 184 YKP-VCNQVECHL-YLNQSKLLDYCKSKDIVLVAYGALGTqrykewvdqNSPvlLDDPILCDVAKKNKRSPALIALRYLF 261
Cdd:PRK10376 178 IAEiVCVQNHYNLaHRADDALIDALARDGIAYVPFFPLGG---------FTP--LQSSTLSDVAASLGATPMQVALAWLL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148230802 262 QRG----VVPLAQSFKenEMRENLQVFEFQLSPEDMKTLDGLN 300
Cdd:PRK10376 247 QRSpnilLIPGTSSVA--HLRENLAAAELVLSEEVLAELDGIA 287
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-259 |
2.48e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 57.48 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 11 NDGHFIPALGFG------TYKPkeVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIqskiKAGVVKRKDMFI 81
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFGP--VSEEDAIASVREAFRLGINFFDTSPYYggtLSEKVLGKAL----KALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 82 TTKlwcsC--------FRTEMVRPALEKSLKNLQLDYVDLFLIHypvpiksSVDESPLDEkgkflldTVDfcDTWEMLEK 153
Cdd:PLN02587 80 STK----CgrygegfdFSAERVTKSVDESLARLQLDYVDILHCH-------DIEFGSLDQ-------IVN--ETIPALQK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 154 CKDAGLVKSIGVSNFNHKQLERLLNK--PG-----LKYkpvcnqveCHLYLNQSKLLD---YCKSKDIVLV-----AYGA 218
Cdd:PLN02587 140 LKESGKVRFIGITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVIsasplAMGL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 148230802 219 LGTQRYKEWvdqnSPVLLDDPILC----DVAKKNKRSPALIALRY 259
Cdd:PLN02587 212 LTENGPPEW----HPAPPELKSACaaaaTHCKEKGKNISKLALQY 252
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-282 |
1.56e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 55.03 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 42 IDVGYRHIDTASAY----------QVEEEIGQAIQSKikaGVvkRKDMFITTKL---------WCSCFR---TEMVRPAL 99
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDR---GN--RDDVVIATKVgagprdpdgGPESPEglsAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 100 EKSLKNLQLDYVDLFLIHypvpikssVD--ESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLER-- 175
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAH--------VDdrDTPLEE-------------TLEAFNELVKAGKVRAIGASNFAAWRLERar 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 176 -LLNKPGLKyKPVCNQVEcHLYL---------NQS----KLLDYCKS-KDIVLVAYGALGTQRY--------KEWVDQNS 232
Cdd:cd19752 161 qIARQQGWA-EFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLLSGAYtrpdrplpEQYDGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 148230802 233 PVLLDdpILCDVAKKNKRSPALIALRYLFQR--GVVPLAQSFKENEMRENLQ 282
Cdd:cd19752 239 DARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIPLLGASTVEQLEENLA 288
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
41-297 |
3.36e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 54.23 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 41 AIDVGYRHIDTASAY-----QVEEEIGQAIQSKIKAgvvKRKDMFITTK----LWCSCFRTEMVR----PALEKSLKNLQ 107
Cdd:PRK09912 52 AFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIISTKagydMWPGPYGSGGSRkyllASLDQSLKRMG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 108 LDYVDLFLIHypvpiksSVDE-SPLDEKGKFLLDTVdfcdtwemlekckDAGLVKSIGVSNFNHKQLER---LLNK---P 180
Cdd:PRK09912 129 LEYVDIFYSH-------RVDEnTPMEETASALAHAV-------------QSGKALYVGISSYSPERTQKmveLLREwkiP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 181 GLKYKPVCNQVecHLYLNQSKLLDYCKSKDIVLVAYGALG----TQRYKEWVDQNS-------------PVLLDDP---- 239
Cdd:PRK09912 189 LLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAqgllTGKYLNGIPQDSrmhregnkvrgltPKMLTEAnlns 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230802 240 --ILCDVAKKNKRSPALIALRYLF--QRGVVPLAQSFKENEMRENLQVFE-FQLSPEDMKTLD 297
Cdd:PRK09912 267 lrLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALNnLTFSTEELAQID 329
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-126 |
4.00e-08 |
|
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: 53.75 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 18 ALGFG---TYKPK-EVPKSKSLEAAhlAIDVGYRHIDTASAY---QVEEEIGQAIqskiKAGVVKRKDMFITTKLWcscF 90
Cdd:cd19143 15 ALSFGswvTFGNQvDVDEAKECMKA--AYDAGVNFFDNAEVYangQSEEIMGQAI----KELGWPRSDYVVSTKIF---W 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148230802 91 RTEMVRP------------ALEKSLKNLQLDYVDLFLIHYP---VPIKSSV 126
Cdd:cd19143 86 GGGGPPPndrglsrkhiveGTKASLKRLQLDYVDLVFCHRPdpaTPIEETV 136
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-167 |
8.41e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 14 HFIP-------ALGFGTYKPKEvpksKSLEA-AH----LAIDVGYRHIDTASAYQV----------EEEIGQAIQSKika 71
Cdd:PRK10625 4 HRIPhsslevsTLGLGTMTFGE----QNSEAdAHaqldYAVAQGINLIDVAEMYPVpprpetqgltETYIGNWLAKR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 72 gvVKRKDMFITTKLWC------SCFRTEM------VRPALEKSLKNLQLDYVDLFLIHYPvpikssvdESPLDEKGKFLL 139
Cdd:PRK10625 77 --GSREKLIIASKVSGpsrnndKGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWP--------QRPTNCFGKLGY 146
|
170 180 190
....*....|....*....|....*....|....
gi 148230802 140 D------TVDFCDTWEMLEKCKDAGLVKSIGVSN 167
Cdd:PRK10625 147 SwtdsapAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
34-266 |
1.48e-07 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 52.02 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 34 SLEAAHLAIDVGYRHIDTASAY-----QVEEEIGQAIQSKIKAgvvKRKDMFITTKL-----------WCScfRTEMVrP 97
Cdd:cd19151 32 SRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKP---YRDELIISTKAgytmwpgpygdWGS--KKYLI-A 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 98 ALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSNFNHKQLE--- 174
Cdd:cd19151 106 SLDQSLKRMGLDYVDIFYHHRPDP------ETPLEE-------------TMGALDQIVRQGKALYVGISNYPPEEAReaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 175 ---RLLNKPGLKYKPVCNQVECHlylNQSKLLDYCKSKDIVLVAYGALG----TQRY-----------KEWVDQNSPVLL 236
Cdd:cd19151 167 ailKDLGTPCLIHQPKYSMFNRW---VEEGLLDVLEEEGIGCIAFSPLAqgllTDRYlngipedsraaKGSSFLKPEQIT 243
|
250 260 270
....*....|....*....|....*....|....*
gi 148230802 237 DDPI-----LCDVAKKNKRSPALIALRYLFQRGVV 266
Cdd:cd19151 244 EEKLakvrrLNEIAQARGQKLAQMALAWVLRNKRV 278
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
41-227 |
2.46e-07 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 51.38 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 41 AIDVGYRHIDTASAY---QVEEEIGQAIqskiKAGVVKRKDMFITTKlwCSCFRT-------EMVRPALEKSLKNLQLDY 110
Cdd:cd19153 42 AFAAGINHFDTSPYYgaeSSEAVLGKAL----AALQVPRSSYTVATK--VGRYRDsefdysaERVRASVATSLERLHTTY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 111 VDLFLIHypvpikssvDESPLDekgkflLDTvDFCDTWEMLEKCKDAGLVKSIGVSNFNHKQLERLLNK--PGlkyKPVC 188
Cdd:cd19153 116 LDVVYLH---------DIEFVD------YDT-LVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRcsPG---SLDA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148230802 189 NQVECHLYLNQSKLLD---YCKSKDIVLV------AYGALGTQRYKEW 227
Cdd:cd19153 177 VLSYCHLTLQDARLESdapGLVRGAGPHVinasplSMGLLTSQGPPPW 224
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
16-117 |
2.08e-06 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 48.61 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYK--PKEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagVVKRKDMFITTKL-W--- 86
Cdd:cd19142 13 VSNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFtsgQAETELGRILKKK----GWKRSSYIVSTKIyWsyg 88
|
90 100 110
....*....|....*....|....*....|....
gi 148230802 87 ---CSCFRTEMVRpALEKSLKNLQLDYVDLFLIH 117
Cdd:cd19142 89 seeRGLSRKHIIE-SVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
3.07e-06 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 47.99 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 17 PALGFGT------YKPkeVPKSKSLEAAHLAIDVGYRHIDTASAYQV---EEEIGQAIQSKikagvvKRKDMFITTKL-W 86
Cdd:cd19152 1 PKLGFGTaplgnlYEA--VSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 87 csCFRTEMVRPA--------------------------LEKSLKNLQLDYVDLFLIHYPvpikssvDESPLDEKGKFLLD 140
Cdd:cd19152 73 --LLVPLQEVEPtfepgfwnplpfdavfdysydgilrsIEDSLQRLGLSRIDLLSIHDP-------DEDLAGAESDEHFA 143
|
170 180
....*....|....*....|....*
gi 148230802 141 TvDFCDTWEMLEKCKDAGLVKSIGV 165
Cdd:cd19152 144 Q-AIKGAFRALEELREEGVIKAIGL 167
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
16-177 |
1.12e-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: 46.12 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGT------YKPkEVPKSKSLEAAHLAIDVGYRHIDTASAYQVEEEI-GQAIQSKIKAgvVKRKDMFITTKlwcs 88
Cdd:cd19164 13 LPPLIFGAatfsyqYTT-DPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRALKALRDE--FPRDTYFIITK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 89 CFR---------TEMVRPALEKSLKNLQLDYVDLFLIHypvpikssvDespldekgkflldtVDFCDTWEMLE------K 153
Cdd:cd19164 86 VGRygpddfdysPEWIRASVERSLRRLHTDYLDLVYLH---------D--------------VEFVADEEVLEalkelfK 142
|
170 180
....*....|....*....|....
gi 148230802 154 CKDAGLVKSIGVSNFnhkQLERLL 177
Cdd:cd19164 143 LKDEGKIRNVGISGY---PLPVLL 163
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
36-297 |
1.31e-05 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 46.26 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 36 EAAHLAIDVGYRH----IDTASAYQVEEE---IGQAIQSKikagvVKRKDMFITTKLWCSCFRTEMV------------- 95
Cdd:cd19146 35 ETAFKLLDAFYEQggnfIDTANNYQGEESerwVGEWMASR-----GNRDEMVLATKYTTGYRRGGPIkiksnyqgnhaks 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 96 -RPALEKSLKNLQLDYVDLFLIH---YPVPIKSSVDE-SPLDEKGKFLLDTVDFCDTWeMLEKC----KDAGLVKSI--- 163
Cdd:cd19146 110 lRLSVEASLKKLQTSYIDILYVHwwdYTTSIPELMQSlNHLVAAGKVLYLGVSDTPAW-VVSKAnayaRAHGLTQFVvyq 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 164 GVSNFNHKQLERllnkpglkykpvcnqvechlylnqsKLLDYCKSKDIVLVAYGALGTQRYK--------------EWVd 229
Cdd:cd19146 189 GHWSAAFRDFER-------------------------DILPMCEAEGMALAPWGVLGQGQFRteeefkrrgrsgrkGGP- 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 230 QNSPVLLDDPILCDVAKKNKRSPALIALRYLFQRG--VVPLAQSFKENEMRENLQVFEFQLSPEDMKTLD 297
Cdd:cd19146 243 QTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIE 312
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
21-294 |
8.30e-05 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 43.60 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 21 FGTYKPKEVPKskslEAAHLAIDVGYRHIDTASAY-----QVEEEIGQAIQSKIKAgvvKRKDMFITTK----LWCSCF- 90
Cdd:cd19150 23 FGDDTPLETQR----AILRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAG---YRDELIISTKagydMWPGPYg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 91 ---RTEMVRPALEKSLKNLQLDYVDLFLIHYPVPikssvdESPLDEkgkflldtvdfcdTWEMLEKCKDAGLVKSIGVSN 167
Cdd:cd19150 96 ewgSRKYLLASLDQSLKRMGLDYVDIFYSHRFDP------DTPLEE-------------TMGALDHAVRSGKALYVGISS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 168 FNHKQ------LERLLNKPGLKYKPVCNQVecHLYLNQSKLLDYCKSKDIVLVAYGALG----TQRYKEWVDQNS----- 232
Cdd:cd19150 157 YSPERtreaaaILRELGTPLLIHQPSYNML--NRWVEESGLLDTLQELGVGCIAFTPLAqgllTDKYLNGIPEGSraske 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148230802 233 ----PVLLDDPILCDV------AKKNKRSPALIALRYLFQRGVVP--LAQSFKENEMRENLQVFE-FQLSPEDMK 294
Cdd:cd19150 235 rslsPKMLTEANLNSIralneiAQKRGQSLAQMALAWVLRDGRVTsaLIGASRPEQLEENVGALDnLTFSADELA 309
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
16-121 |
1.73e-03 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); 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.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 39.74 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 16 IPALGFGTYKP--KEVPKSKSLEAAHLAIDVGYRHIDTASAY---QVEEEIGQAIQSKikagVVKRKDMFITTKL-WCSC 89
Cdd:cd19141 12 VSCLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIfWGGK 87
|
90 100 110
....*....|....*....|....*....|....*...
gi 148230802 90 FRTEM------VRPALEKSLKNLQLDYVDLFLIHYPVP 121
Cdd:cd19141 88 AETERglsrkhIIEGLKASLERLQLEYVDIVFANRPDP 125
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
31-118 |
2.63e-03 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also 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: 381373 [Multi-domain] Cd Length: 319 Bit Score: 39.04 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230802 31 KSKSLEAAHLAIDVGYRHIDTASAYQVEEE---IGQAIQSKikagvVKRKDMFITTKL-----------------WCSCF 90
Cdd:cd19147 33 KEQAFELLDAFYEAGGNFIDTANNYQDEQSetwIGEWMKSR-----KNRDQIVIATKFttdykayevgkgkavnyCGNHK 107
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90 100
....*....|....*....|....*...
gi 148230802 91 RTEMVrpALEKSLKNLQLDYVDLFLIHY 118
Cdd:cd19147 108 RSLHV--SVRDSLRKLQTDWIDILYVHW 133
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