|
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) ... |
6-282 |
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: 631.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 6 QCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------AMEKCKDAGLAKSIGV 139
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKpgeelfpkdengklifdtvdlcatweAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 140 SNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALA 219
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005261232 220 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTL 282
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-293 |
1.13e-156 |
|
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: 439.23 E-value: 1.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTYA-PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 92 PELVRPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------AMEKCKDAGLAKSIGVSNFNHR 145
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiyprdengkwlyhktnlcatweALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 146 LLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRT 225
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261232 226 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPF 293
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-279 |
2.22e-124 |
|
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: 356.98 E-value: 2.22e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 7 CVKLNDGHFMPVLGFGTYApaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK-----------------------AMEKCKDAGLAKSIGVSNFN 143
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKenndsesngdgslsdidyletwrGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 144 HRLLEMILNkpGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvDPNSPVLLEDPVLCALAKKHK 223
Cdd:cd19116 160 SEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRG--QTNPPPRLDDPTLVAIAKKYG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261232 224 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19116 236 KTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-279 |
4.63e-122 |
|
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: 351.69 E-value: 4.63e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 10 LNDGHFMPVLGFGTY--APAEVPkskalEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKI-ADGSVKREDIFYTSKLW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQVK-----AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSV--------------------------KAMEKCKDAGLAKSIGVS 140
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFergdnpfpknpdgtirydsthyketwKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 141 NFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNSPVLLEDPVLCALAK 220
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGS-PDRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005261232 221 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-297 |
8.46e-122 |
|
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: 350.95 E-value: 8.46e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELV 95
Cdd:cd19107 4 MPILGLGTW---KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 96 RPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------AMEKCKDAGLAKSIGVSNFNHRLLEM 149
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKpgkelfpldesgnvipsdttfldtweAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 150 ILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNSPVLLEDPVLCALAKKHKRTPALI 229
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGS-PDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261232 230 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY 297
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-271 |
9.25e-122 |
|
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: 348.70 E-value: 9.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIadgsVKREDIFYTSKLWSNSHRPELV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 96 RPALERSLKNLQLDYVDLYLIHFPVSV-------------KAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPglKYKPVC 162
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGkeggskearletwRALEELVDEGLVRSIGVSNFNVEHLEELLAAA--RIKPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 163 NQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpnspVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVL 242
Cdd:cd19071 152 NQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR---------PLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVI 222
|
250 260
....*....|....*....|....*....
gi 1005261232 243 AKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19071 223 PKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-279 |
6.84e-119 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 341.65 E-value: 6.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 12 DGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWSNSHR 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 92 PELVRPALERSLKNLQLDYVDLYLIHFPVSV------KAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGlkYKPVCNQV 165
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGPGpyvetwRALEELYEEGLIRAIGVSNFDPEHLEELLAETG--VKPAVNQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 166 ECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKS 245
Cdd:COG0656 152 ELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKS 220
|
250 260 270
....*....|....*....|....*....|....
gi 1005261232 246 YNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:COG0656 221 VTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-280 |
6.20e-110 |
|
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: 320.51 E-value: 6.20e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYAPAevpKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK-------------------------AMEKCKDAGLAKSIGVSNF 142
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKkgvgfpesgedllslspipledtwrAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 143 NHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAKK 221
Cdd:cd19123 161 SVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005261232 222 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYL 280
Cdd:cd19123 239 HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-273 |
1.38e-104 |
|
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: 306.58 E-value: 1.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 6 QCVKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK---------------------AMEKCKDAGLAKSIGVSNFNH 144
Cdd:cd19125 78 WCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdipstwkAMEKLVDSGKVRAIGVSNFSV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 145 RLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNspvLLEDPVLCALAKKHKR 224
Cdd:cd19125 158 KKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWVKKN---VLKDPIVTKVAEKLGK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1005261232 225 TPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-297 |
1.55e-104 |
|
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: 306.89 E-value: 1.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTY--APAEVPkskalEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPE 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEVT-----EAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 94 LVRPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------AMEKCKDAGLAKSIGVSNFNHRLL 147
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdfldtweAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 148 EMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwVDpnspvLLEDPVLCALAKKHKRTPA 227
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 228 LIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY 297
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
7-278 |
3.84e-104 |
|
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: 305.88 E-value: 3.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 7 CVKLNDGHFMPVLGFGTY--APAEVpkskaLEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSK 84
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWqsKGAEG-----ITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 LWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------AMEKCKDAGLAKSIG 138
Cdd:cd19154 78 LWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKddegesgtmengmsihdavdvedvwrGMEKVYDEGLTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 139 VSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-----HREEPWVDPnSPVLLEDP 213
Cdd:cd19154 158 VSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranFTKSTGVSP-APNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261232 214 VLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVR 278
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-273 |
1.44e-95 |
|
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: 283.39 E-value: 1.44e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 12 DGHFMPVLGFGTYAPAEVPKsKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVK-REDIFYTSKLWSNSH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVK-----------------------AMEKCKDAGLAKSIGVSNFNHRLL 147
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKpgkfsfpieeedflpfdikgvweAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 148 EMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReEPWvdpNSPVLLEDPVLCALAKKHKRTPA 227
Cdd:cd19124 160 QELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKW---GSNAVMESDVLKEIAAAKGKTVA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1005261232 228 LIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19124 234 QVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-279 |
1.03e-94 |
|
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: 281.31 E-value: 1.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTY--APAEVpkskaLEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSH 90
Cdd:cd19111 1 GFPMPVIGLGTYqsPPEEV-----RAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSV--------------------KAMEKCKDAGLAKSIGVSNFNHRLLEMI 150
Cdd:cd19111 76 EFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFvnkkdkgerelassdvtsvwRAMEALVSEGKVKSIGLSNFNPRQINKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 151 LNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAKKHKRTPALI 229
Cdd:cd19111 156 LAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDKTPAQV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005261232 230 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19111 234 LLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-271 |
3.49e-93 |
|
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: 275.69 E-value: 3.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 96 RPALERSLKNLQLDYVDLYLIHFPVS-------VKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLkyKPVCNQVECH 168
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNPtvpleetLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL--PIAVNQVEFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 169 PYFNQRKLLDFCKSKDIVLVAYSALGsHREepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNE 248
Cdd:cd19073 152 PFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSE 220
|
250 260
....*....|....*....|...
gi 1005261232 249 QRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19073 221 DHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-274 |
8.58e-93 |
|
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: 275.41 E-value: 8.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWS 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPV--------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKyk 159
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVpaqdkyveTWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGV 239
Cdd:cd19131 153 PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGL 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1005261232 240 VVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 274
Cdd:cd19131 222 VVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-278 |
1.76e-92 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 276.33 E-value: 1.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 7 CVKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSV----------------------------KAMEKCKDAGLAKSIG 138
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSlskeddsgkldptgehkqdyttdlldiwKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 139 VSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS----HREEPWVDP--NSPVLLED 212
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaaHFSPGTGSPsgSSPDLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261232 213 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVR 278
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-274 |
3.56e-90 |
|
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: 268.54 E-value: 3.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPK-SKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSkiadGSVKREDIFYTSKLW 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF---QTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPglKYKP 160
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGkdkfidTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA--DVVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 161 VCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVV 240
Cdd:cd19126 152 AVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVV 220
|
250 260 270
....*....|....*....|....*....|....
gi 1005261232 241 VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 274
Cdd:cd19126 221 TIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-274 |
4.32e-90 |
|
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: 268.29 E-value: 4.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVP-KSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV-----SVKAMEKCKDAGLAKSIGVSNFN-HRLLEMILNKpglKYKP 160
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFgdvygAWRAMEELYKEGKIRAIGVSNFYpDRLVDLILHN---EVKP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 161 VCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVV 240
Cdd:cd19133 151 AVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIAEKYGKSVAQVILRWLIQRGIV 221
|
250 260 270
....*....|....*....|....*....|....
gi 1005261232 241 VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 274
Cdd:cd19133 222 VIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-279 |
9.83e-90 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 268.11 E-value: 9.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 7 CVKLNDGHFMPVLGFGTYapaEVPK-SKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKL 85
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVF---KVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPglKYK 159
Cdd:cd19157 74 WNADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVkgkykeTWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADA--EIV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGV 239
Cdd:cd19157 152 PMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEKYNKSVAQVILRWDLQNGV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005261232 240 VVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19157 221 VTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-271 |
4.52e-89 |
|
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: 266.41 E-value: 4.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGT----YAPAEVPKSKAL-EAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWS 87
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLvDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPelvRPALERSLKNLQLDYVDLYLIHFPVSVK-----------AMEKCKDAGLAKSIGVSNFNHRLLEMILNKPgl 156
Cdd:cd19120 77 GIKDP---REALRKSLAKLGVDYVDLYLIHSPFFAKeggptlaeawaELEALKDAGLVRSIGVSNFRIEDLEELLDTA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 157 KYKPVCNQVECHPYFN--QRKLLDFCKSKDIVLVAYSALGSHreepWVDPNSPVlleDPVLCALAKKHKRTPALIALRYQ 234
Cdd:cd19120 152 KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPL----TRDAGGPL---DPVLEKIAEKYGVTPAQVLLRWA 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 1005261232 235 LQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19120 225 LQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-273 |
1.41e-86 |
|
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: 259.87 E-value: 1.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTY---APAEVpkSKALEAvklAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRP 92
Cdd:cd19136 1 MPILGLGTFrlrGEEEV--RQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 93 ELVRPALERSLKNLQLDYVDLYLIHFP-----------------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPg 155
Cdd:cd19136 76 EKARAACLGSLERLGTDYLDLYLIHWPgvqglkpsdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 156 lKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdpNSPVLLEDPVLCALAKKHKRTPALIALRYQL 235
Cdd:cd19136 155 -EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTPAQVLLRWAL 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1005261232 236 QRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19136 225 QQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-273 |
2.74e-86 |
|
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: 259.65 E-value: 2.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 10 LNDGHFMPVLGFGTY--APAEVPKskaleAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIAD-GSVKREDIFYTSKLW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEVGA-----AVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSV-------------------------------KAMEKCKDAGLAK 135
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFkptgdlnpltavptnggevdldlsvslvdtwKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 136 SIGVSNFNHRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpNSPVLLEDPVL 215
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGVV--PAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLA------GLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261232 216 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAIDGL 273
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-275 |
6.86e-86 |
|
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: 257.58 E-value: 6.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 10 LNDGHFMPVLGFGTYApaeVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWSNS 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 90 HRPELVRPALERSLKNLQLDYVDLYLIHFPV--------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKykPV 161
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPNpsrdlyveAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVT--PA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 162 CNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVV 241
Cdd:cd19132 152 VNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVP 221
|
250 260 270
....*....|....*....|....*....|....
gi 1005261232 242 LAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNR 275
Cdd:cd19132 222 IPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-279 |
3.48e-85 |
|
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: 257.80 E-value: 3.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19112 3 ITLNSGHKMPVIGLGVW---RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHrpELVRPALERSLKNLQLDYVDLYLIHFPVSVK------------------------------AMEKCKDAGLAKSI 137
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgttgsalgedgvldidvtislettwhAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 138 GVSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALG-SHREEPWVDPNSPvlLEDPVLC 216
Cdd:cd19112 158 GISNYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDDPVLK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005261232 217 ALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-279 |
3.86e-84 |
|
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: 253.59 E-value: 3.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPK-SKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKiadgSVKREDIFYTSKLW 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVW---RVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKpgLKYKP 160
Cdd:cd19156 74 NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVkgkfkdTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKS--CKVAP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 161 VCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVV 240
Cdd:cd19156 152 MVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGII 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 1005261232 241 VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19156 221 TIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-273 |
3.89e-84 |
|
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: 253.34 E-value: 3.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRP 92
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 93 ELVRPALERSLKNLQLDYVDLYLIHFPV-------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKYkpVCNQV 165
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWPNkdvplaeTLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPL--FTNQV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 166 ECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQR-GVVVLAK 244
Cdd:cd19140 156 EYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPK 224
|
250 260
....*....|....*....|....*....
gi 1005261232 245 SYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19140 225 ATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-291 |
1.81e-83 |
|
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: 253.50 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19115 5 VKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK-------------------------------AMEKCKDAGLAKS 136
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdpavryppgwfydgkkvefsnapiqetwtAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 137 IGVSNFNHRLLeMILnkpgLKY---KPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALG--SHREEPWVDP-NSPVLL 210
Cdd:cd19115 162 IGVSNFSAQLL-MDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqSFLELDLPGAkDTPPLF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 211 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRyltldiFAGPPN 290
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR------FNNPLN 310
|
.
gi 1005261232 291 Y 291
Cdd:cd19115 311 Y 311
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-279 |
9.20e-83 |
|
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: 251.60 E-value: 9.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------------AMEKCKDAGLAK 135
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpieekyppgfycgdgdnfvyedvpildtwkALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 136 SIGVSNFNHRLLEMILNkpGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHR----EEPWVdPNSPVLLE 211
Cdd:cd19113 160 SIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelNQGRA-LNTPTLFE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261232 212 DPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19113 237 HDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-275 |
2.15e-82 |
|
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: 250.11 E-value: 2.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 9 KLNDGHFMPVLGFGTY--APAEVPKskaleAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19117 7 KLNTGAEIPAVGLGTWqsKPNEVAK-----AVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPelVRPALERSLKNLQLDYVDLYLIHFPVSVKA----------------------------MEKCKDAGLAKSIG 138
Cdd:cd19117 78 CTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdfiktwelMQKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 139 VSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdPNSPvLLEDPVLCAL 218
Cdd:cd19117 156 VSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS--------TNAP-LLKEPVIIKI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261232 219 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAIDGLNR 275
Cdd:cd19117 227 AKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-274 |
2.81e-82 |
|
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: 248.86 E-value: 2.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYApaeVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPV---------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKy 158
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVpndfdrtiqAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 159 kPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQR 237
Cdd:cd19127 153 -PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvMRYGASGPTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQN 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1005261232 238 GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 274
Cdd:cd19127 232 GVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-273 |
8.26e-77 |
|
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: 235.50 E-value: 8.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 9 KLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGsVKREDIFYTSKLWSN 88
Cdd:cd19121 5 KLNTGASIPAVGLGTW---QAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 89 SH-RPELvrpALERSLKNLQLDYVDLYLIHFPVSV-----------------------------KAMEKCKDAGLAKSIG 138
Cdd:cd19121 81 YHrRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLnpngnhdlfptlpdgsrdldwdwnhvdtwKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 139 VSNFNHRLLEMILnkPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdPNSPVLLEDPVLcAL 218
Cdd:cd19121 158 VSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDEPVV-EI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1005261232 219 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFqlTSEEMKAIDGL 273
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-279 |
1.40e-76 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 235.43 E-value: 1.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 11 NDGHFMPVLGFGTYAPaevPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSH 90
Cdd:cd19129 1 NGSGAIPALGFGTLIP---DPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVK---------------------------AMEKCKDAGLAKSIGVSNFN 143
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQpgdeqdprdangnviyddgvtlldtwrAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 144 HRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGsHREEpwvdpnsPVLLEDPVLCALAKKHK 223
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-HGME-------PKLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261232 224 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTSEEMKAI-DGLNRNVRY 279
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-273 |
3.98e-76 |
|
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: 233.57 E-value: 3.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVR 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 97 PALERSLKNLQLDYVDLYLIHFPVSV--------------------------KAMEKCKDAGLAKSIGVSNFNHRLLEMI 150
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFdmdtdgdprddnqiqslskkpledtwRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 151 LNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvdpnSPVLLEDPVLCALAKKHKRTPALIA 230
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDG-----NLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1005261232 231 LRYQLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-273 |
5.44e-75 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 230.29 E-value: 5.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 7 CVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKlaiEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSGGYSHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSV--------------KAMEKCKDAGLAKSIGVSNFNHRLLEMILN 152
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPssgknvketraetwRALEELYDEGLCRAIGVSNFLIEHLEQLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 153 KPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALR 232
Cdd:cd19135 157 DCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAKKYQKTPAQILIR 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1005261232 233 YQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19135 224 WSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-279 |
1.34e-74 |
|
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: 229.36 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTyapAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGV---GELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPV--------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGlkYK 159
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAgregkyvdSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTF--FT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGV 239
Cdd:cd19134 154 PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGN 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005261232 240 VVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 279
Cdd:cd19134 223 VVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-274 |
3.09e-74 |
|
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: 228.26 E-value: 3.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 10 LNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNS 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 90 HRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK--------AMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKykPV 161
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAgnyvhtweAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVV--PA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 162 CNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVV 241
Cdd:cd19130 155 VNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVV 223
|
250 260 270
....*....|....*....|....*....|...
gi 1005261232 242 LAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 274
Cdd:cd19130 224 FPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-285 |
5.43e-72 |
|
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: 223.97 E-value: 5.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 93 ELVRPALERSLKNLQLDYVDLYLIHFPVSVK--------------------------------AMEKCKDAGLAKSIGVS 140
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdpaenypflwkdkelkkfpleqspmqecwrEMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 141 NFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPV--LLEDPVLCAL 218
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261232 219 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIF 285
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVVY 302
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-275 |
3.85e-70 |
|
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: 218.91 E-value: 3.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYAPAEvPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPelVRPALERSLKNLQLDYVDLYLIHFPVSVKA--------------------------------MEKCKDAGLAK 135
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEKdsddsgkpftpvnddgktryaasgdhittykqLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 136 SIGVSNFNHRLLEMILNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwvdpnspvLLEDPVL 215
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 216 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTSEEMKAIDGLNR 275
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-274 |
1.39e-69 |
|
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: 217.56 E-value: 1.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFGTYA----PAEVPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIrskiADGSVKREDIFYTSKL------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV-------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPglKY 158
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDpdtpieeTWDALEELKKEGKIRAIGVSNFDAEQIEKALTKG--KI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 159 KPVCNQVECHPYF--NQRKLLDFCKSKDIVLVAYSALGS----------------HREEPWVDPNSPVLLEDPVLCALAK 220
Cdd:pfam00248 155 PIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLLKKGTPLNLEALEALEEIAK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261232 221 KHKRTPALIALRY--QLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 274
Cdd:pfam00248 235 EHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-273 |
1.53e-69 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 215.68 E-value: 1.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTY--APAEVPKSkaleaVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRPE 93
Cdd:cd19139 1 IPAFGLGTFrlKDDVVIDS-----VRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 94 LVRPALERSLKNLQLDYVDLYLIHFP---------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGlKYKPVCNQ 164
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWPspndevpveEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG-AGAIATNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 165 VECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAK 244
Cdd:cd19139 151 IELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPS 219
|
250 260
....*....|....*....|....*....
gi 1005261232 245 SYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19139 220 STKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-278 |
1.06e-66 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 209.54 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWS 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPelVRPALERSLKNLQLDYVDLYLIHFPVSV--------KAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKyk 159
Cdd:PRK11565 80 DDHKR--PREALEESLKKLQLDYVDLYLMHWPVPAidhyveawKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVT-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PVCNQVECHPYFNQRKLLdfckskdivlvAYSALGSHREEPWvdpnSPV------LLEDPVLCALAKKHKRTPALIALRY 233
Cdd:PRK11565 156 PVINQIELHPLMQQRQLH-----------AWNATHKIQTESW----SPLaqggkgVFDQKVIRDLADKYGKTPAQIVIRW 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1005261232 234 QLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVR 278
Cdd:PRK11565 221 HLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-271 |
1.77e-65 |
|
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: 205.93 E-value: 1.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTYA---PAEVPKS---KALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSKLW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDYSddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV-------SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGlKYK 159
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNpsipieeTLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK-KGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PVCNQVECHpYFNQR---KLLDFCKSKDIVLVAYSALGshREEPWVDPNSPVLLEdpvlcaLAKKHKRTPALIALRYQLQ 236
Cdd:cd19072 157 IVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLE--KGKLSNAKGSPLLDE------IAKKYGKTPAQIALNWLIS 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1005261232 237 R-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19072 228 KpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-271 |
5.56e-61 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 195.53 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 9 KLNDGHFMPVLGFGTYApAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADG-SVKREDIFYTSKLWS 87
Cdd:cd19122 2 TLNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSV------------------------------KAMEKCKDAGLAKSI 137
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAekndqrspklgpdgkyvilkdltenpeptwRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 138 GVSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvdPNSPVLLEDPVLCA 217
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVP---STGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1005261232 218 LAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAID 271
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAIN 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-286 |
3.07e-59 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 190.23 E-value: 3.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRPELV 95
Cdd:PRK11172 3 IPAFGLGTF---RLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 96 RPALERSLKNLQLDYVDLYLIHFP-----VSV----KAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGlKYKPVCNQVE 166
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWPspndeVSVeefmQALLEAKKQGLTREIGISNFTIALMKQAIAAVG-AENIATNQIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 167 CHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSY 246
Cdd:PRK11172 155 LSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSST 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005261232 247 NEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFA 286
Cdd:PRK11172 224 KRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSPEGLA 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-271 |
7.22e-58 |
|
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: 186.69 E-value: 7.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 6 QCVKLNDGHFMPVLGFGTYAPAEVPKSKA--LEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAqeIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 81 YTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVS------VKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKP 154
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGvplaetVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 155 GLKyKPVCNQVECHpyFNQR----KLLDFCKSKDIVLVAYSALGSHREEPwvdpnsPVLLEDPVLCALAKKHKRTPALIA 230
Cdd:cd19138 154 GGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLR------RGLLENPTLKEIAARHGATPAQVA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1005261232 231 LRYQL-QRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19138 225 LAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-271 |
2.21e-47 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 159.27 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTYA------PAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSkiadgsVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 84 KLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKpgL 156
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPnpnipleETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK--S 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 157 KYKPVCNQVECHPY---FNQRKLLDFCKSKDIVLVAYSALgshreepwvdpNSPVLLEDPVLCALAKKHKRTPALIALRY 233
Cdd:cd19137 153 QTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRTLEEIAKNYGKTIAQIALAW 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 1005261232 234 QLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19137 222 LIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-271 |
4.96e-45 |
|
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: 154.22 E-value: 4.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTYA-----PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 ---LWSNSH------RPELVRPALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNhrlLE 148
Cdd:cd19084 74 cglRWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWPdpntpieETAEALEKLKKEGKIRYIGVSNFS---VE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 149 MIlnKPGLKY-KPVCNQVechPY--FNQ---RKLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN-----SPVLLE 211
Cdd:cd19084 151 QL--EEARKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLaqglltGKYKKEPTFPPDdrrsrFPFFRG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261232 212 D---------PVLCALAKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19084 226 EnfeknleivDKLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-271 |
4.56e-42 |
|
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: 147.25 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGT----YAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRSKiadgsvKREDIFYTSKL---- 85
Cdd:COG0667 14 SRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKVgrrm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 ----WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFN-HRLLEMILNK 153
Cdd:COG0667 88 gpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPdpdtpieETLGALDELVREGKIRYIGVSNYSaEQLRRALAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 154 PGLkYKPVCNQVEchpY--FNQR---KLLDFCKSKDIVLVAYSALGS------HREEPWVDPNS--------PVLLED-- 212
Cdd:COG0667 168 EGL-PPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLAGglltgkYRRGATFPEGDraatnfvqGYLTERnl 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261232 213 ---PVLCALAKKHKRTPALIALRYQLQRGVVVL----AKSynEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:COG0667 244 alvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDLAALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-277 |
7.56e-42 |
|
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: 145.81 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYAPA------EVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWS 87
Cdd:cd19085 2 SRLGLGCWQFGggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVS-------VKAMEKCKDAGLAKSIGVSNFNHRLLEMILnKPGlkyKP 160
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSdvpleetMEALEKLKEEGKIRAIGVSNFGPAQLEEAL-DAG---RI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 161 VCNQVECHPYFNQ--RKLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN-----SPVLLEDPV----------LCA 217
Cdd:cd19085 151 DSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrLFRHFEPGAeeetfealekLKE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005261232 218 LAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNV 277
Cdd:cd19085 231 IADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-271 |
1.21e-41 |
|
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: 145.45 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYA---------PAEVPKSkALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRskiadGSVKREDIFYTSK 84
Cdd:cd19093 3 SPLGLGTWQwgdrlwwgyGEYGDED-LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 L----WSNSHRPeLVRpALERSLKNLQLDYVDLYLIHFPVSV--------KAMEKCKDAGLAKSIGVSNFNHRLLEMI-- 150
Cdd:cd19093 77 FaplpWRLTRRS-VVK-ALKASLERLGLDSIDLYQLHWPGPWysqiealmDGLADAVEEGLVRAVGVSNYSADQLRRAhk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 151 -LNKPGlkYKPVCNQVE---CHPYFNQRKLLDFCKSKDIVLVAYSALG----------SHR-EEPWVDPNSPVLLE--DP 213
Cdd:cd19093 155 aLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspENPpPGGRRRLFGRKNLEkvQP 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261232 214 VLCAL---AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19093 233 LLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-256 |
7.64e-34 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 123.40 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYA-PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRskiadGSVKREDIFYTSK-----LWS 87
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKgghppGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHR---PELVRPALERSLKNLQLDYVDLYLIHF-----PV--SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILN--KPG 155
Cdd:cd06660 76 PSRSrlsPEHIRRDLEESLRRLGTDYIDLYYLHRddpstPVeeTLEALNELVREGKIRYIGVSNWSAERLAEALAyaKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 156 LKYKPVCNQVE---CHPYFNQRKLLDFCKSKDIVLVAYSALGshreepwvdpnspvlledpvlcalakkhkRTPALIALR 232
Cdd:cd06660 156 GLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA-----------------------------RGPAQLALA 206
|
250 260
....*....|....*....|....*.
gi 1005261232 233 YQLQR--GVVVLAKSYNEQRIRQNVQ 256
Cdd:cd06660 207 WLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-273 |
3.60e-30 |
|
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: 115.46 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYA---------PAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSK- 84
Cdd:cd19102 3 TIGLGTWAiggggwgggWGPQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 --LW------SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV-------SVKAMEKCKDAGLAKSIGVSNFNHRLLEM 149
Cdd:cd19102 76 glLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDpdepieeAWGALAELKEEGKVRAIGVSNFSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 150 IL-------NKPGlkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALGS-------HREE----PWVD--PNSPVL 209
Cdd:cd19102 156 CQaihpiasLQPP--YSLLRRGIE-------AEILPFCAEHGIGVIVYSPMQSglltgkmTPERvaslPADDwrRRSPFF 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261232 210 LED---------PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19102 227 QEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-273 |
5.07e-28 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.68 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVY-NNEEQVGLAIRSKiadgsvkREDIFYTSKLWSNSHRPEL 94
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVRDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 95 VRPALERSLKNLQLDYVDLYLIHFPVSV-------------KAMEKCKDAGLAKSIGVSnfNHRLLEMILnkpglkykpv 161
Cdd:COG1453 86 MRKDLEESLKRLQTDYIDLYLIHGLNTEedlekvlkpggalEALEKAKAEGKIRHIGFS--THGSLEVIK---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 162 cNQVECHP---------YFNQR-----KLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPA 227
Cdd:COG1453 154 -EAIDTGDfdfvqlqynYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LANPPEKLVELLCPPLSPA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005261232 228 LIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFE--FQLTSEEMKAIDGL 273
Cdd:COG1453 222 EWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-266 |
7.09e-27 |
|
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: 106.10 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSK----LWSNSH 90
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgirLGDDPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 91 R---------PELVRPALERSLKNLQLDYVDLYLIHFP--------VSvKAMEKCKDAGLAKSIGVSNFNHRLLEMiLNK 153
Cdd:cd19092 86 PgrikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRPdplmdpeeVA-EAFDELVKSGKVRYFGVSNFTPSQIEL-LQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 154 pGLKYKPVCNQVEC---HPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEdpVLCALAKKHKRTPALIA 230
Cdd:cd19092 164 -YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA--ALEELAEEYGVTIEAIA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1005261232 231 LRYQLQ---RGVVVLAkSYNEQRIRQNVQVFEFQLTSEE 266
Cdd:cd19092 241 LAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-270 |
7.42e-27 |
|
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: 107.14 E-value: 7.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 11 NDGHFMPVLGFGT------YAPAEvPKSKALEAVKLAIEAGFHHIDSAHVY-NNEEQVGLAIrsKIADGsvKREDIFYTS 83
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 84 K-----------LWSNShRPELVRPALERSLKNLQLDYVDLYLIH-----FPV--SVKAMEKCKDAGLAKSIGVSNFNHR 145
Cdd:cd19144 83 KfgieknvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQHrvdgkTPIekTVAAMAELVQEGKIKHIGLSECSAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 146 LLemilnKPGLKYKPVCN-QVECHPYF-----NQRKLLDFCKSKDIVLVAYSALGS------------------HREEPW 201
Cdd:cd19144 162 TL-----RRAHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRgfltgairspddfeegdfRRMAPR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005261232 202 VDP-NSPVLLE--DPvLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAI 270
Cdd:cd19144 237 FQAeNFPKNLElvDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
18-266 |
9.21e-27 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 106.00 E-value: 9.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL------WSN 88
Cdd:COG4989 17 VLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELQTKCgirlpsEAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 89 SHRP-------ELVRPALERSLKNLQLDYVDLYLIHFP--------VSvKAMEKCKDAGLAKSIGVSNFNHRLLEMiLNK 153
Cdd:COG4989 93 DNRVkhydtskEHIIASVEGSLRRLGTDYLDLLLLHRPdplmdpeeVA-EAFDELKASGKVRHFGVSNFTPSQFEL-LQS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 154 pGLKYKPVCNQVECHPYFNQ---RKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEdpVLCALAKKHKRTPALIA 230
Cdd:COG4989 171 -ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVSPEAIA 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1005261232 231 LRYqLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTSEE 266
Cdd:COG4989 248 LAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-255 |
1.06e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 104.49 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN-EEQVGLAIRSKiadgsvkREDIFYTSKLWSNShrPELV 95
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD--YEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 96 RPALERSLKNLQLDYVDLYLIHFPVSVK-------------AMEKCKDAGLAKSIGVSN-FNHRLLEMIlnkpglkykpv 161
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVDTEEdldqvfgpggaleALLEAKEEGKIRFIGISGhSPEVLLRAL----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 162 cnqvechpyfnqrKLLDFckskDIVLVAYSALGSHREEPwvdpnspvllEDPVLCALAKKHK-----------------R 224
Cdd:cd19100 152 -------------ETGEF----DVVLFPINPAGDHIDSF----------REELLPLAREKGVgviamkvlaggrllsgdP 204
|
250 260 270
....*....|....*....|....*....|....*
gi 1005261232 225 TPALIALRYQLQRGVVVLA----KSYNEqrIRQNV 255
Cdd:cd19100 205 LDPEQALRYALSLPPVDVVivgmDSPEE--LDENL 237
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
38-273 |
1.46e-26 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 105.96 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 38 VKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvKREDIFYTSK----------LWSNShrPELVRPALERSLK 104
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgahkfggdgsVLNNS--PEFLRSAVEKSLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 105 NLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMiLNKPGL------KYKPVCNQVECHpyf 171
Cdd:cd19083 111 RLNTDYIDLYYIHFPdgetpkaEAVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGYvdvlqgEYNLLQREAEED--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 172 nqrkLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN--------------SPVLLEDPVLCALAKKHKRTPALIAL 231
Cdd:cd19083 187 ----ILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNdlrndkplfkgerfSENLDKVDKLKSIADEKGVTVAHLAL 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1005261232 232 RYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19083 263 AWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-271 |
1.03e-25 |
|
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: 103.85 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 11 NDGHFMPVLGFG--TYAPAEVPKSK--------ALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkRE 77
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGAwggvdqeeADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 78 DIFYTSKLW---------SNSHRPELVRpALERSLKNLQLDYVDLYLIHF-----PV--SVKAMEKCKDAGLAKSIGVSN 141
Cdd:cd19091 81 DVLIATKVRgrmgegpndVGLSRHHIIR-AVEASLKRLGTDYIDLYQLHGfdaltPLeeTLRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 142 FNHRLLEMIL---NKPGLKyKPVCNQVechpYFN------QRKLLDFCKSKDIVLVAYSALGS-------HREEPWVD-- 203
Cdd:cd19091 160 FSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAGgllsgkyRRGQPAPEgs 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 204 ----------PNSPVLLEDPV--LCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNEQRIRQNVQVFEFQLTSEEM 267
Cdd:cd19091 235 rlrrtgfdfpPVDRERGYDVVdaLREIAKETGATPAQVALAWLLSRptvsSVIIGAR--NEEQLEDNLGAAGLSLTPEEI 312
|
....
gi 1005261232 268 KAID 271
Cdd:cd19091 313 ARLD 316
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-204 |
1.29e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 101.89 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 13 GHFMPVLGFGTYAPAevpkSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSkiadgsVKREDIFYTSK--LWS 87
Cdd:cd19105 10 GLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATKasPRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIH----------FPVSVKAMEKCKDAGLAKSIGVS---NFNHRLLEMIlnKP 154
Cdd:cd19105 80 DKKDKAELLKSVEESLKRLQTDYIDIYQLHgvdtpeerllNEELLEALEKLKKEGKVRFIGFSthdNMAEVLQAAI--ES 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261232 155 G------LKYKPVcnqvecHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDP 204
Cdd:cd19105 158 GwfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLS 207
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-271 |
7.52e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 101.13 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 31 KSKALEAVKLAIEAGFHHIDSAHVYNN-EEQVGLAIRSKIADGSVKREDIFYTsKLWSNSHR----PELVRPALERSLKN 105
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHT-KWVPDPGEltmtRAYVEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 106 LQLDYVDLYLIH--------FPVSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPglkYKPVCNQVEcHPYFNQR--- 174
Cdd:cd19101 101 LGVDRLDLVQFHwwdysdpgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQ-YSLLDRRpen 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 175 KLLDFCKSKDIVLVAYSALGS---------HREEPWVDPNSPV-------------------LLEdpVLCALAKKHKRTP 226
Cdd:cd19101 177 GMAALCEDHGIKLLAYGTLAGgllsekylgVPEPTGPALETRSlqkyklmidewggwdlfqeLLR--TLKAIADKHGVSI 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1005261232 227 ALIALRYQLQR----GVVVLAKsyNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19101 255 ANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-263 |
1.35e-24 |
|
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: 99.21 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 15 FMPVLGFGTYAPAEvPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRSKIAD-------GSVKREDifytsK 84
Cdd:cd19088 8 AMRLTGPGIWGPPA-DREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYPDDvviatkgGLVRTGP-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 LWSNSHRPELVRPALERSLKNLQLDYVDLYLIH-------FPVSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLk 157
Cdd:cd19088 82 WWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHridpkvpFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 158 ykpVCNQVECHPYFNQ-RKLLDFCKSKDIVLVAYSALGSHreepwvdpnsPVLLEDPVLCALAKKHKRTPALIALRYQLQ 236
Cdd:cd19088 161 ---VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGG----------DLAQPGGLLAEVAARLGATPAQVALAWLLA 227
|
250 260
....*....|....*....|....*....
gi 1005261232 237 RG--VVVLAKSYNEQRIRQNVQVFEFQLT 263
Cdd:cd19088 228 RSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-262 |
4.03e-24 |
|
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: 98.78 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTY----APAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN-EEQVGLAIRSkiadgsVKREDIFYTSKL-----W 86
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFP------------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNK- 153
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPervpwvdilapgGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 154 ------PGLKYKPvCNQVechpyfNQRKLLDFCKSKDIVLVAYSALG----SHREEPWVDPNSPVLLEDPV-----LCAL 218
Cdd:cd19090 155 dfdvvlTANRYTL-LDQS------AADELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYRWLSPELLdrakrLYEL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1005261232 219 AKKHKRTPALIALRYQLQ----RGVVVLAKsyNEQRIRQNVQVFEFQL 262
Cdd:cd19090 228 CDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPL 273
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-150 |
1.65e-23 |
|
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: 96.54 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTY----APAEVPKSKALEAVKLAIEAGFHHIDSAHVY-NNEEQVGLAIRSkiadgsVKREDIFYTSKLWSNS-- 89
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005261232 90 ------HRPELVRPALERSLKNLQLDYVDLYLIHFPVS-------VKAMEKCKDAGLAKSIGVSNFNHRLLEMI 150
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDdeltgevLETLEDLKAAGKVRYIGVSGDGEELEAAI 148
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-259 |
3.75e-23 |
|
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: 95.32 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTY-----APAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WS 87
Cdd:cd19096 1 SVLGFGTMrlpesDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVS------------VKAMEKCKDAGLAKSIGVSnFnH---RLLEMILN 152
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSpewlekarkgglLEFLEKAKKEGLIRHIGFS-F-HdspELLKEILD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 153 kpglkykpvCNQVEC----HPYFNQ-----RKLLDFCKSKDIVLVAYSAL--GSHREEPwvdpnspvlledPVLCALAKK 221
Cdd:cd19096 153 ---------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVIIMEPLkgGGLANNP------------PEALAILCG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005261232 222 HKRTPALIALRYQL-QRGV-VVLAKSYNEQRIRQNVQVFE 259
Cdd:cd19096 212 APLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-271 |
1.87e-21 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 91.95 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYA------PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19149 12 SVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 LWSNSH----------------RPELVRPALERSLKNLQLDYVDLYLIH-----FPV--SVKAMEKCKDAGLAKSIGVSN 141
Cdd:cd19149 85 RWDREGgsfffvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHwqdveTPIeeTMEALEELKRQGKIRAIGASN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 142 FN-------HRLLEMILNKPglKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSAL-----------------GSHR 197
Cdd:cd19149 165 VSveqikeyVKAGQLDIIQE--KYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLeqglltgkitpdrefdaGDAR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005261232 198 E-EPWVDPNS--PVLLEDPVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19149 236 SgIPWFSPENreKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
29-271 |
1.80e-20 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 89.18 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 29 VPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKIadgsvKREDIFYTSKLWSNSH---------RPELVR 96
Cdd:cd19079 32 LDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFPMGdgpngrglsRKHIMA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 97 pALERSLKNLQLDYVDLYLIH-----FPV--SVKAMEKCKDAGLAKSIGVSN-FNHRLLEM--ILNKPGLKyKPVCNQve 166
Cdd:cd19079 107 -EVDASLKRLGTDYIDLYQIHrwdyeTPIeeTLEALHDVVKSGKVRYIGASSmYAWQFAKAlhLAEKNGWT-KFVSMQ-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 167 chPYFN------QRKLLDFCKSKDIVLVAYSALGSHR---------EEPWVDPNSPVLLED-------PVLCA---LAKK 221
Cdd:cd19079 183 --NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRlarpwgdttERRRSTTDTAKLKYDyfteadkEIVDRveeVAKE 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1005261232 222 HKRTPALIALRYQLQRGVVV-----LAKSYneqRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19079 261 RGVSMAQVALAWLLSKPGVTapivgATKLE---HLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-271 |
2.26e-20 |
|
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: 88.90 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 33 KALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRskiadGSVKREDIFYTSKL---WSNSH------RPELVRPALE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleWDEGGevvrnsSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 101 RSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEmilnkpglKYKPVCNQVECHPYFN- 172
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPdplvpieETAEALKELLDEGKIRAIGVSNFSPEQME--------TFRKVAPLHTVQPPYNl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 173 -----QRKLLDFCKSKDIVLVAYSAL---------GSHREEPWVD----------PNSPVLLEdPV--LCALAKKH--KR 224
Cdd:cd19148 173 fereiEKDVLPYARKHNIVTLAYGALcrgllsgkmTKDTKFEGDDlrrtdpkfqePRFSQYLA-AVeeLDKLAQERygKS 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1005261232 225 TPALiALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19148 252 VIHL-AVRWLLDQPgvSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-271 |
4.91e-20 |
|
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: 88.04 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 42 IEAGFHHIDSAHVYNN----------EEQVGLAIRSkiadgSVKREDIFYTSKL--WSNSHRPEL----VRPALERSLKN 105
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKS-----RGKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 106 LQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILN---KPGLKyKPVCNQvechPYFN--- 172
Cdd:cd19081 111 LQTDYIDLYQAHWDdpatpleETLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQ----PEYNlvd 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 173 ----QRKLLDFCKSKDIVLVAYSALGS-------HREEP--------------WVDPNSPVLledPVLCALAKKHKRTPA 227
Cdd:cd19081 186 resfEGELLPLCREEGIGVIPYSPLAGgfltgkyRSEADlpgstrrgeaakryLNERGLRIL---DALDEVAAEHGATPA 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1005261232 228 LIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19081 263 QVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-256 |
3.58e-19 |
|
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: 85.30 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGT-YAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLA-------IRSKIadgsvKREDIFYTSK---- 84
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRG-----NRDKVVIATKgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 -LWSNS-HR--PELVRPALERSLKNLQLDYVDLYLIH-----FPVS--VKAMEKCKDAGLAKSIGVSNFNH-RLLEMI-- 150
Cdd:cd19082 76 dLEDMSrSRlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPVGeiVDTLNELVRAGKIRAFGASNWSTeRIAEANay 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 151 LNKPGLkYKPVCNQvechPYFN-----------------QRKLLDFCKSKDIVLVAYSALG----SHREEPWVDPNSPVL 209
Cdd:cd19082 156 AKAHGL-PGFAASS----PQWSlarpneppwpgptlvamDEEMRAWHEENQLPVFAYSSQArgffSKRAAGGAEDDSELR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 210 -----------LEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQ 256
Cdd:cd19082 231 rvyyseenferLE--RAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLRDSLA 288
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-195 |
5.80e-19 |
|
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: 83.68 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYA-----PAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSKL---- 85
Cdd:cd19086 5 EIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 -----WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFP--------VSVKAMEKCKDAGLAKSIGVS-NFNHRLLEMIL 151
Cdd:cd19086 78 dggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpdevldndELFEALEKLKQEGKIRAYGVSvGDPEEALAALR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005261232 152 NkpglkYKPVCNQVECHPyFNQR---KLLDFCKSKDIVLVAYSALGS 195
Cdd:cd19086 158 R-----GGIDVVQVIYNL-LDQRpeeELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-270 |
7.09e-19 |
|
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: 84.57 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGT------YAPAEVPKSKALeaVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19076 13 SALGLGCmgmsafYGPADEEESIAT--LHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 LWS-------NSHRPELVRPALERSLKNLQLDYVDLYLIH-----FPV--SVKAMEKCKDAGLAKSIGVSNFN------- 143
Cdd:cd19076 84 VRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQHrvdpnVPIeeTVGAMAELVEEGKVRYIGLSEASadtirra 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 144 HRL-----LEMilnkpglKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG-----------SHREEPWVDPNSP 207
Cdd:cd19076 164 HAVhpitaVQS-------EYSLWTRDIE-------DEVLPTCRELGIGFVAYSPLGrgfltgaikspEDLPEDDFRRNNP 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261232 208 -----------VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAI 270
Cdd:cd19076 230 rfqgenfdknlKLVE--KLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-265 |
4.10e-18 |
|
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: 82.64 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WSNSHR 91
Cdd:cd19074 6 ELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 92 PE---LVRP----ALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFN-HRLLEM--ILNKP 154
Cdd:cd19074 80 PNdrgLSRKhifeSIHASLKRLQLDYVDIYYCHRYdpetpleETVRAMDDLIRQGKILYWGTSEWSaEQIAEAhdLARQF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 155 GLkYKPVCNQVECHpYFNQRK---LLDFCKSKDIVLVAYSAL-----------------GSHREEPWVDPNSPVLLEDPV 214
Cdd:cd19074 160 GL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsRSRATDEDNRDKKRRLLTDEN 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 215 ------LCALAKKHKRTPALIALRYQLQR-GV--VVLAKSYNEQrIRQNVQVFEFQLTSE 265
Cdd:cd19074 238 lekvkkLKPIADELGLTLAQLALAWCLRNpAVssAIIGASRPEQ-LEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-233 |
8.83e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 81.98 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFGTY--APAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKIADGSVKREDIFYTSK--------- 84
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 -------------------------LWSNSHrPELVRPALERSLKNLQLDYVDLYLIHFPV-----------------SV 122
Cdd:cd19099 86 eplrplkyleeklgrglidvadsagLRHCIS-PAYLEDQIERSLKRLGLDTIDLYLLHNPEeqllelgeeefydrleeAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 123 KAMEKCKDAGLAKSIGVSNFN----------HRLLEMIL--------NKPGLK-----YKPVCNQVECHPYFNQRK---L 176
Cdd:cd19099 165 EALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKviqlpLNLLEPEALTEKNTVKGEalsL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261232 177 LDFCKSKDIVLVAYSALGShreepwVDPNSPVLLEDPvlcaLAKKHKRTPALIALRY 233
Cdd:cd19099 245 LEAAKELGLGVIASRPLNQ------GQLLGELRLADL----LALPGGATLAQRALQF 291
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-268 |
1.51e-17 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 80.67 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 16 MPVLGFGTyAPA-----EVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSK--- 84
Cdd:cd19163 13 VSKLGFGA-SPLggvfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYLATKvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 ---LWSNS--HRPELVRPALERSLKNLQLDYVDLYLIH---FPVSV--------KAMEKCKDAGLAKSIGVSNFNHRLLE 148
Cdd:cd19163 86 yglDPDKMfdFSAERITKSVEESLKRLGLDYIDIIQVHdieFAPSLdqilnetlPALQKLKEEGKVRFIGITGYPLDVLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 149 MILNKPG------LKYkpvcnqveCHpY--FNQR--KLLDFCKSKDIVLVAYSALG----SHREEPwvdPNSPVLLEDPV 214
Cdd:cd19163 166 EVLERSPvkidtvLSY--------CH-YtlNDTSllELLPFFKEKGVGVINASPLSmgllTERGPP---DWHPASPEIKE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 215 LCALAKKHKRTP----ALIALRYQLQ--RGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMK 268
Cdd:cd19163 234 ACAKAAAYCKSRgvdiSKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-273 |
7.25e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 78.91 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 36 EAVKLAIEAGFHHIDSAHVYnneeqvGLAIRSKIAdGSV----KREDIF----YTSKLWSNSHRPelVRPALERSLKNLQ 107
Cdd:cd19103 36 AVFDKAMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPREDYIistkFTPQIAGQSADP--VADMLEGSLARLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 108 LDYVDLYLIHFPVSVKA-MEKCKD---AGLAKSIGVSNFNH---RLLEMILNKPGLKYKPVCNQVE-CHPYFNQRKLLDF 179
Cdd:cd19103 107 TDYIDIYWIHNPADVERwTPELIPllkSGKVKHVGVSNHNLaeiKRANEILAKAGVSLSAVQNHYSlLYRSSEEAGILDY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 180 CKSKDIVLVAYSAL-----------------GSHREEPWvdpnSPVL--LED--PVLCALAKKHKRTPALIALRYQLQRG 238
Cdd:cd19103 187 CKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAEIGAKHGASIAQVAIAWAIAKG 262
|
250 260 270
....*....|....*....|....*....|....*
gi 1005261232 239 VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19103 263 TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-273 |
2.94e-16 |
|
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: 77.21 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLG---FGTYA-PAEVPKSKALeaVKLAIEAGFHHIDSAHVYNN---EEQVGlAIRSKIADGSV--KredifyTSKLWSN 88
Cdd:cd19075 4 ILGtmtFGSQGrFTTAEAAAEL--LDAFLERGHTEIDTARVYPDgtsEELLG-ELGLGERGFKIdtK------ANPGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 89 SHRPELVRPALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILN--------K 153
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAPdrstpleETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwvL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 154 P----GLkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSAL------GSHREEPWV------DPNSPVL-------- 209
Cdd:cd19075 155 PtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLaggfltGKYKYSEDKagggrfDPNNALGklyrdryw 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 210 -------LEdpVLCALAKKHKRTPALIALRY-----QLQRG---VVVLAKSyNEQRIRQNVQ-VFEFQLTSEEMKAIDGL 273
Cdd:cd19075 227 kpsyfeaLE--KVEEAAEKEGISLAEAALRWlyhhsALDGEkgdGVILGAS-SLEQLEENLAaLEKGPLPEEVVKAIDEA 303
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-233 |
4.66e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 76.03 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 29 VPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVglairskIADGSVKREDIFYTSKL----WSNSHRPELVRPALERSLK 104
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDSEKV-------LGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 105 NLQLDYVDLYLIH--------FPVSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKYkpVcnQVechPY--FNQR 174
Cdd:cd19097 96 RLKVDSLDGLLLHnpddllkhGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I--QL---PFniLDQR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 175 ----KLLDFCKSKDIVLVAYSA-----LGSHREEP--WVDPNSPVLLEdpvLCALAKKHKRTPALIALRY 233
Cdd:cd19097 169 flksGLLAKLKKKGIEIHARSVflqglLLMEPDKLpaKFAPAKPLLKK---LHELAKKLGLSPLELALGF 235
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-273 |
2.49e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 74.99 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 34 ALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKL-WSNSHRPEL---VRPALERSLKNL 106
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTKVrLDPDDLGDIggqIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 107 QLDYVDLYLIH------------FPVSVK----------AMEKCKDAGLAKSIGVSNFNH-RLLEMIL--NKPG------ 155
Cdd:cd19104 107 KRDSVDLLQLHnrigderdkpvgGTLSTTdvlglggvadAFERLRSEGKIRFIGITGLGNpPAIRELLdsGKFDavqvyy 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 156 --LKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS---------HREEPwVDPNSPVLLE----DPVLcALAK 220
Cdd:cd19104 187 nlLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAgalttsldrGREAP-PTSDSDVAIDfrraAAFR-ALAR 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261232 221 KHKRTPALIALRYQL-QRGV--VVLAKSyNEQRIRQNVQVFEF-QLTSEEMKAIDGL 273
Cdd:cd19104 265 EWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-271 |
8.94e-15 |
|
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: 73.04 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFG----TYAPAEVP-KSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSK------ 84
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKfgfkid 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 85 ------LWSNShRPELVRPALERSLKNLQLDYVDLYLIH-FPVSV------KAMEKCKDAGLAKSIGVSNFNhrlLEMIl 151
Cdd:cd19078 80 ggkpgpLGLDS-RPEHIRKAVEGSLKRLQTDYIDLYYQHrVDPNVpieevaGTMKELIKEGKIRHWGLSEAG---VETI- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 152 nKPGLKYKPVCN-QVECHPYFN--QRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSP--------------------- 207
Cdd:cd19078 155 -RRAHAVCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfdegddraslprftpealean 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261232 208 -VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19078 234 qALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
31-271 |
4.63e-14 |
|
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: 71.44 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 31 KSKALEAVKLAIEAGFHHIDSAHVY-----------------------NNEEQVGLAirSKIADGSvkrEDIFYTSKLWS 87
Cdd:cd19094 17 EAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgrteeiigswlkkkGNRDKVVLA--TKVAGPG---EGITWPRGGGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 88 NsHRPELVRPALERSLKNLQLDYVDLYLIHFP---------------------VS----VKAMEKCKDAGLAKSIGVSNF 142
Cdd:cd19094 92 R-LDRENIREAVEGSLKRLGTDYIDLYQLHWPdrytplfgggyytepseeedsVSfeeqLEALGELVKAGKIRHIGLSNE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 143 N----HRLLEM--ILNKPglkyKPVCNQvecHPY--FNQRKLLDF---CKSKDIVLVAYSAL------GSHREEPWVDPN 205
Cdd:cd19094 171 TpwgvMKFLELaeQLGLP----RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLaggvltGKYLDGAARPEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 206 SPVLL--------EDP-------VLCALAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTSEEM 267
Cdd:cd19094 244 GRLNLfpgymaryRSPqaleavaEYVKLARKHGLSPAQLALAWVRSRpfvTSTIIGATTLEQ-LKENIDAFDVPLSDELL 322
|
....
gi 1005261232 268 KAID 271
Cdd:cd19094 323 AEID 326
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-273 |
7.97e-14 |
|
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: 70.29 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 41 AIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLW------------SNSHrpelVRPALERSLKN 105
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFgpmgddpndrglSRRH----IRRAVEASLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 106 LQLDYVDLYLIHFPVS-------VKAMEKCKDAGLAKSIGVSNF-------------NHRLLEMILNKPglKYKPVCNQV 165
Cdd:cd19087 108 LQTDYIDLYQMHHFDRdtpleetLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRGLLRFVSEQP--MYNLLKRQA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 166 EchpyfnqRKLLDFCKSKDIVLVAYSALG---------------SHR--------EEPWVDPNSPVLLEdpvLCALAKKH 222
Cdd:cd19087 186 E-------LEILPAARAYGLGVIPYSPLAgglltgkygkgkrpeSGRlveraryqARYGLEEYRDIAER---FEALAAEA 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1005261232 223 KRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 273
Cdd:cd19087 256 GLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-271 |
2.36e-13 |
|
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: 68.80 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 20 GFG----TYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVG--LAIRSKIADGSVKREDIFYTSKLWSNSH--- 90
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKGGLDPDtlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 91 ---RPELVRPALERSLKNL-QLDYVDLYLI-----HFPV--SVKAMEKCKDAGLAKSIGVSNFNHrllEMIlnKPGLKYK 159
Cdd:cd19077 89 pdgSPEAVRKSIENILRALgGTKKIDIFEParvdpNVPIeeTIKALKELVKEGKIRGIGLSEVSA---ETI--RRAHAVH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PV-CNQVECHPYFN---QRKLLDFCKSKDIVLVAYSALGS-----HREEPWVDPNSPVLLEDP---------------VL 215
Cdd:cd19077 164 PIaAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRglltgRIKSLADIPEGDFRRHLDrfngenfeknlklvdAL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005261232 216 CALAKKHKRTPALIAL---RYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19077 244 QELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-271 |
2.40e-13 |
|
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: 69.17 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 42 IEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWSN----------SHRPELVRpALERSLKNLQL 108
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKYTMNrrpgdpnaggNHRKNLRR-SVEASLRRLQT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 109 DYVDLYLIHF-----PVS--VKAMEKCKDAGLAKSIGVSNF------------NHRLLEMilnkpglkykPVCNQVEchp 169
Cdd:cd19080 113 DYIDLLYVHAwdfttPVEevMRALDDLVRAGKVLYVGISDTpawvvarantlaELRGWSP----------FVALQIE--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 170 yFN------QRKLLDFCKSKDIVLVAYSALG-------------SHREEPWVDPNSPVLLED------PVLCALAKKHKR 224
Cdd:cd19080 180 -YSllertpERELLPMARALGLGVTPWSPLGgglltgkyqrgeeGRAGEAKGVTVGFGKLTErnwaivDVVAAVAEELGR 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005261232 225 TPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTSEEMKAID 271
Cdd:cd19080 259 SAAQVALAWVRQKpgvVIPIIGARTLEQ-LKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-270 |
5.81e-13 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 67.84 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKIadgsvkREDIFYTSK----LWSNSHR 91
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKfgihEIGGSGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 92 -----PELVRPALERSLKNLQLDYVDLYLIH-------FPVSVKAMEKCKDAGLAKSIGVSNFN----------HRLLEM 149
Cdd:cd19145 94 evrgdPAYVRAACEASLKRLDVDYIDLYYQHridttvpIEITMGELKKLVEEGKIKYIGLSEASadtirrahavHPITAV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 150 ilnkpGLKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALGshREEPWvdpNSPVLLEDPV--------------- 214
Cdd:cd19145 174 -----QLEWSLWTRDIE-------EEIIPTCRELGIGIVPYSPLG--RGFFA---GKAKLEELLEnsdvrkshprfqgen 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261232 215 ----------LCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAI 270
Cdd:cd19145 237 leknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-256 |
2.28e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 60.04 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 42 IEAGFHHIDSAHVYN----------NEEQVG--LAIRSKiadgsvkREDIFYTSKL---------WSNSHR---PELVRP 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGrwLKDRGN-------RDDVVIATKVgagprdpdgGPESPEglsAETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 98 ALERSLKNLQLDYVDLYLIH--FPV-----SVKAMEKCKDAGLAKSIGVSNFNHRLLEM---ILNKPGLKyKPVCNQVEc 167
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAHvdDRDtpleeTLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGWA-EFSAIQQR- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 168 HPYF---------NQR----KLLDFCKS-KDIVLVAYSAL--GSH------REEPWVDPNSPVLLEdpVLCALAKKHKRT 225
Cdd:cd19752 178 HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLlsGAYtrpdrpLPEQYDGPDSDARLA--VLEEVAGELGAT 255
|
250 260 270
....*....|....*....|....*....|....
gi 1005261232 226 PALIALRYQLQR--GVV-VLAKSYNEQrIRQNVQ 256
Cdd:cd19752 256 PNQVVLAWLLHRtpAIIpLLGASTVEQ-LEENLA 288
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-140 |
3.71e-09 |
|
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: 56.60 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYA---PAEVPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRSKiadgsvKREDIFYTSKL----- 85
Cdd:cd19162 1 PRLGLGAASlgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261232 86 -----WSNSHRPEL------VRPALERSLKNLQLDYVDLYLIHFPVS---------VKAMEKCKDAGLAKSIGVS 140
Cdd:cd19162 75 pgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDPDRhllqaltdaFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-134 |
4.67e-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: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFG---TYApAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRskiaDGSVKREDIFYTSKL-W---- 86
Cdd:cd19143 15 ALSFGswvTFG-NQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIfWgggg 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 --SNSH---RPELVRpALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLA 134
Cdd:cd19143 90 ppPNDRglsRKHIVE-GTKASLKRLQLDYVDLVFCHRPdpatpieETVRAMNDLIDQGKA 148
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
20-259 |
6.61e-09 |
|
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: 56.00 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 20 GFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-----WSNSHR 91
Cdd:cd19153 21 ALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVgryrdSEFDYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 92 PELVRPALERSLKNLQLDYVDLYLIH-------FPV---SVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNK--PGlkyK 159
Cdd:cd19153 97 AERVRASVATSLERLHTTYLDVVYLHdiefvdyDTLvdeALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRcsPG---S 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 160 PVCNQVECHPYFNQRKLLD----FCKSKDIVLVAYSALG----SHREEPWVDPNSPVLLEdpvLCALAKKH-----KRTP 226
Cdd:cd19153 174 LDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmgllTSQGPPPWHPASGELRH---YAAAADAVcasveASLP 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 1005261232 227 ALiALRYQL----QRGVVVLAKSYNEQrIRQNVQVFE 259
Cdd:cd19153 251 DL-ALQYSLaahaGVGTVLLGPSSLAQ-LRSMLAAVD 285
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-240 |
1.23e-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: 54.96 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 20 GFGTYAPAEVpkskALEAVKLAIEAGFHHIDSAhvyNN--------EEQVGLAIRSkiaDGSVKREDIFYTSK----LW- 86
Cdd:cd19089 21 NFGDYTSPEE----ARELLRTAFDLGITHFDLA---NNygpppgsaEENFGRILKR---DLRPYRDELVISTKagygMWp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 ----SNSHRPELVRpALERSLKNLQLDYVDLYLIHFPVSVKAMEKCKDA-------GLAKSIGVSNFN----HRLLEmIL 151
Cdd:cd19089 91 gpygDGGSRKYLLA-SLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTAladavrsGKALYVGISNYPgakaRRAIA-LL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 152 NKpgLKYKPVCNQVechPY--FNQ---RKLLDFCKSKDIVLVAYSAL---------------GSHREEPWVDPNSPVLLE 211
Cdd:cd19089 169 RE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylngippDSRRAAESKFLTEEALTP 243
|
250 260 270
....*....|....*....|....*....|....
gi 1005261232 212 DPV-----LCALAKKHKRTPALIALRYQLQRGVV 240
Cdd:cd19089 244 EKLeqlrkLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-183 |
1.43e-08 |
|
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: 55.16 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTYA--PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-WSNsh 90
Cdd:cd19142 14 SNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWSY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 91 RPE---LVRP----ALERSLKNLQLDYVDLYLIH-----FPVS--VKAMEKCKDAGLAKSIGVSNFNH-RLLEMILNKPG 155
Cdd:cd19142 88 GSEergLSRKhiieSVRASLRRLQLDYIDIVIIHkadpmCPMEevVRAMSYLIDNGLIMYWGTSRWSPvEIMEAFSIARQ 167
|
170 180
....*....|....*....|....*....
gi 1005261232 156 LK-YKPVCNQVECHPyfnqrklldFCKSK 183
Cdd:cd19142 168 FNcPTPICEQSEYHM---------FCREK 187
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-259 |
9.19e-08 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 52.28 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYAPA---EVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQV-GLAIrSKIADgSVKREDIFYTSK-----LWSN 88
Cdd:cd19164 17 IFGAATFSYQyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRD-EFPRDTYFIITKvgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 89 SHRPELVRPALERSLKNLQLDYVDLYLIH---FpVS-------VKAMEKCKDAGLAKSIGVSNFN----HRLLEMILNKP 154
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLVYLHdveF-VAdeevleaLKELFKLKDEGKIRNVGISGYPlpvlLRLAELARTTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 155 G------LKYKPVCNQVECHPYFNQRKlldFCKSKDIVLVAYSALG----SHREEPWVDPNSPVLLEDPV-LCALAKKHK 223
Cdd:cd19164 174 GrpldavLSYCHYTLQNTTLLAYIPKF---LAAAGVKVVLNASPLSmgllRSQGPPEWHPASPELRAAAAkAAEYCQAKG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005261232 224 RTPALIALRYQLQ----RGVVVLAKSyNEQRIRQNVQVFE 259
Cdd:cd19164 251 TDLADVALRYALRewggEGPTVVGCS-NVDELEEAVEAYW 289
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-139 |
1.84e-07 |
|
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: 51.46 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 17 PVLGFGTyAP-----AEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvKREDIFYTSKL--- 85
Cdd:cd19152 1 PKLGFGT-APlgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 86 ---------------WSNS-HRPEL------VRPALERSLKNLQLDYVDLYLIHFPV------------------SVKAM 125
Cdd:cd19152 74 lvplqeveptfepgfWNPLpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDPDedlagaesdehfaqaikgAFRAL 153
|
170
....*....|....
gi 1005261232 126 EKCKDAGLAKSIGV 139
Cdd:cd19152 154 EELREEGVIKAIGL 167
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-255 |
4.44e-07 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 50.55 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTyAP-----AEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKLWSNS 89
Cdd:PLN02587 13 SVGFGA-SPlgsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTKCGRYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 90 H----RPELVRPALERSLKNLQLDYVDLYLIH----------FPVSVKAMEKCKDAGLAKSIGVSNFNHRLLEMILNK-- 153
Cdd:PLN02587 88 EgfdfSAERVTKSVDESLARLQLDYVDILHCHdiefgsldqiVNETIPALQKLKESGKVRFIGITGLPLAIFTYVLDRvp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 154 PG-----LKYkpvcnqveCHPYFNQRKLLD---FCKSKDIVLVAYSALG----SHREEPWVDPNSPVLLEdpvLCALAKK 221
Cdd:PLN02587 168 PGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASPLAmgllTENGPPEWHPAPPELKS---ACAAAAT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005261232 222 H----KRTPALIALRYQL--QRGVVVLAKSYNEQRIRQNV 255
Cdd:PLN02587 237 HckekGKNISKLALQYSLsnKDISTTLVGMNSVQQVEENV 276
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
18-141 |
5.92e-07 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 50.24 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYAPAEV-PKSKALEAVKLAIEAGFHHIDSAHVYN----------NEEQVGLAIRSKiadGSvkREDIFYTSKLW 86
Cdd:PRK10625 15 TLGLGTMTFGEQnSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR---GS--REKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 ------SNSHRPEL------VRPALERSLKNLQLDYVDLYLIHFPV------------------------SVKAMEKCKD 130
Cdd:PRK10625 90 gpsrnnDKGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsapavslleTLDALAEQQR 169
|
170
....*....|.
gi 1005261232 131 AGLAKSIGVSN 141
Cdd:PRK10625 170 AGKIRYIGVSN 180
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
41-271 |
2.21e-06 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 48.45 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 41 AIEAGFHHIDSAHVY-----NNEEQVGLAIRSkiaDGSVKREDIFYTSK----LW-----SNSHRPELVrPALERSLKNL 106
Cdd:PRK09912 52 AFDLGITHFDLANNYgpppgSAEENFGRLLRE---DFAAYRDELIISTKagydMWpgpygSGGSRKYLL-ASLDQSLKRM 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 107 QLDYVDLYLIHFPVSVKAMEKCKDA-------GLAKSIGVSNFN----HRLLEMI--LNKPGLKYKPVCNQVecHPYFNQ 173
Cdd:PRK09912 128 GLEYVDIFYSHRVDENTPMEETASAlahavqsGKALYVGISSYSpertQKMVELLreWKIPLLIHQPSYNLL--NRWVDK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 174 RKLLDFCKSKDIVLVAYSALGS-----------------HREEPWVDPNSPVLLEDP------VLCALAKKHKRTPALIA 230
Cdd:PRK09912 206 SGLLDTLQNNGVGCIAFTPLAQglltgkylngipqdsrmHREGNKVRGLTPKMLTEAnlnslrLLNEMAQQRGQSMAQMA 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1005261232 231 LRYQL--QRGVVVLAKSYNEQRIRQNVQVFE-FQLTSEEMKAID 271
Cdd:PRK09912 286 LSWLLkdERVTSVLIGASRAEQLEENVQALNnLTFSTEELAQID 329
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
18-176 |
2.51e-06 |
|
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: 48.21 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 18 VLGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WSNSHR 91
Cdd:cd19141 14 CLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIfWGGKAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 92 PE--LVRP----ALERSLKNLQLDYVDLYLIHFPVS-------VKAMEKCKDAGLAKSIGVSNFNH----------RLLE 148
Cdd:cd19141 90 TErgLSRKhiieGLKASLERLQLEYVDIVFANRPDPntpmeeiVRAFTHVINQGMAMYWGTSRWSAmeimeaysvaRQFN 169
|
170 180
....*....|....*....|....*...
gi 1005261232 149 MIlnkpglkyKPVCNQVECHpYFNQRKL 176
Cdd:cd19141 170 LI--------PPIVEQAEYH-LFQREKV 188
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-176 |
1.78e-05 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 45.42 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WSNSHRP 92
Cdd:cd19159 16 LGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 93 E--LVRP----ALERSLKNLQLDYVDLYLIHFPVS-------VKAMEKCKDAGLAKSIGVSNFN----------HRLLEM 149
Cdd:cd19159 92 ErgLSRKhiieGLKGSLQRLQLEYVDVVFANRPDSntpmeeiVRAMTHVINQGMAMYWGTSRWSameimeaysvARQFNM 171
|
170 180
....*....|....*....|....*..
gi 1005261232 150 IlnkpglkyKPVCNQVECHpYFNQRKL 176
Cdd:cd19159 172 I--------PPVCEQAEYH-LFQREKV 189
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
19-176 |
1.41e-04 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 42.66 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKLW------- 86
Cdd:cd19160 18 LGLGTWVTfgSQISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSK----GWRRSSYVVTTKIYwggqaet 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 87 ----SNSHRPELVRPALERslknLQLDYVDLYLIH-----FPVS--VKAMEKCKDAGLAKSIGVSNFN----------HR 145
Cdd:cd19160 94 erglSRKHIIEGLRGSLDR----LQLEYVDIVFANrsdpnSPMEeiVRAMTYVINQGMAMYWGTSRWSameimeaysvAR 169
|
170 180 190
....*....|....*....|....*....|.
gi 1005261232 146 LLEMIlnkpglkyKPVCNQVECHpYFNQRKL 176
Cdd:cd19160 170 QFNLI--------PPVCEQAEYH-LFQREKV 191
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
32-268 |
4.15e-04 |
|
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: 41.23 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 32 SKALeaVKLAIEAGFHHIDSAHVY-----NNEEQVGLAIRSKIADgsvKREDIFYTSK----LWSNSH-----RPELVrP 97
Cdd:cd19151 32 SRAM--LRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKP---YRDELIISTKagytMWPGPYgdwgsKKYLI-A 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 98 ALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNH-------RLLEMiLNKPGLKYKPVCN 163
Cdd:cd19151 106 SLDQSLKRMGLDYVDIFYHHRPdpetpleETMGALDQIVRQGKALYVGISNYPPeeareaaAILKD-LGTPCLIHQPKYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 164 QVECHPyfnQRKLLDFCKSKDIVLVAYSALG---------------SHREEPWVDPNSPVLLEDPV-----LCALAKKHK 223
Cdd:cd19151 185 MFNRWV---EEGLLDVLEEEGIGCIAFSPLAqglltdrylngipedSRAAKGSSFLKPEQITEEKLakvrrLNEIAQARG 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1005261232 224 RTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQ-VFEFQLTSEEMK 268
Cdd:cd19151 262 QKLAQMALAWVLRNKRVtsVLIGASKPSQIEDAVGaLDNREFSEEELA 309
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
19-174 |
1.04e-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: 40.07 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 19 LGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WSNSHRP 92
Cdd:cd19158 16 LGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKK----GWRRSSLVITTKIfWGGKAET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 93 E--LVRP----ALERSLKNLQLDYVDLYLIHFP-------VSVKAMEKCKDAGLAKSIGVSNFNH-RLLEM--ILNKPGL 156
Cdd:cd19158 92 ErgLSRKhiieGLKASLERLQLEYVDVVFANRPdpntpmeETVRAMTHVINQGMAMYWGTSRWSSmEIMEAysVARQFNL 171
|
170
....*....|....*...
gi 1005261232 157 kYKPVCNQVECHPYFNQR 174
Cdd:cd19158 172 -IPPICEQAEYHMFQREK 188
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
23-118 |
4.53e-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: 38.17 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261232 23 TYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ---VG-----------LAIRSKIADGSVKREDIFYTSKLWSN 88
Cdd:cd19146 26 KSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESerwVGewmasrgnrdeMVLATKYTTGYRRGGPIKIKSNYQGN 105
|
90 100 110
....*....|....*....|....*....|
gi 1005261232 89 sHRPELvRPALERSLKNLQLDYVDLYLIHF 118
Cdd:cd19146 106 -HAKSL-RLSVEASLKKLQTSYIDILYVHW 133
|
|
| |
