|
Name |
Accession |
Description |
Interval |
E-value |
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-306 |
3.34e-168 |
|
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: 469.38 E-value: 3.34e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKVYWPTGPGK 89
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKVFWPTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 NDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHG 169
Cdd:cd19074 81 NDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 170 YNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDKKSGaGMISEWLREEVLT 249
Cdd:cd19074 161 LIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEDNR-DKKRRLLTDENLE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 250 AVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPS 306
Cdd:cd19074 240 KVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-320 |
3.83e-146 |
|
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: 414.58 E-value: 3.83e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWiTHG---SQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYEL 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 78 FTKVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQ 157
Cdd:COG0667 80 ATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 158 IASALTIqdAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDkksgaG 237
Cdd:COG0667 160 LRRALAI--AEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAAT-----N 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 238 MISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTALGK 317
Cdd:COG0667 233 FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAA 312
|
...
gi 1848926078 318 LPE 320
Cdd:COG0667 313 VPA 315
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-312 |
6.07e-134 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 383.48 E-value: 6.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRESYELF 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKelGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKVYWPT-GPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQ 157
Cdd:cd19143 81 TKIFWGGgGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 158 IASALTIQDAHGYNRFVSSQPQYSALWRV-IEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYlpGKKAPAGSR-ATDKKSG 235
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKY--NNGIPEGSRlALPGYEW 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848926078 236 AGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGV--KLDPSTMRAID 312
Cdd:cd19143 239 LKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlpKLTPEVMEKIE 317
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-314 |
5.29e-127 |
|
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: 366.17 E-value: 5.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYG--------NWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRR 72
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfggggGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 73 ESYELFTKVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSE 152
Cdd:cd19091 80 DDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 153 WSAAQIASALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRatdK 232
Cdd:cd19091 160 FSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGSR---L 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 233 KSGAGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19091 237 RRTGFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLD 316
|
..
gi 1848926078 313 TA 314
Cdd:cd19091 317 KV 318
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-312 |
1.92e-126 |
|
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: 364.20 E-value: 1.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNwITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELFTK 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG-RRDDIVLATK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 81 VYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIAS 160
Cdd:cd19087 79 VFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 161 ALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDKKsgaGMIS 240
Cdd:cd19087 159 AQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERAR---YQAR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848926078 241 EWlREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19087 236 YG-LEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEID 306
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-312 |
6.68e-113 |
|
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: 329.93 E-value: 6.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 2 EYRRLGSTGMYVSEI-----SYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKG-VRRESY 75
Cdd:cd19079 1 EYVRLGNSGLKVSRLclgcmSFGDPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEfAPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 76 ELFTKVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSA 155
Cdd:cd19079 81 VIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 156 AQIASALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYlpgkkAPAGSRATDKKSG 235
Cdd:cd19079 161 WQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPW-----GDTTERRRSTTDT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 236 AGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19079 236 AKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-312 |
3.93e-103 |
|
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: 304.45 E-value: 3.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYGNWI---THGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYeLFTKVY-WPT 85
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVV-IATKCGlRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 86 GPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQiasaltIQ 165
Cdd:cd19084 80 GGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQ------LE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 166 DAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKK-APAGSRATDKKsgagmISEWLR 244
Cdd:cd19084 154 EARKYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTfPPDDRRSRFPF-----FRGENF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848926078 245 EEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19084 229 EKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-312 |
3.55e-98 |
|
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: 292.20 E-value: 3.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 5 RLGSTGMYVSEISYGNWiTHGSQVEAEAAIKCVKTALDEGITTFDTADVY-------AGTRAEVVLGKALKG-VRRESYE 76
Cdd:cd19081 1 PLGRTGLSVSPLCLGTM-VFGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLKSrGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 77 LFTKVYWPTGPgkNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAA 156
Cdd:cd19081 80 IATKVGFPMGP--NGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 157 QIASALTIQDAHGYNRFVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRatdkksG 235
Cdd:cd19081 158 RLQEALELSRQHGLPRYVSLQPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTR------R 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 236 AGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19081 232 GEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-314 |
4.62e-94 |
|
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: 281.40 E-value: 4.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 13 VSEISYGNW----ITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELFTKVyWPtgpg 88
Cdd:cd19085 1 VSRLGLGCWqfggGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG-RRDDVVIATKV-SP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 89 kndRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIasaltiQDAH 168
Cdd:cd19085 75 ---DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQL------EEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 169 GYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDK----KSGAgmisewlR 244
Cdd:cd19085 146 DAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLfrhfEPGA-------E 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 245 EEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTA 314
Cdd:cd19085 219 EETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-312 |
4.61e-86 |
|
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: 260.71 E-value: 4.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWI--THGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKG--VRRESYELFTKVywPTGPGKND 91
Cdd:pfam00248 1 IGLGTWQlgGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDypVKRDKVVIATKV--PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 92 RGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTiqdaHGYN 171
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALT----KGKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 172 RFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDKKSGAgmisewlrEEVLTAV 251
Cdd:pfam00248 155 PIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGT--------PLNLEAL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848926078 252 AKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:pfam00248 227 EALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARID 287
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-299 |
4.48e-85 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 259.11 E-value: 4.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 3 YRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGT--RAEVVLGKALK---GVRREsyEL 77
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPpgSAEENFGRILKrdlRPYRD--EL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 78 F--TKVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSA 155
Cdd:cd19089 79 VisTKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 156 AQIASALTIQDAHGYnRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkAPAGSRAtdKKSG 235
Cdd:cd19089 159 AKARRAIALLRELGV-PLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNG--IPPDSRR--AAES 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 236 AGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19089 234 KFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-297 |
2.57e-82 |
|
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: 248.97 E-value: 2.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 14 SEISYGNWIThGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGV-RRESYELFTKVYWPTGPGKNDR 92
Cdd:cd06660 1 SRLGLGTMTF-GGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRgNRDDVVIATKGGHPPGGDPSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 93 GLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYNR 172
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 173 FVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkkapagsratdkksgagmisewlreevltav 251
Cdd:cd06660 160 FAAVQPQYSLLDRsPMEEELLDWAEENGLPLLAYSPLARG---------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1848926078 252 aklapvakeagltMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVK 297
Cdd:cd06660 200 -------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-315 |
2.84e-82 |
|
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: 251.44 E-value: 2.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 19 GNWITHGSQVEAEAaIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYeLFTKV-YWPTGPGKNDRGLSRK 97
Cdd:cd19102 15 GWGGGWGPQDDRDS-IAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPI-VATKCgLLWDEEGRIRRSLKPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 98 HIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIqdahgynRFVSS- 176
Cdd:cd19102 93 SIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI-------HPIASl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 177 QPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRatDKKSGAGMISEWLREEVLTAVAKLAP 256
Cdd:cd19102 166 QPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVASLPAD--DWRRRSPFFQEPNLARNLALVDALRP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1848926078 257 VAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTAL 315
Cdd:cd19102 244 IAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-312 |
1.10e-80 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 247.52 E-value: 1.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 4 RRLGSTGMYVSEISYG------NWithGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYEL 77
Cdd:cd19080 1 RLLGRSGLRVSPLALGtmtfgtEW---GWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG-NRDRIVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 78 FTKVYWPTGPGK-NDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAA 156
Cdd:cd19080 77 ATKYTMNRRPGDpNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 157 QIASALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkKAPAGSRATDKKSGA 236
Cdd:cd19080 157 VVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRG-EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848926078 237 GMISEwlREEVLtaVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19080 236 GKLTE--RNWAI--VDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-312 |
7.14e-79 |
|
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: 243.33 E-value: 7.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 3 YRRLGSTGMYVSEISYGNWITHG----SQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELF 78
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGgpwwGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG-RRDKVVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKV----------YWPTGPGKN-DRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHY 147
Cdd:cd19149 80 TKCglrwdreggsFFFVRDGVTvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 148 IGFSEWSAAQiasaltIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGs 227
Cdd:cd19149 160 IGASNVSVEQ------IKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAG- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 228 ratDKKSGAGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPST 307
Cdd:cd19149 233 ---DARSGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAED 309
|
....*
gi 1848926078 308 MRAID 312
Cdd:cd19149 310 IATMR 314
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-307 |
1.30e-78 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 242.35 E-value: 1.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 3 YRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKAL--KGVRRESYELFTK 80
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILkkKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 81 VYWpTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIAS 160
Cdd:cd19141 82 IFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 161 ALTIqdAHGYNRF--VSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkAPAGSRATDKKSGag 237
Cdd:cd19141 161 AYSV--ARQFNLIppIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDG--VPEYSRASLKGYQ-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 238 miseWLREEVLTAVAK--------LAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGV--KLDPST 307
Cdd:cd19141 235 ----WLKEKILSEEGRrqqaklkeLQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVlpKLTPNI 310
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-312 |
8.86e-78 |
|
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: 240.93 E-value: 8.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 13 VSEISYGNwITHGSQVEAEAAIKCVKTALDEGITTFDTADVYA-------GTRAEVVLGKALKG-VRRESYELFTKVywp 84
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKkGNRDKVVLATKV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 85 TGPG-------KNDRGLSRKHIIESCNASLKRLKTDHIDLYQMH-----------RFDVE-------TPLEESLSAFDDL 139
Cdd:cd19094 77 AGPGegitwprGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHwpdrytplfggGYYTEpseeedsVSFEEQLEALGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 140 IRAGKVHYIGFSEWSAAQIASALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLP 219
Cdd:cd19094 157 VKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 220 GKKAPAGSRATDKKSGAGmisEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19094 237 GAARPEGGRLNLFPGYMA---RYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF 313
|
330
....*....|...
gi 1848926078 300 GVKLDPSTMRAID 312
Cdd:cd19094 314 DVPLSDELLAEID 326
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-319 |
2.04e-74 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 232.18 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKAL--KGVRRESYELF 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKVYWpTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQI 158
Cdd:cd19160 83 TKIYW-GGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 159 ASALTIqdAHGYNRF--VSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYlpGKKAPAGSRATDKKsg 235
Cdd:cd19160 162 MEAYSV--ARQFNLIppVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKY--DGRVPDTCRAAVKG-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 236 agmiSEWLREEVLT--------AVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGV--KLDP 305
Cdd:cd19160 236 ----YQWLKEKVQSeegkkqqaKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTP 311
|
330
....*....|....
gi 1848926078 306 STMRAIDTALGKLP 319
Cdd:cd19160 312 QTVMEIDALLGNKP 325
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-319 |
3.00e-73 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 229.16 E-value: 3.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKAL--KGVRRESYELF 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKVYWpTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQI 158
Cdd:cd19159 81 TKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 159 ASALTIqdAHGYNRF--VSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkAPAGSRATDKksg 235
Cdd:cd19159 160 MEAYSV--ARQFNMIppVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG--VPESSRASLK--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 236 agmISEWLREEVL--------TAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGV--KLDP 305
Cdd:cd19159 233 ---CYQWLKERIVseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTS 309
|
330
....*....|....
gi 1848926078 306 STMRAIDTALGKLP 319
Cdd:cd19159 310 HVVNEIDNILRNKP 323
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-298 |
7.97e-72 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 224.97 E-value: 7.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 2 EYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVY---AGTrAEVVLGKALKG-VRRESYEL 77
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYgppPGS-AEENFGRILKEdLKPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 78 F--TKVYWPTGPGK-NDRGlSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWS 154
Cdd:cd19151 80 IisTKAGYTMWPGPyGDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 155 AAQIASALTIQDAHGYNRFVsSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkAPAGSRATdkKS 234
Cdd:cd19151 159 PEEAREAAAILKDLGTPCLI-HQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNG--IPEDSRAA--KG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 235 GAGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKA 298
Cdd:cd19151 234 SSFLKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGA 297
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-311 |
2.66e-67 |
|
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: 213.23 E-value: 2.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 2 EYRRLGSTGMYVSEISYG--NWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELFT 79
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmGMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-RRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 80 KVYWPTGPGKNDRGL--SRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEwsaaq 157
Cdd:cd19076 80 KFGIVRDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 158 iASALTIQDAHGYNRFVSSQPQYSaLW-RVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYlpgkKAPAGSRATDKKSGA 236
Cdd:cd19076 155 -ASADTIRRAHAVHPITAVQSEYS-LWtRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAI----KSPEDLPEDDFRRNN 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848926078 237 GMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVL-QNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAI 311
Cdd:cd19076 229 PRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDI-VPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-319 |
6.02e-67 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 213.09 E-value: 6.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRESYELF 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKkkGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKVYWPTGPgkNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQI 158
Cdd:cd19142 81 TKIYWSYGS--EERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 159 ASALTIQDAHGYNRFVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDKKSGAG 237
Cdd:cd19142 159 MEAFSIARQFNCPTPICEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSKYKVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 238 MISEWLREEVLTAVAKLAPVAKEA---GLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGV--KLDPSTMRAID 312
Cdd:cd19142 239 SDGNGIHEETRRASHKLRELSLIAerlGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLlpKLNSAVMEELE 318
|
....*..
gi 1848926078 313 TALGKLP 319
Cdd:cd19142 319 RILDNKP 325
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-319 |
9.68e-67 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 212.64 E-value: 9.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRESYELF 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKVYWpTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQI 158
Cdd:cd19158 81 TKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 159 ASALTIQDAHGYNRFVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkAPAGSRATDKKsgag 237
Cdd:cd19158 160 MEAYSVARQFNLIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG--IPPYSRASLKG---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 238 miSEWLREEVLT--------AVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGV--KLDPST 307
Cdd:cd19158 234 --YQWLKDKILSeegrrqqaKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSI 311
|
330
....*....|..
gi 1848926078 308 MRAIDTALGKLP 319
Cdd:cd19158 312 VHEIDSILGNKP 323
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-314 |
2.19e-64 |
|
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: 206.12 E-value: 2.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 4 RRLGSTGMYVSEISYGNWITHG----SQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFT 79
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGhnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 80 KVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIA 159
Cdd:cd19083 82 KGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 160 SAltiqDAHGYNRFVssQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGsratDKKSGAGMI 239
Cdd:cd19083 162 EA----NKDGYVDVL--QGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDN----DLRNDKPLF 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848926078 240 SEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTA 314
Cdd:cd19083 232 KGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-298 |
2.55e-64 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 205.77 E-value: 2.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 3 YRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVY---AGTrAEVVLGKALK---GVRRESYE 76
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYgppPGS-AEENFGRILRedfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 77 LFTKVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAA 156
Cdd:cd19150 81 ISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 157 QIASALTIQDAHGYNRFVsSQPQYSALWRVIE-AEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkAPAGSRATdkkSG 235
Cdd:cd19150 161 RTREAAAILRELGTPLLI-HQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYLNG--IPEGSRAS---KE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848926078 236 AGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKA 298
Cdd:cd19150 235 RSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGA 297
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-315 |
7.71e-64 |
|
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: 204.39 E-value: 7.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYG----NWiTHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELFTK---VY 82
Cdd:cd19078 1 GLEVSAIGLGcmgmSH-GYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP-FRDQVVIATKfgfKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 83 WPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEwsaaqiASAL 162
Cdd:cd19078 79 DGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSE------AGVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 163 TIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKApagsRATDKKSGAGMISEW 242
Cdd:cd19078 153 TIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKF----DEGDDRASLPRFTPE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 243 LREEVLTAVAKLAPVAKEAGLTMSQLAIAWVL-QNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTAL 315
Cdd:cd19078 229 ALEANQALVDLLKEFAEEKGATPAQIALAWLLaKKPWI-VPIPGTTKLSRLEENIGAADIELTPEELREIEDAL 301
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-314 |
2.74e-59 |
|
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: 192.77 E-value: 2.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 15 EISYG--NWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRResYELFTKVY-WPTGpgknd 91
Cdd:cd19075 2 KIILGtmTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERG--FKIDTKANpGVGG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 92 rGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYN 171
Cdd:cd19075 75 -GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 172 RFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATDKKSGAGMISEW-LREEVLTA 250
Cdd:cd19075 154 LPTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGRFDPNNALGKLYRDRyWKPSYFEA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848926078 251 VAKLAPVAKEAGLTMSQLAIAWVLQNpnvsSA---------IMGATKPSQVRENVKA--AGvKLDPSTMRAIDTA 314
Cdd:cd19075 234 LEKVEEAAEKEGISLAEAALRWLYHH----SAldgekgdgvILGASSLEQLEENLAAleKG-PLPEEVVKAIDEA 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
13-298 |
1.07e-57 |
|
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: 186.53 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 13 VSEISYGNWiTHGSQ----VEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYeLFTKV-YWPTGP 87
Cdd:cd19086 3 VSEIGFGTW-GLGGDwwgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVV-IATKFgNRFDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 88 GKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHR-FDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTiqd 166
Cdd:cd19086 81 PERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNpPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 167 ahgYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKylpgkkapagsratdkksgagmisewlree 246
Cdd:cd19086 158 ---RGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK------------------------------ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1848926078 247 vltavaklapvakeagltMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKA 298
Cdd:cd19086 205 ------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-311 |
1.14e-57 |
|
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: 188.41 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 4 RRLGSTGMYVSEISYGNW---ITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTK 80
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 81 --VYWPTGPGKNDRGlSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEwsaaqi 158
Cdd:cd19145 83 fgIHEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSE------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 159 ASALTIQDAHGYNRFVSSQPQYSaLW-RVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKylpGKKAPAGSRATDKKSGAG 237
Cdd:cd19145 156 ASADTIRRAHAVHPITAVQLEWS-LWtRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKSHPR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 238 MISEWLrEEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAI 311
Cdd:cd19145 232 FQGENL-EKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-304 |
1.02e-56 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 185.74 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRESYELF 78
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKlsPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TK--VYWPTGPGKNDRG---LSRKHIIESCNASLKRLKTDHIDLYQMHRFDvetPL---EESLSAFDDLIRAGKVHYIGF 150
Cdd:COG4989 81 TKcgIRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELKASGKVRHFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 151 SEWSAAQIA---SALTiqdahgyNRFVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGkylpgkkapag 226
Cdd:COG4989 158 SNFTPSQFEllqSALD-------QPLVTNQIELSLLHTdAFDDGTLDYCQLNGITPMAWSPLAGGRLFG----------- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848926078 227 srATDKKSGAgmisewLReevltavAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLD 304
Cdd:COG4989 220 --GFDEQFPR------LR-------AALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELT 282
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-312 |
1.25e-56 |
|
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: 184.35 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 13 VSEISYGNWITHGSQVEA----EAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKVyWPTGPG 88
Cdd:cd19072 4 VPVLGLGTWGIGGGMSKDysddKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTKV-SPDHLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 89 KNDrglsrkhIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAH 168
Cdd:cd19072 83 YDD-------VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 169 GynrFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPgkkapagsratdkksgagmisewlreevl 248
Cdd:cd19072 156 P---IVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS----------------------------- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 249 tavAKLAPVAKEAGLTMSQLAIAWVLQNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19072 204 ---PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-299 |
3.59e-56 |
|
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: 182.78 E-value: 3.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGnwiTHGSQVEAEAAIKcvkTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTK 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG---GGGLPRESPELLR---RALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVFLATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 81 VYWPtgpgknDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPL---EESLSAFDDLIRAGKVHYIGFSEwsaaq 157
Cdd:cd19105 75 ASPR------LDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFST----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 158 iasaltiqdaHGY-----NRFVSS------QPQYS-ALWRVIEAEVVPLSVKEGIGQIVwspMaqgvlsgkylpgkkapa 225
Cdd:cd19105 144 ----------HDNmaevlQAAIESgwfdviMVAYNfLNQPAELEEALAAAAEKGIGVVA---M----------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 226 gsratdkKSGAGMISEWLREEVLtavaklapvaKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19105 194 -------KTLAGGYLQPALLSVL----------KAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-304 |
2.75e-55 |
|
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: 181.60 E-value: 2.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRESYELFTKvywpT 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALAlnPGLREKIEIQTK----C 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 86 G--PGKNDRG-------LSRKHIIESCNASLKRLKTDHIDLYQMHRFDvetPL---EESLSAFDDLIRAGKVHYIGFSEW 153
Cdd:cd19092 77 GirLGDDPRPgrikhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELVKSGKVRYFGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 154 SAAQI---ASALTIqdahgynRFVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLpgkkapagsra 229
Cdd:cd19092 154 TPSQIellQSYLDQ-------PLVTNQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFD----------- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848926078 230 tdkksgagmisewlrEEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLD 304
Cdd:cd19092 216 ---------------ERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-305 |
6.29e-54 |
|
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: 178.51 E-value: 6.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGnwithGSQV--------EAEAaIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRR 72
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFG-----ASPLggvfgpvdEEEA-IRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 73 ESYELFTKV--YWPTGPGKNDrgLSRKHIIESCNASLKRLKTDHIDLYQMHrfDVE-TP-----LEESLSAFDDLIRAGK 144
Cdd:cd19163 75 DSYYLATKVgrYGLDPDKMFD--FSAERITKSVEESLKRLGLDYIDIIQVH--DIEfAPsldqiLNETLPALQKLKEEGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 145 VHYIGFS-----------EWSAAQIASALTiqdahgYNRfvssqpqYSALWRVIEaEVVPLSVKEGIGQIVWSPMAQGVL 213
Cdd:cd19163 151 VRFIGITgypldvlkevlERSPVKIDTVLS------YCH-------YTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 214 SGKYLPgkkapagsratdkksgagmisEW--LREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQ 291
Cdd:cd19163 217 TERGPP---------------------DWhpASPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPEN 275
|
330
....*....|....
gi 1848926078 292 VRENVKAAGVKLDP 305
Cdd:cd19163 276 LRKNLEAAEEPLDA 289
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-312 |
1.35e-53 |
|
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: 177.42 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 17 SYGNWITHGSQVEAEAAIK-CVKTALDEGITTFDTADVYAGTRAEVVLGKALKGV-RRESYELFTKvYWPTgPGKndrgL 94
Cdd:cd19093 11 QWGDRLWWGYGEYGDEDLQaAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELgDRDEVVIATK-FAPL-PWR----L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 95 SRKHIIESCNASLKRLKTDHIDLYQMH-RFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYnRF 173
Cdd:cd19093 85 TRRSVVKALKASLERLGLDSIDLYQLHwPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGV-PL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 174 VSSQPQYSALWRVIEA-EVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRatdkksgaGMISEWLREEVLTAVA 252
Cdd:cd19093 164 ASNQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRR--------RLFGRKNLEKVQPLLD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 253 KLAPVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19093 236 ALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-298 |
9.46e-51 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 171.71 E-value: 9.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNW--ITHGSQVEAEAAIkcVKTALDEGITTFDTADVY---AGTrAEVVLGKALK---GVRR 72
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhnFGHVNALESQRAI--LRKAFDLGITHFDLANNYgppPGS-AEENFGRLLRedfAAYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 73 ESYELFTKVYWPTGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSE 152
Cdd:PRK09912 90 DELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 153 WSAAQIASALTIQDAHGYNRFVsSQPQYSALWRVIEAEVVPLSVKE-GIGQIVWSPMAQGVLSGKYLPGkkAPAGSRATD 231
Cdd:PRK09912 170 YSPERTQKMVELLREWKIPLLI-HQPSYNLLNRWVDKSGLLDTLQNnGVGCIAFTPLAQGLLTGKYLNG--IPQDSRMHR 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848926078 232 KKSGA-GMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKA 298
Cdd:PRK09912 247 EGNKVrGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
13-315 |
1.54e-50 |
|
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: 169.80 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 13 VSEISYGNWITHGSQ---VEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGV-RRESYELFTKV--YWpTG 86
Cdd:cd19148 4 VSRIALGTWAIGGWMwggTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgKRDRVVIATKVglEW-DE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 87 PGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIasaltiqd 166
Cdd:cd19148 83 GGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQM-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 167 ahgyNRFVSS------QPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGS-RATDKKsgagmI 239
Cdd:cd19148 155 ----ETFRKVaplhtvQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDlRRTDPK-----F 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 240 SEWLREEVLTAVAKLAPVAKE-AGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTAL 315
Cdd:cd19148 226 QEPRFSQYLAAVEELDKLAQErYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAIL 302
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-312 |
4.65e-48 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 164.64 E-value: 4.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNwITHGSQ-VEAEAAIKcVKTALDEGITTFDTADVYA-----GTRA--EVVLGKALKGV-R 71
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQnSEADAHAQ-LDYAVAQGINLIDVAEMYPvpprpETQGltETYIGNWLAKRgS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 72 RESYELFTKVywpTGPGKND-------RGLSRKHIIESCNASLKRLKTDHIDLYQMH--------------RFDVETP-- 128
Cdd:PRK10625 79 REKLIIASKV---SGPSRNNdkgirpnQALDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTDSAPav 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 129 -LEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSP 207
Cdd:PRK10625 156 sLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 208 MAQGVLSGKYLPGKKaPAGSRATdkksgagMISEWLR---EEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIM 284
Cdd:PRK10625 236 LAFGTLTGKYLNGAK-PAGARNT-------LFSRFTRysgEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLL 307
|
330 340
....*....|....*....|....*...
gi 1848926078 285 GATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:PRK10625 308 GATTMEQLKTNIESLHLTLSEEVLAEIE 335
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
25-299 |
1.48e-47 |
|
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: 161.95 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 25 GSQVEAEAAIKCVKTALDEGITTFDTADVYAGT----RAEVVLGKALK--GVRRESYeLFTKVYWPTGPGKNDRGLSRKH 98
Cdd:cd19082 11 GTRIDEEEAFALLDAFVELGGNFIDTARVYGDWvergASERVIGEWLKsrGNRDKVV-IATKGGHPDLEDMSRSRLSPED 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 99 IIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYNRFVSSQP 178
Cdd:cd19082 90 IRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 179 QYS-ALW---RVIEAEVVPLS-------VKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSRATdkksgagmiseWLREEV 247
Cdd:cd19082 170 QWSlARPnepPWPGPTLVAMDeemrawhEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRRV-----------YYSEEN 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1848926078 248 LTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19082 239 FERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-298 |
1.92e-47 |
|
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: 160.48 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 14 SEISYGNWITHGSQ--VEAEAAIKCVKTALDEGITTFDTADVYAgtRAEVVLGKALKGVRRESYELFTKVyWPTGPG-KN 90
Cdd:cd19095 1 SVLGLGTSGIGRVWgvPSEAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALAGLRRDDLFIATKV-GTHGEGgRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 91 DRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSewsaaqiASALTIQDAHGY 170
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS-------GDGEELEAAIAS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 171 NRFVSSQPQYSALwRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPgkkapagsratdkksgagmisewlREEVLTA 250
Cdd:cd19095 151 GVFDVVQLPYNVL-DREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRR------------------------RPLYADY 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1848926078 251 VAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKA 298
Cdd:cd19095 206 ARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
31-304 |
3.39e-46 |
|
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: 157.38 E-value: 3.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 31 EAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELFTKVYW-PTGPGKNDRGLSRKHIIESCNASLKR 109
Cdd:cd19088 24 EEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP-YPDDVVIATKGGLvRTGPGWWGPDGSPEYLRQAVEASLRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 110 LKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIAsaltiqDAHGYNRFVSSQPQYSaLWRVIEA 189
Cdd:cd19088 103 LGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIE------EARAIVRIVSVQNRYN-LANRDDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 190 EVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkkAPAGSRATDKKsgagmisewlreevltavaklapVAKEAGLTMSQLA 269
Cdd:cd19088 176 GVLDYCEAAGIAFIPWFPLGGG-----------DLAQPGGLLAE-----------------------VAARLGATPAQVA 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1848926078 270 IAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLD 304
Cdd:cd19088 222 LAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-311 |
2.22e-45 |
|
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: 157.22 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNW---ITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYEL 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGDSEELIGRWFKQNPGKREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 78 FTKV----------YWPTGpgkndrglSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHY 147
Cdd:cd19144 81 ATKFgieknvetgeYSVDG--------SPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 148 IGFSEWSAAqiasalTIQDAHGYNRFVSSQPQYSALwrVIEAEVVPLSV----KE-GIGQIVWSPMAQGVLSGKYlpgkK 222
Cdd:cd19144 153 IGLSECSAE------TLRRAHAVHPIAAVQIEYSPF--SLDIERPEIGVldtcRElGVAIVAYSPLGRGFLTGAI----R 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 223 APAGSRATDKKSGAGMISEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVK 302
Cdd:cd19144 221 SPDDFEEGDFRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVK 300
|
....*....
gi 1848926078 303 LDPSTMRAI 311
Cdd:cd19144 301 LTEEEEKEI 309
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-315 |
7.00e-44 |
|
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: 152.75 E-value: 7.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 24 HGSQVEAEAAIKCVKTALDEGITTFDTADVYAGtrAEVVLGKALKGVRRESYEL-----FTKVYwptgPGKNDRGLSRKH 98
Cdd:cd19101 16 HGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRRERDAAddvqiHTKWV----PDPGELTMTRAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 99 IIESCNASLKRLKTDHIDLYQMHRFDVETP-LEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTiqdaHGYnRFVSSQ 177
Cdd:cd19101 90 VEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD----AGV-PIVSNQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 178 PQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLpGKKAPAGSRATD--KKSGAGMISEW----LREEVLTAv 251
Cdd:cd19101 165 VQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEPTGPALETrsLQKYKLMIDEWggwdLFQELLRT- 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 252 akLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTAL 315
Cdd:cd19101 243 --LKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAVL 304
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-299 |
8.95e-44 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 153.82 E-value: 8.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLGSTGMYVSEISYGNWitHGSQVEAEAAIKCVKTALDEGITTFDTADVYagTRAEVVLGKALKGvRRESYELFTK 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM--RLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG-PRDKVILATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 81 vywpTGPGKNDRGLSRKHIiescNASLKRLKTDHIDLYQMH----RFDVETPLEES--LSAFDDLIRAGKVHYIGFS--- 151
Cdd:COG1453 76 ----LPPWVRDPEDMRKDL----EESLKRLQTDYIDLYLIHglntEEDLEKVLKPGgaLEALEKAKAEGKIRHIGFSthg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 152 ------------EWSAAQIasaltiqdahGYNRFvssQPQYSALWRVIEAevvplSVKEGIGQIVWSPMAQGVLSgkylp 219
Cdd:COG1453 148 slevikeaidtgDFDFVQL----------QYNYL---DQDNQAGEEALEA-----AAEKGIGVIIMKPLKGGRLA----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 220 gkkapagsratdkksgagmisewlreEVLTAVAKLApvakEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:COG1453 205 --------------------------NPPEKLVELL----CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTA 254
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-306 |
5.27e-43 |
|
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: 149.63 E-value: 5.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 14 SEISYGN-WITHG-SQVEAEAAIKCVKTALDEGITTFDTADVYAGtrAEVVLGKALKGVRRESYELFTKVywptGPGKND 91
Cdd:cd19090 1 SALGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAELPREPLVLSTKV----GRLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 92 RG-LSRKHIIESCNASLKRLKTDHIDLYQMHR-----FDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASAltIQ 165
Cdd:cd19090 75 TAdYSADRVRRSVEESLERLGRDRIDLLMIHDpervpWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRA--IE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 166 DAH-----GYNRfvssqpqYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYlpgkkaPAGSRATDkksgagmis 240
Cdd:cd19090 153 TGDfdvvlTANR-------YTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRP------PERVRYTY--------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848926078 241 EWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPS 306
Cdd:cd19090 211 RWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
27-314 |
8.36e-43 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 148.66 E-value: 8.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 27 QVEAEAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK--GVRREsyELF--TKVyWPTGpgkndrgLSRKHIIES 102
Cdd:COG0656 14 QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAasGVPRE--ELFvtTKV-WNDN-------HGYDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 103 CNASLKRLKTDHIDLYQMH-RFDVetPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAhgynRFVSSQPQYS 181
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHwPGPG--PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGV----KPAVNQVELH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 182 ALWRviEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsratdkksgagmisewLREEVLTAvaklapVAKEA 261
Cdd:COG0656 155 PYLQ--QRELLAFCREHGIVVEAYSPLGRGKL-----------------------------LDDPVLAE------IAEKH 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1848926078 262 GLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAIDTA 314
Cdd:COG0656 198 GKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-300 |
1.48e-42 |
|
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: 149.02 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 25 GSQVEAEAAIKCVKTALDEGITTFDTADVYA----GTRA---EVVLGKALK--GVRrESYELFTKVYW----PTGPGKND 91
Cdd:cd19752 11 GTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteGGVGgesERLIGRWLKdrGNR-DDVVIATKVGAgprdPDGGPESP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 92 RGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYN 171
Cdd:cd19752 90 EGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 172 RFVSSQPQYSALW----------RVIEAEVVPLSVKEGIGQIV-WSPMaqgvLSGKYL-PGKKAPAGsratdkksgagmi 239
Cdd:cd19752 170 EFSAIQQRHSYLRprpgadfgvqRIVTDELLDYASSRPDLTLLaYSPL----LSGAYTrPDRPLPEQ------------- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848926078 240 seWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAG 300
Cdd:cd19752 233 --YDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-312 |
4.42e-42 |
|
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: 146.56 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYGNWITHGSQV----EAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKVyWPT 85
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTpdysRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKV-WPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 86 GpgkndrgLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQiasaltIQ 165
Cdd:cd19137 80 N-------LRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRL------LE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 166 DAHGYNR--FVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsratdkksgagMISEW 242
Cdd:cd19137 147 EAISKSQtpIVCNQVKYNLEDRdPERDGLLEYCQKNGITVVAYSPLRRGLE------------------------KTNRT 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 243 LREevltavaklapVAKEAGLTMSQLAIAWVLQNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19137 203 LEE-----------IAKNYGKTIAQIALAWLIQKPNV-VAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-312 |
6.21e-42 |
|
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: 146.62 E-value: 6.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYELFTKVYwPTGP 87
Cdd:cd19138 6 PDGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG-RRDKVFLVSKVL-PSNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 88 gkndrglSRKHIIESCNASLKRLKTDHIDLYQMH-RFDVetPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQD 166
Cdd:cd19138 84 -------SRQGTVRACERSLRRLGTDYLDLYLLHwRGGV--PLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 167 AHgynRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKApagsratdkksgagmisewlree 246
Cdd:cd19138 155 GG---NCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPT----------------------- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848926078 247 vltavakLAPVAKEAGLTMSQLAIAWVLQNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19138 209 -------LKEIAARHGATPAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-313 |
1.75e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 144.33 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 2 EYRRLGSTGMYVSEISYGN------WItHGSQveaEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESY 75
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGggigglMG-RTTR---EEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 76 eLFTKVywptGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMH-RFDVETP--------------LEESLSAFDDLI 140
Cdd:cd19104 77 -ITTKV----RLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHnRIGDERDkpvggtlsttdvlgLGGVADAFERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 141 RAGKVHYIGFSEWSAAQiasalTIQDAHGYNRFVSSQPQY-----SALWRVIEA-------EVVPLSVKEGIGQIVWSPM 208
Cdd:cd19104 152 SEGKIRFIGITGLGNPP-----AIRELLDSGKFDAVQVYYnllnpSAAEARPRGwsaqdygGIIDAAAEHGVGVMGIRVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 209 AQGVLSGKYLPGKKAPAGSRATDkksgagmisewlREEVLTAvAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATK 288
Cdd:cd19104 227 AAGALTTSLDRGREAPPTSDSDV------------AIDFRRA-AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKN 293
|
330 340
....*....|....*....|....*.
gi 1848926078 289 PSQVRENVKAAGV-KLDPSTMRAIDT 313
Cdd:cd19104 294 REELEEAVAAEAAgPLPAENLARLEA 319
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-297 |
3.95e-38 |
|
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: 135.69 E-value: 3.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 3 YRRLGSTGMYVSEISYGNWitHGSQVEAEAAIKCVKTALDEGITTFDTADVYagTRAEVVLGKALKGvRRESYELFTKVy 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGG--PLGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG-RRDKVFLATKT- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 83 wptgpGKNDRGLSRKHIiescNASLKRLKTDHIDLYQMH----RFDVETPLEES--LSAFDDLIRAGKVHYIGFSEWSAA 156
Cdd:cd19100 75 -----GARDYEGAKRDL----ERSLKRLGTDYIDLYQLHavdtEEDLDQVFGPGgaLEALLEAKEEGKIRFIGISGHSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 157 QIASAL------TIQdaHGYNRFVSSQPQYsalwrviEAEVVPLSVKEGIGQIVwspMaqgvlsgkylpgkKAPAGSRat 230
Cdd:cd19100 146 VLLRALetgefdVVL--FPINPAGDHIDSF-------REELLPLAREKGVGVIA---M-------------KVLAGGR-- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 231 dkksgagmiseWLREEVLTAvaklapvakeagltmsQLAIAWVLQNPNVSSAIMGATKPSQVRENVK 297
Cdd:cd19100 199 -----------LLSGDPLDP----------------EQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
13-312 |
8.24e-37 |
|
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: 133.90 E-value: 8.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 13 VSEISYG----NWitHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVvlgkALKGVRR--ESY-ELFTKVYWPT 85
Cdd:cd19077 5 VGPIGLGlmglTW--RPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHA----NLKLLARffRKYpEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 86 GPGKNDRGL----SRKHIIESCNASLKRLK-TDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAqias 160
Cdd:cd19077 79 KGGLDPDTLrpdgSPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAE---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 161 alTIQDAHGYNRFVSSQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYlpgkKAPAGSRATDKKSGAGMI 239
Cdd:cd19077 155 --TIRRAHAVHPIAAVEVEYSLFSReIEENGVLETCAELGIPIIAYSPLGRGLLTGRI----KSLADIPEGDFRRHLDRF 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 240 SEWLREEVLTAVAKLAPVAKEAGLTMSQLAIAWVL-QNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19077 229 NGENFEKNLKLVDALQELAEKKGCTPAQLALAWILaQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
4-315 |
2.61e-36 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 133.32 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 4 RRLGST-GMYVSEI-----SYGN-WITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGK--ALKGVRRES 74
Cdd:cd19146 1 RQLSPTaGVRVSPLclgamSFGEaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwmASRGNRDEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 75 Y--ELFTKVYWPTGPGK---NDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIG 149
Cdd:cd19146 81 VlaTKYTTGYRRGGPIKiksNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 150 FSEWSAAQIASALTIQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkKAPAGSRA 229
Cdd:cd19146 161 VSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQF--------RTEEEFKR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 230 TDKKSGAGmiseWLREEVLTAV-AKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPSTM 308
Cdd:cd19146 233 RGRSGRKG----GPQTEKERKVsEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEI 308
|
....*..
gi 1848926078 309 RAIDTAL 315
Cdd:cd19146 309 QEIEDAY 315
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-303 |
6.64e-36 |
|
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: 131.69 E-value: 6.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 17 SYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKvYWPTGpgkndRGLSR 96
Cdd:cd19103 18 GAGGDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIISTK-FTPQI-----AGQSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 97 KHIIESCNASLKRLKTDHIDLYQMHR-FDVETPLEESLsafdDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYnRFVS 175
Cdd:cd19103 92 DPVADMLEGSLARLGTDYIDIYWIHNpADVERWTPELI----PLLKSGKVKHVGVSNHNLAEIKRANEILAKAGV-SLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 176 SQPQYSALWR-VIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAGSratdkkSGAGMISEWLRE-EVLTAVak 253
Cdd:cd19103 167 VQNHYSLLYRsSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGS------GRAETYNPLLPQlEELTAV-- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1848926078 254 LAPVAKEAGLTMSQLAIAWVLQNPNVSsaIMGATKPSQVRENVKAAGVKL 303
Cdd:cd19103 239 MAEIGAKHGASIAQVAIAWAIAKGTTP--IIGVTKPHHVEDAARAASITL 286
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-299 |
5.34e-35 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 129.51 E-value: 5.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 3 YRRLGSTGMYVSEISYGnwithGS-------QVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRE 73
Cdd:PLN02587 1 LRELGSTGLKVSSVGFG-----ASplgsvfgPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKalGIPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 74 SYELFTKVywptGPGKNDRGLSRKHIIESCNASLKRLKTDHIDLYQMHrfDVE-----TPLEESLSAFDDLIRAGKVHYI 148
Cdd:PLN02587 76 KYVVSTKC----GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCH--DIEfgsldQIVNETIPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 149 GFSEWSAAQIASALTiQDAHGYNRFVSSQPQYSALWRVIEaEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPgkkapagsr 228
Cdd:PLN02587 150 GITGLPLAIFTYVLD-RVPPGTVDVILSYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTENGPP--------- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848926078 229 atdkksgagmisEW--LREEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:PLN02587 219 ------------EWhpAPPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAA 279
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-299 |
1.98e-34 |
|
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: 126.52 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 23 THGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKVYWPTGPGKNDrglSRKHIies 102
Cdd:cd19096 13 SDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLPPWSVKSAED---FRRIL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 103 cNASLKRLKTDHIDLYQMH-----RFDVETPLEESLSAFDDLIRAGKVHYIGFSewSAAQIASALTIQDAHgynRFVSSQ 177
Cdd:cd19096 87 -EESLKRLGVDYIDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFS--FHDSPELLKEILDSY---DFDFVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 178 PQYSAL-WRVIE-AEVVPLSVKEGIGQIVWSPMAQGVLSgkYLPGKkapagsratdkksgagmisewlreevltAVAKLa 255
Cdd:cd19096 161 LQYNYLdQENQAgRPGIEYAAKKGMGVIIMEPLKGGGLA--NNPPE----------------------------ALAIL- 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1848926078 256 pvaKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19096 210 ---CGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAA 250
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-299 |
2.30e-30 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 116.09 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 17 SYGnwITHGS-QVEAEAAIKCVKTALDEGITTFDTADVYaGTrAEVVLGKALKgvRRESYELFTKVywptGPGKNDRGLS 95
Cdd:cd19097 13 DYG--IANKSgKPSEKEAKKILEYALKAGINTLDTAPAY-GD-SEKVLGKFLK--RLDKFKIITKL----PPLKEDKKED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 96 RKHIIESCNASLKRLKTDHIDLYQMHRF-DVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIqdahgyNRFV 174
Cdd:cd19097 83 EAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALES------FKID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 175 SSQPQYSAL-WRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSgkyLPGKKAPAGSratdkksgagmisewlrEEVLTAVAK 253
Cdd:cd19097 157 IIQLPFNILdQRFLKSGLLAKLKKKGIEIHARSVFLQGLLL---MEPDKLPAKF-----------------APAKPLLKK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1848926078 254 LAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19097 217 LHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAF 262
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
16-312 |
9.73e-29 |
|
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: 111.20 E-value: 9.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRREsyELF--TKVyWPTGpgknd 91
Cdd:cd19140 11 LGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY-GNEAQV--GEAIAasGVPRD--ELFltTKV-WPDN----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 92 rgLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAhgyn 171
Cdd:cd19140 75 --YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 172 RFVSSQPQYSALWRviEAEVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkkapagsratdkksgagmisEWLREEVLTAv 251
Cdd:cd19140 149 PLFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARG-----------------------------EVLKDPVLQE- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848926078 252 aklapVAKEAGLTMSQLAIAWVLQNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19140 197 -----IGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDFTLSDEEMARIA 251
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
30-299 |
2.53e-27 |
|
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: 108.22 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 30 AEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKV------YWPTGPGKNDR--GLSRKHIIE 101
Cdd:cd19162 18 EDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVgrllepGAAGRPAGADRrfDFSADGIRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 102 SCNASLKRLKTDHIDLYQMHRFD--VETPLEESLSAFDDLIRAGKVHYIGFS--EWSAAQIASALTIQDAhgynrfVSSQ 177
Cdd:cd19162 98 SIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVVGAIGVGvtDWAALLRAARRADVDV------VMVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 178 PQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsrATDKKSGAGMISEWLREEVLTAVAKLAPV 257
Cdd:cd19162 172 GRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL---------------ATDDPAGDRYDYRPATPEVLARARRLAAV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1848926078 258 AKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAA 299
Cdd:cd19162 237 CRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALL 278
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-312 |
3.48e-27 |
|
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: 106.97 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 15 EISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRRESYELFTKVyWPTGpgkndr 92
Cdd:cd19073 3 ALGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY-NNEAEV--GEAIAesGVPREDLFITTKV-WRDH------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 93 gLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAhgynR 172
Cdd:cd19073 68 -LRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL----P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 173 FVSSQPQYSALWRviEAEVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkkapagsratdkksgagmisEWLREEVLTAva 252
Cdd:cd19073 143 IAVNQVEFHPFLY--QAELLEYCRENDIVITAYSPLARG-----------------------------EVLRDPVIQE-- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 253 klapVAKEAGLTMSQLAIAWVLQNPnvSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19073 190 ----IAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-312 |
4.46e-26 |
|
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: 104.10 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRREsyELF--TKVyWPTGPGknd 91
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY-GNEAEV--GEAIResGVPRE--ELFitTKL-WPTDHG--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 92 rglsRKHIIESCNASLKRLKTDHIDLYQMH------RFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALtiq 165
Cdd:cd19071 70 ----YERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 166 dAHGYNRFVSSQPQYSALWRviEAEVVPLSVKEGIGQIVWSPMAQGVLSGkylpgkkapagsratdkksgagmisewLRE 245
Cdd:cd19071 143 -AAARIKPAVNQIELHPYLQ--QKELVEFCKEHGIVVQAYSPLGRGRRPL---------------------------LDD 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 246 EVLTAvaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19071 193 PVLKE------IAKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-297 |
5.74e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 105.09 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 11 MYVSEISYGNWITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK------GVRREsyELF--TKV- 81
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALReliekgGIKRD--EVVivTKAg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 82 ----------------YWPTGPGKNDRG--------LSRKHIIESCNASLKRLKTDHIDLYQMH---RFDVETP------ 128
Cdd:cd19099 79 yipgdgdeplrplkylEEKLGRGLIDVAdsaglrhcISPAYLEDQIERSLKRLGLDTIDLYLLHnpeEQLLELGeeefyd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 129 -LEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALtiqdahgynrfvssqPQYSALWRVIEAEVVPLSVKEGIgQIVWSP 207
Cdd:cd19099 159 rLEEAFEALEEAVAEGKIRYYGISTWDGFRAPPAL---------------PGHLSLEKLVAAAEEVGGDNHHF-KVIQLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 208 ----MAQGVLSGKYLPGKKAPAGSRAtdKKSGAG-MISEWLRE-EVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSS 281
Cdd:cd19099 223 lnllEPEALTEKNTVKGEALSLLEAA--KELGLGvIASRPLNQgQLLGELRLADLLALPGGATLAQRALQFARSTPGVDS 300
|
330
....*....|....*.
gi 1848926078 282 AIMGATKPSQVRENVK 297
Cdd:cd19099 301 ALVGMRRPEHVDENLA 316
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
15-312 |
1.15e-23 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 99.13 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 15 EISYGN-WITHGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGvRRESYEL-----FTKVYWPTGPG 88
Cdd:cd19147 17 AMSIGDaWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKS-RKNRDQIviatkFTTDYKAYEVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 89 K----NDRGLSRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTI 164
Cdd:cd19147 96 KgkavNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 165 QDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSpmaqgVLSGKYLPGKKApagsRATDKKSGAGMIS---- 240
Cdd:cd19147 176 ATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWD-----VLGGGKFQSKKA----VEERKKNGEGLRSfvgg 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848926078 241 -EWLREEVLTAVAkLAPVAKEAGL-TMSQLAIAWVL-QNPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19147 247 tEQTPEEVKISEA-LEKVAEEHGTeSVTAIALAYVRsKAPNV-FPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-299 |
3.30e-23 |
|
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: 97.40 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 14 SEISYG-----NWITHGSQVEAEAAIKcvkTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKV------- 81
Cdd:cd19161 1 SELGLGtaglgNLYTAVSNADADATLD---AAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVgrllkpa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 82 ---YWPTGPGKNDrGL--------SRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEES------------LSAFDD 138
Cdd:cd19161 78 regSVPDPNGFVD-PLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKerhhfaqlmsggFKALEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 139 LIRAGKVHYIGF--SEWSAaqIASALTIQDahgYNRFVSSQpQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGK 216
Cdd:cd19161 157 LKKAGVIKAFGLgvNEVQI--CLEALDEAD---LDCFLLAG-RYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 217 YLPGKKAPAGSratdkksgAGmisewlrEEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENV 296
Cdd:cd19161 231 TKSGAKFNYGD--------AP-------AEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNV 295
|
...
gi 1848926078 297 KAA 299
Cdd:cd19161 296 EAF 298
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
26-306 |
3.72e-23 |
|
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: 97.29 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 26 SQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRRESYELFTKVYW---PT-GPGKNDRGL------- 94
Cdd:cd19152 15 EAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVGRllvPLqEVEPTFEPGfwnplpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 95 ------SRKHIIESCNASLKRLKTDHIDLYQMHRFDVETPLEESLSAFDDLIR-----------AGKVHYIGF--SEWSA 155
Cdd:cd19152 95 davfdySYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKgafraleelreEGVIKAIGLgvNDWEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 156 AQIASALTIQD----AHGYNRFvsSQPQysalwrviEAEVVPLSVKEGIGQIVWSPMAQGVLSG----KYLPGKKAPags 227
Cdd:cd19152 175 ILRILEEADLDwvmlAGRYTLL--DHSA--------ARELLPECEKRGVKVVNAGPFNSGFLAGgdnfDYYEYGPAP--- 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848926078 228 ratdkksgagmisewlrEEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPS 306
Cdd:cd19152 242 -----------------PELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
19-306 |
1.47e-19 |
|
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: 87.33 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 19 GNWITHGSQVEAEAAikcVKTALDEGITTFDTADVYAgtRAEVVLGKALKGVR----RESYELFTKV--YwptgpGKNDR 92
Cdd:cd19164 25 YQYTTDPESIPPVDI---VRRALELGIRAFDTSPYYG--PSEIILGRALKALRdefpRDTYFIITKVgrY-----GPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 93 GLSRKHIIESCNASLKRLKTDHIDLYQMHrfDVE-TPLEESLSAFDDLIR---AGKVHYIGFSEW------SAAQIASAL 162
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLVYLH--DVEfVADEEVLEALKELFKlkdEGKIRNVGISGYplpvllRLAELARTT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 163 TIQ--DA-HGYNRFvssQPQYSALWRVIEAevvpLSVKEGIGQIV-WSPMAQGVLSGKYlPGKKAPAgsratdkksgagm 238
Cdd:cd19164 173 AGRplDAvLSYCHY---TLQNTTLLAYIPK----FLAAAGVKVVLnASPLSMGLLRSQG-PPEWHPA------------- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848926078 239 iSEWLREevltAVAKLAPVAKEAGLTMSQLAIAWVLQNPN-VSSAIMGATKPSQVRENVKAAGVKLDPS 306
Cdd:cd19164 232 -SPELRA----AAAKAAEYCQAKGTDLADVALRYALREWGgEGPTVVGCSNVDELEEAVEAYWSVLAGA 295
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
16-314 |
2.92e-19 |
|
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: 85.75 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGN---WITHGSQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRREsyELF--TKVywptGPG 88
Cdd:cd19120 7 IAFGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMY-GNEKEV--GEALKesGVPRE--DLFitTKV----SPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 89 KNDrglsrkhIIESCNASLKRLKTDHIDLYQMH--RFDVE--TPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASAL-- 162
Cdd:cd19120 78 IKD-------PREALRKSLAKLGVDYVDLYLIHspFFAKEggPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLdt 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 163 -TIQDA------HGYNrfvssQPQYSALwrvieaevVPLSVKEGIgqIVwspMAQGVLSgkylPGKKAPAGSratdkksg 235
Cdd:cd19120 151 aKIKPAvnqiefHPYL-----YPQQPAL--------LEYCREHGI--VV---SAYSPLS----PLTRDAGGP-------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 236 agmisewlreevltAVAKLAPVAKEAGLTMSQLAIAWVLQnpnvssaiMGA------TKPSQVRENVKAAGVKLDPSTMR 309
Cdd:cd19120 201 --------------LDPVLEKIAEKYGVTPAQVLLRWALQ--------KGIvvvttsSKEERMKEYLEAFDFELTEEEVE 258
|
....*
gi 1848926078 310 AIDTA 314
Cdd:cd19120 259 EIDKA 263
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-298 |
9.48e-19 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 84.89 E-value: 9.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 4 RRLGSTGMYVSEISYGNWI---THGSQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALK--GVRRESYELF 78
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAAlggVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAalQVPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 79 TKVywptGPGKNDR-GLSRKHIIESCNASLKRLKTDHIDLYQMHrfDVE-----TPLEESLSAFDDLIRAGKVHYIGFSE 152
Cdd:cd19153 83 TKV----GRYRDSEfDYSAERVRASVATSLERLHTTYLDVVYLH--DIEfvdydTLVDEALPALRTLKDEGVIKRIGIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 153 WSAAQIASALTiQDAHGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSgkylpgkkaPAGSRATDK 232
Cdd:cd19153 157 YPLDTLTRATR-RCSPGSLDAVLSYCHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLT---------SQGPPPWHP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 233 KSGAgmisewLREEVLTAVAklapVAKEAGLTMSQLAIAWVLQNPN-VSSAIMGATKPSQVRENVKA 298
Cdd:cd19153 227 ASGE------LRHYAAAADA----VCASVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSMLAA 283
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
31-312 |
3.16e-18 |
|
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: 82.40 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 31 EAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRREsyELF--TKVYWPTgpgkndrgLSRKHIIESCNAS 106
Cdd:cd19139 14 DVVIDSVRTALELGYRHIDTAQIY-DNEAAV--GQAIAesGVPRD--ELFitTKIWIDN--------LSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 107 LKRLKTDHIDLYQMH--RFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALtiqDAHGYNRFVSSQPQYSALW 184
Cdd:cd19139 81 LEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAI---AVVGAGAIATNQIELSPYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 185 RviEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsratdkksgagmisewLREEVLTAvaklapVAKEAGLT 264
Cdd:cd19139 158 Q--NRKLVAHCKQHGIHVTSYMTLAYGKV-----------------------------LDDPVLAA------IAERHGAT 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1848926078 265 MSQLAIAWVLQNPnvSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19139 201 PAQIALAWAMARG--YAVIPSSTKREHLRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-311 |
3.79e-17 |
|
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: 80.53 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALKG------VRREsyELF--T 79
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAElleegvVKRE--DLFitT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 80 KVyWPTGpgkndrgLSRKHIIESCNASLKRLKTDHIDLYQMH-------------------RFDVETPLEESLSAFDDLI 140
Cdd:cd19154 77 KL-WTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHapaafkddegesgtmengmSIHDAVDVEDVWRGMEKVY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 141 RAGKVHYIGFSEWSAAQIASALTIQDAhgynRFVSSQPQYSALWRviEAEVVPLSVKEGIGQIVWSPMAQgvlsgkylPG 220
Cdd:cd19154 149 DEGLTKAIGVSNFNNDQIQRILDNARV----KPHNNQVECHLYFP--QKELVEFCKKHNISVTSYATLGS--------PG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 221 KKAPAGSRATDKksgagmisewLREEVLTAVAKlaPVAKEAGLTMSQLAIAWVLQNPnvSSAIMGATKPSQVRENVKAAG 300
Cdd:cd19154 215 RANFTKSTGVSP----------APNLLQDPIVK--AIAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIKENFNIFD 280
|
330
....*....|.
gi 1848926078 301 VKLDPSTMRAI 311
Cdd:cd19154 281 FSLSEEDMATL 291
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-313 |
3.83e-17 |
|
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: 79.87 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYAGTRAevvLGKALK------GVRRESYELFTKVyWPTGpgk 89
Cdd:cd19128 4 LGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYGNEAF---IGIAFSeifkdgGVKREDLFITSKL-WPTM--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 ndrgLSRKHIIESCNASLKRLKTDHIDLYQMH-------------------RFDVETPLEESLSAFDDLIRAGKVHYIGF 150
Cdd:cd19128 72 ----HQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 151 SEWSAAQIASALTIQDAHGYNRFVSSQPQYSalwrviEAEVVPLSVKEGIGQIVWSPMAqgvlsGKYLPGKKAPAGSRAt 230
Cdd:cd19128 148 SNYSTKLLTDLLNYCKIKPFMNQIECHPYFQ------NDKLIKFCIENNIHVTAYRPLG-----GSYGDGNLTFLNDSE- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 231 dkksgagmisewlreevltavakLAPVAKEAGLTMSQLAIAWVLQN-PNVSSAIMGATKPSQVRENVKAAGVKLDPSTMR 309
Cdd:cd19128 216 -----------------------LKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTKEDMD 272
|
....
gi 1848926078 310 AIDT 313
Cdd:cd19128 273 AINT 276
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-312 |
7.74e-17 |
|
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: 78.83 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWITHGSqveaEAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK------GVRRESYELFTKVyWPtgpgk 89
Cdd:cd19136 4 LGLGTFRLRGE----EEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpkyGLSREDIFITSKL-AP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 NDRGLSRKhiIESCNASLKRLKTDHIDLYQMH-----RFDVETPLE-----ESLSAFDDLIRAGKVHYIGFSEWSAAQIA 159
Cdd:cd19136 71 KDQGYEKA--RAACLGSLERLGTDYLDLYLIHwpgvqGLKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 160 SAL---TIQDAhgYNRfVSSQPQYsalwrvIEAEVVPLSVKEGIGQIVWSPMAQGVLSgkylpgkkapagsratdkksga 236
Cdd:cd19136 149 ELLkycEVPPA--VNQ-VEFHPHL------VQKELLKFCKDHGIHLQAYSSLGSGDLR---------------------- 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848926078 237 gmiseWLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNpNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19136 198 -----LLEDPTVLA------IAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENIKVFDFELSEEDMAELN 260
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-311 |
1.05e-15 |
|
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: 75.49 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYAGtraEVVLGKALK--GVRREsyELF--TKVyWPT 85
Cdd:cd19131 7 GNTIPQLGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRasGVPRE--ELFitTKL-WNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 86 GPGKnDRGLsrkhiiESCNASLKRLKTDHIDLYQMHRfdvETPLE----ESLSAFDDLIRAGKVHYIGFSEWSAAQIASa 161
Cdd:cd19131 76 DQGY-DSTL------RAFDESLRKLGLDYVDLYLIHW---PVPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQR- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 162 ltIQDAHGynrFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsratdkksgagmise 241
Cdd:cd19131 145 --LIDETG---VVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGL---------------------------- 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 242 wLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAI 311
Cdd:cd19131 192 -LSDPVIGE------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
29-312 |
2.10e-15 |
|
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: 74.73 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 29 EAEAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK--GVRREsyELF--TKVYwptgpgKNDRGLSRKhiIESCN 104
Cdd:cd19157 22 EGSEVVNAVKTALKNGYRSIDTAAIY---GNEEGVGKGIKesGIPRE--ELFitSKVW------NADQGYDST--LKAFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 105 ASLKRLKTDHIDLYQMHrFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYNRFVSSQPQYSalw 184
Cdd:cd19157 89 ASLERLGLDYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHPRLT--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 185 rviEAEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsratdkksgagmisewLREEVLTAvaklapVAKEAGLT 264
Cdd:cd19157 165 ---QKELRDYCKKQGIQLEAWSPLMQGQL-----------------------------LDNPVLKE------IAEKYNKS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1848926078 265 MSQLAIAWVLQNPNVSsaIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19157 207 VAQVILRWDLQNGVVT--IPKSIKEHRIIENADVFDFELSQEDMDKID 252
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
44-313 |
2.83e-15 |
|
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: 74.67 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 44 GITTFDTADVYagtRAEVVLGKALK--GVRRESYELFTKVyWPTGPGKndrglsrKHIIESCNASLKRLKTDHIDLYQMH 121
Cdd:cd19135 39 GYRHIDTAKRY---GCEELLGKAIKesGVPREDLFLTTKL-WPSDYGY-------ESTKQAFEASLKRLGVDYLDLYLLH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 122 -------RFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSaaqiasaltIQDAHGYNRFVSSQPQYSALWRVI---EAEV 191
Cdd:cd19135 108 wpdcpssGKNVKETRAETWRALEELYDEGLCRAIGVSNFL---------IEHLEQLLEDCSVVPHVNQVEFHPfqnPVEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 192 VPLSVKEGIGQIVWSPMAQGvlsgkylpgkkapagsratdkksgagmisEWLREEVLTAVAKLapvakeAGLTMSQLAIA 271
Cdd:cd19135 179 IEYCRDNNIVFEGYCPLAKG-----------------------------KALEEPTVTELAKK------YQKTPAQILIR 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1848926078 272 WVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAIDT 313
Cdd:cd19135 224 WSIQNGVV--TIPKSTKEERIKENCQVFDFSLSEEDMATLDS 263
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
16-313 |
4.40e-15 |
|
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: 74.24 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWithgSQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKAL------KGVRRESYELFTKVyWPTGPgk 89
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLY-GNEAEV--GEAIrekiaeGVVKREDLFITTKL-WNSYH-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 ndrglSRKHIIESCNASLKRLKTDHIDLYQMH-------RFDVETPLEESLSAFD---------DLIRAGKVHYIGFSEW 153
Cdd:cd19116 84 -----EREQVEPALRESLKRLGLDYVDLYLIHwpvafkeNNDSESNGDGSLSDIDyletwrgmeDLVKLGLTRSIGVSNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 154 SAAQIASAL---TIQDAHgyNRfVSSQPQYSalwrviEAEVVPLSVKEGIGQIVWSPMaqgvlsGKYLPGKKAPAGSRAT 230
Cdd:cd19116 159 NSEQINRLLsncNIKPAV--NQ-IEVHPTLT------QEKLVAYCQSNGIVVMAYSPF------GRLVPRGQTNPPPRLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 231 DKksgagmisewlreevltavaKLAPVAKEAGLTMSQLAIAWVLQNPNVSsaIMGATKPSQVRENVKAAGVKLDPSTMRA 310
Cdd:cd19116 224 DP--------------------TLVAIAKKYGKTTAQIVLRYLIDRGVVP--IPKSSNKKRIKENIDIFDFQLTPEEVAA 281
|
...
gi 1848926078 311 IDT 313
Cdd:cd19116 282 LNS 284
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
31-312 |
1.36e-14 |
|
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: 72.47 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 31 EAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK--GVRRESYELFTKVyWPTGPGkNDRGLSRKHiiescnASLK 108
Cdd:cd19126 23 DETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIResGVPREELFVTTKL-WNDDQR-ARRTEDAFQ------ESLD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 109 RLKTDHIDLYQMHrFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDAHGYNRFVSSQPQYSalwrviE 188
Cdd:cd19126 92 RLGLDYVDLYLIH-WPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPYLT------Q 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 189 AEVVPLSVKEGIGQIVWSPMAQGVLsgkylpgkkapagsratdkksgagmisewLREEVLTAvaklapVAKEAGLTMSQL 268
Cdd:cd19126 165 KELRGYCKSKGIVVEAWSPLGQGGL-----------------------------LSNPVLAA------IGEKYGKSAAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1848926078 269 AIAWVLQNPNVSsaIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19126 210 VLRWDIQHGVVT--IPKSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
16-313 |
7.23e-14 |
|
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: 70.38 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYAGtraEVVLGKALK--GVRRESYELFTKVywptgPGKNDRg 93
Cdd:cd19132 10 IGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRrsGVPREELFVTTKL-----PGRHHG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 94 lsRKHIIESCNASLKRLKTDHIDLYQMH----RFDVETpleESLSAFDDLIRAGKVHYIGFSEWSAAQIAsalTIQDAHG 169
Cdd:cd19132 76 --YEEALRTIEESLYRLGLDYVDLYLIHwpnpSRDLYV---EAWQALIEAREEGLVRSIGVSNFLPEHLD---RLIDETG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 170 YNRFVsSQPQYSALWRviEAEVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkkapagsratdkksgagmiSEWLREEVLT 249
Cdd:cd19132 148 VTPAV-NQIELHPYFP--QAEQRAYHREHGIVTQSWSPLGRG----------------------------SGLLDEPVIK 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 250 AvaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAIDT 313
Cdd:cd19132 197 A------IAEKHGKTPAQVVLRWHVQLGVV--PIPKSANPERQRENLAIFDFELSDEDMAAIAA 252
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-311 |
1.33e-13 |
|
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: 70.13 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 1 MEYRRLgSTGMYVSEISYGNWITHGSQVEaeaaiKCVKTALDEGITTFDTADVYaGTRAEV--VLGKALK--GVRREsyE 76
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTWKSKPGEVG-----QAVKQALEAGYRHIDCAAIY-GNEAEIgaALAEVFKegKVKRE--D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 77 LF-TKVYWPTGPGKNDrglsrkhIIESCNASLKRLKTDHIDLYQMH-----RFDV-------------ETPLEESLSAFD 137
Cdd:cd19123 72 LWiTSKLWNNSHAPED-------VLPALEKTLADLQLDYLDLYLMHwpvalKKGVgfpesgedllslsPIPLEDTWRAME 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 138 DLIRAGKVHYIGFSEWSA---------AQIASALTIQDAHGYnrfvSSQPQysalwrvieaeVVPLSVKEGIGQIVWSPM 208
Cdd:cd19123 145 ELVDKGLCRHIGVSNFSVkkledllatARIKPAVNQVELHPY----LQQPE-----------LLAFCRDNGIHLTAYSPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 209 AQGVlsgkylpgkkAPAGSRATDkksgagmisewlrEEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPnvSSAIMGATK 288
Cdd:cd19123 210 GSGD----------RPAAMKAEG-------------EPVLLEDPVINKIAEKHGASPAQVLIAWAIQRG--TVVIPKSVN 264
|
330 340
....*....|....*....|...
gi 1848926078 289 PSQVRENVKAAGVKLDPSTMRAI 311
Cdd:cd19123 265 PERIQQNLEAAEVELDASDMATI 287
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
29-313 |
2.72e-13 |
|
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: 68.76 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 29 EAEAAIKCVKTALDEGITTFDTADVYAGTRAevvLGKALK--GVRREsyELF--TKVyWPTGPGKNDrglsrkhIIESCN 104
Cdd:cd19133 21 DPEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKksGIPRE--ELFitTKL-WIQDAGYEK-------AKKAFE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 105 ASLKRLKTDHIDLYQMHR--FDVetplEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDA---------HGYNRf 173
Cdd:cd19133 88 RSLKRLGLDYLDLYLIHQpfGDV----YGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVkpavnqietHPFNQ- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 174 vssqpqysalwrviEAEVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkkapagsratdkKSGAgmisewLREEVLTAvak 253
Cdd:cd19133 163 --------------QIEAVEFLKKYGVQIEAWGPFAEG---------------------RNNL------FENPVLTE--- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 254 lapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAIDT 313
Cdd:cd19133 199 ---IAEKYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-312 |
4.38e-13 |
|
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: 68.57 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWITHGSQVEAeaaikCVKTALDEGITTFDTADVYaGTRAEVvlGKALK-------GVRREsyELF-T 79
Cdd:cd19106 2 HTGQKMPLIGLGTWKSKPGQVKA-----AVKYALDAGYRHIDCAAVY-GNEQEV--GEALKekvgpgkAVPRE--DLFvT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 80 KVYWPTgpgkndrglsrKH----IIESCNASLKRLKTDHIDLYQMH--------------------RFDvETPLEESLSA 135
Cdd:cd19106 72 SKLWNT-----------KHhpedVEPALRKTLKDLQLDYLDLYLIHwpyafergdnpfpknpdgtiRYD-STHYKETWKA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 136 FDDLIRAGKVHYIGFSEWSAAQIASALTIqdahgynrfVSSQPQysalwrVIEAEVVPLSVKEGIGQIVWspmAQGVLSG 215
Cdd:cd19106 140 MEKLVDKGLVKAIGLSNFNSRQIDDILSV---------ARIKPA------VLQVECHPYLAQNELIAHCK---ARGLVVT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 216 KYlpgkkAPAGS--RAtdkksgagmiseWLR--EEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQ 291
Cdd:cd19106 202 AY-----SPLGSpdRP------------WAKpdEPVLLEEPKVKALAKKYNKSPAQILLRWQVQRGVV--VIPKSVTPSR 262
|
330 340
....*....|....*....|.
gi 1848926078 292 VRENVKAAGVKLDPSTMRAID 312
Cdd:cd19106 263 IKQNIQVFDFTLSPEEMKQLD 283
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
31-313 |
4.86e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 68.13 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 31 EAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKAL--KGVRREsyELF--TKVyWPTGpgkndrgLSRKHIIESCNAS 106
Cdd:PRK11172 16 QVVIDSVKTALELGYRAIDTAQIY-DNEAAV--GQAIaeSGVPRD--ELFitTKI-WIDN-------LAKDKLIPSLKES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 107 LKRLKTDHIDLYQMH--RFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALtiqDAHGYNRFVSSQPQYSALW 184
Cdd:PRK11172 83 LQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAI---AAVGAENIATNQIELSPYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 185 RviEAEVVPLSVKEGIGQIVWSPMAQGvlsgkylpgkKApagsratdkksgagmisewLREEVLTAvaklapVAKEAGLT 264
Cdd:PRK11172 160 Q--NRKVVAFAKEHGIHVTSYMTLAYG----------KV-------------------LKDPVIAR------IAAKHNAT 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1848926078 265 MSQLAIAWVLQNPnvSSAIMGATKPSQVRENVKAAGVKLDPSTMRAIDT 313
Cdd:PRK11172 203 PAQVILAWAMQLG--YSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAA 249
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
27-312 |
4.98e-13 |
|
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: 68.20 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 27 QVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRRESYELFTKVyWPT--GPGKNDRGLsrkhiies 102
Cdd:cd19127 18 QTPPEETADAVATALADGYRLIDTAAAY-GNEREV--GEGIRrsGVDRSDIFVTTKL-WISdyGYDKALRGF-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 103 cNASLKRLKTDHIDLYQMHrFDVETPLEESLSAFDDLIR---AGKVHYIG---FSEWSAAQIASALTIQDAhgYNRfVSS 176
Cdd:cd19127 86 -DASLRRLGLDYVDLYLLH-WPVPNDFDRTIQAYKALEKllaEGRVRAIGvsnFTPEHLERLIDATTVVPA--VNQ-VEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 177 QPQYSalwrviEAEVVPLSVKEGIGQIVWSPMAqGVLsgKYLPGKKAPAGSRATDkksgagmisewlreEVLTAvaklap 256
Cdd:cd19127 161 HPYFS------QKDLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQD--------------PTITG------ 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1848926078 257 VAKEAGLTMSQLAIAWVLQNPnvSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19127 212 LAEKYGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFDFALSAEDMAAID 265
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-313 |
6.94e-13 |
|
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: 67.91 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK------GVRRESYELFTKVyWPTGpgk 89
Cdd:cd19111 7 IGLGTY-----QSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKwwlkngKLKREEVFITTKL-PPVY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 ndrgLSRKHIIESCNASLKRLKTDHIDLYQMH-------------RFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAA 156
Cdd:cd19111 75 ----LEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 157 QIASALTIQDAHGYNRFVSSQPQYSalwrviEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGkkaPAGSRATDKKsga 236
Cdd:cd19111 151 QINKILAYAKVKPSNLQLECHAYLQ------QRELRKFCNKKNIVVTAYAPLGSPGRANQSLWP---DQPDLLEDPT--- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 237 gmisewlreeVLTavaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAIDT 313
Cdd:cd19111 219 ----------VLA-------IAKELDKTPAQVLLRFVLQRGTG--VLPKSTNKERIEENFEVFDFELTEEHFKKLKT 276
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-325 |
1.04e-12 |
|
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: 67.51 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALKG------VRRESYELFTKV 81
Cdd:cd19112 6 NSGHKMPVIGLGVW-----RMEPGEIKELILNAIKIGYRHFDCAADY-KNEKEV--GEALAEafktglVKREDLFITTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 82 yWPTgpgknDRGlsrkHIIESCNASLKRLKTDHIDLYQMH-----------------------RFDVETPLEESLSAFDD 138
Cdd:cd19112 78 -WNS-----DHG----HVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAMEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 139 LIRAGKVHYIGFSEW---------SAAQIASALTIQDAHGYNRFVSsqpqysalwrvieaeVVPLSVKEGIGQIVWSPMA 209
Cdd:cd19112 148 LVSAGLVRSIGISNYdifltrdclAYSKIKPAVNQIETHPYFQRDS---------------LVKFCQKHGISVTAHTPLG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 210 qGVLSGKYLPGKKAPagsratdkksgagmisewLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKP 289
Cdd:cd19112 213 -GAAANAEWFGSVSP------------------LDDPVLKD------LAKKYGKSAAQIVLRWGIQRNTA--VIPKSSKP 265
|
330 340 350
....*....|....*....|....*....|....*.
gi 1848926078 290 SQVRENVKAAGVKLDPSTMRAIDTALGKLPEKDPAK 325
Cdd:cd19112 266 ERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPAK 301
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-307 |
2.50e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 63.52 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 40 ALDEGITTFDTADVYAgtRAEVVLGKALKGVRRESYELFTKVYWP---TGPGKND------RGLSRKHIIESCNASLKRL 110
Cdd:cd19098 44 AWAAGVRYFDAARSYG--RAEEFLGSWLRSRNIAPDAVFVGSKWGytyTADWQVDaavhevKDHSLARLLKQWEETRSLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 111 KtDHIDLYQMHRFDVETPLEESLSAFDDL--IRAGKVHyIGFSEWSAAQ---IASALTIQdAHGYNRFVSSQpqysALWR 185
Cdd:cd19098 122 G-KHLDLYQIHSATLESGVLEDADVLAALaeLKAEGVK-IGLSLSGPQQaetLRRALEIE-IDGARLFDSVQ----ATWN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 186 VIE---AEVVPLSVKEGIGQIVwspmaqgvlsgkylpgKKAPAGSRATDKKSgagmisewlREEVLTAVAKLAPVAKEAG 262
Cdd:cd19098 195 LLEqsaGEALEEAHEAGMGVIV----------------KEALANGRLTDRNP---------SPELAPLMAVLKAVADRLG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1848926078 263 LTMSQLAIAWVLQNPNVSSAIMGATKPSQVRENVKAAGVKLDPST 307
Cdd:cd19098 250 VTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLEL 294
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
31-312 |
8.71e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 61.91 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 31 EAAIKCVKTALDEGITTFDTADVYAGTRAEVVLGKALKGVRrESYELFTKVywptGPGKNDRG-----LSRKHIIESCNA 105
Cdd:PRK10376 40 DAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYP-DDLTIVTKV----GARRGEDGswlpaFSPAELRRAVHD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 106 SLKRLKTDHIDLYQMH-RFDVETP----LEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTIQDahgynrFVSSQPQY 180
Cdd:PRK10376 115 NLRNLGLDVLDVVNLRlMGDGHGPaegsIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE------IVCVQNHY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 181 SALWRVIEAEVVPLSvKEGIGQIVWSPMaqgvlsGKYLPgkkapagsratdkksgagmisewLREEVLTAVAKlapvakE 260
Cdd:PRK10376 189 NLAHRADDALIDALA-RDGIAYVPFFPL------GGFTP-----------------------LQSSTLSDVAA------S 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1848926078 261 AGLTMSQLAIAWVLQ-NPNVsSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:PRK10376 233 LGATPMQVALAWLLQrSPNI-LLIPGTSSVAHLRENLAAAELVLSEEVLAELD 284
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-312 |
1.05e-10 |
|
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: 61.77 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYGNWitHGSQVEAEAAIKcvkTALDEGITTFDTADVYagtRAEVVLGKALK------GVRRESYELFTKVyw 83
Cdd:cd19155 9 GEKMPVVGLGTW--QSSPEEIETAVD---TALEAGYRHIDTAYVY---RNEAAIGNVLKkwidsgKVKREELFIVTKL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 84 PtgPGKNdrglsRKHIIESC-NASLKRLKTDHIDLY---------------------QMHRFDVETPLEESLSAFDDLIR 141
Cdd:cd19155 79 P--PGGN-----RREKVEKFlLKSLEKLQLDYVDLYlihfpvgslskeddsgkldptGEHKQDYTTDLLDIWKAMEAQVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 142 AGKVHYIGFSEWSAAQIASALTIQDAHGYNRFVSSQPQYSalwrviEAEVVPLSVKEGIGQIVWSPMAQGVLSgKYLPGK 221
Cdd:cd19155 152 QGLTRSIGLSNFNREQMARILKNARIKPANLQVELHVYLQ------QKDLVDFCSTHSITVTAYAPLGSPGAA-HFSPGT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 222 KAPAGSratdkksgagmISEWLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGV 301
Cdd:cd19155 225 GSPSGS-----------SPDLLQDPVVKA------IAERHGKSPAQVLLRWLMQRGVV--VIPKSTNAARIKENFQVFDF 285
|
330
....*....|.
gi 1848926078 302 KLDPSTMRAID 312
Cdd:cd19155 286 ELTEADMAKLS 296
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
37-295 |
3.82e-10 |
|
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: 59.78 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 37 VKTALDEGITTFDTADVYagtRAEVVLGKALK------GVRRESYELFTKVyWPTgpgkNDRGLSRKHIIEscnASLKRL 110
Cdd:cd19129 25 VKAALEAGFRHFDCAERY---RNEAEVGEAMQevfkagKIRREDLFVTTKL-WNT----NHRPERVKPAFE---ASLKRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 111 KTDHIDLYQMHR--------------------FDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQ---IASALTIQDA 167
Cdd:cd19129 94 QLDYLDLYLIHTpfafqpgdeqdprdangnviYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKlreIFEAARIKPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 168 HGYnrfVSSQPqYSALWrvieaEVVPLSVKEGIGQIVWSPMaqgvlsgkylpgkkapagsratdkksGAGMISEWLREEV 247
Cdd:cd19129 174 VVQ---VESHP-YLPEW-----ELLDFCKNHGIVLQAFAPL--------------------------GHGMEPKLLEDPV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1848926078 248 LTAvaklapVAKEAGLTMSQLAIAWVLQNPnvSSAIMGATKPSQVREN 295
Cdd:cd19129 219 ITA------IARRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIREN 258
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
26-312 |
6.36e-10 |
|
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: 59.10 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 26 SQVEAEAAikcVKTALDEGITTFDTADVYAGtraEVVLGKALK--GVRREsyELF--TKVYWPtgpgknDRGLSRKhiIE 101
Cdd:cd19134 22 SDDEAERS---VSAALEAGYRLIDTAAAYGN---EAAVGRAIAasGIPRG--ELFvtTKLATP------DQGFTAS--QA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 102 SCNASLKRLKTDHIDLYQMHRfdVETPLEESLSAFDDLIRA---GKVHYIGFSEWSAAQIASALtiqdahGYNRFVSSQP 178
Cdd:cd19134 86 ACRASLERLGLDYVDLYLIHW--PAGREGKYVDSWGGLMKLreeGLARSIGVSNFTAEHLENLI------DLTFFTPAVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 179 QYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSgkylpgkKAPAGSRatdkksgagmisewlreevltavaklapVA 258
Cdd:cd19134 158 QIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLL-------DNPAVTA----------------------------IA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 259 KEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19134 203 AAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLDVFDFELTADHMDALD 254
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-297 |
8.07e-10 |
|
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: 58.66 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 9 TGMYVSEISYGNWITHGSQVEaeaaiKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK--GVRRESYELFTKVyWPTg 86
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNEVA-----KAVEAALKAGYRHIDTAAIY-GNEEEV--GQGIKdsGVPREEIFITTKL-WCT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 87 pgkndrglSRKHIIESCNASLKRLKTDHIDLYQMH-------RFDVETPLEESLSAFDD--------------LIRAGKV 145
Cdd:cd19117 80 --------WHRRVEEALDQSLKKLGLDYVDLYLMHwpvpldpDGNDFLFKKDDGTKDHEpdwdfiktwelmqkLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 146 HYIGFSEWSAAQIASALTIQDahgyNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMaqgvlsgkylpgkkapa 225
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPS----AKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPL----------------- 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848926078 226 GSratdkkSGAGMisewLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNPnvSSAIMGATKPSQVRENVK 297
Cdd:cd19117 211 GS------TNAPL----LKEPVIIK------IAKKHGKTPAQVIISWGLQRG--YSVLPKSVTPSRIESNFK 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
27-331 |
1.58e-09 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 57.78 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 27 QVEAEAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK--GVRREsyELF--TKVyWptgpgkNDRglsRKHIIES 102
Cdd:PRK11565 24 QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKeaSVARE--ELFitTKL-W------NDD---HKRPREA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 103 CNASLKRLKTDHIDLYQMHrfdveTPLEES---LSAFDDLI---RAGKVHYIGFSEWsaaqiasaltiQDAHgynrfvss 176
Cdd:PRK11565 89 LEESLKKLQLDYVDLYLMH-----WPVPAIdhyVEAWKGMIelqKEGLIKSIGVCNF-----------QIHH-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 177 qpqysaLWRVI-EAEVVPLsvkegIGQI-----------------------VWSPMAQGvlsgkylpgkkapagsratdk 232
Cdd:PRK11565 145 ------LQRLIdETGVTPV-----INQIelhplmqqrqlhawnathkiqteSWSPLAQG--------------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 233 ksGAGMISEWLreevltaVAKLapvAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMraid 312
Cdd:PRK11565 193 --GKGVFDQKV-------IRDL---ADKYGKTPAQIVIRWHLDSGLV--VIPKSVTPSRIAENFDVFDFRLDKDEL---- 254
|
330
....*....|....*....
gi 1848926078 313 TALGKLpekDPAKNESPNP 331
Cdd:PRK11565 255 GEIAKL---DQGKRLGPDP 270
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-297 |
1.66e-09 |
|
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: 57.74 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 9 TGMYVSEISYGNWITHGSQVeAEAaikcVKTALDEGITTFDTADVYaGTRAEV--VLGKALKG--VRREsyELF-TKVYW 83
Cdd:cd19125 7 TGAKIPAVGLGTWQADPGVV-GNA----VKTAIKEGYRHIDCAAIY-GNEKEIgkALKKLFEDgvVKRE--DLFiTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 84 PTGpgkndrgLSRKHIIESCNASLKRLKTDHIDLYQMH---RFD-----------VETPLEESLSAFDDLIRAGKVHYIG 149
Cdd:cd19125 79 CTD-------HAPEDVPPALEKTLKDLQLDYLDLYLIHwpvRLKkgahmpepeevLPPDIPSTWKAMEKLVDSGKVRAIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 150 FSEWSAAQ----IASALTIQDAHgynrfvssQPQYSALWRviEAEVVPLSVKEGIGQIVWSPMaqgvlsgkylpgkkapa 225
Cdd:cd19125 152 VSNFSVKKledlLAVARVPPAVN--------QVECHPGWQ--QDKLHEFCKSKGIHLSAYSPL----------------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 226 GSRATdkksgagmisEWLREEVLT--AVAKlapVAKEAGLTMSQLAIAWVLQNPNvsSAIMGATKPSQVRENVK 297
Cdd:cd19125 205 GSPGT----------TWVKKNVLKdpIVTK---VAEKLGKTPAQVALRWGLQRGT--SVLPKSTNEERIKENID 263
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-312 |
5.40e-09 |
|
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: 56.37 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWithgsQVEA-EAAIKCVKTALDEGITTFDTADVYagtRAEVVLGKALK--GVRRESYELFTKVyWP 84
Cdd:cd19156 4 ANGVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIResGVPREEVFVTTKL-WN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 85 TgpgknDRGLsrKHIIESCNASLKRLKTDHIDLYQMHrFDVETPLEESLSAFDDLIRAGKVHYIGFSEWSAAQIASALTi 164
Cdd:cd19156 75 S-----DQGY--ESTLAAFEESLEKLGLDYVDLYLIH-WPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 165 qdahgynrfvssqpqysalwrviEAEVVPLsvkegIGQIVWSPMAQGVLSGKYLPGKK------APAGSratdkksgagm 238
Cdd:cd19156 146 -----------------------SCKVAPM-----VNQIELHPLLTQEPLRKFCKEKNiaveawSPLGQ----------- 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848926078 239 iSEWLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNPNVSsaIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19156 187 -GKLLSNPVLKA------IGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQENFDVFDFELTAEEIRQID 251
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-312 |
4.24e-08 |
|
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: 53.57 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWITHGSQVEAeaaikCVKTALDEGITTFDTADVYaGTRAEVvlGKALK-------GVRREsyELF-T 79
Cdd:cd19118 2 NTGNKIPAIGLGTWQAEPGEVGA-----AVKIALKAGYRHLDLAKVY-QNQHEV--GQALKellkeepGVKRE--DLFiT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 80 KVYWptgpgkNDRGlSRKHIIESCNASLKRLKTDHIDLYQMH-----------RFDVETPLEESLSAFDD---------- 138
Cdd:cd19118 72 SKLW------NNSH-RPEYVEPALDDTLKELGLDYLDLYLIHwpvafkptgdlNPLTAVPTNGGEVDLDLsvslvdtwka 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 139 ---LIRAGKVHYIGFSEWSAAQIAsalTIQDAHGYnrfVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMaqgvlsg 215
Cdd:cd19118 145 mveLKKTGKVKSIGVSNFSIDHLQ---AIIEETGV---VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPL------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 216 kylpGKKAPAGSRATDkksgagmisewlREEVLTAVAKLapvakeaGLTMSQLAIAWVLQNPNvsSAIMGATKPSQVREN 295
Cdd:cd19118 212 ----GNNLAGLPLLVQ------------HPEVKAIAAKL-------GKTPAQVLIAWGIQRGH--SVIPKSVTPSRIRSN 266
|
330
....*....|....*..
gi 1848926078 296 VKAagVKLDPSTMRAID 312
Cdd:cd19118 267 FEQ--VELSDDEFNAVT 281
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-312 |
3.69e-07 |
|
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: 50.68 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 10 GMYVSEISYGNWITHGSQVEaeaaiKCVKTALDEGITTFDTADVYaGTRAEVVLGKALKGVRRESYELFTKVYwptgpgk 89
Cdd:cd19130 7 GNSIPQLGYGVFKVPPADTQ-----RAVATALEVGYRHIDTAAIY-GNEEGVGAAIAASGIPRDELFVTTKLW------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 NDRGlSRKHIIESCNASLKRLKTDHIDLYQMHRfdvETPLE----ESLSAFDDLIRAGKVHYIGFSEWSAAQIASALtiq 165
Cdd:cd19130 74 NDRH-DGDEPAAAFAESLAKLGLDQVDLYLVHW---PTPAAgnyvHTWEAMIELRAAGRTRSIGVSNFLPPHLERIV--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 166 dahGYNRFVSSQPQYSALWRVIEAEVVPLSVKEGIGQIVWSPMAQGVLSGKYLPGKKAPAgsratdkksgagmisewlre 245
Cdd:cd19130 147 ---AATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAA-------------------- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848926078 246 evltavaklapvakeAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19130 204 ---------------HGKTPAQIVLRWHLQKGHV--VFPKSVRRERMEDNLDVFDFDLTDTEIAAID 253
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-121 |
6.48e-07 |
|
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: 50.19 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 9 TGMYVSEISYGNWITHGSQVEAEaaiKCVKTALDEGITTFDTADVYAgtrAEVVLGKALK------GVRREsyELF--TK 80
Cdd:cd19119 8 TGASIPALGLGTASPHEDRAEVK---EAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKraiddgSIKRE--ELFitTK 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1848926078 81 VyWPTgpgkndrglSRKHIIESCNASLKRLKTDHIDLYQMH 121
Cdd:cd19119 80 V-WPT---------FYDEVERSLDESLKALGLDYVDLLLVH 110
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
37-162 |
1.11e-06 |
|
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: 49.57 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 37 VKTALDEGITTFDTADVYAGTRaEVVLGKALK----GVRRESYELFTKVyWPTgpgkndrgLSRKHIIES-CNASLKRLK 111
Cdd:cd19110 23 VKVAIDAGYRHFDCAYLYHNES-EVGAGIREKikegVVRREDLFIVSKL-WCT--------CHKKSLVKTaCTRSLKALK 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 112 TDHIDLYQMH---RF---DVETPLEES-------------LSAFDDLIRAGKVHYIGFSEWSAAQIASAL 162
Cdd:cd19110 93 LNYLDLYLIHwpmGFkpgEPDLPLDRSgmvipsdtdfldtWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-298 |
1.34e-06 |
|
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: 49.16 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWITHGSQVEAEAAikcVKTALDEGITTFDTADVYAGtraEVVLGKALK-------GVRRESYELFTK 80
Cdd:cd19122 4 NNGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFYLN---EDEVGDAVRdflkenpSVKREDLFICTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 81 VYwptgpgkndRGLSR-KHIIESCNASLKRLKTDHIDLYQMH------RFDVETPL-----------------EESLSAF 136
Cdd:cd19122 78 VW---------NHLHEpEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaeKNDQRSPKlgpdgkyvilkdltenpEPTWRAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 137 DDLIRAGKVHYIGFSEWsaaqiasalTIQDAHGYNRFVSSQPQysalwrVIEAEVVPLSVKEGIGQIVWSpmaQGVLSGK 216
Cdd:cd19122 149 EEIYESGKAKAIGVSNW---------TIPGLKKLLSFAKVKPH------VNQIEIHPFLPNEELVDYCFS---NDILPEA 210
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 217 YlpgkkAPAGSRATDKKSGagmisewlreEVLTAVAKLAPVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENV 296
Cdd:cd19122 211 Y-----SPLGSQNQVPSTG----------ERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNF 273
|
..
gi 1848926078 297 KA 298
Cdd:cd19122 274 KS 275
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-121 |
2.77e-06 |
|
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: 48.30 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 8 STGMYVSEISYGNWithgsQVEAEAAIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALK-----GVRRESYELFTKVy 82
Cdd:cd19121 7 NTGASIPAVGLGTW-----QAKAGEVKAAVAHALKIGYRHIDGALCY-QNEDEV--GEGIKeaiagGVKREDLFVTTKL- 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1848926078 83 WPTGPGKNDRGLSRkhiiescnaSLKRLKTDHIDLYQMH 121
Cdd:cd19121 78 WSTYHRRVELCLDR---------SLKSLGLDYVDLYLVH 107
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
19-158 |
3.96e-06 |
|
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: 47.80 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 19 GNWITHGSQVEaEAaikcVKTALDEGITTFDTADVYagtRAEVVLGKAL------KGVRRESYELFTKVyWPTgpgKNDR 92
Cdd:cd19107 10 GTWKSPPGQVT-EA----VKVAIDAGYRHIDCAYVY---QNENEVGEAIqekikeQVVKREDLFIVSKL-WCT---FHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 93 GLSRkhiiESCNASLKRLKTDHIDLYQMH---RFDV----------------ETPLEESLSAFDDLIRAGKVHYIGFSEW 153
Cdd:cd19107 78 GLVK----GACQKTLSDLKLDYLDLYLIHwptGFKPgkelfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNF 153
|
....*
gi 1848926078 154 SAAQI 158
Cdd:cd19107 154 NHLQI 158
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
23-312 |
4.55e-04 |
|
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: 41.48 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 23 THGSQVEAEAAIKCVKTALDEGITTFDTADVYaGTraEVVLGKALK-----GVRRESYELF--TKVyWPTGpgkndrgLS 95
Cdd:cd19124 12 TASDPPSPEDIKAAVLEAIEVGYRHFDTAAAY-GT--EEALGEALAealrlGLVKSRDELFvtSKL-WCSD-------AH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 96 RKHIIESCNASLKRLKTDHIDLYQMH--------RFDVETPLEESL--------SAFDDLIRAGKVHYIGFSEWSAAQIA 159
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHwpvslkpgKFSFPIEEEDFLpfdikgvwEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 160 SALtiqdAHGYNRFVSSQPQYSALWRviEAEVVPLSVKEGIGQIVWSPmaqgvlsgkyLPGKKAPAGSRATdkksgagMI 239
Cdd:cd19124 161 ELL----SFATIPPAVNQVEMNPAWQ--QKKLREFCKANGIHVTAYSP----------LGAPGTKWGSNAV-------ME 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848926078 240 SEWLREevltavaklapVAKEAGLTMSQLAIAWVLQNPnvSSAIMGATKPSQVRENVKAAGVKLDPSTMRAID 312
Cdd:cd19124 218 SDVLKE-----------IAAAKGKTVAQVSLRWVYEQG--VSLVVKSFNKERMKQNLDIFDWELTEEDLEKIS 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
16-312 |
6.01e-04 |
|
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: 41.00 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 16 ISYGNWITHGSQVEaEAAIKCVKTaldeGITTFDTADVYAGtraEVVLGKALKG------VRRESYELFTKVyWPTGPGK 89
Cdd:cd19114 7 VGFGTAKIKANETE-EVIYNAIKV----GYRLIDGALLYGN---EAEVGRGIRKaiqeglVKREDLFIVTKL-WNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 90 ndrglsrKHIIESCNASLKRLKTDHIDLYQMH------------------------RFDVE-TPLEESLSAFDDLIRAGK 144
Cdd:cd19114 78 -------DHVREAFDRQLKDYGLDYIDLYLIHfpipaayvdpaenypflwkdkelkKFPLEqSPMQECWREMEKLVDAGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 145 VHYIGFSEWSAAQIASALTiqdahgYNRFvssQPQysalwrVIEAEVVPLSVKEGIgqIVWSpMAQGVLSGKYlpgkkAP 224
Cdd:cd19114 151 VRNIGIANFNVQLILDLLT------YAKI---KPA------VLQIEHHPYLQQKRL--IDWA-KKQGIQITAY-----SS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 225 AGSRATDK--KSGAGMISeWLREEVLTAvaklapVAKEAGLTMSQLAIAWVLQNPNVssAIMGATKPSQVRENVKAAGVK 302
Cdd:cd19114 208 FGNAVYTKvtKHLKHFTN-LLEHPVVKK------LADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTNLDITSYK 278
|
330
....*....|
gi 1848926078 303 LDPSTMRAID 312
Cdd:cd19114 279 LDEEDMEALY 288
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
33-121 |
1.82e-03 |
|
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: 39.52 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848926078 33 AIKCVKTALDEGITTFDTADVYaGTRAEVvlGKALKG------VRRESYELFTKVyWPTgpgkndrgLSRKHIIESC-NA 105
Cdd:cd19108 29 ALEATKLAIDAGFRHIDSAYLY-QNEEEV--GQAIRSkiadgtVKREDIFYTSKL-WCT--------FHRPELVRPAlEK 96
|
90
....*....|....*.
gi 1848926078 106 SLKRLKTDHIDLYQMH 121
Cdd:cd19108 97 SLKKLQLDYVDLYLIH 112
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