|
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) ... |
7-309 |
0e+00 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 662.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 7 RSVKLNDGNLMPVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKI 86
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 WITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGV 166
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 167 SNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIA 246
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQM 309
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
14-320 |
2.68e-176 |
|
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: 490.08 E-value: 2.68e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGTFAS-KEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLR 92
Cdd:cd19109 1 GNSIPIIGLGTYSEpKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 93 PELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHK 172
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 173 QLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIAKKHNQT 252
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 253 PGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPF 320
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
14-324 |
3.89e-144 |
|
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: 408.73 E-value: 3.89e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGTFASkeiPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRP 93
Cdd:cd19107 1 GAKMPILGLGTWKS---PPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 94 ELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQ 173
Cdd:cd19107 78 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 174 LELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGShRDSSWVSSDSPYLLEDPVLMTIAKKHNQTP 253
Cdd:cd19107 158 IERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGS-PDRPWAKPEDPSLLEDPKIKEIAAKHNKTT 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138555 254 GQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPFLEEY 324
Cdd:cd19107 237 AQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-306 |
6.10e-134 |
|
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: 382.89 E-value: 6.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 11 LNDGNLMPVLGFGTFASKeipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKM-ADGTVKREDLFYTTKIWIT 89
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSK---PGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 90 FLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNF 169
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 170 NHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGShRDSSWVSSDSPYLLEDPVLMTIAKKH 249
Cdd:cd19106 158 NSRQIDDILSVARI--KPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGS-PDRPWAKPDEPVLLEEPKVKALAKKY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 158138555 250 NQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19106 235 NKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-306 |
1.71e-130 |
|
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: 373.54 E-value: 1.71e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFASKEIPKSKAAeaTKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIW 87
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRQA--VKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKpgeELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNkpRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHrDSSWVSSDSPYlLEDPVLMTIAK 247
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRL-VPRGQTNPPPR-LDDPTLVAIAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158138555 248 KHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
17-298 |
6.90e-127 |
|
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: 362.57 E-value: 6.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMadgtVKREDLFYTTKIWITFLRPELV 96
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHIPIAMKPGEellpkdangkfifDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLEL 176
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 177 ILNKPRlkYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSswvssdspyLLEDPVLMTIAKKHNQTPGQV 256
Cdd:cd19071 141 LLAAAR--IKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 158138555 257 ALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19071 210 LLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
17-324 |
7.22e-124 |
|
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: 356.96 E-value: 7.22e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFasKEIPkSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELV 96
Cdd:cd19110 4 IPAVGLGTW--KASP-GEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLEL 176
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 177 ILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGShrdsswvSSDSPYLLEDPVLMTIAKKHNQTPGQV 256
Cdd:cd19110 161 LLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGG-------SCEGVDLIDDPVIQRIAKKHGKSPAQI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 257 ALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPFLEEY 324
Cdd:cd19110 234 LIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-306 |
3.34e-119 |
|
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: 345.16 E-value: 3.34e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 6 SRSVKLNDGNLMPVLGFGTFASKeipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTK 85
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGeELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIG 165
Cdd:cd19123 78 LWNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 166 VSNFNHKQLELILNKPRlkYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-HRDSSWVSSDSPYLLEDPVLMT 244
Cdd:cd19123 157 VSNFSVKKLEDLLATAR--IKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138555 245 IAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19123 235 IAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
6-305 |
5.88e-119 |
|
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: 344.78 E-value: 5.88e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 6 SRSVKLNDGNLMPVLGFGTFASKEipkSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTK 85
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKG---AEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIG 165
Cdd:cd19154 78 LWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 166 VSNFNHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-----HRDSSWVSSdSPYLLEDP 240
Cdd:cd19154 158 VSNFNNDQIQRILDNARV--KPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranFTKSTGVSP-APNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 241 VLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFR 305
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
13-306 |
2.74e-118 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 341.26 E-value: 2.74e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 13 DGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDkmADgtVKREDLFYTTKIWITFLR 92
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA--SG--VPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 93 PELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdangkfifdtVDIRDTWEALEKCKDAGLSKSIGVSNFNHK 172
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 173 QLELILNKPRlkYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAKKHNQT 252
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 253 PGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
7-300 |
3.08e-111 |
|
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: 324.30 E-value: 3.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 7 RSVKLNDGNLMPVLGFGTFASkeiPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKI 86
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQA---DPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 WITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEellPKDANGKFIfdTVDIRDTWEALEKCKDAGLSKSIGV 166
Cdd:cd19125 78 WCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 167 SNFNHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGShRDSSWVSSDspyLLEDPVLMTIA 246
Cdd:cd19125 153 SNFSVKKLEDLLAVARV--PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWVKKN---VLKDPIVTKVA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19125 227 EKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-305 |
8.12e-103 |
|
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: 303.68 E-value: 8.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFASkeiPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIW 87
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQS---SPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKpGEEL--LPKDANGKFIFD-TVDIRDTWEALEKCKDAGLSKSI 164
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSL-SKEDdsGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNHKQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS------HRDSSWVSSDSPYLLE 238
Cdd:cd19155 159 GLSNFNREQMARILKNARIK--PANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfSPGTGSPSGSSPDLLQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138555 239 DPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFR 305
Cdd:cd19155 237 DPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
13-300 |
4.52e-100 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 295.72 E-value: 4.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 13 DGNLMPVLGFGTFASKEIPKsKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVK-REDLFYTTKIWITFL 91
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 92 RPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANgkfIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNH 171
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 172 KQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdSSWVSSDspyLLEDPVLMTIAKKHNQ 251
Cdd:cd19124 157 KKLQELLSFATIP--PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKWGSNA---VMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158138555 252 TPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
14-306 |
5.80e-98 |
|
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: 290.55 E-value: 5.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGTFASkeiPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRP 93
Cdd:cd19111 1 GFPMPVIGLGTYQS---PPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 94 ELVRQCLERSLKKLGLDYVDLCIIHIPIAMKpgeellpKDANGKFIFDT-VDIRDTWEALEKCKDAGLSKSIGVSNFNHK 172
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPCGFV-------NKKDKGERELAsSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 173 QLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-HRDSSWVSSDSPYLLEDPVLMTIAKKHNQ 251
Cdd:cd19111 151 QINKILAYAKV--KPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 252 TPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19111 229 TPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
17-298 |
1.63e-95 |
|
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: 283.01 E-value: 1.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALrdkmADGTVKREDLFYTTKIWITFLRPELV 96
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdangkfifdTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLEL 176
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 177 ILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGsHRDsswvssdspyLLEDPVLMTIAKKHNQTPGQV 256
Cdd:cd19073 135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 158138555 257 ALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
6-304 |
1.95e-95 |
|
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: 284.39 E-value: 1.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 6 SRSVKLNDGNLMPVLGFGTFASKEIPKSKAAEAtkvAIDVGFRHIDAAYFYQNEEEVGQALRDKmadgTVKREDLFYTTK 85
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGIKDS----GVPREEIFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLRPelVRQCLERSLKKLGLDYVDLCIIHIPIAMKPG--EELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKS 163
Cdd:cd19117 76 LWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 164 IGVSNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGshrdsswvSSDSPyLLEDPVLM 243
Cdd:cd19117 154 IGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLG--------STNAP-LLKEPVII 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138555 244 TIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVfdFELTPEDMKTIDSLNRNF 304
Cdd:cd19117 225 KIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEY 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-302 |
4.21e-95 |
|
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: 283.58 E-value: 4.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 12 NDGNLMPVLGFGTFaskeIPK-SKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITF 90
Cdd:cd19129 1 NGSGAIPALGFGTL----IPDpSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 LRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDT-VDIRDTWEALEKCKDAGLSKSIGVSNF 169
Cdd:cd19129 77 HRPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 170 NHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGsHrdsswvsSDSPYLLEDPVLMTIAKKH 249
Cdd:cd19129 157 SLEKLREIFEAARI--KPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-H-------GMEPKLLEDPVITAIARRV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 158138555 250 NQTPGQVALRYQLQRGVVVLAKSFNEKRIKENfqvFDFELTPEDmkTIDSLNR 302
Cdd:cd19129 227 NKTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPED--AMREINE 274
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-301 |
4.33e-93 |
|
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: 277.15 E-value: 4.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 9 VKLNDGNLMPVLGFGTFaskEIPKSKAAE-ATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKmadgTVKREDLFYTTKIW 87
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS----GIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdangkfifdtvDIRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQL-ELILNKprlKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSswvssdspyLLEDPVLMTIA 246
Cdd:cd19133 133 NFYPDRLvDLILHN---EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLN 301
Cdd:cd19133 201 EKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-300 |
4.35e-93 |
|
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: 277.88 E-value: 4.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 7 RSVKLNDGNLMPVLGFGTFASKeipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGtVKREDLFYTTKI 86
Cdd:cd19121 2 TSFKLNTGASIPAVGLGTWQAK---AGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 WITF-LRPELvrqCLERSLKKLGLDYVDLCIIHIPIAMKP--GEELLPKDANGKFIFD-TVDIRDTWEALEKCKDAGLSK 162
Cdd:cd19121 78 WSTYhRRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 163 SIGVSNFNHKQLELILnkPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGShrdsswvsSDSPyLLEDPVL 242
Cdd:cd19121 155 AIGVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSP-LISDEPV 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 243 MTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFelTPEDMKTIDSL 300
Cdd:cd19121 224 VEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-300 |
8.55e-92 |
|
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: 274.12 E-value: 8.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFASKEipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELV 96
Cdd:cd19136 1 MPILGLGTFRLRG--EEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHIPIAMKpgeeLLPKDAngkfifDTVDIR-DTWEALEKCKDAGLSKSIGVSNFNHKQLE 175
Cdd:cd19136 79 RAACLGSLERLGTDYLDLYLIHWPGVQG----LKPSDP------RNAELRrESWRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 176 LILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSswvssdspyLLEDPVLMTIAKKHNQTPGQ 255
Cdd:cd19136 149 ELLKYCEVP--PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLR---------LLEDPTVLAIAKKYGRTPAQ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158138555 256 VALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19136 218 VLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-301 |
9.58e-92 |
|
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: 273.54 E-value: 9.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 9 VKLNDGNLMPVLGFGTFaskEIPKSKAAE-ATKVAIDVGFRHIDAAYFYQNEEEVGQALRDkmadGTVKREDLFYTTKIW 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF---QTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdanGKFIfdtvdirDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK-------------DKFI-------DTWKALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAK 247
Cdd:cd19126 134 NFQEHHLEELLAHADVV--PAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 248 KHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLN 301
Cdd:cd19126 201 KYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-301 |
1.64e-91 |
|
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: 273.09 E-value: 1.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDkmadGTVKREDLFYTTKIW 87
Cdd:cd19131 1 TITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKpgeellpkdanGKFIfdtvdirDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19131 74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQ-----------DKYV-------ETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAK 247
Cdd:cd19131 136 NFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAE 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 248 KHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLN 301
Cdd:cd19131 203 KHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
14-300 |
1.54e-90 |
|
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: 270.67 E-value: 1.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGTFASKEIPkskAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALrdkmADGTVKREDLFYTTKIWITFLRP 93
Cdd:cd19140 5 GVRIPALGLGTYPLTGEE---CTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 94 ELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdangkfifdTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQ 173
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWPNK-------------------DVPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 174 LELILnkpRLKYKP-TCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAKKHNQT 252
Cdd:cd19140 139 LREAV---ELSEAPlFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKT 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158138555 253 PGQVALRYQLQR-GVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19140 205 PAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
11-300 |
2.31e-90 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 271.21 E-value: 2.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 11 LNDGNLMPVLGFGTFASKeipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMAD-GTVKREDLFYTTKIWIT 89
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAE---PGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 90 FLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPK---DANGKFIF--DTVDIRDTWEALEKCKDAGLSKSI 164
Cdd:cd19118 78 SHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavPTNGGEVDldLSVSLVDTWKAMVELKKTGKVKSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvsSDSPYLLEDPVLMT 244
Cdd:cd19118 158 GVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 158138555 245 IAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQvfDFELTPEDMKTIDSL 300
Cdd:cd19118 230 IAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
14-298 |
2.47e-90 |
|
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: 270.64 E-value: 2.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGT-----FASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMadgtVKREDLFYTTKIwi 88
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 tFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGeellpkdangkfifdTVDIRDTWEALEKCKDAGLSKSIGVSN 168
Cdd:cd19120 75 -SPGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 169 FNHKQLELILNKPrlKYKPTCNQVECHPYLN--QSKLLEFCKSKDIVLVAYSALGShrdsSWVSSDSPYlleDPVLMTIA 246
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP----LTRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-306 |
1.71e-89 |
|
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: 268.49 E-value: 1.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFASKEipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDkmadGTVKREDLFYTTKIW 87
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIamkpgeellpkdaNGKFifdtvdiRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPV-------------KGKY-------KETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPrlKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAK 247
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158138555 248 KHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-310 |
2.14e-89 |
|
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: 269.74 E-value: 2.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIW 87
Cdd:cd19112 2 TITLNSGHKMPVIGLGVW---RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITflRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKF----IFDTVDIRDTWEALEKCKDAGLSKS 163
Cdd:cd19112 79 NS--DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDgvldIDVTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 164 IGVSNFnhkqlELILNKPRLKY---KPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALG-SHRDSSWVSSDSPylLED 239
Cdd:cd19112 157 IGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138555 240 PVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMA 310
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-306 |
3.96e-89 |
|
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: 267.46 E-value: 3.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 9 VKLNDGNLMPVLGFGTFASKEipKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKmadgTVKREDLFYTTKIWI 88
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 TFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdanGKFIfdtvdirDTWEALEKCKDAGLSKSIGVSN 168
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK-------------GKFK-------DTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 169 FNHKQLELILNKprLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAKK 248
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 249 HNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-306 |
6.45e-88 |
|
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: 265.85 E-value: 6.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIW 87
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMK--PGEELLPKD----ANGKFIFDTVDIRDTWEALEKCKDAGLS 161
Cdd:cd19113 79 NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPGfycgDGDNFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 162 KSIGVSNFNHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHrdsSWV------SSDSPY 235
Cdd:cd19113 159 KSIGVSNFPGALILDLLRGATI--KPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQ---SFVelnqgrALNTPT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138555 236 LLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19113 234 LFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-308 |
9.90e-88 |
|
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: 265.44 E-value: 9.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 6 SRSVKLNDGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTK 85
Cdd:cd19115 2 SPTVKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMK---PGEELLP--KDANGKFIFDTVDIRDTWEALEKCKDAGL 160
Cdd:cd19115 79 LWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 161 SKSIGVSNFNHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALG-------SHRDsswvSSDS 233
Cdd:cd19115 159 ARSIGVSNFSAQLLMDLLRYARI--RPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsflelDLPG----AKDT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 234 PYLLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQ 308
Cdd:cd19115 233 PPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNN 307
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
18-300 |
1.01e-85 |
|
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: 259.38 E-value: 1.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELVR 97
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 98 QCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELI 177
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 178 LNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSAL-GSHRDSSWVssdspyLLEDPVLMTIAKKHNQTPGQV 256
Cdd:cd19128 159 LNYCKI--KPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLgGSYGDGNLT------FLNDSELKALATKYNTTPPQV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 158138555 257 ALRYQLQR---GVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19128 231 IIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-302 |
3.14e-83 |
|
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: 253.57 E-value: 3.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 6 SRSVKLNDGNLMPVLGFGTfASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTK 85
Cdd:cd19119 1 EISFKLNTGASIPALGLGT-ASPHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLRPelVRQCLERSLKKLGLDYVDLCIIHIPIAMK-----PGEELLPKDANGKFIF-DTVDIRDTWEALEKCKDAG 159
Cdd:cd19119 80 VWPTFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYaASGDHITTYKQLEKIYLDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 160 LSKSIGVSNFNHKQLELILNKprLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSswvssdspyLLED 239
Cdd:cd19119 158 RAKAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 240 PVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVfdFELTPEDMKTIDSLNR 302
Cdd:cd19119 227 PLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-302 |
1.68e-81 |
|
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: 247.57 E-value: 1.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 11 LNDGNLMPVLGFGTFASKEipkSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDkmadGTVKREDLFYTTKIWITF 90
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKG---DEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeelLPKdaNGKFIfdtvdirDTWEALEKCKDAGLSKSIGVSNFN 170
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWP---------NPS--RDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 171 HKQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGshRDSSwvssdspyLLEDPVLMTIAKKHN 250
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG--RGSG--------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158138555 251 QTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNR 302
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
14-308 |
1.02e-79 |
|
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: 244.77 E-value: 1.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRP 93
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 94 ELVRQCLERSLKKLGLDYVDLCIIHIPIAMK---PGEELLPKDANG---KFIFDTVDIRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKelkKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPRLkyKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPY--LLEDPVLMTI 245
Cdd:cd19114 158 NFNVQLILDLLTYAKI--KPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 246 AKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQ 308
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFND 298
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
9-301 |
1.68e-79 |
|
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: 243.08 E-value: 1.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 9 VKLNDGNLMPVLGFGTFASkeiPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKmadgTVKREDLFYTTKIWI 88
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQT---PPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 TFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKpgeellpkdangkfiFD-TVDirdTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPND---------------FDrTIQ---AYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNkpRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGS-HRDSSWVSSDSPYLLEDPVLMTIA 246
Cdd:cd19127 136 NFTPEHLERLID--ATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvMRYGASGPTGPGDVLQDPTITGLA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLN 301
Cdd:cd19127 214 EKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-300 |
1.16e-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: 235.68 E-value: 1.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 7 RSVKLNDGNLMPVLGFGTFASKeipkSKAAEATKVAI-DVGFRHIDAAYFYQNEEEVGQALRdkmADGtVKREDLFYTTK 85
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHSG----GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIK---ESG-VPREDLFLTTK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEEllPKDAngkfifdtvdIRDTWEALEKCKDAGLSKSIG 165
Cdd:cd19135 75 LWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN--VKET----------RAETWRALEELYDEGLCRAIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 166 VSNFNHKQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTI 245
Cdd:cd19135 143 VSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTEL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 246 AKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19135 210 AKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-300 |
6.80e-75 |
|
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: 232.13 E-value: 6.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 10 KLNDGNLMPVLGFGTFASkEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADG-TVKREDLFYTTKIWI 88
Cdd:cd19122 2 TLNNGVKIPAVGFGTFAN-EGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 TFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPK-DANGKFIFD---TVDIRDTWEALEKCKDAGLSKSI 164
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILkdlTENPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNHKQLELILNKPrlKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDsswVSSDSPYLLEDPVLMT 244
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 158138555 245 IAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVfdFELTPEDMKTIDSL 300
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQV 289
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-306 |
9.28e-72 |
|
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: 223.19 E-value: 9.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRdkmADGtVKREDLFYTTKIW 87
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVG---ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdANGKFIfdtvdirDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNkprLKY-KPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIA 246
Cdd:cd19134 137 NFTAEHLENLID---LTFfTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIA 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:cd19134 203 AAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
20-301 |
2.52e-71 |
|
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: 222.96 E-value: 2.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 20 LGFGTFA----SKEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKMadgtVKREDLFYTTKI------ 86
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYP----VKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 WITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdangkfifdTVDIRDTWEALEKCKDAGLSKSIGV 166
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 167 SNFNHKQLELILNKPrlKYKPTCNQVECHPY--LNQSKLLEFCKSKDIVLVAYSALGS----------------HRDSSW 228
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 229 VSSDSPYLLEDPVLMTIAKKHNQTPGQVALRY--QLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLN 301
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
17-300 |
3.71e-71 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 221.07 E-value: 3.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFASKEipkSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQAlrdkMADGTVKREDLFYTTKIWITFLRPELV 96
Cdd:cd19139 1 IPAFGLGTFRLKD---DVVIDSVRTALELGYRHIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHIPIamkpgeellpkdangkfIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLEL 176
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIHWPS-----------------PNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 177 ILNKPRlKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAKKHNQTPGQV 256
Cdd:cd19139 137 AIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQI 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 158138555 257 ALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19139 205 ALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-301 |
5.90e-70 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 218.24 E-value: 5.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 8 SVKLNDGNLMPVLGFGTFaskEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALrdkmADGTVKREDLFYTTKIW 87
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeelLPkdANGKFIfdtvdirDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWP---------TP--AAGNYV-------HTWEAMIELRAAGRTRSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPRLKykPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAK 247
Cdd:cd19130 136 NFLPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 248 KHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLN 301
Cdd:cd19130 203 AHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
17-298 |
3.55e-64 |
|
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: 203.61 E-value: 3.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGT-----FASKEIPKSKAA-EATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDkmadgtVKREDLFYTTKIW 87
Cdd:cd19072 4 VPVLGLGTwgiggGMSKDYSDDKKAiEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkdaNgkfifDTVDIRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP--------------N-----PSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPRlKYKPTCNQVECHpYLNQ---SKLLEFCKSKDIVLVAYSALGSHRdsswVSSDSPYlledPVLMT 244
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDReeeSGLLPYCQKNGIAIIAYSPLEKGK----LSNAKGS----PLLDE 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 245 IAKKHNQTPGQVALRYQLQR-GVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-305 |
7.43e-63 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 200.25 E-value: 7.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFASKEIPkskAAEATKVAIDVGFRHIDAAYFYQNEEEVGQAlrdkMADGTVKREDLFYTTKIWITFLRPELV 96
Cdd:PRK11172 3 IPAFGLGTFRLKDQV---VIDSVKTALELGYRAIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHIPiamKPGeellpkdangkfifDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLEL 176
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWP---SPN--------------DEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 177 ---ILNKPRLkykpTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLEDPVLMTIAKKHNQTP 253
Cdd:PRK11172 139 aiaAVGAENI----ATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158138555 254 GQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFR 305
Cdd:PRK11172 204 AQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
9-305 |
1.71e-62 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 199.53 E-value: 1.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 9 VKLNDGNLMPVLGFGTF-ASKEipksKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDkmadGTVKREDLFYTTKIW 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWqASNE----EVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITflRPELVRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellpkdANGKFIfdtvdirDTWEALEKCKDAGLSKSIGVS 167
Cdd:PRK11565 79 ND--DHKRPREALEESLKKLQLDYVDLYLMHWPVP-----------AIDHYV-------EAWKGMIELQKEGLIKSIGVC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKPRLKykPTCNQVECHPYLNQSKLLefckskdivlvAYSALGSHRDSSWvssdSPY------LLEDPV 241
Cdd:PRK11565 139 NFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLH-----------AWNATHKIQTESW----SPLaqggkgVFDQKV 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138555 242 LMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFR 305
Cdd:PRK11565 202 IRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-298 |
1.15e-50 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 168.97 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 7 RSVKLNDGNLMPVLGFGTFASKEIPKSKAAE--ATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgtvkREDLF 81
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEieALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 82 YTTKIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkdangkfifDTVDIRDTWEALEKCKDAGLS 161
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR--------------------GGVPLAETVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 162 KSIGVSNFNHKQLELILNKPRLKyKPTCNQVECHpyLNQS----KLLEFCKSKDIVLVAYSALGSHRDSSWVssdspyLL 237
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLRRG------LL 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138555 238 EDPVLMTIAKKHNQTPGQVALRYQL-QRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19138 205 ENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
14-298 |
6.10e-47 |
|
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: 159.27 E-value: 6.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 14 GNLMPVLGFGTF--ASKEIPK----SKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDkmadgtVKREDLFYTT 84
Cdd:cd19137 1 GEKIPALGLGTWgiGGFLTPDysrdEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 85 KIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEEllpkdangkfifdtvdirdTWEALEKCKDAGLSKSI 164
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNHKQLELILNKPRLKYkpTCNQVECHPY---LNQSKLLEFCKSKDIVLVAYSALgshrdsswvssDSPYLLEDPV 241
Cdd:cd19137 136 GVSNFNRRLLEEAISKSQTPI--VCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 242 LMTIAKKHNQTPGQVALRYQLQR-GVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
18-300 |
2.57e-46 |
|
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: 159.19 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA-SKEIPKSKAAEATKV---AIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvKREDLFYTTKIWITF 90
Cdd:COG0667 14 SRLGLGTMTfGGPWGGVDEAEAIAIldaALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATKVGRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 --------LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkDANgkfifdtVDIRDTWEALEKCKDAGLSK 162
Cdd:COG0667 88 gpgpngrgLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 163 SIGVSNFNHKQLELILNKPRLKYKPTCNQVEchpY--LNQS---KLLEFCKSKDIVLVAYSALGS------HRDSSWVSS 231
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLAGglltgkYRRGATFPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 232 DS--------PYLLED-----PVLMTIAKKHNQTPGQVALRYQLQRGVVVL----AKSfnEKRIKENFQVFDFELTPEDM 294
Cdd:COG0667 226 GDraatnfvqGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDL 303
|
....*.
gi 158138555 295 KTIDSL 300
Cdd:COG0667 304 AALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-298 |
3.75e-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: 144.98 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA-----SKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgtvkREDLFYTTK---I 86
Cdd:cd19084 5 SRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATKcglR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 WITF------LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkDANgkfifdtVDIRDTWEALEKCKDAGL 160
Cdd:cd19084 78 WDGGkgvtkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLKKEGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 161 SKSIGVSNFNHKQLELIlnkprLKY-KPTCNQVechPY--LNQ---SKLLEFCKSKDIVLVAYSALGS-------HRDSS 227
Cdd:cd19084 139 IRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAQglltgkyKKEPT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 228 WVSSD----SPYLLED---------PVLMTIAKKHNQTPGQVALRYQLQR-GV-VVLAKSFNEKRIKENFQVFDFELTPE 292
Cdd:cd19084 211 FPPDDrrsrFPFFRGEnfeknleivDKLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWELTEE 290
|
....*.
gi 158138555 293 DMKTID 298
Cdd:cd19084 291 ELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-304 |
1.01e-39 |
|
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: 141.18 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGT--FASKEIPKS---KAAEAT-KVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgtvkREDLFYTTKIWI 88
Cdd:cd19085 2 SRLGLGCwqFGGGYWWGDqddEESIATiHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 TFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMkpgeellpkdangkfifdtVDIRDTWEALEKCKDAGLSKSIGVSN 168
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-------------------VPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 169 FNHKQLELILNKPRLkykpTCNQVechPY--LNQSK---LLEFCKSKDIVLVAYSALGS-------HRDSSWVSSDS--- 233
Cdd:cd19085 136 FGPAQLEEALDAGRI----DSNQL---PYnlLWRAIeyeILPFCREHGIGVLAYSPLAQglltgkfSSAEDFPPGDArtr 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 234 -PYLLEDPV----------LMTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19085 209 lFRHFEPGAeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
....
gi 158138555 301 NRNF 304
Cdd:cd19085 289 SDPL 292
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
18-298 |
8.05e-39 |
|
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: 138.90 E-value: 8.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA--------SKEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKMAdgtvkREDLFYTTKI 86
Cdd:cd19093 3 SPLGLGTWQwgdrlwwgYGEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 WITFLR--PELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLpkdangkfifdtvdirdtWEALEKCKDAGLSKSI 164
Cdd:cd19093 78 APLPWRltRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNHKQLELILNK-PRLKYKPTCNQVE---CHPYLNQSKLLEFCKSKDIVLVAYSAL------GSHRDSSWVSSD-- 232
Cdd:cd19093 140 GVSNYSADQLRRAHKAlKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLaqglltGKYSPENPPPGGrr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138555 233 ---SPYLLE--DPVLMT---IAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19093 220 rlfGRKNLEkvQPLLDAleeIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
18-283 |
1.24e-32 |
|
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: 120.70 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA-SKEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRdkmadGTVKREDLFYTTKIWITF--- 90
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLK-----GRGNRDDVVIATKGGHPPggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 -----LRPELVRQCLERSLKKLGLDYVDLCIIHIPIamkpgeellpkdangkfifDTVDIRDTWEALEKCKDAGLSKSIG 165
Cdd:cd06660 76 psrsrLSPEHIRRDLEESLRRLGTDYIDLYYLHRDD-------------------PSTPVEETLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 166 VSNFNHKQLELILN--KPRLKYKPTCNQVE---CHPYLNQSKLLEFCKSKDIVLVAYSALGshrdsswvssdspylledp 240
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158138555 241 vlmtiakkhnQTPGQVALRYQLQR--GVVVLAKSFNEKRIKENFQ 283
Cdd:cd06660 198 ----------RGPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
19-293 |
1.88e-28 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 111.40 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAA--Y-FYQNEEEVGQALRDKmadgTVKREDLFYTTKIWITFLRPEL 95
Cdd:COG4989 17 VLGCMRLGEWDLSPAEAAALIEAALELGITTFDHAdiYgGYTCEALFGEALKLS----PSLREKIELQTKCGIRLPSEAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 96 -------------VRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkdangkfifDT-VDIRDTWEALEKCKDAGLS 161
Cdd:COG4989 93 dnrvkhydtskehIIASVEGSLRRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELKASGKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 162 KSIGVSNFNHKQLELiLNKpRLKYKPTCNQVECHPyLNQSKL----LEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLL 237
Cdd:COG4989 153 RHFGVSNFTPSQFEL-LQS-ALDQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLR 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158138555 238 EdpVLMTIAKKHNQTPGQVALRYqLQR---GVVVLAKSFNEKRIKENFQVFDFELTPED 293
Cdd:COG4989 230 A--ALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
19-293 |
3.36e-28 |
|
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: 110.34 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgTVKREDLFYTTKIWITF----- 90
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKCGIRLgddpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 --------LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkdangkfifDT-VDIRDTWEALEKCKDAGLS 161
Cdd:cd19092 86 pgrikhydTSKEHILASVEGSLKRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 162 KSIGVSNFNHKQLELiLNKpRLKYKPTCNQVEC---HPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLE 238
Cdd:cd19092 146 RYFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 239 dpVLMTIAKKHNQTPGQVALRYQLQ---RGVVVLAkSFNEKRIKENFQVFDFELTPED 293
Cdd:cd19092 224 --ALEELAEEYGVTIEAIALAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-300 |
8.44e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 106.99 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 42 AIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvkREDLFYTTK---IW------ITFLRPELVRQCLERSLKKLGL 109
Cdd:cd19102 35 ALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKcglLWdeegriRRSLKPASIRAECEASLRRLGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 110 DYVDLCIIHIPiamkpgeelLPkdangkfifdTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELIlnkprLKYKP-T 188
Cdd:cd19102 108 DVIDLYQIHWP---------DP----------DEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRC-----QAIHPiA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 189 CNQVechPY--LN---QSKLLEFCKSKDIVLVAYSALGS-----HRDSSWVSSD--------SPYLLED---------PV 241
Cdd:cd19102 164 SLQP---PYslLRrgiEAEILPFCAEHGIGVIVYSPMQSglltgKMTPERVASLpaddwrrrSPFFQEPnlarnlalvDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 242 LMTIAKKHNQTPGQVALRYQLQR----GVVVLAKsfNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19102 241 LRPIAERHGRTVAQLAIAWVLRRpevtSAIVGAR--RPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
40-300 |
2.46e-26 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 105.96 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 40 KVAIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvKREDLFYTTKIWITFL--------RPELVRQCLERSLKKLG 108
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFGgdgsvlnnSPEFLRSAVEKSLKRLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 109 LDYVDLCIIHIPiamkpgEELLPKDangkfifdtvdirDTWEALEKCKDAGLSKSIGVSNFNHKQlelilnkprLKYKPT 188
Cdd:cd19083 114 TDYIDLYYIHFP------DGETPKA-------------EAVGALQELKDEGKIRAIGVSNFSLEQ---------LKEANK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 189 CNQVEC--HPY--LNQ---SKLLEFCKSKDIVLV-----AYSALGSHRDSSWVSSDSPYLLEDPV--------------- 241
Cdd:cd19083 166 DGYVDVlqGEYnlLQReaeEDILPYCVENNISFIpyfplASGLLAGKYTKDTKFPDNDLRNDKPLfkgerfsenldkvdk 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138555 242 LMTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19083 246 LKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
12-297 |
5.46e-26 |
|
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: 105.22 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 12 NDGNLMPVLGFGT--FASKEIPKSKAAEATKV---AIDVGFRHIDAAYFYQ-NEEEVGQALrdKMADGtvKREDLFYTTK 85
Cdd:cd19144 8 RNGPSVPALGFGAmgLSAFYGPPKPDEERFAVldaAFELGCTFWDTADIYGdSEELIGRWF--KQNPG--KREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 IWITFLR----------PELVRQCLERSLKKLGLDYVDLCIIHipiamkpgeELLPKdangkfifdtVDIRDTWEALEKC 155
Cdd:cd19144 84 FGIEKNVetgeysvdgsPEYVKKACETSLKRLGVDYIDLYYQH---------RVDGK----------TPIEKTVAAMAEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 156 KDAGLSKSIGVSnfnhkqlELILNKPRLKYK--P-TCNQVECHPYL-----NQSKLLEFCKSKDIVLVAYSALGSHRDSS 227
Cdd:cd19144 145 VQEGKIKHIGLS-------ECSAETLRRAHAvhPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGFLTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 228 WVSSDSPYLLED-------------PVLMT-------IAKKHNQTPGQVALRYQLQRG--VVVLAKSFNEKRIKENFQVF 285
Cdd:cd19144 218 AIRSPDDFEEGDfrrmaprfqaenfPKNLElvdkikaIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|..
gi 158138555 286 DFELTPEDMKTI 297
Cdd:cd19144 298 KVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-299 |
9.18e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 104.21 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 27 SKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEE-VGQALRDKMADGTVKREDLFYTtKiWITFLR-----PELVRQCL 100
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHT-K-WVPDPGeltmtRAYVEAAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 101 ERSLKKLGLDYVDLCIIHIpiamkpgeellpkdangkfiFDTVDIR--DTWEALEKCKDAGLSKSIGVSNFNHKQLELIL 178
Cdd:cd19101 95 DRSLKRLGVDRLDLVQFHW--------------------WDYSDPGylDAAKHLAELQEEGKIRHLGLTNFDTERLREIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 179 NKPrlkYKPTCNQVEcHPYLNQ---SKLLEFCKSKDIVLVAYSALGS---------HRDSSWVSSDSP----Y------- 235
Cdd:cd19101 155 DAG---VPIVSNQVQ-YSLLDRrpeNGMAALCEDHGIKLLAYGTLAGgllsekylgVPEPTGPALETRslqkYklmidew 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138555 236 --------LLEdpVLMTIAKKHNQTPGQVALRYQLQR----GVVVLAKsfNEKRIKENFQVFDFELTPEDMKTIDS 299
Cdd:cd19101 231 ggwdlfqeLLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-290 |
6.57e-25 |
|
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: 100.75 E-value: 6.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGT--FASKEI-----PKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvkREDLFYTTKI- 86
Cdd:cd19088 2 SRLGYGAmrLTGPGIwgppaDREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPY-------PDDVVIATKGg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 --------WITFLRPELVRQCLERSLKKLGLDYVDLCIIHIpiamkpgeellpkdangkfIFDTVDIRDTWEALEKCKDA 158
Cdd:cd19088 75 lvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHR-------------------IDPKVPFEEQLGALAELQDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 159 GLSKSIGVSNFNHKQLELILNKPRLkykpTCNQVECHPYLNQS-KLLEFCKSKDIVLVAYSALGSHRDsswvssdspyLL 237
Cdd:cd19088 136 GLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGGGDL----------AQ 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 238 EDPVLMTIAKKHNQTPGQVALRYQLQRG--VVVLAKSFNEKRIKENFQVFDFELT 290
Cdd:cd19088 202 PGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-300 |
1.09e-24 |
|
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: 101.54 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 12 NDGNLMPVLGFG--TFASKEIPKSK-----AAEAT---KVAIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvkRE 78
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGAwggvdQEEADrlvDIALDAGINFFDTADVYsegESEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 79 DLFYTTKiwiTFLRPE------------LVRQClERSLKKLGLDYVDLCIIHIPIAMKPGEELLpkdangkfifdtvdir 146
Cdd:cd19091 81 DVLIATK---VRGRMGegpndvglsrhhIIRAV-EASLKRLGTDYIDLYQLHGFDALTPLEETL---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 147 dtwEALEKCKDAGLSKSIGVSNFNHKQLELILN-KPRLKY-KPTCNQVechpYLN------QSKLLEFCKSKDIVLVAYS 218
Cdd:cd19091 141 ---RALDDLVRQGKVRYIGVSNFSAWQIMKALGiSERRGLaRFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 219 ALGSHRDSSWVSSDSP----------------------YLLEDpVLMTIAKKHNQTPGQVALRYQLQR----GVVVLAKs 272
Cdd:cd19091 214 PLAGGLLSGKYRRGQPapegsrlrrtgfdfppvdrergYDVVD-ALREIAKETGATPAQVALAWLLSRptvsSVIIGAR- 291
|
330 340
....*....|....*....|....*...
gi 158138555 273 fNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19091 292 -NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
17-305 |
3.55e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 101.05 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFAskeIPKSKAAEATKV---AIDVGFRHIDAAYFYQNEEE-VGQALRDKmadgtvkREDLFYTTKIWITFLR 92
Cdd:COG1453 13 VSVLGFGGMR---LPRKDEEEAEALirrAIDNGINYIDTARGYGDSEEfLGKALKGP-------RDKVILATKLPPWVRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 93 PELVRQCLERSLKKLGLDYVDLCIIHipiAMKPGEELlpkdangKFIFDTVDIrdtWEALEKCKDAGLSKSIGVSnfNHK 172
Cdd:COG1453 83 PEDMRKDLEESLKRLQTDYIDLYLIH---GLNTEEDL-------EKVLKPGGA---LEALEKAKAEGKIRHIGFS--THG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 173 QLELILnkprlkykptcNQVECHP---------YLNQS-----KLLEFCKSKDIVLVAYSALGSHRdsswvssdspyLLE 238
Cdd:COG1453 148 SLEVIK-----------EAIDTGDfdfvqlqynYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LAN 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138555 239 DP-VLMTIAKKhNQTPGQVALRYQLQR-GVVVL---AKSFNEkrIKENFQVFD-FE-LTPEDMKTIDSLNRNFR 305
Cdd:COG1453 206 PPeKLVELLCP-PLSPAEWALRFLLSHpEVTTVlsgMSTPEQ--LDENLKTADnLEpLTEEELAILERLAEELG 276
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
42-297 |
1.55e-23 |
|
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: 98.06 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 42 AIDVGFRHIDAAYFYQ---NEEEVGQALRDKmadgtvkREDLFYTTKIWITFL----------RPELVRQCLERSLKKLG 108
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKFGIVRDpgsgfrgvdgRPEYVRAACEASLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 109 LDYVDLCIIHIPiamkpgeellpkDANgkfifdtVDIRDTWEALEKCKDAGLSKSIGVSNFN-------HK-------QL 174
Cdd:cd19076 114 TDVIDLYYQHRV------------DPN-------VPIEETVGAMAELVEEGKVRYIGLSEASadtirraHAvhpitavQS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 175 ElilnkprlkYKPTCNQVECHpylnqskLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLED-----P--------- 240
Cdd:cd19076 175 E---------YSLWTRDIEDE-------VLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDfrrnnPrfqgenfdk 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 241 ------VLMTIAKKHNQTPGQVALRYQLQRG--VVVLAKSFNEKRIKENFQVFDFELTPEDMKTI 297
Cdd:cd19076 239 nlklveKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-270 |
1.32e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 94.09 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN-EEEVGQALRDKmadgtvkREDLFYTTKIWITflRPELV 96
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGAR--DYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 97 RQCLERSLKKLGLDYVDLCIIHipiAMKPGEEllpkdangkfiFDTVDIRD-TWEALEKCKDAGLSKSIGVSNFNHKQLE 175
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH---AVDTEED-----------LDQVFGPGgALEALLEAKEEGKIRFIGISGHSPEVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 176 LILNKPrlkykptcnqvechpylnqskllEFckskDIVLVAYSALGSHRDSswvssdspyllEDPVLMTIAKKHN----- 250
Cdd:cd19100 149 RALETG-----------------------EF----DVVLFPINPAGDHIDS-----------FREELLPLAREKGvgvia 190
|
250 260 270
....*....|....*....|....*....|....
gi 158138555 251 --------------QTPGQvALRYQLQRGVVVLA 270
Cdd:cd19100 191 mkvlaggrllsgdpLDPEQ-ALRYALSLPPVDVV 223
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
18-292 |
1.87e-22 |
|
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: 94.54 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTF----ASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEE-VGQALRdkmadgTVKREDLFYTTKI-----W 87
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDSEErLGLALA------ELPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPkdaNGKFifdtvdirdtwEALEKCKDAGLSKSIGVS 167
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP---GGAL-----------EALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLELILNKprlkykptcNQVEC----HPY--LNQS---KLLEFCKSKDIVLVAYSALG----SHRDSSWVSSDSP 234
Cdd:cd19090 141 GGPPDLLRRAIET---------GDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYR 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138555 235 YLLEDPV-----LMTIAKKHNQTPGQVALRYQLQ----RGVVVLAKsfNEKRIKENFQVFDFELTPE 292
Cdd:cd19090 212 WLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPLPEE 276
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
18-286 |
6.73e-22 |
|
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: 92.62 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGT-----FASKEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDkmadgtVKREDLFYTTKI-WI 88
Cdd:cd19096 1 SVLGFGTmrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 TFLRPELVRQCLERSLKKLGLDYVDLCIIHipiAMkpgeellpkdaNGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSn 168
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH---GL-----------NSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 169 FnHKQLELILnkpRLkykptcnqVECHP---------YLNQ-----SKLLEFCKSKDIVLVAYSALGSHRdsswvssdsp 234
Cdd:cd19096 140 F-HDSPELLK---EI--------LDSYDfdfvqlqynYLDQenqagRPGIEYAAKKGMGVIIMEPLKGGG---------- 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 235 yLLEDP-VLMTIAKKHNQTPGQVALRYQL-QRGVVVLAKSFNEKR-IKENFQVFD 286
Cdd:cd19096 198 -LANNPpEALAILCGAPLSPAEWALRFLLsHPEVTTVLSGMSTPEqLDENIAAAD 251
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-167 |
3.25e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 92.00 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 20 LGFGTF--ASKEIPKSKAAEATKVAIDVGFRHIDAA--YFYQ-NEEEVGQALRDKMADGTVKREDLFYTTKI-------- 86
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAinYRGGrSERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 -------WITF------------------LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgEELLPKDANGKFiFD 141
Cdd:cd19099 86 eplrplkYLEEklgrglidvadsaglrhcISPAYLEDQIERSLKRLGLDTIDLYLLHNP------EEQLLELGEEEF-YD 158
|
170 180
....*....|....*....|....*.
gi 158138555 142 TvdIRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19099 159 R--LEEAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
18-299 |
3.65e-21 |
|
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: 91.95 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA------SKEIPKSKAAEATKVAIDVGFRHIDAA--YFYQNEEE-VGQALRDKmadgtvkREDLFYTTKIWI 88
Cdd:cd19149 12 SVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTApaYGFGHSEEiVGKAIKGR-------RDKVVLATKCGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 89 TF-------------------LRPELVRQCLERSLKKLGLDYVDLCIIHIPIamkpgeellpkdangkfifDTVDIRDTW 149
Cdd:cd19149 85 RWdreggsfffvrdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQD-------------------VETPIEETM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 150 EALEKCKDAGLSKSIGVSNFNHKQLElilnkprlKYKpTCNQVEchpyLNQSK-----------LLEFCKSKDIVLVAYS 218
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSVEQIK--------EYV-KAGQLD----IIQEKysmldrgiekeLLPYCKKNNIAFQAYS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 219 AL-----------------GSHRdsSWVSSDSPYLLEDPVLMT-----IAKKHNQTPGQVALRYQLQRG--VVVLAKSFN 274
Cdd:cd19149 213 PLeqglltgkitpdrefdaGDAR--SGIPWFSPENREKVLALLekwkpLCEKYGCTLAQLVIAWTLAQPgiTSALCGARK 290
|
330 340
....*....|....*....|....*
gi 158138555 275 EKRIKENFQVFDFELTPEDMKTIDS 299
Cdd:cd19149 291 PEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
40-298 |
6.81e-20 |
|
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: 88.02 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 40 KVAIDVGFRHIDAAYFYQN---EEEVGQALRDKMadgtvKREDLFYTTKIWIT---------FLRPELVRQClERSLKKL 107
Cdd:cd19079 42 KRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFPmgdgpngrgLSRKHIMAEV-DASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 108 GLDYVDLCIIHIPiamkpgeellpkDANgkfifdtVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRLK--Y 185
Cdd:cd19079 116 GTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNgwT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 186 KPTCNQvechPYLN------QSKLLEFCKSKDIVLVAYSAL------GSHRDSS---WVSSDSPYLLED-------PVL- 242
Cdd:cd19079 177 KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLargrlaRPWGDTTerrRSTTDTAKLKYDyfteadkEIVd 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 243 --MTIAKKHNQTPGQVALRYQLQRGVVV-----LAKsfnEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19079 253 rvEEVAKERGVSMAQVALAWLLSKPGVTapivgATK---LEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-284 |
1.36e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 86.10 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGTFASKeipkSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDkmadgtVKREDLFYTTKIWIT--FL 91
Cdd:cd19105 13 VSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKASPRldKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 92 RPELVRQCLERSLKKLGLDYVDLCIIHipiAMKPGEELLpkdANGKFIfdtvdirdtwEALEKCKDAGLSKSIGVS--NF 169
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLH---GVDTPEERL---LNEELL----------EALEKLKKEGKVRFIGFSthDN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 170 NHKQLELILNKPR-----LKYkptcNqvechpYLNQS----KLLEFCKSKDIVLVAYSALGSHRDSSWvsSDSPYLLEDP 240
Cdd:cd19105 147 MAEVLQAAIESGWfdvimVAY----N------FLNQPaeleEALAAAAEKGIGVVAMKTLAGGYLQPA--LLSVLKAKGF 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 158138555 241 vlmtiakkhnqTPGQVALRYQLQR----GVVVLAKSFneKRIKENFQV 284
Cdd:cd19105 215 -----------SLPQAALKWVLSNprvdTVVPGMRNF--AELEENLAA 249
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
41-300 |
2.53e-19 |
|
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: 86.85 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 41 VAIDVGFRHIDAAYFY----------QNEEEVGQALRDKmadgtVKREDLFYTTKI-----WITFLR-------PELVRQ 98
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKK-----GNRDKVVLATKVagpgeGITWPRgggtrldRENIRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 99 CLERSLKKLGLDYVDLCIIHIP---IAMKPGEELLPKDANGkfifDTVDIRDTWEALEKCKDAGLSKSIGVSN------- 168
Cdd:cd19094 101 AVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE----DSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvm 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 169 -FNH--KQLELilnkPRlkykPTCNQvecHPY--LNQSK---LLEFCKSKDIVLVAYSAL------GSHRDSSWVSSDS- 233
Cdd:cd19094 177 kFLElaEQLGL----PR----IVSIQ---NPYslLNRNFeegLAEACHRENVGLLAYSPLaggvltGKYLDGAARPEGGr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 234 --------PYLLEDPVLMT------IAKKHNQTPGQVALRYQLQR----GVVVLAKSFNEkrIKENFQVFDFELTPEDMK 295
Cdd:cd19094 246 lnlfpgymARYRSPQALEAvaeyvkLARKHGLSPAQLALAWVRSRpfvtSTIIGATTLEQ--LKENIDAFDVPLSDELLA 323
|
....*
gi 158138555 296 TIDSL 300
Cdd:cd19094 324 EIDAV 328
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
18-281 |
1.01e-18 |
|
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: 83.82 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGT---FASKEIP-KSKAAEATKVAIDVGFRHIDAAYFYQNEEEV-GQALRdkmadgTVKREDLFYTTKIWITFLR 92
Cdd:cd19095 1 SVLGLGTsgiGRVWGVPsEAEAARLLNTALDLGINLIDTAPAYGRSEERlGRALA------GLRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 93 --------PELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLpkdangkfifdtvdirdtwEALEKCKDAGLSKSI 164
Cdd:cd19095 75 grdrkdfsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVL-------------------ETLEDLKAAGKVRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNhKQLELILNKPRLkykpTCNQVechPY--LNQS--KLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDP 240
Cdd:cd19095 136 GVSGDG-EELEAAIASGVF----DVVQL---PYnvLDREeeELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYAR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 158138555 241 VLMTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKRIKEN 281
Cdd:cd19095 208 RPEFAAEIGGATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
43-298 |
3.25e-18 |
|
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: 83.42 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 43 IDVGFRHIDAAYFY----------QNEEEVGQALRDKmadgtVKREDLFYTTKI--WITFLRPEL----VRQCLERSLKK 106
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSR-----GKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 107 LGLDYVDLCIIHIPiamkpgeellpkDangkfifDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPR---- 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------------D-------PATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhgl 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 183 LKY---KPTCNQVECHPYlnQSKLLEFCKSKDIVLVAYSALGS-------HRD-----SSWVSSDSPYLLEDP------V 241
Cdd:cd19081 172 PRYvslQPEYNLVDRESF--EGELLPLCREEGIGVIPYSPLAGgfltgkyRSEadlpgSTRRGEAAKRYLNERglrildA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158138555 242 LMTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKRIKENFQVFDFELTPEDMKTID 298
Cdd:cd19081 250 LDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-167 |
3.68e-18 |
|
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: 82.14 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFA-----SKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgtvkREDLFYTTKI---- 86
Cdd:cd19086 5 EIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 -----WITFLRPELVRQCLERSLKKLGLDYVDLCIIHIpiamkPGEELLPKDangkfifdtvdirDTWEALEKCKDAGLS 161
Cdd:cd19086 78 dggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHN-----PPDEVLDND-------------ELFEALEKLKQEGKI 139
|
....*.
gi 158138555 162 KSIGVS 167
Cdd:cd19086 140 RAYGVS 145
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
34-300 |
5.67e-18 |
|
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: 82.74 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 34 KAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKMadgtvKREDLFYTTKI---WI---TFLR---PELVRQCLE 101
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-----KRDRVVIATKVgleWDeggEVVRnssPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 102 RSLKKLGLDYVDLCIIHIPiamkpgeellpkDangkfifDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKP 181
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWP------------D-------PLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 182 RLKykptcnqvECHPYLN------QSKLLEFCKSKDIVLVAYSAL------GS-HRDSSWVSSD-------------SPY 235
Cdd:cd19148 162 PLH--------TVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrgllsGKmTKDTKFEGDDlrrtdpkfqeprfSQY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 236 LLEDPVLMTIAKKHNQTP-GQVALRYQLQRGVVVLAKSFNEKR--IKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19148 234 LAAVEELDKLAQERYGKSvIHLAVRWLLDQPGVSIALWGARKPeqLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
17-221 |
7.17e-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: 79.52 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFGT--FAS--KEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDkmadgtVKREDLFYTTKI--- 86
Cdd:cd19163 13 VSKLGFGAspLGGvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALKG------IPRDSYYLATKVgry 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 87 ----WITF-LRPELVRQCLERSLKKLGLDYVDLCIIHiPIAMKPGEELLpkdangkfifdtvdIRDTWEALEKCKDAGLS 161
Cdd:cd19163 87 gldpDKMFdFSAERITKSVEESLKRLGLDYIDIIQVH-DIEFAPSLDQI--------------LNETLPALQKLKEEGKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 162 KSIGVSNFNHKQLELILnkPRLKYKPTCNQVECHPYLNQSKLLE---FCKSKDIVLVAYSALG 221
Cdd:cd19163 152 RFIGITGYPLDVLKEVL--ERSPVKIDTVLSYCHYTLNDTSLLEllpFFKEKGVGVINASPLS 212
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
19-292 |
1.24e-15 |
|
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: 75.71 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFA--SKEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDkmadgtVKREDLFYTTKI-WIT--- 89
Cdd:cd19074 6 ELSLGTWLtfGGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKVfWPTgpg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 90 -----FLRPELVRQClERSLKKLGLDYVDLCIIHIPIAMKPGEEllpkdangkfifdtvdirdTWEALEKCKDAGLSKSI 164
Cdd:cd19074 80 pndrgLSRKHIFESI-HASLKRLQLDYVDIYYCHRYDPETPLEE-------------------TVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 165 GVSNFNHKQLE--LILNKPRLKYKPTCNQVECHpYLNQSK---LLEFCKSKDIVLVAYSAL------GSHRD-------S 226
Cdd:cd19074 140 GTSEWSAEQIAeaHDLARQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltGKYRDgipppsrS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138555 227 SWVSSDSPYLLEDPV----------LMTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKRIKENFQVFDFELTPE 292
Cdd:cd19074 219 RATDEDNRDKKRRLLtdenlekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-298 |
7.88e-15 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 73.81 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 21 GFG----TFASKEIPKSKAAEATKVAIDVGFRHIDAAYFY------QNEEEVGQALR--DKMAD-------GTVKREDLF 81
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRkyPEYADkvvlsvkGGLDPDTLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 82 YTTkiwitflRPELVRQCLERSLKKLG-LDYVDlciihipiamkpgeellpkdangkfIF------DTVDIRDTWEALEK 154
Cdd:cd19077 89 PDG-------SPEAVRKSIENILRALGgTKKID-------------------------IFeparvdPNVPIEETIKALKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 155 CKDAGLSKSIGVSNFNHKQLElilnKPRLKYKPTCNQVECHPYLN---QSKLLEFCKSKDIVLVAYSALGS-----HRDS 226
Cdd:cd19077 137 LVKEGKIRGIGLSEVSAETIR----RAHAVHPIAAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRglltgRIKS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 227 SWVSSDSPYLLEDP---------------VLMTIAKKHNQTPGQVAL---RYQLQRGVVVLAKSFNEKRIKENFQVFDFE 288
Cdd:cd19077 213 LADIPEGDFRRHLDrfngenfeknlklvdALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVE 292
|
330
....*....|
gi 158138555 289 LTPEDMKTID 298
Cdd:cd19077 293 LTDEELKEIN 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
20-297 |
9.64e-15 |
|
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: 73.62 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 20 LGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKMadgtvkREDLFYTTKIWITFLR---- 92
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIHEIGgsgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 93 -----PELVRQCLERSLKKLGLDYVDLCIIHipiamkpgeellpkdangkFIFDTVDIRDTWEALEKCKDAGLSKSIGVS 167
Cdd:cd19145 94 evrgdPAYVRAACEASLKRLDVDYIDLYYQH-------------------RIDTTVPIEITMGELKKLVEEGKIKYIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 168 NFNHKQLElilnKPRLKYKPTCNQVECHPYLN--QSKLLEFCKSKDIVLVAYSALG-----------SHRDSSWVSSDSP 234
Cdd:cd19145 155 EASADTIR----RAHAVHPITAVQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLGrgffagkakleELLENSDVRKSHP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138555 235 YLLEDPV---------LMTIAKKHNQTPGQVALRYQLQRG--VVVLAKSFNEKRIKENFQVFDFELTPEDMKTI 297
Cdd:cd19145 231 RFQGENLeknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-260 |
1.02e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.95 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 32 KSKAAEATKV---AIDVGFRHIDAAYFYQNEEEV-GQALRDKmadgtvkrEDLFYTTKI----WITFLRPELVRQCLERS 103
Cdd:cd19097 22 KPSEKEAKKIleyALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 104 LKKLGLDYVDLCIIHipiamkpGEELLPKDANgkfifdtvdirDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRL 183
Cdd:cd19097 94 LKRLKVDSLDGLLLH-------NPDDLLKHGG-----------KLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 184 KYkptcnqVEChPY------LNQSKLLEFCKSKDIVLVAYSA-----LGSHRD--SSWVSSDSPYLLEdpvLMTIAKKHN 250
Cdd:cd19097 156 DI------IQL-PFnildqrFLKSGLLAKLKKKGIEIHARSVflqglLLMEPDklPAKFAPAKPLLKK---LHELAKKLG 225
|
250
....*....|
gi 158138555 251 QTPGQVALRY 260
Cdd:cd19097 226 LSPLELALGF 235
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
42-267 |
8.42e-14 |
|
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: 70.75 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 42 AIDVGFRHIDAAYFY-----QNEEEVGQALRDKMADgtvKREDLFYTTKIWITFL---------RPELVRQcLERSLKKL 107
Cdd:cd19089 38 AFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVISTKAGYGMWpgpygdggsRKYLLAS-LDQSLKRM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 108 GLDYVDLCIIHIPIAMKPGEEllpkdangkfifdtvdirdTWEALEKCKDAGLSKSIGVSNFNHKQLEL---ILNKprLK 184
Cdd:cd19089 114 GLDYVDIFYHHRYDPDTPLEE-------------------TMTALADAVRSGKALYVGISNYPGAKARRaiaLLRE--LG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 185 YKPTCNQVechPY--LNQS---KLLEFCKSKDIVLVAYSAL-----------GSHRDSSW---------VSSDSPYLLED 239
Cdd:cd19089 173 VPLIIHQP---RYslLDRWaedGLLEVLEEAGIGFIAFSPLaqglltdkylnGIPPDSRRaaeskflteEALTPEKLEQL 249
|
250 260
....*....|....*....|....*...
gi 158138555 240 PVLMTIAKKHNQTPGQVALRYQLQRGVV 267
Cdd:cd19089 250 RKLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-299 |
1.14e-13 |
|
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: 70.34 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 20 LGFG----TFASKEIP-KSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvkREDLFYTTKIWITF- 90
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKId 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 ----------LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkDANgkfifdtVDIRDTWEALEKCKDAGL 160
Cdd:cd19078 80 ggkpgplgldSRPEHIRKAVEGSLKRLQTDYIDLYYQHRV------------DPN-------VPIEEVAGTMKELIKEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 161 SKSIGVSNFNHKQLelilnkpRLKYK--P-TCNQVECH-----PylnQSKLLEFCKSKDIVLVAYSALG----------- 221
Cdd:cd19078 141 IRHWGLSEAGVETI-------RRAHAvcPvTAVQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGkgfltgkiden 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 222 ----SHRDSSWVSSDSPY-------LLEdpVLMTIAKKHNQTPGQVALRYQLQRG--VVVLAKSFNEKRIKENFQVFDFE 288
Cdd:cd19078 211 tkfdEGDDRASLPRFTPEaleanqaLVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIE 288
|
330
....*....|.
gi 158138555 289 LTPEDMKTIDS 299
Cdd:cd19078 289 LTPEELREIED 299
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
18-292 |
2.40e-13 |
|
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: 69.56 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA----SKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKMadgtvkREDLFYTTKI-WIt 89
Cdd:cd19152 1 PKLGFGTAPlgnlYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELG------REDYVISTKVgRL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 90 fLRPEL--------------------------VRQCLERSLKKLGLDYVDLCIIHipiamKPGEELLpkDANGKFIFDTv 143
Cdd:cd19152 74 -LVPLQeveptfepgfwnplpfdavfdysydgILRSIEDSLQRLGLSRIDLLSIH-----DPDEDLA--GAESDEHFAQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 144 DIRDTWEALEKCKDAGLSKSIGV-SNfnhkQLELILnKPRLKYKPTCNQVECHpY--LNQSKLLEF---CKSKDIVLV-- 215
Cdd:cd19152 145 AIKGAFRALEELREEGVIKAIGLgVN----DWEVIL-RILEEADLDWVMLAGR-YtlLDHSAARELlpeCEKRGVKVVna 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 216 -AYSA---LGSHRDSSWVSSDSPYLLEDPV--LMTIAKKHNQTPGQVALRYQLQ----RGVVVLAKSfnEKRIKENFQVF 285
Cdd:cd19152 219 gPFNSgflAGGDNFDYYEYGPAPPELIARRdrIEALCEQHGVSLAAAALQFALAppavASVAPGASS--PERVEENVALL 296
|
....*..
gi 158138555 286 DFELTPE 292
Cdd:cd19152 297 ATEIPAA 303
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-300 |
3.94e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 68.83 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 32 KSKAAEATKV---AIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvkREDLFYTTKIWITFLRPE----LVRQCLE 101
Cdd:cd19104 28 RTTREEQIAAvrrALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 102 RSLKKLGLDYVDLCIIHIPIAMkpgEELLPKDANGKFIfDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQL--ELILN 179
Cdd:cd19104 101 KSLKRLKRDSVDLLQLHNRIGD---ERDKPVGGTLSTT-DVLGLGGVADAFERLRSEGKIRFIGITGLGNPPAirELLDS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 180 KprlkyKPTCNQVechPY--LNQS---------------KLLEFCKSKDIVLVAYSALGS---------HRDSSwVSSDS 233
Cdd:cd19104 177 G-----KFDAVQV---YYnlLNPSaaearprgwsaqdygGIIDAAAEHGVGVMGIRVLAAgalttsldrGREAP-PTSDS 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138555 234 PYLLE----DPVlMTIAKKHNQTPGQVALRYQL-QRGV--VVLAKSfNEKRIKENFQVFDF-ELTPEDMKTIDSL 300
Cdd:cd19104 248 DVAIDfrraAAF-RALAREWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
59-269 |
6.39e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 68.13 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 59 EEEVGQALRDKMAdgtvkREDLFYTTK------------IWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpg 126
Cdd:cd19752 53 ERLIGRWLKDRGN-----RDDVVIATKvgagprdpdggpESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVD------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 127 eellpkdangkfiFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELI--LNKPRLKYKPTCNQVEcHPYL------ 198
Cdd:cd19752 122 -------------DRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERArqIARQQGWAEFSAIQQR-HSYLrprpga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 199 ---NQS----KLLEFCKS-KDIVLVAYSAL--GSHrDSSWVSSDSPYLLEDP-----VLMTIAKKHNQTPGQVALRYQLQ 263
Cdd:cd19752 188 dfgVQRivtdELLDYASSrPDLTLLAYSPLlsGAY-TRPDRPLPEQYDGPDSdarlaVLEEVAGELGATPNQVVLAWLLH 266
|
....*.
gi 158138555 264 RGVVVL 269
Cdd:cd19752 267 RTPAII 272
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-300 |
2.06e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 66.59 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 42 AIDVGFRHIDAAYFY---QNEEEVGQALRDkmadgtVKREDLFYTTKI--WITFLRPELVRQCLERSLKKLGLDYVDLCI 116
Cdd:cd19103 41 AMAAGLNLWDTAAVYgmgASEKILGEFLKR------YPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 117 IHIPiamkpgeellpkdangkfifdtVDI-RDTWEALEKCKDaGLSKSIGVSNFNHKQLEL---ILNKPRLKYKptcnQV 192
Cdd:cd19103 115 IHNP----------------------ADVeRWTPELIPLLKS-GKVKHVGVSNHNLAEIKRaneILAKAGVSLS----AV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 193 ECHPYL-----NQSKLLEFCKSKDIVLVAYSAL-----------------GSHRDSSWvssdSPYL--LED--PVLMTIA 246
Cdd:cd19103 168 QNHYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAEIG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 247 KKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19103 244 AKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
18-167 |
3.57e-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: 65.84 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFASKEIPKSKAAEATKV---AIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgtvKREDLFYTTKIWITFL 91
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAAATldaAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 92 RPEL----------------VRQCLERSLKKLGLDYVDLCIIHipiamkpgeellpkDANGKfifDTVDIRDTWEALEKC 155
Cdd:cd19162 75 PGAAgrpagadrrfdfsadgIRRSIEASLERLGLDRLDLVFLH--------------DPDRH---LLQALTDAFPALEEL 137
|
170
....*....|..
gi 158138555 156 KDAGLSKSIGVS 167
Cdd:cd19162 138 RAEGVVGAIGVG 149
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
19-263 |
8.10e-12 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 64.88 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFASKeIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVG---QALRDKMAdGTVKREDLFYTTK--------IW 87
Cdd:cd19082 4 VLGTADFGTR-IDEEEAFALLDAFVELGGNFIDTARVYGDWVERGaseRVIGEWLK-SRGNRDKVVIATKgghpdledMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ITFLRPELVRQCLERSLKKLGLDYVDLCIIH-----IPIamkpgEELLpkdangkfifdtvdirdtwEALEKCKDAGLSK 162
Cdd:cd19082 82 RSRLSPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV-----GEIV-------------------DTLNELVRAGKIR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 163 SIGVSNFNHKQLELiLN---KPRLKYKPTCNQV---------ECHP-----YLNQSkLLEFCKSKDIVLVAYSALG---- 221
Cdd:cd19082 138 AFGASNWSTERIAE-ANayaKAHGLPGFAASSPqwslarpnePPWPgptlvAMDEE-MRAWHEENQLPVFAYSSQArgff 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 158138555 222 SHRDSSWVSSDSP----YLLED-----PVLMTIAKKHNQTPGQVALRYQLQ 263
Cdd:cd19082 216 SKRAAGGAEDDSElrrvYYSEEnferlERAKELAEEKGVSPTQIALAYVLN 266
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
19-222 |
2.05e-11 |
|
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: 63.73 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFASKEIPK--SKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALrdkmadgtVKREDLFYTTKIWITF--- 90
Cdd:cd19075 4 ILGTMTFGSQGRFTtaEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELG--------LGERGFKIDTKANPGVggg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 91 LRPELVRQCLERSLKKLGLDYVDLCIIHIPiamkpgeellpkDAngkfifdTVDIRDTWEALEKCKDAGLSKSIGVSNFN 170
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEFGLSNYS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 171 HKQLELILN--------KPRL---KYKPTCNQVEchpylnqSKLLEFCKSKDIVLVAYSALGS 222
Cdd:cd19075 137 AWEVAEIVEickengwvLPTVyqgMYNAITRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
20-298 |
4.78e-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: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 20 LGFGTFASKEIPKSKAAEATKVA---IDVGFRHIDAAYFYQN---EEEVGQALRDKmadgtvkREDLFYTTKIWITFLRP 93
Cdd:cd19080 15 LGTMTFGTEWGWGADREEARAMFdayVEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKYTMNRRPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 94 EL---------VRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLpkDA------NGKFIFdtVDIRDT--WEAlekCK 156
Cdd:cd19080 88 DPnaggnhrknLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVM--RAlddlvrAGKVLY--VGISDTpaWVV---AR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 157 DAGLSKSIGVSNFNHKQLElilnkprlkYkptcNQVECHPylnQSKLLEFCKSKDIVLVAYSALGS-------HRDSSWV 229
Cdd:cd19080 161 ANTLAELRGWSPFVALQIE---------Y----SLLERTP---ERELLPMARALGLGVTPWSPLGGglltgkyQRGEEGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 230 SSDSPYLLEDP------------VLMTIAKKHNQTPGQVALRYQLQR--GVVVLAKSFNEKRIKENFQVFDFELTPEDMK 295
Cdd:cd19080 225 AGEAKGVTVGFgklternwaivdVVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPEQLA 304
|
...
gi 158138555 296 TID 298
Cdd:cd19080 305 RLD 307
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
19-167 |
1.08e-08 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 55.36 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFA---SKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEV-GQALrDKMADGtVKREDLFYTTK-----IWIT 89
Cdd:cd19164 17 IFGAATFSyqyTTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRDE-FPRDTYFIITKvgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 90 FLRPELVRQCLERSLKKLGLDYVDLCIIHipiamkpgeellpkDAngKFifdtVDIRDTWEA---LEKCKDAGLSKSIGV 166
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLVYLH--------------DV--EF----VADEEVLEAlkeLFKLKDEGKIRNVGI 154
|
.
gi 158138555 167 S 167
Cdd:cd19164 155 S 155
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
17-298 |
1.13e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 55.77 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 17 MPVLGFG---TFASKEIPKSKAAEATKvAIDVGFRHIDAAYFY-----QNEEEVGQALRDKMAdgtVKREDLFYTTK--- 85
Cdd:PRK09912 25 LPALSLGlwhNFGHVNALESQRAILRK-AFDLGITHFDLANNYgpppgSAEENFGRLLREDFA---AYRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 86 -IWI----TFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEEllpkdangkfifdtvdirdTWEALEKCKDAGL 160
Cdd:PRK09912 101 dMWPgpygSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEE-------------------TASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 161 SKSIGVSNFN----HKQLELI--LNKPRLKYKPTCNQVecHPYLNQSKLLEFCKSKDIVLVAYSALGS------------ 222
Cdd:PRK09912 162 ALYVGISSYSpertQKMVELLreWKIPLLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQglltgkylngip 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 223 -----HRDSSWVSSDSPYLLEDPVLMTI------AKKHNQTPGQVALRYQL--QRGVVVLAKSFNEKRIKENFQVF-DFE 288
Cdd:PRK09912 240 qdsrmHREGNKVRGLTPKMLTEANLNSLrllnemAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALnNLT 319
|
330
....*....|
gi 158138555 289 LTPEDMKTID 298
Cdd:PRK09912 320 FSTEELAQID 329
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
19-306 |
2.04e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 54.86 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFASKEIPKSKAAEAT-KVAIDVGFRHIDAAYFYQ----------NEEEVGQALRDKMAdgtvkREDLFYTTKIW 87
Cdd:PRK10625 15 TLGLGTMTFGEQNSEADAHAQlDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRGS-----REKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 88 ------ITFLRPEL------VRQCLERSLKKLGLDYVDLCIIHIPIAmkpgeellPKDANGKFIFD------TVDIRDTW 149
Cdd:PRK10625 90 gpsrnnDKGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtdsapAVSLLETL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 150 EALEKCKDAGLSKSIGVSN------FNHKQLELILNKPRLkykpTCNQvecHPY--LNQS---KLLEFCKSKDIVLVAYS 218
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSNetafgvMRYLHLAEKHDLPRI----VTIQ---NPYslLNRSfevGLAEVSQYEGVELLAYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 219 ALG--------------SHRDSSWVSSDSPYLLEDPVL-----MTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKR 277
Cdd:PRK10625 235 CLAfgtltgkylngakpAGARNTLFSRFTRYSGEQTQKavaayVDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQ 314
|
330 340
....*....|....*....|....*....
gi 158138555 278 IKENFQVFDFELTPEDMKTIDSLNRNFRY 306
Cdd:PRK10625 315 LKTNIESLHLTLSEEVLAEIEAVHQVYTY 343
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
21-204 |
3.77e-08 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 53.69 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 21 GFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgTVKREDLFYTTKIW----ITF-LR 92
Cdd:cd19153 21 ALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGryrdSEFdYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 93 PELVRQCLERSLKKLGLDYVDLCIIHipiamkpgeellpkdaNGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHK 172
Cdd:cd19153 97 AERVRASVATSLERLHTTYLDVVYLH----------------DIEFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLD 160
|
170 180 190
....*....|....*....|....*....|..
gi 158138555 173 QLELILNKPRLKyKPTCNQVECHPYLNQSKLL 204
Cdd:cd19153 161 TLTRATRRCSPG-SLDAVLSYCHLTLQDARLE 191
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
19-128 |
6.23e-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: 53.37 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFG---TFAsKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDkmadGTVKREDLFYTTKIWITFLR 92
Cdd:cd19143 15 ALSFGswvTFG-NQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDYVVSTKIFWGGGG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 158138555 93 PELVRQCLER---------SLKKLGLDYVDLCIIHIPIAMKPGEE 128
Cdd:cd19143 90 PPPNDRGLSRkhivegtkaSLKRLQLDYVDLVFCHRPDPATPIEE 134
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
42-267 |
1.74e-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: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 42 AIDVGFRHIDAAYFY-----QNEEEVGQALRDKMADgtvKREDLFYTTKIWITFL---------RPELVRQcLERSLKKL 107
Cdd:cd19151 39 AFDLGITHFDLANNYgpppgSAEENFGRILKEDLKP---YRDELIISTKAGYTMWpgpygdwgsKKYLIAS-LDQSLKRM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 108 GLDYVDLCIIHIPIAMKPGEEllpkdangkfifdtvdirdTWEALEKCKDAGLSKSIGVSNFNHKQLEL---ILNK---P 181
Cdd:cd19151 115 GLDYVDIFYHHRPDPETPLEE-------------------TMGALDQIVRQGKALYVGISNYPPEEAREaaaILKDlgtP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 182 RLKYKPTCNQVECHPylnQSKLLEFCKSKDIVLVAYSAL-----------GSHRDSSwVSSDSPYLLEDPV--------- 241
Cdd:cd19151 176 CLIHQPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLaqglltdrylnGIPEDSR-AAKGSSFLKPEQIteeklakvr 251
|
250 260
....*....|....*....|....*..
gi 158138555 242 -LMTIAKKHNQTPGQVALRYQLQRGVV 267
Cdd:cd19151 252 rLNEIAQARGQKLAQMALAWVLRNKRV 278
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
42-300 |
2.24e-07 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 51.42 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 42 AIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgtvkREDLFYTTKI----------------WItflrpelvRQCLER 102
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVfgpmgddpndrglsrrHI--------RRAVEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 103 SLKKLGLDYVDLCIIHIPIAMKPGEEllpkdangkfifdtvdirdTWEALEKCKDAGLSKSIGVSNF------------- 169
Cdd:cd19087 104 SLRRLQTDYIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 170 NHKQLELILNKPRlkYKPTCNQVECHpylnqskLLEFCKSKDIVLVAYSAL------GSHRDSSWVSSDSPYLLEDPV-- 241
Cdd:cd19087 165 RRGLLRFVSEQPM--YNLLKRQAELE-------ILPAARAYGLGVIPYSPLagglltGKYGKGKRPESGRLVERARYQar 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138555 242 ------------LMTIAKKHNQTPGQVALRYQLQRGVV--VLAKSFNEKRIKENFQVFDFELTPEDMKTIDSL 300
Cdd:cd19087 236 ygleeyrdiaerFEALAAEAGLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
31-302 |
3.18e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 51.12 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 31 PKSKAAeATKV---AIDVGFRHIDAAYFY----QNeeevgQALRDKMADGtvkREDLFYTTKI---------WITFLRPE 94
Cdd:PRK10376 36 PKDRDA-AIAVlreAVALGVNHIDTSDFYgphvTN-----QLIREALHPY---PDDLTIVTKVgarrgedgsWLPAFSPA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 95 LVRQCLERSLKKLGLDYVDLCIIHIPI-AMKPGEEllpkdangkfifdtvDIRDTWEALEKCKDAGLSKSIGVSNFNHKQ 173
Cdd:PRK10376 107 ELRRAVHDNLRNLGLDVLDVVNLRLMGdGHGPAEG---------------SIEEPLTVLAELQRQGLVRHIGLSNVTPTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 174 LElilnKPRLKYKPTCnqVECHPYL---NQSKLLEFCKSKDIVLVAYSALGSHrdsswvssdSPylLEDPVLMTIAKKHN 250
Cdd:PRK10376 172 VA----EARKIAEIVC--VQNHYNLahrADDALIDALARDGIAYVPFFPLGGF---------TP--LQSSTLSDVAASLG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 251 QTPGQVALRYQLQRG--VVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNR 302
Cdd:PRK10376 235 ATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
18-129 |
6.96e-07 |
|
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: 50.16 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 18 PVLGFGTFA--SKEIPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgTVKREDLFYTTKI-WITfl 91
Cdd:cd19142 14 SNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWSY-- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 158138555 92 RPE---LVR----QCLERSLKKLGLDYVDLCIIHIPIAMKPGEEL 129
Cdd:cd19142 88 GSEergLSRkhiiESVRASLRRLQLDYIDIVIIHKADPMCPMEEV 132
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
30-220 |
1.12e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 43.23 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 30 IPKSKAAEATKVAIDVGFRHIDAAYFYQN---EEEVGQALRDKmadgTVKREDLFYTTKIW-----ITFlRPELVRQCLE 101
Cdd:PLN02587 28 VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTKCGrygegFDF-SAERVTKSVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 102 RSLKKLGLDYVDLCIIHipiamkpgeellpkdangKFIFDTVD--IRDTWEALEKCKDAGLSKSIGVSNFnhkqleliln 179
Cdd:PLN02587 103 ESLARLQLDYVDILHCH------------------DIEFGSLDqiVNETIPALQKLKESGKVRFIGITGL---------- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158138555 180 kPRLKYKPTCNQVE----------CHPYLNQSKLLE---FCKSKDIVLVAYSAL 220
Cdd:PLN02587 155 -PLAIFTYVLDRVPpgtvdvilsyCHYSLNDSSLEDllpYLKSKGVGVISASPL 207
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
19-129 |
3.89e-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: 38.58 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138555 19 VLGFGTFAS--KEIPKSKAAEATKVAIDVGFRHIDAAYFY---QNEEEVGQALRDKmadgTVKREDLFYTTKI-WITFLR 92
Cdd:cd19141 14 CLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIfWGGKAE 89
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 158138555 93 PE--LVR----QCLERSLKKLGLDYVDLCIIHIPIAMKPGEEL 129
Cdd:cd19141 90 TErgLSRkhiiEGLKASLERLQLEYVDIVFANRPDPNTPMEEI 132
|
|
| |
