|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
15-295 |
0e+00 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 584.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTYSDPR-PVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHD 93
Cdd:cd19109 1 GNSIPIIGLGTYSEPKtTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 94 PEMVRPALERTLQTLKLDYIDLYIIEMPMAFK--------------------------ALEACKDAGLVKSLGVSNFNRR 147
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiyprdengkwlyhktnlcatweALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 148 QLEVILNKPGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPLWVNVSSPPLLKDELLTSLGKKYNKT 227
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958767997 228 QAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPF 295
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-282 |
4.10e-158 |
|
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: 442.82 E-value: 4.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 8 HHIPLNDGNSIPIIGLGTYSdPRPVP-GKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGK 86
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYA-PEEVPkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 87 LWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK--------------------------ALEACKDAGLVKSLG 140
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKpgeelfpkdengklifdtvdlcatweAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 141 VSNFNRRQLEVILNKPGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPLWVNVSSPPLLKDELLTSL 220
Cdd:cd19108 160 VSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958767997 221 GKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 282
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-299 |
1.31e-134 |
|
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: 383.31 E-value: 1.31e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19107 1 GAKMPILGLGTWKSP---PGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAFK--------------------------ALEACKDAGLVKSLGVSNFNRRQ 148
Cdd:cd19107 78 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKpgkelfpldesgnvipsdttfldtweAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 149 LEVILNKPGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPlWVNVSSPPLLKDELLTSLGKKYNKTQ 228
Cdd:cd19107 158 IERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP-WAKPEDPSLLEDPKIKEIAAKHNKTT 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767997 229 AQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPFHDEY 299
Cdd:cd19107 237 AQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-282 |
1.69e-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: 357.36 E-value: 1.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSDPRPVPGKTfiAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLKDDEGVRQ--AVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK-----------------------ALEACKDAGLVKSLGVSNFNR 146
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKenndsesngdgslsdidyletwrGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 147 RQLEVILNkpGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPLWVNvsSPPLLKDELLTSLGKKYNK 226
Cdd:cd19116 161 EQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTN--PPPRLDDPTLVAIAKKYGK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767997 227 TQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 282
Cdd:cd19116 237 TTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
12-282 |
3.01e-123 |
|
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: 354.77 E-value: 3.01e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGK-VKREEIFYCGKLWST 90
Cdd:cd19106 1 LHTGQKMPLIGLGTW---KSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAF--------------------------KALEACKDAGLVKSLGVSNF 144
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFergdnpfpknpdgtirydsthyketwKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 145 NRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPlWVNVSSPPLLKDELLTSLGKKY 224
Cdd:cd19106 158 NSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRP-WAKPDEPVLLEEPKVKALAKKY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958767997 225 NKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 282
Cdd:cd19106 235 NKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
18-273 |
8.56e-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: 8.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWSTDHDPEMV 97
Cdd:cd19071 1 MPLIGLGTYKLK---PEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRES----GVPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 98 RPALERTLQTLKLDYIDLYIIEMPMAF-------------KALEACKDAGLVKSLGVSNFNRRQLEVILNKPglKYKPVT 164
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGkeggskearletwRALEELVDEGLVRSIGVSNFNVEHLEELLAAA--RIKPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 165 NQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPLwvnvsspplLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVI 244
Cdd:cd19071 152 NQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPL---------LDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVI 222
|
250 260
....*....|....*....|....*....
gi 1958767997 245 PKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19071 223 PKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
14-281 |
1.34e-119 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 343.58 E-value: 1.34e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 14 DGNSIPIIGLGTYsdprPVPGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWSTDH 92
Cdd:COG0656 1 NGVEIPALGLGTW----QLPGEEAAaAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA----SGVPREELFVTTKVWNDNH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPM------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGlkYKPVTNQ 166
Cdd:COG0656 73 GYDDTLAAFEESLERLGLDYLDLYLIHWPGpgpyveTWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG--VKPAVNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 167 VECHPYFTQTKLLKFCQQHDIVIVAYSPLGtcrnplwvnvsSPPLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPK 246
Cdd:COG0656 151 VELHPYLQQRELLAFCREHGIVVEAYSPLG-----------RGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPK 219
|
250 260 270
....*....|....*....|....*....|....*
gi 1958767997 247 STTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:COG0656 220 SVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
18-299 |
5.91e-113 |
|
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: 328.46 E-value: 5.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPEMV 97
Cdd:cd19110 4 IPAVGLGTW---KASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 98 RPALERTLQTLKLDYIDLYIIEMPMAFK-----------------------ALEACKD---AGLVKSLGVSNFNRRQLEV 151
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdfldTWEAMEDlviEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 152 ILNKPGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcrnplwvNVSSPPLLKDELLTSLGKKYNKTQAQI 231
Cdd:cd19110 161 LLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGG-------SCEGVDLIDDPVIQRIAKKHGKSPAQI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958767997 232 VLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPFHDEY 299
Cdd:cd19110 234 LIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-280 |
1.59e-110 |
|
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: 322.05 E-value: 1.59e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 9 HIPLNDGNSIPIIGLGTYsDPRPVPGKTfiAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLW 88
Cdd:cd19154 3 SITLSNGVKMPLIGLGTW-QSKGAEGIT--AVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK--------------------------ALEACKDAGLVKSLGVS 142
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKddegesgtmengmsihdavdvedvwrGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 143 NFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTC--RNPLWVNVSSPP--LLKDELLT 218
Cdd:cd19154 160 NFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPgrANFTKSTGVSPApnLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958767997 219 SLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 280
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-270 |
3.56e-108 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 315.82 E-value: 3.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 9 HIPLNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLW 88
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK---------------------ALEACKDAGLVKSLGVSNFNRR 147
Cdd:cd19125 79 CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdipstwkAMEKLVDSGKVRAIGVSNFSVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 148 QLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcRNPLWVNvssPPLLKDELLTSLGKKYNKT 227
Cdd:cd19125 159 KLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWVK---KNVLKDPIVTKVAEKLGKT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958767997 228 QAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMK 270
Cdd:cd19125 233 PAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFA 275
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-282 |
1.92e-103 |
|
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: 303.95 E-value: 1.92e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 11 PLNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWST 90
Cdd:cd19123 5 PLSNGDLIPALGLGTW---KSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK-------------------------ALEACKDAGLVKSLGVSNFN 145
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKkgvgfpesgedllslspipledtwrAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 146 RRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTC-RNPLWVNVSSPPLLKDELLTSLGKKY 224
Cdd:cd19123 162 VKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdRPAAMKAEGEPVLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958767997 225 NKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 282
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-276 |
2.52e-96 |
|
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: 284.47 E-value: 2.52e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWS 89
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQ--IPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS----GIPREELFITTKLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMP-----MAFKALEACKDAGLVKSLGVSNFNRRQLEVILnkPGLKYKPVT 164
Cdd:cd19133 75 QDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPfgdvyGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLI--LHNEVKPAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 165 NQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPLwvnvsspplLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVI 244
Cdd:cd19133 153 NQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNL---------FENPVLTEIAEKYGKSVAQVILRWLIQRGIVVI 223
|
250 260 270
....*....|....*....|....*....|..
gi 1958767997 245 PKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:cd19133 224 PKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-281 |
1.02e-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: 1.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19111 1 GFPMPVIGLGTYQSP---PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAF--------------------KALEACKDAGLVKSLGVSNFNRRQLEVILN 154
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPCGFvnkkdkgerelassdvtsvwRAMEALVSEGKVKSIGLSNFNPRQINKILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 155 KPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcrnPLWVNVSSPP----LLKDELLTSLGKKYNKTQAQ 230
Cdd:cd19111 158 YA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGS---PGRANQSLWPdqpdLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958767997 231 IVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-276 |
8.19e-94 |
|
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: 278.10 E-value: 8.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWS 89
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVS---NDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM--------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKyk 161
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVpaqdkyveTWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 162 PVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGL 241
Cdd:cd19131 153 PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGL 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1958767997 242 VVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:cd19131 222 VVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-273 |
2.21e-90 |
|
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: 268.76 E-value: 2.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYSDPrpvpGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDPEM 96
Cdd:cd19073 1 IPALGLGTWQLR----GDDCAnAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 97 VRPALERTLQTLKLDYIDLYII-------EMPMAFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKykPVTNQVEC 169
Cdd:cd19073 73 LKKSVDRSLEKLGTDYVDLLLIhwpnptvPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP--IAVNQVEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 170 HPYFTQTKLLKFCQQHDIVIVAYSPLG-TCrnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKST 248
Cdd:cd19073 151 HPFLYQAELLEYCRENDIVITAYSPLArGE------------VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKAS 218
|
250 260
....*....|....*....|....*
gi 1958767997 249 TPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19073 219 SEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-280 |
2.50e-90 |
|
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: 270.94 E-value: 2.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 9 HIPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLW 88
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSS---PEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAF----------------------------KALEACKDAGLVKSLG 140
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSlskeddsgkldptgehkqdyttdlldiwKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 141 VSNFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGT-CRNPLWVNVSSPP-----LLKD 214
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpGAAHFSPGTGSPSgsspdLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767997 215 ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 280
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
10-280 |
8.15e-90 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 269.74 E-value: 8.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19112 3 ITLNSGHKMPVIGLGVW---RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHdpEMVRPALERTLQTLKLDYIDLYIIEMPMAFK------------------------------ALEACKDAGLVKSL 139
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgttgsalgedgvldidvtislettwhAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 140 GVSNFnrrqlEVILNKPGLKY---KPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLG-TCRNPLWVNVSSPplLKDE 215
Cdd:cd19112 158 GISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDDP 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958767997 216 LLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 280
Cdd:cd19112 231 VLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
12-281 |
3.38e-89 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 266.56 E-value: 3.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYSDPRpvpGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWST 90
Cdd:cd19157 4 LNNGVKMPWLGLGVFKVEE---GSEVVnAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPM------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPglKYKPVT 164
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVkgkykeTWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADA--EIVPMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 165 NQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVI 244
Cdd:cd19157 155 NQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTI 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958767997 245 PKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19157 224 PKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
18-275 |
1.28e-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: 1.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYSdprpVPGKTFI--AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPE 95
Cdd:cd19136 1 MPILGLGTFR----LRGEEEVrqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 96 MVRPALERTLQTLKLDYIDLYIIEMPMA-----------------FKALEACKDAGLVKSLGVSNFNRRQLEVILNKPgl 158
Cdd:cd19136 77 KARAACLGSLERLGTDYLDLYLIHWPGVqglkpsdprnaelrresWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 159 KYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcrnplwvnvSSPPLLKDELLTSLGKKYNKTQAQIVLRFDIQ 238
Cdd:cd19136 155 EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQ 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958767997 239 RGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19136 226 QGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-275 |
1.45e-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: 260.42 E-value: 1.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAE-GKVKREEIFYCGKLWST 90
Cdd:cd19118 1 LNTGNKIPAIGLGTW---QAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAF-------------------------------KALEACKDAGLVKSL 139
Cdd:cd19118 78 SHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFkptgdlnpltavptnggevdldlsvslvdtwKAMVELKKTGKVKSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 140 GVSNFNRRQLEVILNKPGLkyKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnVSSPPLLKDELLTS 219
Cdd:cd19118 158 GVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767997 220 LGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQifDFSLTKEEMKDIEAL 275
Cdd:cd19118 230 IAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-276 |
9.87e-85 |
|
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: 255.05 E-value: 9.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSDPRPvpGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWS 89
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDG--DETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPglKYKPV 163
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGkdkfidTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA--DVVPA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 164 TNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVV 243
Cdd:cd19126 153 VNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVT 221
|
250 260 270
....*....|....*....|....*....|...
gi 1958767997 244 IPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:cd19126 222 IPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-276 |
7.62e-84 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 252.58 E-value: 7.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYsdprPVPGKT-FIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKLWST 90
Cdd:cd19132 1 LNDGTQIPAIGFGTY----PLKGDEgVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPM--------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKykP 162
Cdd:cd19132 73 HHGYEEALRTIEESLYRLGLDYVDLYLIHWPNpsrdlyveAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVT--P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 163 VTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLV 242
Cdd:cd19132 151 AVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVV 220
|
250 260 270
....*....|....*....|....*....|....
gi 1958767997 243 VIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:cd19132 221 PIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-275 |
1.59e-83 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 251.79 E-value: 1.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 95 EMVRPALERTLQTLKLDYIDLYII-----EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLE--VILNKPGLkykpVTN 165
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLhwpnkDVPLAetLGALNEAQEAGLARHIGVSNFTVALLReaVELSEAPL----FTN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 166 QVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQR-GLVVI 244
Cdd:cd19140 154 QVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAI 222
|
250 260 270
....*....|....*....|....*....|.
gi 1958767997 245 PKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19140 223 PKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
10-287 |
1.87e-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: 253.52 E-value: 1.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSDPRPVPGKTfiaVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQ---IYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK--------------------------------ALEACKDAGLVK 137
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpieekyppgfycgdgdnfvyedvpildtwkALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 138 SLGVSNFNRRQLEVILNkpGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLG-----TCRNPLWVNVssPPLL 212
Cdd:cd19113 160 SIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvELNQGRALNT--PTLF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958767997 213 KDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMW 287
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDPWDW 310
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-281 |
2.55e-83 |
|
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: 251.77 E-value: 2.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGT----YSDPRPVPGKTFI-AVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWS 89
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLVdSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPemvRPALERTLQTLKLDYIDLYIIEMPM-----------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPgl 158
Cdd:cd19120 77 GIKDP---REALRKSLAKLGVDYVDLYLIHSPFfakeggptlaeAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 159 KYKPVTNQVECHPYFT--QTKLLKFCQQHDIVIVAYSPLgtcrNPLWVNVSSPpllKDELLTSLGKKYNKTQAQIVLRFD 236
Cdd:cd19120 152 KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPL----SPLTRDAGGP---LDPVLEKIAEKYGVTPAQVLLRWA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958767997 237 IQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19120 225 LQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-275 |
5.19e-83 |
|
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: 251.42 E-value: 5.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 14 DGNSIPIIGLGTYSDPrPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVK-REEIFYCGKLWSTDH 92
Cdd:cd19124 1 SGQTMPVIGMGTASDP-PSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRPALERTLQTLKLDYIDLYII-----------------------EMPMAFKALEACKDAGLVKSLGVSNFNRRQL 149
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIhwpvslkpgkfsfpieeedflpfDIKGVWEAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 150 EVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPlWvnvSSPPLLKDELLTSLGKKYNKTQA 229
Cdd:cd19124 160 QELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-W---GSNAVMESDVLKEIAAAKGKTVA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958767997 230 QIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19124 234 QVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-276 |
1.04e-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: 250.40 E-value: 1.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWS 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP---PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM---------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKy 160
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVpndfdrtiqAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 161 kPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNPLWVNVSSPP-LLKDELLTSLGKKYNKTQAQIVLRFDIQR 239
Cdd:cd19127 153 -PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGdVLQDPTITGLAEKYGKTPAQIVLRWHLQN 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958767997 240 GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:cd19127 232 GVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-281 |
6.12e-82 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 248.20 E-value: 6.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYSDPRPvpGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKvaegKVKREEIFYCGKLWSTD 91
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDG--AEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 92 HDPEMVRPALERTLQTLKLDYIDLYIIEMPMA------FKALEACKDAGLVKSLGVSNFNRRQLEVILNKpgLKYKPVTN 165
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKgkfkdtWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKS--CKVAPMVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 166 QVECHPYFTQTKLLKFCQQHDIVIVAYSPLGtcrnplwvnvsSPPLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIP 245
Cdd:cd19156 155 QIELHPLLTQEPLRKFCKEKNIAVEAWSPLG-----------QGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIP 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958767997 246 KSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19156 224 KSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-277 |
2.88e-80 |
|
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: 244.71 E-value: 2.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIRekvAEGkVKREEIFYCGKLWSTD 91
Cdd:cd19117 8 LNTGAEIPAVGLGTW---QSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 92 H-DPEMvrpALERTLQTLKLDYIDLYIIEMPMAFKA----------------------------LEACKDAGLVKSLGVS 142
Cdd:cd19117 81 HrRVEE---ALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdfiktwelMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 143 NFNRRQLEVILNKPGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcrnplwvnvSSPPLLKDELLTSLGK 222
Cdd:cd19117 158 NFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS---------TNAPLLKEPVIIKIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958767997 223 KYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIfdFSLTKEEMKDIEALNK 277
Cdd:cd19117 229 KHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
12-281 |
7.75e-78 |
|
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: 239.24 E-value: 7.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYSDPRPVPGKTfiaVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTD 91
Cdd:cd19115 7 LNSGYDMPLVGFGLWKVNNDTCADQ---VYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 92 HDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK-------------------------------ALEACKDAGLVKSLG 140
Cdd:cd19115 84 HDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdpavryppgwfydgkkvefsnapiqetwtAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 141 VSNFNRrQLEVILnkpgLKY---KPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGtcrnPLWV-------NVSSPP 210
Cdd:cd19115 164 VSNFSA-QLLMDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG----PQSFleldlpgAKDTPP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767997 211 LLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19115 235 LFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-275 |
2.34e-77 |
|
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: 236.45 E-value: 2.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 9 HIPLNDGNSIPIIGLGTYSdprpVPGKTFIAVKTAIDE-GYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKL 87
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSH----SGGYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 88 WSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM--------------AFKALEACKDAGLVKSLGVSNFNRRQLEVIL 153
Cdd:cd19135 76 WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDcpssgknvketraeTWRALEELYDEGLCRAIGVSNFLIEHLEQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 154 NKPGLKykPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLgtcrnplwvnvSSPPLLKDELLTSLGKKYNKTQAQIVL 233
Cdd:cd19135 156 EDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-----------AKGKALEEPTVTELAKKYQKTPAQILI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958767997 234 RFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19135 223 RWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-281 |
6.43e-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: 233.89 E-value: 6.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 13 NDGNSIPIIGLGTYSdprPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDH 92
Cdd:cd19129 1 NGSGAIPALGFGTLI---PDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMAFK---------------------------ALEACKDAGLVKSLGVSNFN 145
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQpgdeqdprdangnviyddgvtlldtwrAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 146 RRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGtcrnplwvNVSSPPLLKDELLTSLGKKYN 225
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG--------HGMEPKLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958767997 226 KTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIfdFSLTKEEMKDI-EALNKNVRF 281
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-276 |
7.39e-76 |
|
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: 232.49 E-value: 7.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 9 HIPLNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLW 88
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVP---PADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM--------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKy 160
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTpaagnyvhTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 161 kPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRG 240
Cdd:cd19130 153 -PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHGKTPAQIVLRWHLQKG 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958767997 241 LVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:cd19130 221 HVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
10-280 |
9.23e-75 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 230.34 E-value: 9.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTY--SDPRPVpgktfIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREkvaeGKVKREEIFYCGKL 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWqaSNEEVI-----TAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 88 WSTDHDPemVRPALERTLQTLKLDYIDLYIIEMPM--------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLK 159
Cdd:PRK11565 78 WNDDHKR--PREALEESLKKLQLDYVDLYLMHWPVpaidhyveAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 160 ykPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNplwvNVSSPPLLKDelltsLGKKYNKTQAQIVLRFDIQR 239
Cdd:PRK11565 156 --PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK----GVFDQKVIRD-----LADKYGKTPAQIVIRWHLDS 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958767997 240 GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVR 280
Cdd:PRK11565 225 GLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
12-275 |
1.85e-74 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 229.73 E-value: 1.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGkVKREEIFYCGKLWSTD 91
Cdd:cd19121 6 LNTGASIPAVGLGTWQAK---AGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 92 HDpeMVRPALERTLQTLKLDYIDLYIIEMPMA-----------------------------FKALEACKDAGLVKSLGVS 142
Cdd:cd19121 82 HR--RVELCLDRSLKSLGLDYVDLYLVHWPVLlnpngnhdlfptlpdgsrdldwdwnhvdtWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 143 NFNRRQLEVILnkPGLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcrnplwvnvSSPPLLKDELLTSLGK 222
Cdd:cd19121 160 NYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS---------TGSPLISDEPVVEIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958767997 223 KYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFslTKEEMKDIEAL 275
Cdd:cd19121 229 KHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
19-275 |
2.40e-72 |
|
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: 223.94 E-value: 2.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 19 PIIGLGTYSDPrpvPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPEMVR 98
Cdd:cd19128 2 PRLGFGTYKIT---ESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 99 PALERTLQTLKLDYIDLYIIEMPMAF--------------------------KALEACKDAGLVKSLGVSNFNRRQLEVI 152
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFdmdtdgdprddnqiqslskkpledtwRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 153 LNKpgLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPL-GTCRNPLWVnvssppLLKDELLTSLGKKYNKTQAQI 231
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLgGSYGDGNLT------FLNDSELKALATKYNTTPPQV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958767997 232 VLRFDIQRGL---VVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19128 231 IIAWHLQKWPknySVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-281 |
2.04e-70 |
|
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: 218.57 E-value: 2.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTY--SDprpvpGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKL 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGelSD-----DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 88 WSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM--------AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGlk 159
Cdd:cd19134 74 ATPDQGFTASQAACRASLERLGLDYVDLYLIHWPAgregkyvdSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTF-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 160 YKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQR 239
Cdd:cd19134 152 FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAAHGRTPAQVLLRWSLQL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958767997 240 GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19134 221 GNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-281 |
2.30e-69 |
|
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: 216.98 E-value: 2.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 10 IPLNDGNSIPIIGLGTYSdPRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWS 89
Cdd:cd19119 4 FKLNTGASIPALGLGTAS-PHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPemVRPALERTLQTLKLDYIDLYIIEMPMAFKA--------------------------------LEACKDAGLVK 137
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEKdsddsgkpftpvnddgktryaasgdhittykqLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 138 SLGVSNFNRRQLEVILNKpgLKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTcrnplwvnvSSPPLLKDELL 217
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGS---------HGAPNLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767997 218 TSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIfdFSLTKEEMKDIE--ALNKNVRF 281
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDdiGEKYPVRF 293
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-281 |
2.52e-69 |
|
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: 217.43 E-value: 2.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDP 94
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 95 EMVRPALERTLQTLKLDYIDLYIIEMPMAFK--------------------------------ALEACKDAGLVKSLGVS 142
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdpaenypflwkdkelkkfpleqspmqecwrEMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 143 NFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGtcrNPLWVNVSS-----PPLLKDELL 217
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFG---NAVYTKVTKhlkhfTNLLEHPVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958767997 218 TSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRF 281
Cdd:cd19114 233 KKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-275 |
9.16e-68 |
|
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: 211.44 E-value: 9.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYsdpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDPEMV 97
Cdd:cd19139 1 IPAFGLGTF---RLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 98 RPALERTLQTLKLDYIDLYII-------EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGlKYKPVTNQVE 168
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIhwpspndEVPVEeyIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG-AGAIATNQIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 169 CHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKST 248
Cdd:cd19139 153 LSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSST 221
|
250 260
....*....|....*....|....*..
gi 1958767997 249 TPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19139 222 KREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
12-277 |
1.76e-60 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 194.38 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 12 LNDGNSIPIIGLGTYSDpRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEG-KVKREEIFYCGKLWST 90
Cdd:cd19122 3 LNNGVKIPAVGFGTFAN-EGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 DHDPEMVRPALERTLQTLKLDYIDLYIIEMPMA------------------------------FKALEACKDAGLVKSLG 140
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAaekndqrspklgpdgkyvilkdltenpeptWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 141 VSNFNRRQLEVILNKPglKYKPVTNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRNplwVNVSSPPLLKDELLTSL 220
Cdd:cd19122 162 VSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNEV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958767997 221 GKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSltkeeMKDIEALNK 277
Cdd:cd19122 237 AEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELS-----DEDFEAINQ 288
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
21-276 |
2.22e-60 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 193.68 E-value: 2.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTYS----DPRPVPGKTFIAVKTAIDEGYRHIDGAYVYR---NEHEVGEAIREKvaegKVKREEIFYCGKL------ 87
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 88 WSTDHDPEMVRPALERTLQTLKLDYIDLYII-----EMPM--AFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPglKY 160
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLhwpdpDTPIeeTWDALEELKKEGKIRAIGVSNFDAEQIEKALTKG--KI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 161 KPVTNQVECHPYF--TQTKLLKFCQQHDIVIVAYSPLG----------------TCRNPLWVNVSSPPLLKDELLTSLGK 222
Cdd:pfam00248 155 PIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpGERRRLLKKGTPLNLEALEALEEIAK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767997 223 KYNKTQAQIVLRF--DIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALN 276
Cdd:pfam00248 235 EHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-273 |
2.71e-59 |
|
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: 190.13 E-value: 2.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTY------SDPRPVPGKTFIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFYCG 85
Cdd:cd19072 1 GEEVPVLGLGTWgigggmSKDYSDDKKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 86 KLWSTDHDPEMVRPALERTLQTLKLDYIDLYII-----EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGl 158
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIhwpnpSIPIEetLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 159 KYKPVTNQVECHPYFT--QTKLLKFCQQHDIVIVAYSPLG---TCRNPLwvnvssppllkDELLTSLGKKYNKTQAQIVL 233
Cdd:cd19072 154 KGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEkgkLSNAKG-----------SPLLDEIAKKYGKTPAQIAL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958767997 234 RFDIQR-GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19072 223 NWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-282 |
1.48e-57 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 186.00 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 17 SIPIIGLGTYSdprpVPGKTFIA-VKTAIDEGYRHIDGAYVYRNEHEVGEAIrekvAEGKVKREEIFYCGKLWSTDHDPE 95
Cdd:PRK11172 2 SIPAFGLGTFR----LKDQVVIDsVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 96 MVRPALERTLQTLKLDYIDLYII-------EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGlKYKPVTNQ 166
Cdd:PRK11172 74 KLIPSLKESLQKLRTDYVDLTLIhwpspndEVSVEefMQALLEAKKQGLTREIGISNFTIALMKQAIAAVG-AENIATNQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 167 VECHPYFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnvssppLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPK 246
Cdd:PRK11172 153 IELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPS 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958767997 247 STTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFV 282
Cdd:PRK11172 222 STKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-273 |
6.92e-48 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 160.88 E-value: 6.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 8 HHIPLNDGNSIPIIGLGT-YSDPRPVPGKTFI-AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIF 82
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTwYMGEDPAKRAQEIeALRAGIDLGMTLIDTAEMYgdgGSEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 83 YCGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYII----EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLEVILNKP 156
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLhwrgGVPLAetVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 157 GLKyKPVTNQVECH-----PYFTqtkLLKFCQQHDIVIVAYSPLGTCRNPlwvnvsSPPLLKDELLTSLGKKYNKTQAQI 231
Cdd:cd19138 154 GGG-NCAANQVLYNlgsrgIEYD---LLPWCREHGVPVMAYSPLAQGGLL------RRGLLENPTLKEIAARHGATPAQV 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958767997 232 VLRFDIQRGLVV-IPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19138 224 ALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-270 |
1.61e-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: 159.66 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGT----------YSDPRPVPGktfiAVKTAIDEGYRHIDGAYVYRNEHE---VGEAIREkvaegkVKREEI 81
Cdd:cd19137 1 GEKIPALGLGTwgiggfltpdYSRDEEMVE----LLKTAIELGYTHIDTAEMYGGGHTeelVGKAIKD------FPREDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 82 FYCGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMP-------MAFKALEACKDAGLVKSLGVSNFNRRQLEVILN 154
Cdd:cd19137 71 FIVTKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPnpnipleETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 155 KpgLKYKPVTNQVECHPY---FTQTKLLKFCQQHDIVIVAYSPLgtcrnplwvnvSSPPLLKDELLTSLGKKYNKTQAQI 231
Cdd:cd19137 151 K--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRTLEEIAKNYGKTIAQI 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958767997 232 VLRFDIQR-GLVVIPKSTTPERIKENFQIFDFSLTKEEMK 270
Cdd:cd19137 218 ALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMK 257
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
39-273 |
3.13e-38 |
|
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: 136.59 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVAegkvkREEIFYCGKLWST--DHDPEMVRPALERTLQTLKLDYI 113
Cdd:cd19093 31 AFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATKFAPLpwRLTRRSVVKALKASLERLGLDSI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 114 DLYIIEMPMAF--------KALEACKDAGLVKSLGVSNFNRRQLEVI---LNKPGlkYKPVTNQVE---CHPYFTQTKLL 179
Cdd:cd19093 106 DLYQLHWPGPWysqiealmDGLADAVEEGLVRAVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 180 KFCQQHDIVIVAYSPLG--------TCRNP------------LWVNVssPPLLkdELLTSLGKKYNKTQAQIVLRFDIQR 239
Cdd:cd19093 184 PACDELGITLIAYSPLAqglltgkySPENPppggrrrlfgrkNLEKV--QPLL--DALEEIAEKYGKTPAQVALNWLIAK 259
|
250 260 270
....*....|....*....|....*....|....
gi 1958767997 240 GLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19093 260 GVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-275 |
4.90e-37 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 134.15 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 13 NDGNSIPIIGLGTYS---DPRPVPGKTFIA-VKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvKREEIFYCG 85
Cdd:COG0667 8 RSGLKVSRLGLGTMTfggPWGGVDEAEAIAiLDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 86 KL--------WSTDHDPEMVRPALERTLQTLKLDYIDLYII-----EMPM--AFKALEACKDAGLVKSLGVSNFNRRQLE 150
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLhrpdpDTPIeeTLGALDELVREGKIRYIGVSNYSAEQLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 151 VILNKPGLKYKPVTNQVEchpY--FTQT---KLLKFCQQHDIVIVAYSPL-----------------GTCRNPLWVNVSS 208
Cdd:COG0667 162 RALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLagglltgkyrrgatfpeGDRAATNFVQGYL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767997 209 PPLLKD--ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:COG0667 239 TERNLAlvDALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-273 |
1.27e-36 |
|
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: 132.26 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYS----DPRPVPGKTFI-AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIrekvaegKVKREEIFY---CGK 86
Cdd:cd19084 4 VSRIGLGTWAiggtWWGEVDDQESIeAIKAAIDLGINFFDTAPVYgfgHSEEILGKAL-------KGRRDDVVIatkCGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 87 LWSTDH------DPEMVRPALERTLQTLKLDYIDLYII-----EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLEVIl 153
Cdd:cd19084 77 RWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIhwpdpNTPIEetAEALEKLKKEGKIRYIGVSNFSVEQLEEA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 154 nkpgLKY-KPVTNQVechPY--FTQ---TKLLKFCQQHDIVIVAYSPLGT-----------------CRNPLwVNVSSPP 210
Cdd:cd19084 156 ----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAQglltgkykkeptfppddRRSRF-PFFRGEN 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958767997 211 LLKD----ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19084 228 FEKNleivDKLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-279 |
2.14e-33 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 123.85 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYSdprPVPGKTFI---------AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCG 85
Cdd:cd19085 1 VSRLGLGCWQ---FGGGYWWGdqddeesiaTIHAALDAGINFFDTAEAYgdgHSEEVLGKALKGR-------RDDVVIAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 86 KLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM-------AFKALEACKDAGLVKSLGVSNFNRRQLEVILnKPGl 158
Cdd:cd19085 71 KVSPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSsdvpleeTMEALEKLKEEGKIRAIGVSNFGPAQLEEAL-DAG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 159 kyKPVTNQVECHPYFTQ--TKLLKFCQQHDIVIVAYSPL-----------------GTCRNPLwVNVSSPPLLKD----- 214
Cdd:cd19085 149 --RIDSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLaqglltgkfssaedfppGDARTRL-FRHFEPGAEEEtfeal 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958767997 215 ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNV 279
Cdd:cd19085 226 EKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
21-275 |
1.04e-31 |
|
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: 119.83 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGT--------YSDPRPVPGKTFiaVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvKREEIFYCGK--- 86
Cdd:cd19083 14 IGLGTnavgghnlYPNLDEEEGKDL--VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgah 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 87 LWST-----DHDPEMVRPALERTLQTLKLDYIDLYIIEMP-------MAFKALEACKDAGLVKSLGVSNFNRRQLEViLN 154
Cdd:cd19083 86 KFGGdgsvlNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPdgetpkaEAVGALQELKDEGKIRAIGVSNFSLEQLKE-AN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 155 KPGL------KYKPVTNQVECHpyftqtkLLKFCQQHDIVIVAYSPL-----------------GTCRN--PLWVNVS-S 208
Cdd:cd19083 165 KDGYvdvlqgEYNLLQREAEED-------ILPYCVENNISFIPYFPLasgllagkytkdtkfpdNDLRNdkPLFKGERfS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958767997 209 PPLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19083 238 ENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-278 |
1.24e-29 |
|
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: 114.46 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 13 NDGNSIPIIGLGT-----YSDPRPVPGKTFIAVKTAIDEGYRHIDGAYVYR-NEHEVGEAIreKVAEGKvkREEIFYCGK 86
Cdd:cd19144 8 RNGPSVPALGFGAmglsaFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWF--KQNPGK--REKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 87 L----------WSTDHDPEMVRPALERTLQTLKLDYIDLYI---------IEMPMAfkALEACKDAGLVKSLGVSNFN-- 145
Cdd:cd19144 84 FgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYqhrvdgktpIEKTVA--AMAELVQEGKIKHIGLSECSae 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 146 --RRQLEVilnkpglkyKPVTN-QVECHPYFT-----QTKLLKFCQQHDIVIVAYSPLGtcRNPLWVNVSSP-------- 209
Cdd:cd19144 162 tlRRAHAV---------HPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLG--RGFLTGAIRSPddfeegdf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 210 ----PLLKDE----------LLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19144 231 rrmaPRFQAEnfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIR 310
|
....*
gi 1958767997 274 ALNKN 278
Cdd:cd19144 311 EIAEE 315
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-258 |
2.63e-29 |
|
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: 111.46 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTYSDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVaegkvKREEIFYCGKL--------W 88
Cdd:cd06660 3 LGLGTMTFGGDGDEEEAFAlLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-----NRDDVVIATKGghppggdpS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYII-----EMPM--AFKALEACKDAGLVKSLGVSNFNRRQLEVILN--KPGLK 159
Cdd:cd06660 78 RSRLSPEHIRRDLEESLRRLGTDYIDLYYLhrddpSTPVeeTLEALNELVREGKIRYIGVSNWSAERLAEALAyaKAHGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 160 YKPVTNQVE---CHPYFTQTKLLKFCQQHDIVIVAYSPLGtcRNPlwvnvssppllkdelltslgkkynktqAQIVLRFD 236
Cdd:cd06660 158 PGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA--RGP---------------------------AQLALAWL 208
|
250 260
....*....|....*....|....
gi 1958767997 237 IQRGLV--VIPKSTTPERIKENFQ 258
Cdd:cd06660 209 LSQPFVtvPIVGARSPEQLEENLA 232
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
39-268 |
5.40e-29 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 112.17 E-value: 5.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 39 AVKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKvaegKVKREEIFY---CG-KLWST---------DHDPEMVRPALE 102
Cdd:COG4989 36 LIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELqtkCGiRLPSEardnrvkhyDTSKEHIIASVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 103 RTLQTLKLDYIDLYIIEMPMAF-------KALEACKDAGLVKSLGVSNFNRRQLEViLNKpGLKYKPVTNQVECHPYFTQ 175
Cdd:COG4989 112 GSLRRLGTDYLDLLLLHRPDPLmdpeevaEAFDELKASGKVRHFGVSNFTPSQFEL-LQS-ALDQPLVTNQIELSLLHTD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 176 T---KLLKFCQQHDIVIVAYSPLGTCRnplWVNVSSPPLLK-DELLTSLGKKYNKTQAQIVLRFdIQR---GLVVIPKST 248
Cdd:COG4989 190 AfddGTLDYCQLNGITPMAWSPLAGGR---LFGGFDEQFPRlRAALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTT 265
|
250 260
....*....|....*....|
gi 1958767997 249 TPERIKENFQIFDFSLTKEE 268
Cdd:COG4989 266 NPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
39-268 |
3.33e-28 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 109.95 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 39 AVKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKvaegKVKREEIFY---CG-KLWST---------DHDPEMVRPALE 102
Cdd:cd19092 29 LIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIqtkCGiRLGDDprpgrikhyDTSKEHILASVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 103 RTLQTLKLDYIDLYIIEMP--------MAfKALEACKDAGLVKSLGVSNFNRRQLEvILNKpGLKYKPVTNQVEC---HP 171
Cdd:cd19092 105 GSLKRLGTDYLDLLLLHRPdplmdpeeVA-EAFDELVKSGKVRYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 172 YFTQTKLLKFCQQHDIVIVAYSPLGTCRnplwvnVSSPPLLKDE----LLTSLGKKYNKTQAQIVLRFdIQR---GLVVI 244
Cdd:cd19092 182 EAIDDGTLDYCQLLDITPMAWSPLGGGR------LFGGFDERFQrlraALEELAEEYGVTIEAIALAW-LLRhpaRIQPI 254
|
250 260
....*....|....*....|....
gi 1958767997 245 PKSTTPERIKENFQIFDFSLTKEE 268
Cdd:cd19092 255 LGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-275 |
7.03e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 103.91 E-value: 7.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFY---CGKLW------STDHDPEMVRPALERTLQ 106
Cdd:cd19102 31 AIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVatkCGLLWdeegriRRSLKPASIRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 107 TLKLDYIDLYIIEMPM-------AFKALEACKDAGLVKSLGVSNFNRRQLEVIlnkpgLKYKPVT-NQVechPYF----- 173
Cdd:cd19102 104 RLGVDVIDLYQIHWPDpdepieeAWGALAELKEEGKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYSllrrg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 174 TQTKLLKFCQQHDIVIVAYSPLG----TCR------NPLWVN-------VSSPPLLKD-----ELLTSLGKKYNKTQAQI 231
Cdd:cd19102 176 IEAEILPFCAEHGIGVIVYSPMQsgllTGKmtpervASLPADdwrrrspFFQEPNLARnlalvDALRPIAERHGRTVAQL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958767997 232 VLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19102 256 AIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-265 |
4.03e-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: 98.06 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGT------YSDPRPVPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIRE---------KVaeGKVKR 78
Cdd:cd19088 1 VSRLGYGAmrltgpGIWGPPADREEAIAVlRRALELGVNFIDTADSYgpdVNERLIAEALHPypddvviatKG--GLVRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 79 EeifycGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMA-------FKALEACKDAGLVKSLGVSNFNRRQLEV 151
Cdd:cd19088 79 G-----PGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPkvpfeeqLGALAELQDEGLIRHIGLSNVTVAQIEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 152 ILNKPGLkykpVTNQVECHPYFTQT-KLLKFCQQHDIVIVAYSPLGtcrnplwvnvSSPPLLKDELLTSLGKKYNKTQAQ 230
Cdd:cd19088 154 ARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLG----------GGDLAQPGGLLAEVAARLGATPAQ 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958767997 231 IVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLT 265
Cdd:cd19088 220 VALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-273 |
3.46e-22 |
|
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: 93.84 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTYS---DPRPVPGKTFIAV-KTAIDEGYRHIDGAYVY------RNEHEVGEAIReKVAEgkvKREEIFYC------ 84
Cdd:cd19077 8 IGLGLMGltwRPNPTPDEEAFETmKAALDAGSNLWNGGEFYgppdphANLKLLARFFR-KYPE---YADKVVLSvkggld 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 85 GKLWSTDHDPEMVRPALERTLQTLK-LDYIDLY---------IIEMPMafKALEACKDAGLVKSLGVSNFN----RRQLE 150
Cdd:cd19077 84 PDTLRPDGSPEAVRKSIENILRALGgTKKIDIFeparvdpnvPIEETI--KALKELVKEGKIRGIGLSEVSaetiRRAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 151 VilnkpglkYKPVTNQVECHPYFT---QTKLLKFCQQHDIVIVAYSPLGtcRNPLWVNVSSPPLLKD------------- 214
Cdd:cd19077 162 V--------HPIAAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLG--RGLLTGRIKSLADIPEgdfrrhldrfnge 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767997 215 ---------ELLTSLGKKYNKTQAQIVLRFDIQRG---LVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19077 232 nfeknlklvDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
19-256 |
1.05e-21 |
|
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: 92.23 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 19 PIIGLGTY---SDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVYRN-EHEVGEAIREkvaegkVKREEIFYCGKL-----W 88
Cdd:cd19090 1 SALGLGTAglgGVFGGVDDDEAVAtIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM------------AFKALEACKDAGLVKSLGVS----NFNRR----- 147
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPErvpwvdilapggALEALLELKEEGLIKHIGLGggppDLLRRaietg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 148 QLEVILnkPGLKYKPVTNQVEchpyftqTKLLKFCQQHDIVIVAYSPLG----TCRNPLWVNVSSPPLLKDEL-----LT 218
Cdd:cd19090 155 DFDVVL--TANRYTLLDQSAA-------DELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYRWLSPELLdrakrLY 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958767997 219 SLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKEN 256
Cdd:cd19090 226 ELCDEHGVPLPALALRFLLRDPRIstVLVGASSPEELEQN 265
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-274 |
1.56e-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: 92.34 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNS---IPIIGLGTYS---DPRPVPGKTFIAVKT---AIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIF 82
Cdd:cd19149 5 GKSgieASVIGLGTWAiggGPWWGGSDDNESIRTihaALDLGINLIDTAPAYgfgHSEEIVGKAIKGR-------RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 83 Y---CGKLW----------STDHD------PEMVRPALERTLQTLKLDYIDLYI---------IEMPMAfkALEACKDAG 134
Cdd:cd19149 78 LatkCGLRWdreggsfffvRDGVTvyknlsPESIREEVEQSLKRLGTDYIDLYQthwqdvetpIEETME--ALEELKRQG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 135 LVKSLGVSNFNRRQLevilnKPGLKYKPV-TNQVechPY-----FTQTKLLKFCQQHDIVIVAYSPL------------- 195
Cdd:cd19149 156 KIRAIGASNVSVEQI-----KEYVKAGQLdIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYSPLeqglltgkitpdr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 196 ----GTCRN--PLWVNVSSPPLLK-DELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLTK 266
Cdd:cd19149 228 efdaGDARSgiPWFSPENREKVLAlLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSA 307
|
....*...
gi 1958767997 267 EEMKDIEA 274
Cdd:cd19149 308 EDIATMRS 315
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-275 |
1.54e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 89.32 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 39 AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFYcgklwSTDHDPEM-------VRPALERTLQTL 108
Cdd:cd19103 37 VFDKAMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYII-----STKFTPQIagqsadpVADMLEGSLARL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 109 KLDYIDLYIIEMPMAFKA----LEACKDAGLVKSLGVSNFNRRQLEV---ILNKPGLKYKPVTNQVE-CHPYFTQTKLLK 180
Cdd:cd19103 106 GTDYIDIYWIHNPADVERwtpeLIPLLKSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQNHYSlLYRSSEEAGILD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 181 FCQQHDIVIVAYS-----------------PLGTCR----NPLWvnvsspPLLKD--ELLTSLGKKYNKTQAQIVLRFDI 237
Cdd:cd19103 186 YCKENGITFFAYMvleqgalsgkydtkhplPEGSGRaetyNPLL------PQLEEltAVMAEIGAKHGASIAQVAIAWAI 259
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958767997 238 QRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19103 260 AKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-256 |
4.71e-20 |
|
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: 86.76 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTYSDPRPVPGKT-----FIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEI---------FY 83
Cdd:cd19086 6 IGFGTWGLGGDWWGDVddaeaIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVviatkfgnrFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 84 CGKLWSTDHDPEMVRPALERTLQTLKLDYIDLY--------IIEMPMAFKALEACKDAGLVKSLGVSnfnrrqleviLNK 155
Cdd:cd19086 79 GGPERPQDFSPEYIREAVEASLKRLGTDYIDLYqlhnppdeVLDNDELFEALEKLKQEGKIRAYGVS----------VGD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 156 P--GLKYKpVTNQVEC--HPY--FTQT---KLLKFCQQHDIVIVAYSPLgtcrnplwvnvssppllkDE-LLTslGKKyn 225
Cdd:cd19086 149 PeeALAAL-RRGGIDVvqVIYnlLDQRpeeELFPLAEEHGVGVIARVPL------------------ASgLLT--GKL-- 205
|
250 260 270
....*....|....*....|....*....|...
gi 1958767997 226 ktqAQIVLRFDIQRGLV--VIPKSTTPERIKEN 256
Cdd:cd19086 206 ---AQAALRFILSHPAVstVIPGARSPEQVEEN 235
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-196 |
1.17e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 85.61 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYSDPRpVPGKTFIA-VKTAIDEGYRHIDGAYVYRNEHE-VGEAIREKvaegkvkREEIFYCGKLWStdHDPE 95
Cdd:cd19100 11 VSRLGFGGGPLGR-LSQEEAAAiIRRALDLGINYFDTAPSYGDSEEkIGKALKGR-------RDKVFLATKTGA--RDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 96 MVRPALERTLQTLKLDYIDLYII---------EMPM----AFKALEACKDAGLVKSLGVSN---------FNRRQLEVIL 153
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLhavdteedlDQVFgpggALEALLEAKEEGKIRFIGISGhspevllraLETGEFDVVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958767997 154 NkpglkykPVtNQVECHPYFTQTKLLKFCQQHDIVIVAYSPLG 196
Cdd:cd19100 161 F-------PI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLA 195
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
13-272 |
1.44e-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: 86.50 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 13 NDGNSIPIIGLGT------YSDPrpvPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIF 82
Cdd:cd19076 7 TQGLEVSALGLGCmgmsafYGPA---DEEESIATlHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 83 Y---CGKLWS-------TDHDPEMVRPALERTLQTLKLDYIDLYII-----EMPMAfKALEACKD---AGLVKSLGVSNF 144
Cdd:cd19076 77 IatkFGIVRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQhrvdpNVPIE-ETVGAMAElveEGKVRYIGLSEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 145 N----RR----------QLEvilnkpglkYKPVTNQVEchpyftqTKLLKFCQQHDIVIVAYSPLGtcRNPLWVNVSSPP 210
Cdd:cd19076 156 SadtiRRahavhpitavQSE---------YSLWTRDIE-------DEVLPTCRELGIGFVAYSPLG--RGFLTGAIKSPE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 211 LLKD----------------------ELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLTK 266
Cdd:cd19076 218 DLPEddfrrnnprfqgenfdknlklvEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTP 297
|
....*.
gi 1958767997 267 EEMKDI 272
Cdd:cd19076 298 EELAEI 303
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-259 |
4.15e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 84.56 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYSDPRPVPGktfiAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFYCGKLWSTDH-- 92
Cdd:cd19105 13 VSRLGFGGGGLPRESPE----LLRRALDLGINYFDTAEGYgngNSEEIIGEALK------GLRRDKVFLATKASPRLDkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRPALERTLQTLKLDYIDLYIIEMPMA----------FKALEACKDAGLVKSLGVS-NFNRRQL----------EV 151
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLHGVDTpeerllneelLEALEKLKKEGKVRFIGFStHDNMAEVlqaaiesgwfDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 152 ILnkpgLKYKPVtnqvecHPYFTQTKLLKFCQQHDIVIVAYSPLGtcrnplwvnvsSPPLLKDELLTSLGKKYNKTQAqi 231
Cdd:cd19105 163 IM----VAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLA-----------GGYLQPALLSVLKAKGFSLPQA-- 219
|
250 260 270
....*....|....*....|....*....|
gi 1958767997 232 VLRFDIQRGLV--VIPKSTTPERIKENFQI 259
Cdd:cd19105 220 ALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
19-256 |
1.42e-18 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 83.05 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 19 PIIGLGTYS--DPRPVP--GKTFIAVKTAIDEGYRHIDGAYVY-RNEHEVGEAIREkvaegkVKREEIFYCGKLWST--- 90
Cdd:cd19095 1 SVLGLGTSGigRVWGVPseAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 91 -----DHDPEMVRPALERTLQTLKLDYIDLYII-------EMPMAFKALEACKDAGLVKSLGVSNFN--------RRQLE 150
Cdd:cd19095 75 grdrkDFSPAAIRASIERSLRRLGTDYIDLLQLhgpsddeLTGEVLETLEDLKAAGKVRYIGVSGDGeeleaaiaSGVFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 151 VIlnkpglkykpvtnQVechPY----FTQTKLLKFCQQHDIVIVAYSPLGTCRNPLWVNVSSPPLLKDELLTSLGKKYNK 226
Cdd:cd19095 155 VV-------------QL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIGGA 218
|
250 260 270
....*....|....*....|....*....|..
gi 1958767997 227 TQAQIVLRFDIQRGLV--VIPKSTTPERIKEN 256
Cdd:cd19095 219 TWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-275 |
2.52e-18 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 84.10 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 15 GNSIPIIGLGTYSDPRpVPGKTFIA-VKTAIDEGYRHIDGAYVYRN-EHEVGEAIREKvaegkvkREEIFYCGKLWSTDH 92
Cdd:COG1453 10 GLEVSVLGFGGMRLPR-KDEEEAEAlIRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLPPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRPALERTLQTLKLDYIDLYII---------EMPM----AFKALEACKDAGLVKSLGVSNFNRrqLEVILnkpglk 159
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIhglnteedlEKVLkpggALEALEKAKAEGKIRHIGFSTHGS--LEVIK------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 160 yKPV-TNQVEC-----HPYFTQ----TKLLKFCQQHDIVIVAYSPL--GTCRNPlwvnvssPPLLKDELltslgkKYNKT 227
Cdd:COG1453 154 -EAIdTGDFDFvqlqyNYLDQDnqagEEALEAAAEKGIGVIIMKPLkgGRLANP-------PEKLVELL------CPPLS 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958767997 228 QAQIVLRF--DIQRGLVVIPKSTTPERIKENFQIFD--FSLTKEEMKDIEAL 275
Cdd:COG1453 220 PAEWALRFllSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
21-275 |
5.87e-18 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 81.97 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTY---------SDPRPvpgktfiAVKT---AIDEGYRHIDGAYVY---RNEHEVGEAIrekvaEGKVKREEIFY-- 83
Cdd:cd19148 7 IALGTWaiggwmwggTDEKE-------AIETihkALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIat 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 84 -CGKLWSTDH------DPEMVRPALERTLQTLKLDYIDLYIIEMP-------MAFKALEACKDAGLVKSLGVSNFNRRQL 149
Cdd:cd19148 75 kVGLEWDEGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPdplvpieETAEALKELLDEGKIRAIGVSNFSPEQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 150 EVIlnkpgLKYKPV-TNQVechPY--FTQT---KLLKFCQQHDIVIVAYSPLgtCRNPLwvnvsSPPLLKD--------- 214
Cdd:cd19148 155 ETF-----RKVAPLhTVQP---PYnlFEREiekDVLPYARKHNIVTLAYGAL--CRGLL-----SGKMTKDtkfegddlr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 215 ------------------ELLTSLGKK-YNKTQAQIVLRFDIQRGLVVIP--KSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19148 220 rtdpkfqeprfsqylaavEELDKLAQErYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
..
gi 1958767997 274 AL 275
Cdd:cd19148 300 AI 301
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
21-273 |
1.14e-17 |
|
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: 81.13 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLG----TYSDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVY---RNEHEVGEAIrekvaegKVKREEIFYCGKL-WSTD 91
Cdd:cd19078 7 IGLGcmgmSHGYGPPPDKEEMIElIRKAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFgFKID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 92 HD----------PEMVRPALERTLQTLKLDYIDLYII-----EMPMAFKAlEACKD---AGLVKSLGVS----NFNRRQL 149
Cdd:cd19078 80 GGkpgplgldsrPEHIRKAVEGSLKRLQTDYIDLYYQhrvdpNVPIEEVA-GTMKElikEGKIRHWGLSeagvETIRRAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 150 EVilnkpglkyKPVTN-QVECHPYF--TQTKLLKFCQQHDIVIVAYSPLG-----------------TCRNplWVNVSSP 209
Cdd:cd19078 159 AV---------CPVTAvQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdegDDRA--SLPRFTP 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958767997 210 -------PLLkdELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19078 228 ealeanqALV--DLLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
21-273 |
2.95e-17 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 80.32 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLG--TYSDPRPVP-------GKTFIavKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKVaegkvKREEIFYCGKLW 88
Cdd:cd19079 15 LCLGcmSFGDPKWRPwvldeeeSRPII--KRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 -STDHDPEM-------VRPALERTLQTLKLDYIDLYII-----EMPM--AFKALEACKDAGLVKSLGVSNFNRRQLEVIL 153
Cdd:cd19079 88 fPMGDGPNGrglsrkhIMAEVDASLKRLGTDYIDLYQIhrwdyETPIeeTLEALHDVVKSGKVRYIGASSMYAWQFAKAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 154 N---KPGLKyKPVTNQvechPYFT------QTKLLKFCQQHDIVIVAYSPL-----------------GTCRNPLWVNVS 207
Cdd:cd19079 168 HlaeKNGWT-KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLargrlarpwgdtterrrSTTDTAKLKYDY 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 208 SPPLLKD--ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIP--KSTTPERIKENFQIFDFSLTKEEMKDIE 273
Cdd:cd19079 243 FTEADKEivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-196 |
6.77e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 79.28 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTYS-DPRPVPGKTFI-AVKTAIDEGYRHIDGAYVYRN---EHEVGEAIREKVAEGKVKREEIFYC---GKLwsTDH 92
Cdd:cd19099 6 LGLGTYRgDSDDETDEEYReALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVtkaGYI--PGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRP--------------------------------ALERTLQTLKLDYIDLYII-----------------EMPMA 123
Cdd:cd19099 84 GDEPLRPlkyleeklgrglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLhnpeeqllelgeeefydRLEEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 124 FKALEACKDAGLVKSLGVSNFN------------------RRQLEVILNKPGLKYkpVtnQVECHPYFTQ---------- 175
Cdd:cd19099 164 FEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKV--I--QLPLNLLEPEaltekntvkg 239
|
250 260
....*....|....*....|...
gi 1958767997 176 --TKLLKFCQQHDIVIVAYSPLG 196
Cdd:cd19099 240 eaLSLLEAAKELGLGVIASRPLN 262
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-274 |
1.11e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 78.41 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 39 AVKTAIDEGYRHIDGAYVY-RNEHEVGEAIREKVAEGKVKREEIF---YCGKLWSTDHDPEMVRPALERTLQTLKLDYID 114
Cdd:cd19101 28 AMAAYVDAGLTTFDCADIYgPAEELIGEFRKRLRRERDAADDVQIhtkWVPDPGELTMTRAYVEAAIDRSLKRLGVDRLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 115 L------------YIiempMAFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPglkYKPVTNQVEC-----HPyftQTK 177
Cdd:cd19101 108 LvqfhwwdysdpgYL----DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 178 LLKFCQQHDIVIVAYSPLG----TCRnplWVNVSSPP--------LLKD--------------ELLTSL---GKKYNKTQ 228
Cdd:cd19101 178 MAALCEDHGIKLLAYGTLAggllSEK---YLGVPEPTgpaletrsLQKYklmidewggwdlfqELLRTLkaiADKHGVSI 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958767997 229 AQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEA 274
Cdd:cd19101 255 ANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
19-261 |
2.27e-16 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 76.83 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 19 PIIGLGT----YSDPRPVPGKTFIA-VKTAIDEGYRHIDGAYVYRN---EHEVGEAIREkvaegkVKREEIFYCGKL-WS 89
Cdd:cd19096 1 SVLGFGTmrlpESDDDSIDEEKAIEmIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDHDPEMVRPALERTLQTLKLDYIDLYIIEMPM------------AFKALEACKDAGLVKSLGVSnF--NRRQLEVILNk 155
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNspewlekarkggLLEFLEKAKKEGLIRHIGFS-FhdSPELLKEILD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 156 pglkykpvTNQVEC----HPYFTQ-----TKLLKFCQQHDIVIVAYSPLGTCRNPlwvnvSSPPLLKDELltslgKKYNK 226
Cdd:cd19096 153 --------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVIIMEPLKGGGLA-----NNPPEALAIL-----CGAPL 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958767997 227 TQAQIVLRF--DIQRGLVVIPKSTTPERIKENFQIFD 261
Cdd:cd19096 215 SPAEWALRFllSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
21-272 |
1.83e-14 |
|
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: 72.08 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLG----TYSDPRPVPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVAEgKVKREEIFYC----GKLW 88
Cdd:cd19145 15 QGLGcmglSGDYGAPKPEEEGIALiHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPRE-KVQLATKFGIheigGSGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDLYI---------IEMPMAfkALEACKDAGLVKSLGVSNFN----RRQLEVilnk 155
Cdd:cd19145 94 EVRGDPAYVRAACEASLKRLDVDYIDLYYqhridttvpIEITMG--ELKKLVEEGKIKYIGLSEASadtiRRAHAV---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 156 pglkyKPVTN-QVECHPYF--TQTKLLKFCQQHDIVIVAYSPLGtcRNPLWvnvSSPPLLKD------------------ 214
Cdd:cd19145 168 -----HPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG--RGFFA---GKAKLEELlensdvrkshprfqgenl 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958767997 215 -------ELLTSLGKKYNKTQAQIVLRFDIQRG--LVVIPKSTTPERIKENFQIFDFSLTKEEMKDI 272
Cdd:cd19145 238 eknkvlyERVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
43-275 |
3.40e-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: 71.83 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 43 AIDEGYRHIDGAYVY----RNEHE-VGEAIREKVAEGKVKREEIFYCGKL--------W----STDHDPEMVRPALERTL 105
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppSPETQgRTEEIIGSWLKKKGNRDKVVLATKVagpgegitWprggGTRLDRENIREAVEGSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 106 QTLKLDYIDLYII-----------------------EMPMA--FKALEACKDAGLVKSLGVSN--------FNR--RQLE 150
Cdd:cd19094 107 KRLGTDYIDLYQLhwpdrytplfgggyytepseeedSVSFEeqLEALGELVKAGKIRHIGLSNetpwgvmkFLElaEQLG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 151 VilnkPglkyKPVTNQvecHPY--FTQTK---LLKFCQQHDIVIVAYSPLG--------------TCR-----NPLWVNV 206
Cdd:cd19094 187 L----P----RIVSIQ---NPYslLNRNFeegLAEACHRENVGLLAYSPLAggvltgkyldgaarPEGgrlnlFPGYMAR 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958767997 207 SSPPLLKDEL--LTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMKDIEAL 275
Cdd:cd19094 256 YRSPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
40-277 |
4.77e-13 |
|
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: 68.41 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 40 VKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCGKLWS-TDHDP--------EMVRpALERTLQT 107
Cdd:cd19091 45 VDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDVLIATKVRGrMGEGPndvglsrhHIIR-AVEASLKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 108 LKLDYIDLY----------IIEmpmAFKALEACKDAGLVKSLGVSNFNRRQLEVIL---NKPGLKyKPVTNQVechpYFT 174
Cdd:cd19091 117 LGTDYIDLYqlhgfdaltpLEE---TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 175 ------QTKLLKFCQQHDIVIVAYSPLG----------------TCRNPLwVNVSSPPLLKD------ELLTSLGKKYNK 226
Cdd:cd19091 189 llgrdlEHELMPLALDQGVGLLVWSPLAggllsgkyrrgqpapeGSRLRR-TGFDFPPVDRErgydvvDALREIAKETGA 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958767997 227 TQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEmkdIEALNK 277
Cdd:cd19091 268 TPAQVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEE---IARLDK 317
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
40-267 |
1.49e-12 |
|
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: 66.46 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 40 VKTAIDEGYRHIDGAYVYRN---EHEVGEAIRekvaegKVKREEIFYCGKL-WSTDHDP-------EMVRPALERTLQTL 108
Cdd:cd19074 28 VRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKVfWPTGPGPndrglsrKHIFESIHASLKRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 109 KLDYIDLYII-----EMPMAfKALEACKD---AGLVKSLGVSNFNRRQLE--VILNKPGLKYKPVTNQVECHPYFTQ--T 176
Cdd:cd19074 102 QLDYVDIYYChrydpETPLE-ETVRAMDDlirQGKILYWGTSEWSAEQIAeaHDLARQFGLIPPVVEQPQYNMLWREieE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 177 KLLKFCQQHDIVIVAYSPL---------------------GTCRNPLWVNvsspPLLKDEL------LTSLGKKYNKTQA 229
Cdd:cd19074 181 EVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsrsraTDEDNRDKKR----RLLTDENlekvkkLKPIADELGLTLA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958767997 230 QIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKE 267
Cdd:cd19074 257 QLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
44-270 |
2.68e-11 |
|
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: 63.00 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 44 IDEGYRHIDGAYVY----------RNEHEVGEAIREKVaegkvKREEIFYCGKL-WSTDHD-----PEMVRPALERTLQT 107
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-----KRDRVVIATKVgFPMGPNgpglsRKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 108 LKLDYIDLYII-----EMPMA--FKALEACKDAGLVKSLGVSNFNRRQLEVILN---KPGLKyKPVTNQVEchpY----- 172
Cdd:cd19081 111 LQTDYIDLYQAhwddpATPLEetLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQPE---Ynlvdr 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 173 -FTQTKLLKFCQQHDIVIVAYSPLG--------TCRNPLWVNVSSPPLLKD----------ELLTSLGKKYNKTQAQIVL 233
Cdd:cd19081 187 eSFEGELLPLCREEGIGVIPYSPLAggfltgkyRSEADLPGSTRRGEAAKRylnerglrilDALDEVAAEHGATPAQVAL 266
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958767997 234 RFDIQRGLV--VIPKSTTPERIKENFQIFDFSLTKEEMK 270
Cdd:cd19081 267 AWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVA 305
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
45-196 |
2.71e-11 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 62.96 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 45 DEGYRHIDGAYVYRN-EHE--VGEAireKVAEGKVKreeIfyCGK---LWSTDHDPEMVRPALERTLQTLKLDYIDLYII 118
Cdd:cd19075 31 ERGHTEIDTARVYPDgTSEelLGEL---GLGERGFK---I--DTKanpGVGGGLSPENVRKQLETSLKRLKVDKVDVFYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 119 EMP-----MAfKALEACKD---AGLVKSLGVSNFNRRQLEVILN--------KP----GLkYKPVTNQVEchpyftqTKL 178
Cdd:cd19075 103 HAPdrstpLE-ETLAAIDElykEGKFKEFGLSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TEL 173
|
170
....*....|....*...
gi 1958767997 179 LKFCQQHDIVIVAYSPLG 196
Cdd:cd19075 174 FPCLRKLGIRFYAYSPLA 191
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-196 |
3.06e-09 |
|
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: 56.81 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 41 KTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvkREEIFYCGKLW-STDHDPEM-------VRPALERTLQTLK 109
Cdd:cd19087 37 DRALDAGINFFDTADVYgggRSEEIIGRWIAGR-------RDDIVLATKVFgPMGDDPNDrglsrrhIRRAVEASLRRLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 110 LDYIDLYII-----EMPM--AFKALEACKDAGLVKSLGVSNF-------------NRRQLEVILNKPglKYKPVTNQVEC 169
Cdd:cd19087 110 TDYIDLYQMhhfdrDTPLeeTLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRGLLRFVSEQP--MYNLLKRQAEL 187
|
170 180
....*....|....*....|....*..
gi 1958767997 170 HpyftqtkLLKFCQQHDIVIVAYSPLG 196
Cdd:cd19087 188 E-------ILPAARAYGLGVIPYSPLA 207
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
21-258 |
6.64e-09 |
|
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: 55.64 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGTySDPRPVPGKT--FIAVKTAIDEGYRHIDGAYVYRNEHEVGEAirEKV----AEGKVKREEIFYCGK-----LWS 89
Cdd:cd19082 3 IVLGT-ADFGTRIDEEeaFALLDAFVELGGNFIDTARVYGDWVERGAS--ERVigewLKSRGNRDKVVIATKgghpdLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 90 TDH---DPEMVRPALERTLQTLKLDYIDLYII-----EMPMA--FKALEACKDAGLVKSLGVSNFN--R-RQLEVILNKP 156
Cdd:cd19082 80 MSRsrlSPEDIRADLEESLERLGTDYIDLYFLhrddpSVPVGeiVDTLNELVRAGKIRAFGASNWSteRiAEANAYAKAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 157 GLkYKPVTNQV---------ECHPYFTQT----KLLKFCQQHDIVIVAYSPL-----------GTCRNPLWVNV--SSPP 210
Cdd:cd19082 160 GL-PGFAASSPqwslarpnePPWPGPTLVamdeEMRAWHEENQLPVFAYSSQargffskraagGAEDDSELRRVyySEEN 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958767997 211 LLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIP--KSTTPERIKENFQ 258
Cdd:cd19082 239 FERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLA 288
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
18-270 |
1.53e-08 |
|
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: 54.86 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 18 IPIIGLGTYS---DPRPVPGKTFI-AVKTAIDEGYRHIDGAYVY---RNEHEVGEAIRekvaegKVKREEIFY---CGK- 86
Cdd:cd19163 13 VSKLGFGASPlggVFGPVDEEEAIrTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLatkVGRy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 87 --LWSTDHD--PEMVRPALERTLQTLKLDYIDLY-------------IIEmpMAFKALEACKDAGLVKSLGVSNFNRRQL 149
Cdd:cd19163 87 glDPDKMFDfsAERITKSVEESLKRLGLDYIDIIqvhdiefapsldqILN--ETLPALQKLKEEGKVRFIGITGYPLDVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 150 -EVILNKPG-----LKYkpvtnqveCHpYFTQ----TKLLKFCQQHDIVIVAYSPLG----TCRN-PLWvnVSSPPLLKD 214
Cdd:cd19163 165 kEVLERSPVkidtvLSY--------CH-YTLNdtslLELLPFFKEKGVGVINASPLSmgllTERGpPDW--HPASPEIKE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 215 --ELLTSLGKKYNKTQAQIVLRFDIQ--RGLVVIPKSTTPERIKENFQIFDFSLTKEEMK 270
Cdd:cd19163 234 acAKAAAYCKSRGVDISKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
20-268 |
4.77e-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: 53.43 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 20 IIGLGTYS-----DPRPVPgkTFIAVKTAIDEGYRHIDGAYVYRNEHEV-GEAIreKVAEGKVKREEIFYCGK-----LW 88
Cdd:cd19164 17 IFGAATFSyqyttDPESIP--PVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL--KALRDEFPRDTYFIITKvgrygPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 89 STDHDPEMVRPALERTLQTLKLDYIDL-Y-----------IIEmpmAFKALEACKDAGLVKSLGVSNFnrrQLEVILNKP 156
Cdd:cd19164 93 DFDYSPEWIRASVERSLRRLHTDYLDLvYlhdvefvadeeVLE---ALKELFKLKDEGKIRNVGISGY---PLPVLLRLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 157 GLKYKPVTNQVE-----CHPYFTQTKLLKF-----CQQHDIVIVAYSPL--GTCRN---PLWvnVSSPPLLKD------E 215
Cdd:cd19164 167 ELARTTAGRPLDavlsyCHYTLQNTTLLAYipkflAAAGVKVVLNASPLsmGLLRSqgpPEW--HPASPELRAaaakaaE 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958767997 216 LLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPErIKENFQIFDFSLTKEE 268
Cdd:cd19164 245 YCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDE-LEEAVEAYWSVLAGAS 296
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-193 |
8.44e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 52.14 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 40 VKTAIDEGYRHIDGAYVYRNEHEV-GEAIREKvaegkvkrEEIFYCGKL----WSTDHDPEMVRPALERTLQTLKLDYID 114
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 115 LY--------IIEMPMAFKALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKYkpVtnQVECHPY---FTQTKLLKFCQ 183
Cdd:cd19097 104 GLllhnpddlLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I--QLPFNILdqrFLKSGLLAKLK 179
|
170
....*....|
gi 1958767997 184 QHDIVIVAYS 193
Cdd:cd19097 180 KKGIEIHARS 189
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
21-144 |
8.88e-07 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 49.63 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 21 IGLGT------YsdpRPVPGKTFIAV-KTAIDEGYRHIDGAYVY---RNEHEVGEAIREK-----VAEGKVkreeifycG 85
Cdd:cd19161 3 LGLGTaglgnlY---TAVSNADADATlDAAWDSGIRYFDTAPMYghgLAEHRLGDFLREKprdefVLSTKV--------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 86 KLWSTDHDPEMVRP----------------------ALERTLQTLKLDYID-LYI------------------IEMPMAF 124
Cdd:cd19161 72 RLLKPAREGSVPDPngfvdplpfeivydysydgimrSFEDSLQRLGLNRIDiLYVhdigvythgdrkerhhfaQLMSGGF 151
|
170 180
....*....|....*....|..
gi 1958767997 125 KALEACKDAGLVK--SLGVSNF 144
Cdd:cd19161 152 KALEELKKAGVIKafGLGVNEV 173
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
93-256 |
1.40e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 48.87 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 93 DPEMVRPALERTLQTLKLDYIDLY----------IIEMPMAFKALeacKDAGLVKSLGVSNFNRRQLEV---ILNKPGL- 158
Cdd:cd19752 93 SAETIEQEIDKSLRRLGTDYIDLYyahvddrdtpLEETLEAFNEL---VKAGKVRAIGASNFAAWRLERarqIARQQGWa 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 159 KYKPVTNQvecHPYF-------------TQTKLLKFCQQH-DIVIVAYSPLgtcrnpLWVNVSSP--PLLKD-------- 214
Cdd:cd19752 170 EFSAIQQR---HSYLrprpgadfgvqriVTDELLDYASSRpDLTLLAYSPL------LSGAYTRPdrPLPEQydgpdsda 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958767997 215 --ELLTSLGKKYNKTQAQIVLRFDIQRGLVVIP--KSTTPERIKEN 256
Cdd:cd19752 241 rlAVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEEN 286
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
37-142 |
2.07e-06 |
|
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: 48.12 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 37 FIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKvaegkvKREEIFYCGKL----------WSTDHDPEM------V 97
Cdd:cd19162 22 AATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrllepgaagRPAGADRRFdfsadgI 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958767997 98 RPALERTLQTLKLDYIDL-YIIEMPM--------AFKALEACKDAGLVKSLGVS 142
Cdd:cd19162 96 RRSIEASLERLGLDRLDLvFLHDPDRhllqaltdAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
19-263 |
8.72e-05 |
|
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: 43.37 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 19 PIIGLGT------YsdpRPVP-GKTFIAVKTAIDEGYRHIDGAYVY---RNEHEVGEAIREKVAEG-----KV------- 76
Cdd:cd19152 1 PKLGFGTaplgnlY---EAVSdEEAKATLVAAWDLGIRYFDTAPWYgagLSEERLGAALRELGREDyvistKVgrllvpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 77 -KREEIFYCGkLWST-DHDPEM------VRPALERTLQTLKLDYID-LYI--IEMPM---------------AFKALEAC 130
Cdd:cd19152 78 qEVEPTFEPG-FWNPlPFDAVFdysydgILRSIEDSLQRLGLSRIDlLSIhdPDEDLagaesdehfaqaikgAFRALEEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 131 KDAGLVKSLGV-SN---FNRRQLEV-------------ILNKPGLkykpvtnqvechpyftqTKLLKFCQQHDIVIVAYS 193
Cdd:cd19152 157 REEGVIKAIGLgVNdweVILRILEEadldwvmlagrytLLDHSAA-----------------RELLPECEKRGVKVVNAG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767997 194 PL------GTCRNPLWVNVSSPPLLKD--ELLTSLGKKYNKTQAQIVLRFDIQRGLV--VIPKSTTPERIKENFQIFDFS 263
Cdd:cd19152 220 PFnsgflaGGDNFDYYEYGPAPPELIArrDRIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALLATE 299
|
|
| |
