|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-283 |
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: 623.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRLSDGHFIPVLGFGTYAPREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 WCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 166 SNFNRRQLEKILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPVLLADPVLCAIA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 564392038 246 KKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQV 278
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-283 |
1.92e-151 |
|
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: 425.75 E-value: 1.92e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYA-PREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNH 91
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 PERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 172 QLEKILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPVLLADPVLCAIAKKYNWT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270
....*....|....*....|....*....|..
gi 564392038 252 PALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQI 272
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-283 |
3.90e-117 |
|
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: 336.38 E-value: 3.90e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIadgtVKREDIFYTSKVWCTFNHPERV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 96 QVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLkakdenekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGSK-------------EARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 176 ILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHREtrcvdkslpVLLADPVLCAIAKKYNWTPALI 255
Cdd:cd19071 141 LLAAARIK--PAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR---------PLLDDPVLKEIAKKYGKTPAQV 209
|
250 260
....*....|....*....|....*...
gi 564392038 256 ALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19071 210 LLRWALQRGVVVIPKSSNPERIKENLDV 237
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-283 |
4.00e-117 |
|
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: 338.10 E-value: 4.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGTYAprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDEnekLLFDVVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGD---GSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNkpGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetRCVDKSLPVLLADPVLCAIAK 246
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLV--PRGQTNPPPRLDDPTLVAIAK 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDI 269
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-283 |
1.81e-111 |
|
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: 324.37 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPERV 95
Cdd:cd19107 4 MPILGLGTW---KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 96 QVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 176 ILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGShrETRCVDK-SLPVLLADPVLCAIAKKYNWTPAL 254
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGS--PDRPWAKpEDPSLLEDPKIKEIAAKHNKTTAQ 238
|
250 260
....*....|....*....|....*....
gi 564392038 255 IALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKV 267
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-283 |
2.89e-111 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 323.57 E-value: 2.89e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 10 LSDGHFIPVLGFGTY--APREVPkskalEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKI-ADGTVKREDIFYTSKVW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQVK-----AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGS-HRETRCVDKslPVLLADPVLCAIA 245
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSpDRPWAKPDE--PVLLEEPKVKALA 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 564392038 246 KKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19106 232 KKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQV 269
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
7-281 |
9.72e-106 |
|
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: 309.34 E-value: 9.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGTYAPRevpKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVW 86
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEdLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGS-HRETRCVDKSLPVLLADPVLCAIA 245
Cdd:cd19123 159 NFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIA 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 564392038 246 KKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENM 281
Cdd:cd19123 237 EKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNL 272
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-283 |
1.94e-105 |
|
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: 308.96 E-value: 1.94e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 8 VRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWC 87
Cdd:cd19154 4 ITLSNGVKMPLIGLGTW---QSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSN 167
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 168 FNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGS-----HRETRCVDKSlPVLLADPVLC 242
Cdd:cd19154 161 FNNDQIQRILDNARVK--PHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranFTKSTGVSPA-PNLLQDPIVK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564392038 243 AIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNI 278
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-283 |
1.47e-101 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 297.35 E-value: 1.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 12 DGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiADGtVKREDIFYTSKVWCTFNH 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASG-VPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 PERVQVCLEQSLKQLQLEYVDLYLIHFPMAlkpeedlkakdenekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 172 QLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAKKYNWT 251
Cdd:COG0656 134 HLEELLAETGVK--PAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270
....*....|....*....|....*....|..
gi 564392038 252 PALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
10-283 |
1.96e-100 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 295.41 E-value: 1.96e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 10 LSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTF 89
Cdd:cd19125 5 LNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 NHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDlkaKDENEKLLfdVVDICDTWKAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAH---MPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 170 RRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGShRETRCVDKSlpvLLADPVLCAIAKKYN 249
Cdd:cd19125 157 VKKLEDLLAVARVP--PAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWVKKN---VLKDPIVTKVAEKLG 230
|
250 260 270
....*....|....*....|....*....|....
gi 564392038 250 WTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19125 231 KTPAQVALRWGLQRGTSVLPKSTNEERIKENIDV 264
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-283 |
8.11e-100 |
|
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: 294.56 E-value: 8.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTY--APREVPkskalEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPE 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEVT-----EAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 94 RVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 174 EKILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETrcVDkslpvLLADPVLCAIAKKYNWTPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270
....*....|....*....|....*....|
gi 564392038 254 LIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQV 261
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-282 |
3.55e-96 |
|
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: 284.69 E-value: 3.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 10 LSDGHFIPVLGFGTY--APREVPKskaleATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIAD-GTVKREDIFYTSKVW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEVGA-----AVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAK-----DENEKLLFDVVDICDTWKAMEKCKDAGLAK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavptNGGEVDLDLSVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 162 SIGVSNFNRRQLEKILNKPGLkhRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdKSLPVLLADPVL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564392038 242 CAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQ 282
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE 268
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-283 |
5.40e-90 |
|
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: 268.75 E-value: 5.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 12 DGHFIPVLGFGTYAPREVPKsKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVK-REDIFYTSKVWCTFN 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 91 HPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFdvvDICDTWKAMEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPF---DIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 171 RQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHReTRCVDKSlpvLLADPVLCAIAKKYNW 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKWGSNA---VMESDVLKEIAAAKGK 230
|
250 260 270
....*....|....*....|....*....|...
gi 564392038 251 TPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDI 263
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-283 |
7.65e-89 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 265.90 E-value: 7.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 5 QQTVRLSDGHFIPVLGFGTY--APREVPKskaleATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiaDGTVKREDIFYT 82
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWqsKPNEVAK-----AVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 83 SKVWCTFNHpeRVQVCLEQSLKQLQLEYVDLYLIHFPMALKPE--EDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLA 160
Cdd:cd19117 74 TKLWCTWHR--RVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 161 KSIGVSNFNRRQLEKILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGShretrcvdkSLPVLLADPV 240
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS---------TNAPLLKEPV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564392038 241 LCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL 265
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-283 |
1.37e-88 |
|
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: 266.31 E-value: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 5 QQTVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSK 84
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 VWCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEED--LKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKS 162
Cdd:cd19155 78 LPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDdsGKLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 163 IGVSNFNRRQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGS------HRETRCVDKSLPVLL 236
Cdd:cd19155 158 IGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfSPGTGSPSGSSPDLL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 564392038 237 ADPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19155 236 QDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQV 282
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-283 |
4.51e-88 |
|
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: 263.97 E-value: 4.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHP 92
Cdd:cd19111 1 GFPMPVIGLGTY---QSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 93 ERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDlkaKDENEKLLFDVVdicDTWKAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKD---KGERELASSDVT---SVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 173 LEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGS-HRETRCVDKSLPVLLADPVLCAIAKKYNWT 251
Cdd:cd19111 152 INKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDKT 229
|
250 260 270
....*....|....*....|....*....|..
gi 564392038 252 PALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19111 230 PAQVLLRFVLQRGTGVLPKSTNKERIEENFEV 261
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-283 |
4.67e-86 |
|
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: 258.62 E-value: 4.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 5 QQTVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGtVKREDIFYTSK 84
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTW---QAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 VWCTFNhpERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPE--EDLKAKDENEKLLFD-VVDICDTWKAMEKCKDAGLAK 161
Cdd:cd19121 77 LWSTYH--RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNgnHDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 162 SIGVSNFNRRQLEKILnkPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGShretrcvdKSLPVLLADPVL 241
Cdd:cd19121 155 AIGVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDEPVV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564392038 242 cAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19121 225 -EIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEI 265
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
16-287 |
5.64e-85 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 256.62 E-value: 5.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYAPrevPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPERV 95
Cdd:cd19129 6 IPALGFGTLIP---DPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 96 QVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDV-VDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLE 174
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 175 KILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHREtrcvdkslPVLLADPVLCAIAKKYNWTPAL 254
Cdd:cd19129 163 EIFEAARIK--PAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME--------PKLLEDPVITAIARRVNKTPAQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 564392038 255 IALRYQLERGVVVLAKSFTEKRIKENMQIPGPP 287
Cdd:cd19129 233 VLLAWAIQRGTALLTTSKTPSRIRENFDISTLP 265
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-280 |
7.69e-82 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 247.29 E-value: 7.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiaDGTVKREDIFYTSKVW 86
Cdd:cd19131 1 TITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMalkPEEDLkakdenekllfdvvdICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19131 74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQDK---------------YVETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAK 246
Cdd:cd19131 136 NFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAE 202
|
250 260 270
....*....|....*....|....*....|....
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKEN 280
Cdd:cd19131 203 KHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAEN 236
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-285 |
1.67e-80 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 243.33 E-value: 1.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFNHPERV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 96 QVCLEQSLKQLQLEYVDLYLIHFPmalKPEedlkakdenekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWP---NPT----------------VPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 176 ILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGsHREtrcvdkslpvLLADPVLCAIAKKYNWTPALI 255
Cdd:cd19073 135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270
....*....|....*....|....*....|
gi 564392038 256 ALRYQLERGVVVLAKSFTEKRIKENMQIPG 285
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFD 231
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-283 |
2.44e-80 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 243.31 E-value: 2.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYAPREVPK-SKALEAtkiAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPER 94
Cdd:cd19136 1 MPILGLGTFRLRGEEEvRQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 95 VQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKllfdvvdicDTWKAMEKCKDAGLAKSIGVSNFNRRQLE 174
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELRR---------ESWRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 175 KILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGShretrcvdkSLPVLLADPVLCAIAKKYNWTPAL 254
Cdd:cd19136 149 ELLKYCEVP--PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTPAQ 217
|
250 260
....*....|....*....|....*....
gi 564392038 255 IALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19136 218 VLLRWALQQGIGVIPKSTNPERIAENIKV 246
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-287 |
1.00e-79 |
|
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: 242.14 E-value: 1.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGT-----YAPREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiaDGTVKREDIFYTSKVWC 87
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNHPERVqvcLEQSLKQLQLEYVDLYLIHFPMALKPeedlkakdenekllfDVVDICDTWKAMEKCKDAGLAKSIGVSN 167
Cdd:cd19120 77 GIKDPREA---LRKSLAKLGVDYVDLYLIHSPFFAKE---------------GGPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 168 FNRRQLEKILNKPglKHRPVCNQVECHPYLN--QRKLLDFCKSKDIVLVAYSALGShrETRCVDKSLpvllaDPVLCAIA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP--LTRDAGGPL-----DPVLEKIA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564392038 246 KKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQIPGPP 287
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFE 251
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-283 |
2.03e-77 |
|
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: 237.40 E-value: 2.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 8 VRLSDGHFIPVLGFGTYAPREvPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWC 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNhpERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAK-----DENEKLLFDV-VDICDTWKAMEKCKDAGLAK 161
Cdd:cd19119 83 TFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKpftpvNDDGKTRYAAsGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 162 SIGVSNFNRRQLEKILNKpgLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETrcvdkslpvLLADPVL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564392038 242 CAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI 271
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-283 |
6.65e-77 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 235.49 E-value: 6.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPERVQ 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 97 VCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 177 LNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGShretRCVDKSLpVLLADPVLCAIAKKYNWTPALIA 256
Cdd:cd19128 159 LNYCKIK--PFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGG----SYGDGNL-TFLNDSELKALATKYNTTPPQVI 231
|
250 260 270
....*....|....*....|....*....|
gi 564392038 257 LRYQLER---GVVVLAKSFTEKRIKENMQI 283
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDI 261
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-283 |
1.89e-76 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 233.48 E-value: 1.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 8 VRLSDGHFIPVLGFGTYaprEVPK-SKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSkiadGTVKREDIFYTSKVW 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF---QTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKpeedlkakdenekllfdvvdICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK--------------------FIDTWKALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAK 246
Cdd:cd19126 134 NFQEHHLEELLAHADVV--PAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGE 200
|
250 260 270
....*....|....*....|....*....|....*..
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19126 201 KYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADI 237
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-283 |
3.54e-76 |
|
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: 234.65 E-value: 3.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 WCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKP---EEDLKAK---DENEKLLFDVVDICDTWKAMEKCKDAGL 159
Cdd:cd19113 78 WNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFvpiEEKYPPGfycGDGDNFVYEDVPILDTWKALEKLVDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 160 AKSIGVSNFNRRQLEKILNkpGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALG--SHRE-TRCVDKSLPVLL 236
Cdd:cd19113 158 IKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqSFVElNQGRALNTPTLF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 564392038 237 ADPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSV 282
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-285 |
1.71e-74 |
|
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: 230.39 E-value: 1.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 WCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALK---------PEedlkAKDENEKLLFDVVDICDTWKAMEKCKD 156
Cdd:cd19115 80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdpavrypPG----WFYDGKKVEFSNAPIQETWTAMEKLVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 157 AGLAKSIGVSNFNRRQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALG--SHRETRCVD-KSLP 233
Cdd:cd19115 156 KGLARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqSFLELDLPGaKDTP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564392038 234 VLLADPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQIPG 285
Cdd:cd19115 234 PLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTG 285
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-283 |
4.78e-73 |
|
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: 224.76 E-value: 4.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 8 VRLSDGHFIPVLGFGTYaprEVP-KSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiaDGTVKREDIFYTSKVW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMAlkpeedlkakdenekllfdvvDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILnkPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslPVLLADPVLCAIAK 246
Cdd:cd19133 133 NFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR---------NNLFENPVLTEIAE 201
|
250 260 270
....*....|....*....|....*....|....*..
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDI 238
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-283 |
6.42e-73 |
|
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: 224.58 E-value: 6.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGTYAPREvpKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiaDGTVKREDIFYTSKVW 86
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMalkpeedlkaKDENEkllfdvvdicDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPV----------KGKYK----------ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAK 246
Cdd:cd19157 135 NFQVHHLEDLLADAEIV--PMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAE 201
|
250 260 270
....*....|....*....|....*....|....*..
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADV 238
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-283 |
8.96e-73 |
|
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: 224.06 E-value: 8.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFNHP 92
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 93 ERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkAKDenekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 173 LEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAKKYNWTP 252
Cdd:cd19140 139 LREAVELSEAP--LFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270
....*....|....*....|....*....|..
gi 564392038 253 ALIALRYQLER-GVVVLAKSFTEKRIKENMQI 283
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDI 237
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-283 |
9.07e-72 |
|
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: 221.37 E-value: 9.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 10 LSDGHFIPVLGFGTYAPREvpkSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSkiadGTVKREDIFYTSKVWCTF 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKG---DEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 NHPERVQVCLEQSLKQLQLEYVDLYLIHFPMalkPEEDLkakdenekllfdvvdICDTWKAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPN---PSRDL---------------YVEAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 170 RRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGshRETRcvdkslpvLLADPVLCAIAKKYN 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG--RGSG--------LLDEPVIKAIAEKHG 203
|
250 260 270
....*....|....*....|....*....|....
gi 564392038 250 WTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAI 237
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-283 |
4.55e-70 |
|
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: 218.89 E-value: 4.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGTY-APREVPKSKALEATKIaidaGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWrMEPGEIKELILNAIKI----GYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 WCTfNHPERVQVClEQSLKQLQLEYVDLYLIHFPMALKPE---EDLKAKDENEKLLFDV-VDICDTWKAMEKCKDAGLAK 161
Cdd:cd19112 78 WNS-DHGHVIEAC-KDSLKKLQLDYLDLYLVHFPVATKHTgvgTTGSALGEDGVLDIDVtISLETTWHAMEKLVSAGLVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 162 SIGVSNFNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALG---SHRE----TRCVDkslpv 234
Cdd:cd19112 156 SIGISNYDIFLTRDCLAYSKIK--PAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaaANAEwfgsVSPLD----- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564392038 235 llaDPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19112 229 ---DPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDV 274
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-283 |
2.59e-69 |
|
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: 215.46 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 8 VRLSDGHFIPVLGFGTYapREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKiadgTVKREDIFYTSKVWC 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVW--RVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKpeedlkakdenekllfdvvdICDTWKAMEKCKDAGLAKSIGVSN 167
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 168 FNRRQLEKILNKpgLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAKK 247
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270
....*....|....*....|....*....|....*.
gi 564392038 248 YNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDV 237
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-283 |
6.15e-67 |
|
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: 209.49 E-value: 6.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGT-----YAPrevpkskalEATKIAI-DAGFRHIDSAAVYQNEKEVGLAIRskiADGtVKREDIF 80
Cdd:cd19135 4 TVRLSNGVEMPILGLGTshsggYSH---------EAVVYALkECGYRHIDTAKRYGCEELLGKAIK---ESG-VPREDLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 81 YTSKVWCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLK-AKDEnekllfdvvdicdTWKAMEKCKDAGL 159
Cdd:cd19135 71 LTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKeTRAE-------------TWRALEELYDEGL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 160 AKSIGVSNFNRRQLEKILNKPGLkhRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADP 239
Cdd:cd19135 138 CRAIGVSNFLIEHLEQLLEDCSV--VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEP 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564392038 240 VLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19135 205 TVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQV 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-284 |
3.50e-65 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 205.93 E-value: 3.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 10 LSDGHFIPVLGFGTYApREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADG-TVKREDIFYTSKVWCT 88
Cdd:cd19122 3 LNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 89 FNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAK---DENEKLLFDVVDICD-TWKAMEKCKDAGLAKSIG 164
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlgpDGKYVILKDLTENPEpTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 165 VSNFNRRQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHREtrcVDKSLPVLLADPVLCAI 244
Cdd:cd19122 162 VSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNEV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 564392038 245 AKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQIP 284
Cdd:cd19122 237 AEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSI 276
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-283 |
4.12e-65 |
|
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: 205.87 E-value: 4.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 93 ERVQVCLEQSLKQLQLEYVDLYLIHFPMALK---PEEDLKA---KDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFlwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPglKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVD--KSLPVLLADPVLCAI 244
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKhlKHFTNLLEHPVVKKL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 564392038 245 AKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDI 274
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-283 |
1.55e-64 |
|
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: 203.41 E-value: 1.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 8 VRLSDGHFIPVLGFGTYApreVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKiadgTVKREDIFYTSKVWC 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMalkpeedlkakdeneKLLFDvvDICDTWKAMEKCKDAGLAKSIGVSN 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------------PNDFD--RTIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 168 FNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPV-LLADPVLCAIAK 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGdVLQDPTITGLAE 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDI 251
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-283 |
5.95e-61 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 194.52 E-value: 5.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 3 SKQQTVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSkiadGTVKREDIFYT 82
Cdd:PRK11565 2 ANPTVIKLQDGNVMPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 83 SKVWCtfNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMalkPEEDLkakdenekllfdvvdICDTWKAMEKCKDAGLAKS 162
Cdd:PRK11565 75 TKLWN--DDHKRPREALEESLKKLQLDYVDLYLMHWPV---PAIDH---------------YVEAWKGMIELQKEGLIKS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 163 IGVSNFNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETrcvdkslpvLLADPVLC 242
Cdd:PRK11565 135 IGVCNFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG---------VFDQKVIR 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564392038 243 AIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:PRK11565 204 DLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDV 244
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-282 |
1.09e-60 |
|
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: 192.95 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTY--APREVPKSkaleaTKIAIDAGFRHIDSAAVYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFNHPE 93
Cdd:cd19139 1 IPAFGLGTFrlKDDVVIDS-----VRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 94 RVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkAKDenekllfDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWP----------SPN-------DEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 174 EKILNKPGlKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAKKYNWTPA 253
Cdd:cd19139 135 DEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPA 202
|
250 260
....*....|....*....|....*....
gi 564392038 254 LIALRYQLERGVVVLAKSFTEKRIKENMQ 282
Cdd:cd19139 203 QIALAWAMARGYAVIPSSTKREHLRSNLL 231
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-283 |
1.63e-60 |
|
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: 192.82 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 10 LSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTF 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 NHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedLKAKDenekllfdvvDICDTWKAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWP--------TPAAG----------NYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 170 RRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAKKYN 249
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHG 205
|
250 260 270
....*....|....*....|....*....|....
gi 564392038 250 WTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDV 239
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-282 |
3.35e-60 |
|
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: 192.91 E-value: 3.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 19 LGFGTYA----PREVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIrskiADGTVKREDIFYTSKV------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 WCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------------DPD-------TPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 166 SNFNRRQLEKILNKPglKHRPVCNQVECHPY--LNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPV--------- 234
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKgpgerrrll 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564392038 235 -------LLADPVLCAIAKKYNWTPALIALRY--QLERGVVVLAKSFTEKRIKENMQ 282
Cdd:pfam00248 216 kkgtplnLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLG 272
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-281 |
4.82e-58 |
|
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: 186.67 E-value: 4.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYA---PREVPKS---KALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRskiadgTVKREDIFYTSKVW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDYSddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakdeNekllfDVVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP--------------N-----PSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPGlKHRPVCNQVECHpYLNQR---KLLDFCKSKDIVLVAYSALGShreTRCVDKSLPVLLADpvlca 243
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEK---GKLSNAKGSPLLDE----- 208
|
250 260 270
....*....|....*....|....*....|....*....
gi 564392038 244 IAKKYNWTPALIALRYQLER-GVVVLAKSFTEKRIKENM 281
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENA 247
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-283 |
3.58e-57 |
|
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: 184.29 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRLSDGHFIPVLGFGTYaprEVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRskiADGtVKREDIFYTSKVW 86
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVG---ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMAlkpeedlkakdenekllfDVVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILNKPGLKhrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAK 246
Cdd:cd19134 137 NFTAEHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAA 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 564392038 247 KYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQI 283
Cdd:cd19134 204 AHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDV 240
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-280 |
4.72e-49 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 163.57 E-value: 4.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRLSDGHFIPVLGFGTYAPREVPKSKA--LEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAqeIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 81 YTSKVWCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMAlkpeedlkakdenekllfdvVDICDTWKAMEKCKDAGLA 160
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG--------------------VPLAETVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 161 KSIGVSNFNRRQLEKILNKPGLKHrPVCNQVECHpyLNQR----KLLDFCKSKDIVLVAYSALGSHRETRCvdkslpVLL 236
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGGN-CAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLRR------GLL 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564392038 237 ADPVLCAIAKKYNWTPALIALRYQLERG-VVVLAKSFTEKRIKEN 280
Cdd:cd19138 205 ENPTLKEIAARHGATPAQVALAWVLRDGnVIAIPKSGSPEHAREN 249
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-282 |
4.32e-48 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 160.96 E-value: 4.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYAPREVPkskALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFNHPERV 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQV---VIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 96 QVCLEQSLKQLQLEYVDLYLIHFPmalKPEedlkakdenekllfDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWP---SPN--------------DEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 176 ILNKPGLKHrPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvLLADPVLCAIAKKYNWTPALI 255
Cdd:PRK11172 139 AIAAVGAEN-IATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQV 206
|
250 260
....*....|....*....|....*..
gi 564392038 256 ALRYQLERGVVVLAKSftEKRikENMQ 282
Cdd:PRK11172 207 ILAWAMQLGYSVIPSS--TKR--ENLA 229
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-282 |
2.83e-39 |
|
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: 138.09 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYA------PREVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSkiadgtVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 84 KVWCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakdeNEKLLFDvvdicDTWKAMEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP--------------NPNIPLE-----ETLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 164 GVSNFNRRQLEKILNKpgLKHRPVCNQVECHPY---LNQRKLLDFCKSKDIVLVAYSALgshretrcvDKSLpvLLADPV 240
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---------RRGL--EKTNRT 202
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564392038 241 LCAIAKKYNWTPALIALRYQLER-GVVVLAKSFTEKRIKENMQ 282
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLK 245
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
6-269 |
1.41e-37 |
|
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: 134.92 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRL-SDGHFIPVLGFGT----YAPREVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvKRE 77
Cdd:COG0667 2 EYRRLgRSGLKVSRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 78 DIFYTSKV--------WCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWK 149
Cdd:COG0667 76 DVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 150 AMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGLKHRPVCNQVEchpY--LNQR---KLLDFCKSKDIVLVAYSALGS--- 221
Cdd:COG0667 137 ALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLAGgll 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564392038 222 -------------HRETRCVDKSLP---VLLADPVLCAIAKKYNWTPALIALRYQLERGVVVLA 269
Cdd:COG0667 214 tgkyrrgatfpegDRAATNFVQGYLterNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSV 277
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-282 |
9.56e-37 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 132.35 E-value: 9.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYA---------PREVPKSkALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRskiadGTVKREDIFYTS 83
Cdd:cd19093 2 VSPLGLGTWQwgdrlwwgyGEYGDED-LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 84 KVWCTFNHPERVQV--CLEQSLKQLQLEYVDLYLIHFPMALKPEedlkakdenekllfdvvdICDTWKAMEKCKDAGLAK 161
Cdd:cd19093 76 KFAPLPWRLTRRSVvkALKASLERLGLDSIDLYQLHWPGPWYSQ------------------IEALMDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 162 SIGVSNFNRRQLEKILNKpgLKHR---PVCNQVE---CHPYLNQRKLLDFCKSKDIVLVAYSALG--------------- 220
Cdd:cd19093 138 AVGVSNYSADQLRRAHKA--LKERgvpLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenppp 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564392038 221 SHRETRCVDKSLP---VLLAdpVLCAIAKKYNWTPALIALRYQLERGVVVL--AKSftEKRIKENMQ 282
Cdd:cd19093 216 GGRRRLFGRKNLEkvqPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIpgAKN--AEQAEENAG 278
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-280 |
1.01e-34 |
|
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: 126.87 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYA-----PREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIFYTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 VWCTFNHPERVQVCL---------EQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCK 155
Cdd:cd19084 74 CGLRWDGGKGVTKDLspesirkevEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 156 DAGLAKSIGVSNFNRRQLEKIlnkpgLKHRP-VCNQVechPY--LNQ---RKLLDFCKSKDIVLVAYSAL------GSHR 223
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEA-----RKYGPiVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLaqglltGKYK 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564392038 224 ETRCVDKS--------------LPVLLADPVLCAIAKKYNWTPALIALRYQLER-GV-VVLAKSFTEKRIKEN 280
Cdd:cd19084 207 KEPTFPPDdrrsrfpffrgenfEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEEN 279
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-282 |
3.20e-34 |
|
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: 125.78 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGT------YAPREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVW 86
Cdd:cd19085 1 VSRLGLGCwqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 CTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALkpeedlkakdenekllfdvVDICDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-------------------VPLEETMEALEKLKEEGKIRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 NFNRRQLEKILnKPGlkhRPVCNQVechPY-LNQR----KLLDFCKSKDIVLVAYSALGS-------------------- 221
Cdd:cd19085 135 NFGPAQLEEAL-DAG---RIDSNQL---PYnLLWRaieyEILPFCREHGIGVLAYSPLAQglltgkfssaedfppgdart 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564392038 222 ----HRETRCVDKSLPVLladPVLCAIAKKYNWTPALIALRYQLERGVV--VLAKSFTEKRIKENMQ 282
Cdd:cd19085 208 rlfrHFEPGAEEETFEAL---EKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAA 271
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-221 |
2.74e-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: 118.78 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTYA-PREVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtVKREDIFYTSKVWCTF--- 89
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 -----NHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGLAKSIG 164
Cdd:cd06660 76 psrsrLSPEHIRRDLEESLRRLGTDYIDLYYLHRD------------DPS-------TPVEETLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564392038 165 VSNFNRRQLEKILN--KPGLKHRPVCNQVE---CHPYLNQRKLLDFCKSKDIVLVAYSALGS 221
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-257 |
6.17e-24 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 98.01 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 18 VLGFGTYAPREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgTVKREDIFYTSKvwC------- 87
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTK--Cgirlgdd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 ----TFNH----PERVQVCLEQSLKQLQLEYVDLYLIHFPMAL-KPEEdlkakdenekllfdvvdicdTWKAMEKCKDAG 158
Cdd:cd19092 84 prpgRIKHydtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPLmDPEE--------------------VAEAFDELVKSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 159 LAKSIGVSNFNRRQLEkILNKpGLKHRPVCNQVEC---HPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPVL 235
Cdd:cd19092 144 KVRYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRL 221
|
250 260
....*....|....*....|..
gi 564392038 236 LAdpVLCAIAKKYNWTPALIAL 257
Cdd:cd19092 222 RA--ALEELAEEYGVTIEAIAL 241
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-269 |
1.09e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 97.74 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYA---------PREVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvkREDIFYTS 83
Cdd:cd19102 1 LTTIGLGTWAiggggwgggWGPQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 84 K---VWCTFNH------PERVQVCLEQSLKQLQLEYVDLYLIHFPmalKPEEDLKakdenekllfdvvdicDTWKAMEKC 154
Cdd:cd19102 74 KcglLWDEEGRirrslkPASIRAECEASLRRLGVDVIDLYQIHWP---DPDEPIE----------------EAWGALAEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 155 KDAGLAKSIGVSNFNRRQLEKIL-------NKPG--LKHRPVcnqvechpylnQRKLLDFCKSKDIVLVAYSALGS---- 221
Cdd:cd19102 135 KEEGKVRAIGVSNFSVDQMKRCQaihpiasLQPPysLLRRGI-----------EAEILPFCAEHGIGVIVYSPMQSgllt 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564392038 222 HRETRCVDKSLPV--------LLADP----------VLCAIAKKYNWTPALIALRYQLERGVVVLA 269
Cdd:cd19102 204 GKMTPERVASLPAddwrrrspFFQEPnlarnlalvdALRPIAERHGRTVAQLAIAWVLRRPEVTSA 269
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
31-257 |
4.09e-23 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 95.99 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 31 KSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgTVKREDIFYTSKvwC-----------TFNH----P 92
Cdd:COG4989 30 PAEAAALIEAALELGITTFDHADIYggyTCEALFGEALKLS----PSLREKIELQTK--CgirlpseardnRVKHydtsK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 93 ERVQVCLEQSLKQLQLEYVDLYLIHFPMAL-KPEEdlkakdenekllfdvvdicdTWKAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:COG4989 104 EHIIASVEGSLRRLGTDYLDLLLLHRPDPLmDPEE--------------------VAEAFDELKASGKVRHFGVSNFTPS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 172 QLEkILNKpGLKHRPVCNQVECHPyLNQRKL----LDFCKSKDIVLVAYSALGSHRETRCVDKSLPVLLAdpVLCAIAKK 247
Cdd:COG4989 164 QFE-LLQS-ALDQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEK 238
|
250
....*....|
gi 564392038 248 YNWTPALIAL 257
Cdd:COG4989 239 YGVSPEAIAL 248
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-269 |
9.73e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 93.70 E-value: 9.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYAPREVPKSKALEATKIAIDAGFRHIDSAAVYQN-EKEVGLAIRSKiadgtvkREDIFYTSKVWCTfnH 91
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGAR--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 PERVQVCLEQSLKQLQLEYVDLYLIHfpmALKPEEDL-KAKDENEkllfdvvdicdTWKAMEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19100 79 YEGAKRDLERSLKRLGTDYIDLYQLH---AVDTEEDLdQVFGPGG-----------ALEALLEAKEEGKIRFIGISGHSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 171 RQLEKILNKPglkhrpvcnqvechpylnqrkllDFckskDIVLVAYSALGSHRET-------RCVDKSLPVL----LADP 239
Cdd:cd19100 145 EVLLRALETG-----------------------EF----DVVLFPINPAGDHIDSfreellpLAREKGVGVIamkvLAGG 197
|
250 260 270
....*....|....*....|....*....|
gi 564392038 240 VLCAIAKKynwTPALiALRYQLERGVVVLA 269
Cdd:cd19100 198 RLLSGDPL---DPEQ-ALRYALSLPPVDVV 223
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-282 |
1.55e-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: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 19 LGFGTY--APREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKIADGTVKREDIFYTSKV-WCTFN-- 90
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgYIPGDgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 91 ------------------------------HPERVQVCLEQSLKQLQLEYVDLYLIHfpmalKPEEDLKAKDENEklLFD 140
Cdd:cd19099 86 eplrplkyleeklgrglidvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLH-----NPEEQLLELGEEE--FYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 141 VVDicDTWKAMEKCKDAGLAKSIGVSNFN------------------RRQLEKILNKPGLKH-----RPVCNQVECHPYL 197
Cdd:cd19099 159 RLE--EAFEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKViqlplNLLEPEALTEKNT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 198 NQRK---LLDFCKSKDIVLVAYSALGSHRETRcvdkslPVLLADPVlcaiAKKYNWTPALIALRYQLE-RGV-VVLAKSF 272
Cdd:cd19099 237 VKGEalsLLEAAKELGLGVIASRPLNQGQLLG------ELRLADLL----ALPGGATLAQRALQFARStPGVdSALVGMR 306
|
330
....*....|
gi 564392038 273 TEKRIKENMQ 282
Cdd:cd19099 307 RPEHVDENLA 316
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-282 |
1.12e-20 |
|
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: 88.43 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGT--------YAPREvPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKIAD-------GTVKRE 77
Cdd:cd19088 1 VSRLGYGAmrltgpgiWGPPA-DREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYPDDvviatkgGLVRTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 78 DifytsKVWCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakdenekllFDVVDICDTWKAMEKCKDA 157
Cdd:cd19088 80 P-----GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI-------------------DPKVPFEEQLGALAELQDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 158 GLAKSIGVSNFNRRQLEKILNKPGLkhrpVCNQVECHPYlNQR--KLLDFCKSKDIVLVAYSALGSHretrcvdkslPVL 235
Cdd:cd19088 136 GLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLA-NRDdeGVLDYCEAAGIAFIPWFPLGGG----------DLA 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564392038 236 LADPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEK--RIKENMQ 282
Cdd:cd19088 201 QPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSveHLEENLA 249
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-261 |
2.83e-20 |
|
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: 87.99 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTY----APREVPKSKALEATKIAIDAGFRHIDSAAVYQN-EKEVGLAIRskiadgTVKREDIFYTSKVWC---- 87
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKVGRlped 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNH-PERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLkAKDEnekllfdVVDicdtwkAMEKCKDAGLAKSIGVS 166
Cdd:cd19090 75 TADYsADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIL-APGG-------ALE------ALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 nfnrrqlekiLNKPGLkHRPVCNQVEC------HPY--LNQ---RKLLDFCKSKDIVLVAYSALGS-------HRETRCV 228
Cdd:cd19090 141 ----------GGPPDL-LRRAIETGDFdvvltaNRYtlLDQsaaDELLPAAARHGVGVINASPLGMgllagrpPERVRYT 209
|
250 260 270
....*....|....*....|....*....|....*
gi 564392038 229 DKSLPVLLADPV--LCAIAKKYNWTPALIALRYQL 261
Cdd:cd19090 210 YRWLSPELLDRAkrLYELCDEHGVPLPALALRFLL 244
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-281 |
6.00e-20 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 87.88 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRLS-DGHFIPVLGFGT------YAPREvPKSKALEATKIAIDAGFRHIDSAAVYQ-NEKEVGLAIrsKIADGtvKRE 77
Cdd:cd19144 2 PTRTLGrNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWF--KQNPG--KRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 78 DIFYTSKV----------WCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHfpmALKPEedlkakdenekllfdvVDICDT 147
Cdd:cd19144 77 KIFLATKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH---RVDGK----------------TPIEKT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 148 WKAMEKCKDAGLAKSIGVSNFNRRQLEKilnkpGLKHRPVCN-QVECHPYL-----NQRKLLDFCKSKDIVLVAYSAL-- 219
Cdd:cd19144 138 VAAMAELVQEGKIKHIGLSECSAETLRR-----AHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLgr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 220 ----GSHR-----ETRCVDKSLP----------VLLADPvLCAIAKKYNWTPALIALRYQLERG--VVVLAKSFTEKRIK 278
Cdd:cd19144 213 gfltGAIRspddfEEGDFRRMAPrfqaenfpknLELVDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLE 291
|
...
gi 564392038 279 ENM 281
Cdd:cd19144 292 ENL 294
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-166 |
1.48e-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: 85.33 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFGTYA-PREVPKskALEAtkiAIDAGFRHIDSAAVYQN---EKEVGLAIRskiadgTVKREDIFYTSKVWCT 88
Cdd:cd19105 10 GLKVSRLGFGGGGlPRESPE--LLRR---ALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 89 FNH--PERVQVCLEQSLKQLQLEYVDLYLIHfpMALKPEEDLKakdeNEKLLfdvvdicdtwKAMEKCKDAGLAKSIGVS 166
Cdd:cd19105 79 LDKkdKAELLKSVEESLKRLQTDYIDIYQLH--GVDTPEERLL----NEELL----------EALEKLKKEGKVRFIGFS 142
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
2.21e-19 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 84.98 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTY----APREVPKSKALEATKIAIDAGFRHIDSAAVYQN-EKEVGLAIRskiadgTVKREDIFYTSKVWCTFNH 91
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 PERVQVC--------LEQSLKQLQLEYVDLYLIHFPmalkPEEDLKAkdenekllfDVVDicdtwkAMEKCKDAGLAKSI 163
Cdd:cd19095 75 GRDRKDFspaairasIERSLRRLGTDYIDLLQLHGP----SDDELTG---------EVLE------TLEDLKAAGKVRYI 135
|
....*.
gi 564392038 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-283 |
5.89e-19 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 85.64 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGT-YAPRevpKSKAlEATKI---AIDAGFRHIDSAAVY-QNEKEVGLAIRSKiadgtvkREDIFYTSKVWCTFN 90
Cdd:COG1453 13 VSVLGFGGmRLPR---KDEE-EAEALirrAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 91 HPERVQVCLEQSLKQLQLEYVDLYLIHfpmALKPEEDL-KAKDENEkllfdvvdicdTWKAMEKCKDAGLAKSIGVSNFN 169
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIH---GLNTEEDLeKVLKPGG-----------ALEALEKAKAEGKIRHIGFSTHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 170 RRQ-LEKILNKpglkhrpvcNQVEC----HPYLNQR-----KLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvlLADP 239
Cdd:COG1453 148 SLEvIKEAIDT---------GDFDFvqlqYNYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR------------LANP 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 564392038 240 --VLCAIAKKyNWTPALIALRY--QLERGVVVLAKSFTEKRIKENMQI 283
Cdd:COG1453 207 peKLVELLCP-PLSPAEWALRFllSHPEVTTVLSGMSTPEQLDENLKT 253
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-219 |
2.32e-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: 83.13 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 33 KALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRskiadGTVKREDIFYTSKV---W------CTFNHPERVQVCLE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALK-----EYGKRDRVVIATKVgleWdeggevVRNSSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 101 QSLKQLQLEYVDLYLIHFPMALKPEEdlkakdenekllfdvvdicDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKIlnkp 180
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPLVPIE-------------------ETAEALKELLDEGKIRAIGVSNFSPEQMETF---- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564392038 181 glkhRPVCNQVECHPYLN------QRKLLDFCKSKDIVLVAYSAL 219
Cdd:cd19148 158 ----RKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
39-221 |
2.49e-18 |
|
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: 82.85 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 39 KIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvKREDIFYTSKVWCTF--------NHPERVQVCLEQSLKQLQ 107
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFggdgsvlnNSPEFLRSAVEKSLKRLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 108 LEYVDLYLIHFPmalkpeedlkakdENEKLLFDVVDicdtwkAMEKCKDAGLAKSIGVSNFNRRQLeKILNKPGlkhrpv 187
Cdd:cd19083 114 TDYIDLYYIHFP-------------DGETPKAEAVG------ALQELKDEGKIRAIGVSNFSLEQL-KEANKDG------ 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564392038 188 cnQVEC--HPY-LNQRK----LLDFCKSKDIVLVAYSALGS 221
Cdd:cd19083 168 --YVDVlqGEYnLLQREaeedILPYCVENNISFIPYFPLAS 206
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-221 |
2.69e-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: 81.75 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYA-----PREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVWC 87
Cdd:cd19086 3 VSEIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNH---------PERVQVCLEQSLKQLQLEYVDLYLIHFPmalkPEEDLKAKdenekllfdvvdicDTWKAMEKCKDAG 158
Cdd:cd19086 76 RFDGgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNP----PDEVLDND--------------ELFEALEKLKQEG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564392038 159 LAKSIGVSNFNRRQLEKILnkpglkHRPVCNQVEcHPY--LNQR---KLLDFCKSKDIVLVAYSALGS 221
Cdd:cd19086 138 KIRAYGVSVGDPEEALAAL------RRGGIDVVQ-VIYnlLDQRpeeELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-219 |
4.24e-18 |
|
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: 82.32 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYA------PREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIFYTSK-- 84
Cdd:cd19149 11 ASVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 -VWCT----FNH------------PERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPeedlkakdenekllfdvvdICDT 147
Cdd:cd19149 84 lRWDReggsFFFvrdgvtvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQDVETP-------------------IEET 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 148 WKAMEKCKDAGLAKSIGVSNFNRRQLEKILNkpglkhrpvCNQVEchpyLNQRK-----------LLDFCKSKDIVLVAY 216
Cdd:cd19149 145 MEALEELKRQGKIRAIGASNVSVEQIKEYVK---------AGQLD----IIQEKysmldrgiekeLLPYCKKNNIAFQAY 211
|
...
gi 564392038 217 SAL 219
Cdd:cd19149 212 SPL 214
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
36-267 |
7.27e-18 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 81.86 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 36 EATKI---AIDAGFRHIDSAAVYQN---EKEVGLAIRSKIadgtvKREDIFYTSKVwctfNHPER------------VQV 97
Cdd:cd19079 36 ESRPIikrALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKV----YFPMGdgpngrglsrkhIMA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 98 CLEQSLKQLQLEYVDLYLIHFPMALKP-EEDLKAkdeneklLFDVVdicdtwkamekckDAGLAKSIGVSNFNRRQLEKI 176
Cdd:cd19079 107 EVDASLKRLGTDYIDLYQIHRWDYETPiEETLEA-------LHDVV-------------KSGKVRYIGASSMYAWQFAKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 177 LN---KPGLkHRPVCNQvechPYLN------QRKLLDFCKSKDIVLVAYSALGSHR---------ETRCVDKSLPVLLAD 238
Cdd:cd19079 167 LHlaeKNGW-TKFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRlarpwgdttERRRSTTDTAKLKYD 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 564392038 239 -------PVLCA---IAKKYNWTPALIALRYQLERGVVV 267
Cdd:cd19079 242 yfteadkEIVDRveeVAKERGVSMAQVALAWLLSKPGVT 280
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-282 |
7.40e-18 |
|
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: 81.89 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 13 GHFIPVLGFG--TYAPREVPKSK-----ALEAT---KIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvkREDI 79
Cdd:cd19091 10 GLKVSELALGtmTFGGGGGFFGAwggvdQEEADrlvDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 80 FYTSKVwcTFNHPERV-----------QVClEQSLKQLQLEYVDLYLIHFPMALKP-EEDLKAKDenekllfDVVdicdt 147
Cdd:cd19091 83 LIATKV--RGRMGEGPndvglsrhhiiRAV-EASLKRLGTDYIDLYQLHGFDALTPlEETLRALD-------DLV----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 148 wkamekckDAGLAKSIGVSNFNRRQLEKIL---NKPGLKhRPVCNQVechpYLN------QRKLLDFCKSKDIVLVAYSA 218
Cdd:cd19091 148 --------RQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 219 LGSHR-------------ETRCVDKSLPVLLADP--------VLCAIAKKYNWTPALIALRYQLER----GVVVLAKSft 273
Cdd:cd19091 215 LAGGLlsgkyrrgqpapeGSRLRRTGFDFPPVDRergydvvdALREIAKETGATPAQVALAWLLSRptvsSVIIGARN-- 292
|
....*....
gi 564392038 274 EKRIKENMQ 282
Cdd:cd19091 293 EEQLEDNLG 301
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-283 |
1.43e-16 |
|
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: 77.22 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTY-APREVPKSKALE-ATKI---AIDAGFRHIDSAAVY---QNEKEVGLAIRskiadgTVKREDIFYTSK--VW 86
Cdd:cd19096 1 SVLGFGTMrLPESDDDSIDEEkAIEMiryAIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKlpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 cTFNHPERVQVCLEQSLKQLQLEYVDLYLIHfpMALKPEEDLKAKDenekllfdvvdiCDTWKAMEKCKDAGLAKSIGVS 166
Cdd:cd19096 75 -SVKSAEDFRRILEESLKRLGVDYIDFYLLH--GLNSPEWLEKARK------------GGLLEFLEKAKKEGLIRHIGFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 167 nF--NRRQLEKILNkpglkhrpvCNQVEC----HPYLNQ-----RKLLDFCKSKDIVLVAYSALGSHRetrcvdkslpvL 235
Cdd:cd19096 140 -FhdSPELLKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVIIMEPLKGGG-----------L 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564392038 236 LADP-VLCAIAKKYNWTPALIALRYQLERG---VVVLAKSfTEKRIKENMQI 283
Cdd:cd19096 199 ANNPpEALAILCGAPLSPAEWALRFLLSHPevtTVLSGMS-TPEQLDENIAA 249
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-219 |
1.69e-16 |
|
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: 77.63 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYAP--REVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRskiadgTVKREDIFYTSKV-WCTF 89
Cdd:cd19074 4 VSELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALK------GWPRESYVISTKVfWPTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 NHPE-----RVQV--CLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGLAKS 162
Cdd:cd19074 78 PGPNdrglsRKHIfeSIHASLKRLQLDYVDIYYCHRY------------DPE-------TPLEETVRAMDDLIRQGKILY 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564392038 163 IGVSNFNRRQLEKILN--KPGLKHRPVCNQVECHpYLNQRK---LLDFCKSKDIVLVAYSAL 219
Cdd:cd19074 139 WGTSEWSAEQIAEAHDlaRQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPL 199
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-281 |
2.09e-16 |
|
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: 77.64 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 42 IDAGFRHIDSAAVY----------QNEKEVGLAIRSKiadgtVKREDIFYTSKV--WCTFNHP----ERVQVCLEQSLKQ 105
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSR-----GKRDRVVIATKVgfPMGPNGPglsrKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 106 LQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKILN---KPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------------DPA-------TPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 183 KhRPVCNQVEchpY-LNQRK-----LLDFCKSKDIVLVAYSALGS------HRETRCVDKSLPV-----LLADP------ 239
Cdd:cd19081 172 P-RYVSLQPE---YnLVDREsfegeLLPLCREEGIGVIPYSPLAGgfltgkYRSEADLPGSTRRgeaakRYLNErglril 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564392038 240 -VLCAIAKKYNWTPALIALRYQLERGVV--VLAKSFTEKRIKENM 281
Cdd:cd19081 248 dALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLL 292
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-267 |
3.40e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 74.17 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 9 RLSDGHfipvlgfgTYAPREvpkSKALEATKIAIDAGFRHIDSAAVYQNEKE-VGLAIRSKIADGTVKREDIFYTSkvWC 87
Cdd:cd19101 11 QLSGGH--------GGIRDE---DAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHTK--WV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 88 TFNHPER-----VQVCLEQSLKQLQLEYVDLYLIHFpmalkpeEDlkakdenekllFDVVDICDTWKAMEKCKDAGLAKS 162
Cdd:cd19101 78 PDPGELTmtrayVEAAIDRSLKRLGVDRLDLVQFHW-------WD-----------YSDPGYLDAAKHLAELQEEGKIRH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 163 IGVSNFNRRQLEKILNKPGlkhRPVCNQVEcHPYLNQR---KLLDFCKSKDIVLVAYSALG----SHR------------ 223
Cdd:cd19101 140 LGLTNFDTERLREILDAGV---PIVSNQVQ-YSLLDRRpenGMAALCEDHGIKLLAYGTLAggllSEKylgvpeptgpal 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 224 ETRCVDKSLPV------------LLAdpVLCAIAKKYNWTPALIALRYQLER----GVVV 267
Cdd:cd19101 216 ETRSLQKYKLMidewggwdlfqeLLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIV 273
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-220 |
4.82e-15 |
|
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: 73.35 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTyAP-----REVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRskiadgTVKREDIF------- 80
Cdd:cd19163 13 VSKLGFGA-SPlggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYlatkvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 81 YTSKVWCTFNH-PERVQVCLEQSLKQLQLEYVDLYLIHfpmalkpeeDLKAKDeneklLFDVVdICDTWKAMEKCKDAGL 159
Cdd:cd19163 86 YGLDPDKMFDFsAERITKSVEESLKRLGLDYIDIIQVH---------DIEFAP-----SLDQI-LNETLPALQKLKEEGK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564392038 160 AKSIGVSNFNRRQLEKILNKpglkhrpVCNQVE-----CHPYLNQR---KLLDFCKSKDIVLVAYSALG 220
Cdd:cd19163 151 VRFIGITGYPLDVLKEVLER-------SPVKIDtvlsyCHYTLNDTsllELLPFFKEKGVGVINASPLS 212
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-259 |
1.12e-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: 72.17 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 36 EATKI---AIDAGFRHIDSAAVYQN-EKEVGLAIRSKiadgtvkrEDIFYTSKV----WCTFNHPERVQVCLEQSLKQLQ 107
Cdd:cd19097 27 EAKKIleyALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 108 LEYVDLYLIHFPmalkpeEDLKAKDEnekllfdvvdicDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGLKHrpV 187
Cdd:cd19097 99 VDSLDGLLLHNP------DDLLKHGG------------KLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 188 cnQVechPY--LNQR----KLLDFCKSKDIVLVAYSAL--GshretrcvdkslpVLLADPV---------------LCAI 244
Cdd:cd19097 159 --QL---PFniLDQRflksGLLAKLKKKGIEIHARSVFlqG-------------LLLMEPDklpakfapakpllkkLHEL 220
|
250
....*....|....*
gi 564392038 245 AKKYNWTPALIALRY 259
Cdd:cd19097 221 AKKLGLSPLELALGF 235
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-266 |
2.66e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 68.51 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 41 AIDAGFRHIDSAAVY---QNEKEVGLAIRskiadgTVKREDIFYTSKV--WCTFNHPERVQVCLEQSLKQLQLEYVDLYL 115
Cdd:cd19103 41 AMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 116 IHFPMalkpeeDLkakdenEKLLFDVVDIcdtwkamekcKDAGLAKSIGVSNFNRRQLEK---ILNKPGLKHRPVCNqve 192
Cdd:cd19103 115 IHNPA------DV------ERWTPELIPL----------LKSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 193 cHPYLNQRK-----LLDFCKSKDIVLVAYSAL-----------------GSHR-ETrcVDKSLPVLLA-DPVLCAIAKKY 248
Cdd:cd19103 170 -HYSLLYRSseeagILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRaET--YNPLLPQLEElTAVMAEIGAKH 246
|
250
....*....|....*...
gi 564392038 249 NWTPALIALRYQLERGVV 266
Cdd:cd19103 247 GASIAQVAIAWAIAKGTT 264
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
6-220 |
3.37e-13 |
|
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: 68.40 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 6 QTVRL-SDGHFIPVLGFGT------YAPREVPKSKALeaTKIAIDAGFRHIDSAAVYQ---NEKEVGLAIRSKiadgtvk 75
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGCmgmsafYGPADEEESIAT--LHRALELGVTFLDTADMYGpgtNEELLGKALKDR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 76 REDIFYTSK---VWCTF-------NHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDIC 145
Cdd:cd19076 72 RDEVVIATKfgiVRDPGsgfrgvdGRPEYVRAACEASLKRLGTDVIDLYYQHRV------------DPN-------VPIE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 146 DTWKAMEKCKDAGLAKSIGVSNFNRRQLEKilnkpglKHR--PVCN-QVEchpY-LNQR----KLLDFCKSKDIVLVAYS 217
Cdd:cd19076 133 ETVGAMAELVEEGKVRYIGLSEASADTIRR-------AHAvhPITAvQSE---YsLWTRdiedEVLPTCRELGIGFVAYS 202
|
...
gi 564392038 218 ALG 220
Cdd:cd19076 203 PLG 205
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-263 |
4.25e-13 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 68.36 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 36 EATKI---AIDAGFRHIDSAAVY----------QNEKEVGLAIRSKiadgtVKREDIFYTSKV-----WCTFNH------ 91
Cdd:cd19094 19 EAHEQldyAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKK-----GNRDKVVLATKVagpgeGITWPRgggtrl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 -PERVQVCLEQSLKQLQLEYVDLYLIHFP---MALKPEEDLKAKDENEkllfDVVDICDTWKAMEKCKDAGLAKSIGVSN 167
Cdd:cd19094 94 dRENIREAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE----DSVSFEEQLEALGELVKAGKIRHIGLSN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 168 --------FNRrqLEKILNKPglkhRPVCNQvecHPY--LNQRKLLDF---CKSKDIVLVAYSALG-------------- 220
Cdd:cd19094 170 etpwgvmkFLE--LAEQLGLP----RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAggvltgkyldgaar 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564392038 221 ---------SHRETRCvdKSLPVLLADPVLCAIAKKYNWTPALIALRYQLER 263
Cdd:cd19094 241 peggrlnlfPGYMARY--RSPQALEAVAEYVKLARKHGLSPAQLALAWVRSR 290
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-221 |
1.74e-11 |
|
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: 63.15 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTYA---PREVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvKREDIFYTSKVWCTFN 90
Cdd:cd19162 1 PRLGLGAASlgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 91 HPE----------------RVQVCLEQSLKQLQLEYVDLYLIHFPmalkPEEDLKAkdenekllfdvvdICDTWKAMEKC 154
Cdd:cd19162 75 PGAagrpagadrrfdfsadGIRRSIEASLERLGLDRLDLVFLHDP----DRHLLQA-------------LTDAFPALEEL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 155 KDAGLAKSIGVSNFNRRQLEKILNKPGLKHRPVCNQvecHPYLNQR---KLLDFCKSKDIVLVAYSALGS 221
Cdd:cd19162 138 RAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVFNS 204
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
36-220 |
4.81e-11 |
|
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: 62.20 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 36 EATKI---AIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVWC-TFNHPER--------VQVClE 100
Cdd:cd19087 31 TSFAImdrALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFGpMGDDPNDrglsrrhiRRAV-E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 101 QSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKILNKP 180
Cdd:cd19087 103 ASLRRLQTDYIDLYQMHHF------------DRD-------TPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564392038 181 GLKH--RPVCNQvecHPY-LNQR----KLLDFCKSKDIVLVAYSALG 220
Cdd:cd19087 164 ARRGllRFVSEQ---PMYnLLKRqaelEILPAARAYGLGVIPYSPLA 207
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-221 |
8.49e-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: 61.42 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 18 VLGFGT--YAPREVPKSKALEATKIAIDAGFRHIDSAAVYQ-----------NEKEVGLAIRSKIADGTVKRedifytsk 84
Cdd:cd19075 4 ILGTMTfgSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPdgtseellgelGLGERGFKIDTKANPGVGGG-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 vwctfNHPERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGLAKSIG 164
Cdd:cd19075 76 -----LSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DRS-------TPLEETLAAIDELYKEGKFKEFG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564392038 165 VSNFNRRQLEKILN--------KP----GLkHRPVCNQVEchpylnqRKLLDFCKSKDIVLVAYSALGS 221
Cdd:cd19075 132 LSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-261 |
8.82e-11 |
|
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: 61.51 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 34 ALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvkREDIFYTSKVWCTFNHPE----RVQVCLEQSLKQL 106
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 107 QLEYVDLYLIHfpMALKPEEDLKAKDENEKLLFDVVDicDTWKAMEKCKDAGLAKSIGVSnfnrrqlekilnkpGLKHRP 186
Cdd:cd19104 107 KRDSVDLLQLH--NRIGDERDKPVGGTLSTTDVLGLG--GVADAFERLRSEGKIRFIGIT--------------GLGNPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 187 VCNQVECH--------PY--LNQ---------------RKLLDFCKSKDIVLVAYSALGS---------HRE---TRCVD 229
Cdd:cd19104 169 AIRELLDSgkfdavqvYYnlLNPsaaearprgwsaqdyGGIIDAAAEHGVGVMGIRVLAAgalttsldrGREappTSDSD 248
|
250 260 270
....*....|....*....|....*....|..
gi 564392038 230 KSLPVLLADPVLcAIAKKYNWTPALIALRYQL 261
Cdd:cd19104 249 VAIDFRRAAAFR-ALAREWGETLAQLAHRFAL 279
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-282 |
4.21e-10 |
|
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: 59.10 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGT-YAPREVPKSKALEATKIAIDAGFRHIDSAAVYQN-------EKEVGLAIRSKIadgtvKREDIFYTSK---- 84
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwvergasERVIGEWLKSRG-----NRDKVVIATKgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 VWCTFN----HPERVQVCLEQSLKQLQLEYVDLYLIHfpmalkpeedlkaKDENEKllfDVVDICDTwkaMEKCKDAGLA 160
Cdd:cd19082 76 DLEDMSrsrlSPEDIRADLEESLERLGTDYIDLYFLH-------------RDDPSV---PVGEIVDT---LNELVRAGKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 161 KSIGVSNFNrrqLEKIL--NKPGLKH---RPVCNQV---------ECHP-----YLNQrKLLDFCKSKDIVLVAYSALGS 221
Cdd:cd19082 137 RAFGASNWS---TERIAeaNAYAKAHglpGFAASSPqwslarpnePPWPgptlvAMDE-EMRAWHEENQLPVFAYSSQAR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 222 ---HRETRCVDKSLPVLLAD----------PVLCAIAKKYNWTPALIALRYqlergvvVLAKSF---------TEKRIKE 279
Cdd:cd19082 213 gffSKRAAGGAEDDSELRRVyyseenferlERAKELAEEKGVSPTQIALAY-------VLNQPFptvpiigprTPEQLRD 285
|
...
gi 564392038 280 NMQ 282
Cdd:cd19082 286 SLA 288
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
4.60e-10 |
|
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: 59.16 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTyAP-----REVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvKREDIFYTSKV--- 85
Cdd:cd19152 1 PKLGFGT-APlgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 ---------------WCTFNHpERVQV--------CLEQSLKQLQLEYVDLYLIHfpmalKPEEDLkAKDENEKLLFDvv 142
Cdd:cd19152 74 lvplqeveptfepgfWNPLPF-DAVFDysydgilrSIEDSLQRLGLSRIDLLSIH-----DPDEDL-AGAESDEHFAQ-- 144
|
170 180
....*....|....*....|...
gi 564392038 143 DICDTWKAMEKCKDAGLAKSIGV 165
Cdd:cd19152 145 AIKGAFRALEELREEGVIKAIGL 167
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-192 |
3.57e-09 |
|
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: 56.45 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 18 VLGFG---TYApREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRskiaDGTVKREDIFYTSKVWCTFNH 91
Cdd:cd19143 15 ALSFGswvTFG-NQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIFWGGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 PERVQVCL---------EQSLKQLQLEYVDLYLIHFPMALKPEEdlkakdenekllfdvvdicDTWKAMEKCKDAGLAKS 162
Cdd:cd19143 90 PPPNDRGLsrkhivegtKASLKRLQLDYVDLVFCHRPDPATPIE-------------------ETVRAMNDLIDQGKAFY 150
|
170 180 190
....*....|....*....|....*....|...
gi 564392038 163 IGVSNFNRRQLEK---ILNKPGLkHRPVCNQVE 192
Cdd:cd19143 151 WGTSEWSAQQIEEaheIADRLGL-IPPVMEQPQ 182
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-280 |
6.60e-09 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 55.70 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 19 LGFG----TYAPREVP-KSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKiadgtvkREDIFYTSKVWCTFN 90
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 91 H-----------PERVQVCLEQSLKQLQLEYVDLYLIHFPmalkpeedlkakDENekllfdvVDICDTWKAMEKCKDAGL 159
Cdd:cd19078 80 GgkpgplgldsrPEHIRKAVEGSLKRLQTDYIDLYYQHRV------------DPN-------VPIEEVAGTMKELIKEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 160 AKSIGVS----NFNRRQ-----LEKILNKPGLKHRpvcnqvecHPylnQRKLLDFCKSKDIVLVAYSALGSHRETRCVDK 230
Cdd:cd19078 141 IRHWGLSeagvETIRRAhavcpVTAVQSEYSMMWR--------EP---EKEVLPTLEELGIGFVPFSPLGKGFLTGKIDE 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564392038 231 -----------SLP-----------VLLAdpVLCAIAKKYNWTPALIALRYQLERG--VVVLAKSFTEKRIKEN 280
Cdd:cd19078 210 ntkfdegddraSLPrftpealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEEN 281
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-282 |
6.98e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 55.42 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 42 IDAGFRHIDSAAVY----------QNEKEVG--LAIRSKiadgtvkREDIFYTSKVWCTFNHP------------ERVQV 97
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGrwLKDRGN-------RDDVVIATKVGAGPRDPdggpespeglsaETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 98 CLEQSLKQLQLEYVDLYLIHfpmalkpeedlkAKDENekllfdvVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEK-- 175
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAH------------VDDRD-------TPLEETLEAFNELVKAGKVRAIGASNFAAWRLERar 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 176 -ILNKPGLkHRPVCNQVEcHPYL---------NQR----KLLDFCKS-KDIVLVAYSALGSHRETRcVDKSLPVLLADP- 239
Cdd:cd19752 161 qIARQQGW-AEFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLLSGAYTR-PDRPLPEQYDGPd 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564392038 240 ------VLCAIAKKYNWTPALIALRYQLER--GVVVLAKSFTEKRIKENMQ 282
Cdd:cd19752 238 sdarlaVLEEVAGELGATPNQVVLAWLLHRtpAIIPLLGASTVEQLEENLA 288
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
7-264 |
1.01e-08 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 55.13 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 7 TVRL-SDGHFIPVLGFG------TYAPrEVPKSKALEATKIAIDAGFRHIDSAAVY---QNEKEVGLAIRSKIadgtvkR 76
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGcmglsgDYGA-PKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 77 EDIFYTSKVWCTF---------NHPERVQVCLEQSLKQLQLEYVDLYLIHfpmalkpEEDLKakdenekllfdvVDICDT 147
Cdd:cd19145 75 EKVQLATKFGIHEiggsgvevrGDPAYVRAACEASLKRLDVDYIDLYYQH-------RIDTT------------VPIEIT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 148 WKAMEKCKDAGLAKSIGVSNFN----RR----------QLEKilnkpGLKHRPVcnqvechpylnQRKLLDFCKSKDIVL 213
Cdd:cd19145 136 MGELKKLVEEGKIKYIGLSEASadtiRRahavhpitavQLEW-----SLWTRDI-----------EEEIIPTCRELGIGI 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564392038 214 VAYSALG-----------SHRETRCVDKSLPVLLADPV---------LCAIAKKYNWTPALIALRYQLERG 264
Cdd:cd19145 200 VPYSPLGrgffagkakleELLENSDVRKSHPRFQGENLeknkvlyerVEALAKKKGCTPAQLALAWVLHQG 270
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
1.99e-08 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 54.19 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 20 GFGTYAPREVPKSKALEAtkiaIDAGFRHIDSAAVY-----QNEKEVGLAIRSkiaDGTVKREDIFYTSKV--------- 85
Cdd:cd19089 21 NFGDYTSPEEARELLRTA----FDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVISTKAgygmwpgpy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 --WCTFNHperVQVCLEQSLKQLQLEYVDLYLIHFPMALKP-EEDLKAkdeneklLFDVVdicdtwkamekckDAGLAKS 162
Cdd:cd19089 94 gdGGSRKY---LLASLDQSLKRMGLDYVDIFYHHRYDPDTPlEETMTA-------LADAV-------------RSGKALY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 163 IGVSNFNRRQLEK---ILNKpgLKHRPVCNQVechPY--LNQ---RKLLDFCKSKDIVLVAYSAL--------------G 220
Cdd:cd19089 151 VGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylngipP 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564392038 221 SHRETRCVDKSLPVLLADPV------LCAIAKKYNWTPALIALRYQLERGVV 266
Cdd:cd19089 226 DSRRAAESKFLTEEALTPEKleqlrkLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-282 |
4.99e-08 |
|
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: 53.01 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 20 GFG----TYAPREVPKSKALEATKIAIDAGFRHIDSAAVY------QNEKEVG--LAIRSKIADG---TVKREDIFYTSK 84
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLArfFRKYPEYADKvvlSVKGGLDPDTLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 85 VWCTfnhPERVQVCLEQSLKQL-QLEYVDLYlihfpmalkpeeDLKAKDENekllfdvVDICDTWKAMEKCKDAGLAKSI 163
Cdd:cd19077 89 PDGS---PEAVRKSIENILRALgGTKKIDIF------------EPARVDPN-------VPIEETIKALKELVKEGKIRGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 164 GVSNFNRRQLEKILNKpglkHRPVCNQVECHPYLN---QRKLLDFCKSKDIVLVAYSALGS------------------- 221
Cdd:cd19077 147 GLSEVSAETIRRAHAV----HPIAAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRglltgriksladipegdfr 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 222 ------HRETrcVDKSLPvlLADpVLCAIAKKYNWTPALIAL---RYQLERGVVVLAKSFTEKRIKENMQ 282
Cdd:cd19077 223 rhldrfNGEN--FEKNLK--LVD-ALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLK 287
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-267 |
9.31e-08 |
|
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: 52.22 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 42 IDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVwcTF-----------NHPERVQVCLEQSLKQLQ 107
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKY--TMnrrpgdpnaggNHRKNLRRSVEASLRRLQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 108 LEYVDLYLIHFPMALKP-EEDLKAKDE---NEKLLFdvVDICDT--WKAmekCKDAGLAKSIGVSNFNRRQLEKILnkpg 181
Cdd:cd19080 112 TDYIDLLYVHAWDFTTPvEEVMRALDDlvrAGKVLY--VGISDTpaWVV---ARANTLAELRGWSPFVALQIEYSL---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 182 lkhrpvcnqVECHPylnQRKLLDFCKSKDIVLVAYSALGS-------HRETRCVDKSLPVLLADP------------VLC 242
Cdd:cd19080 183 ---------LERTP---ERELLPMARALGLGVTPWSPLGGglltgkyQRGEEGRAGEAKGVTVGFgklternwaivdVVA 250
|
250 260
....*....|....*....|....*
gi 564392038 243 AIAKKYNWTPALIALRYQLERGVVV 267
Cdd:cd19080 251 AVAEELGRSAAQVALAWVRQKPGVV 275
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-166 |
4.42e-07 |
|
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: 50.35 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 18 VLGFGTYAPR---EVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEV-GLAIrSKIADGtVKREDIFYTSKV----WCTF 89
Cdd:cd19164 17 IFGAATFSYQyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRDE-FPRDTYFIITKVgrygPDDF 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564392038 90 NH-PERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDEneklLFdvvdicdtwkameKCKDAGLAKSIGVS 166
Cdd:cd19164 95 DYsPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVLEALKE----LF-------------KLKDEGKIRNVGIS 155
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
20-204 |
5.34e-07 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 49.84 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 20 GFGTYAPREVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgTVKREDIFYTSKVW----CTFNHP 92
Cdd:cd19153 21 ALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGryrdSEFDYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 93 -ERVQVCLEQSLKQLQLEYVDLYLIHfpmalkpeeDLKAKDeneklLFDVVDicDTWKAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19153 97 aERVRASVATSLERLHTTYLDVVYLH---------DIEFVD-----YDTLVD--EALPALRTLKDEGVIKRIGIAGYPLD 160
|
170 180 190
....*....|....*....|....*....|...
gi 564392038 172 QLEKILNKPGLKHRPVCnQVECHPYLNQRKLLD 204
Cdd:cd19153 161 TLTRATRRCSPGSLDAV-LSYCHLTLQDARLES 192
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-167 |
8.58e-06 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 46.39 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 14 HFIP-------VLGFGTYAPREV-PKSKALEATKIAIDAGFRHIDSAAVYQ----------NEKEVGLAIRSKiadgtVK 75
Cdd:PRK10625 4 HRIPhsslevsTLGLGTMTFGEQnSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR-----GS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 76 REDIFYTSKVwctfNHPER----------------VQVCLEQSLKQLQLEYVDLYLIHFPMalkpeedlKAKDENEKLLF 139
Cdd:PRK10625 79 REKLIIASKV----SGPSRnndkgirpnqaldrknIREALHDSLKRLQTDYLDLYQVHWPQ--------RPTNCFGKLGY 146
|
170 180 190
....*....|....*....|....*....|....
gi 564392038 140 D------VVDICDTWKAMEKCKDAGLAKSIGVSN 167
Cdd:PRK10625 147 SwtdsapAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-253 |
2.08e-05 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 45.01 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 17 PVLGFGTyAP-----REVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgtvKREDIFYTSKV--- 85
Cdd:cd19161 1 SELGLGT-AGlgnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK------PRDEFVLSTKVgrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 86 ------WCTFNHPERVQ----VC------------LEQSLKQLQLEYVDLYLIHfpmalkpeeDLKA---KDENEKLLFD 140
Cdd:cd19161 74 lkpareGSVPDPNGFVDplpfEIvydysydgimrsFEDSLQRLGLNRIDILYVH---------DIGVythGDRKERHHFA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 141 VvdICDT-WKAMEKCKDAGLAKSIGVsnfnrrqlekilnkpGLKHRPVCNQVechpyLNQRKLldfckskDIVLVA--YS 217
Cdd:cd19161 145 Q--LMSGgFKALEELKKAGVIKAFGL---------------GVNEVQICLEA-----LDEADL-------DCFLLAgrYS 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 564392038 218 ALGSHRET----RCVDKSLPVLLADP----VLCAIAK---KYNWTPA 253
Cdd:cd19161 196 LLDQSAEEeflpRCEQRGTSLVIGGVfnsgILATGTKsgaKFNYGDA 242
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
16-219 |
2.48e-05 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 45.15 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFG------TYAPreVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgTVKREDIFYTSKvw 86
Cdd:PLN02587 11 VSSVGFGasplgsVFGP--VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTK-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 87 C-------TFNhPERVQVCLEQSLKQLQLEYVDLYLIHfpmalkpeeDLKakdenekllFDVVD--ICDTWKAMEKCKDA 157
Cdd:PLN02587 83 CgrygegfDFS-AERVTKSVDESLARLQLDYVDILHCH---------DIE---------FGSLDqiVNETIPALQKLKES 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564392038 158 GLAKSIGVSNFNRRQLEKILNK--PGlkhrpvcnQVE-----CHPYLNQRKLLD---FCKSKDIVLVAYSAL 219
Cdd:PLN02587 144 GKVRFIGITGLPLAIFTYVLDRvpPG--------TVDvilsyCHYSLNDSSLEDllpYLKSKGVGVISASPL 207
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
99-220 |
4.18e-05 |
|
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: 44.32 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 99 LEQSLKQLQLEYVDLYLIHFPmalKPEEDLKakdenekllfdvvdicDTWKAMEKCKDAGLAKSIGVSNFN---RRQLEK 175
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRP---DPETPLE----------------ETMGALDQIVRQGKALYVGISNYPpeeAREAAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564392038 176 ILNK---PGLKHRPVCNQVECHPylnQRKLLDFCKSKDIVLVAYSALG 220
Cdd:cd19151 168 ILKDlgtPCLIHQPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLA 212
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
16-209 |
1.28e-04 |
|
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: 42.84 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGT---YAPReVPKSKALEATKIAIDAGFRHIDSAAVYQN---EKEVGLAIRSKiadgTVKREDIFYTSKVWCTF 89
Cdd:cd19142 13 VSNVGLGTwstFSTA-ISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIYWSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 NHPER------VQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEdlkakdenekllfDVVdicdtwKAMEKCKDAGLAKSI 163
Cdd:cd19142 88 GSEERglsrkhIIESVRASLRRLQLDYIDIVIIHKADPMCPME-------------EVV------RAMSYLIDNGLIMYW 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564392038 164 GVSNF----------NRRQlekiLNKPglkhRPVCNQVECHPylnqrklldFCKSK 209
Cdd:cd19142 149 GTSRWspveimeafsIARQ----FNCP----TPICEQSEYHM---------FCREK 187
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
28-118 |
3.32e-03 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 38.56 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 28 EVPKSKALEATKIAIDAGFRHIDSAAVYQ---NEKEVG-----------LAIRSKIADGTVKREDIfyTSKVWCTFNHPE 93
Cdd:cd19146 31 ECDKETAFKLLDAFYEQGGNFIDTANNYQgeeSERWVGewmasrgnrdeMVLATKYTTGYRRGGPI--KIKSNYQGNHAK 108
|
90 100
....*....|....*....|....*
gi 564392038 94 RVQVCLEQSLKQLQLEYVDLYLIHF 118
Cdd:cd19146 109 SLRLSVEASLKKLQTSYIDILYVHW 133
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
16-194 |
5.47e-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: 37.81 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYAP--REVPKSKALEATKIAIDAGFRHIDSAAVYQNEK-EV--GLAIRSKiadgTVKREDIFYTSKV-WCTF 89
Cdd:cd19141 12 VSCLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYAAGKaEIvlGKILKKK----GWRRSSYVITTKIfWGGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 90 NHPER------VQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEdlkakdenekllfdvvdicDTWKAMEKCKDAGLAKSI 163
Cdd:cd19141 88 AETERglsrkhIIEGLKASLERLQLEYVDIVFANRPDPNTPME-------------------EIVRAFTHVINQGMAMYW 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564392038 164 GVSNFNR----------RQLEKIlnkPglkhrPVCNQVECH 194
Cdd:cd19141 149 GTSRWSAmeimeaysvaRQFNLI---P-----PIVEQAEYH 181
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
16-200 |
5.95e-03 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 37.76 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 16 IPVLGFGTYAP--REVPKSKALEATKIAIDAGFRHIDSAAVYQNEK-EVGLAirSKIADGTVKREDIFYTSKV-WCTFNH 91
Cdd:cd19158 13 VSCLGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKaEVVLG--NIIKKKGWRRSSLVITTKIfWGGKAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392038 92 PER------VQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEdlkakdenekllfdvvdicDTWKAMEKCKDAGLAKSIGV 165
Cdd:cd19158 91 TERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTPME-------------------ETVRAMTHVINQGMAMYWGT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564392038 166 SNFNRRQlekILNKPGLKHR-----PVCNQVECHPYLNQR 200
Cdd:cd19158 152 SRWSSME---IMEAYSVARQfnlipPICEQAEYHMFQREK 188
|
|
| |
