|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
2-329 |
2.34e-149 |
|
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: 423.10 E-value: 2.34e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 2 PTSTDVQaFRTGVNGVALGSVGLGGLYQDlpGEAVTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQTPRH 79
Cdd:cd19153 1 FGETLEI-ALGNVSPVGLGTAALGGVYGD--GLEQDEAVAIVAEAFAAGINHFDTSPYYGAesSEAVLGKALAALQVPRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 80 EYYLATKVGRYRSdkhpnGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVLHEAIPALAELQAEGVIKLI 159
Cdd:cd19153 78 SYTVATKVGRYRD-----SEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPALRTLKDEGVIKRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 160 GICGYPLDVLDDIVQR-SPRPLQVVQSYSHLTLQNDAlLTKAASWHAKGNtvspihrrvllkhyvlpGIVVINAAPLSMG 238
Cdd:cd19153 153 GIAGYPLDTLTRATRRcSPGSLDAVLSYCHLTLQDAR-LESDAPGLVRGA-----------------GPHVINASPLSMG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 239 LLTSRGPPAWHPASSALRASCAAALTWLASVEFateqqkpSVEGLAIQYALDAqkehHNVVTTMVVGSMGEAEVLSSIRA 318
Cdd:cd19153 215 LLTSQGPPPWHPASGELRHYAAAADAVCASVEA-------SLPDLALQYSLAA----HAGVGTVLLGPSSLAQLRSMLAA 283
|
330
....*....|.
gi 698810080 319 RDNPSLLSKAH 329
Cdd:cd19153 284 VDAVASLGAAI 294
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
11-322 |
1.45e-92 |
|
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: 278.67 E-value: 1.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTG--VNGVALGSVGLGGLYQDLpgeAVTIAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRVqtPRHEYYLATK 86
Cdd:cd19163 8 KTGlkVSKLGFGASPLGGVFGPV---DEEEAIRTVHEALDSGINYIDTAPWYgqGRSETVLGKALKGI--PRDSYYLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 87 VGRYRSDkhPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDR-DTVLHEAIPALAELQAEGVIKLIGICGYP 165
Cdd:cd19163 83 VGRYGLD--PDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSlDQILNETLPALQKLKEEGKVRFIGITGYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 166 LDVLDDIVQRSPRPLQVVQSYSHLTLQNDALLTKAASWHAKgntvspihrrvllkhyvlpGIVVINAAPLSMGLLTSRGP 245
Cdd:cd19163 161 LDVLKEVLERSPVKIDTVLSYCHYTLNDTSLLELLPFFKEK-------------------GVGVINASPLSMGLLTERGP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 698810080 246 PAWHPASSALRASCAAAltwlasVEFATEQQKPSVEgLAIQYALDaqkeHHNVVTTMvVGSMGEAEVLSSIRARDNP 322
Cdd:cd19163 222 PDWHPASPEIKEACAKA------AAYCKSRGVDISK-LALQFALS----NPDIATTL-VGTASPENLRKNLEAAEEP 286
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
19-312 |
2.73e-83 |
|
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: 255.28 E-value: 2.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 19 LGSVGLGGLYQDLPGEAVTiaVETFETAFPRGVRLIDTAPWYNNAEDVVGQALRRVQT--PRHEYYLATKVGRYrsdkhP 96
Cdd:cd19164 18 FGAATFSYQYTTDPESIPP--VDIVRRALELGIRAFDTSPYYGPSEIILGRALKALRDefPRDTYFIITKVGRY-----G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 97 NGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVLhEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQR- 175
Cdd:cd19164 91 PDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVL-EALKELFKLKDEGKIRNVGISGYPLPVLLRLAELa 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 176 ---SPRPLQVVQSYSHLTLQNDALLTKAASWHAKGNTvspihrrvllkhyvlpgIVVINAAPLSMGLLTSRGPPAWHPAS 252
Cdd:cd19164 170 rttAGRPLDAVLSYCHYTLQNTTLLAYIPKFLAAAGV-----------------KVVLNASPLSMGLLRSQGPPEWHPAS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698810080 253 SALRASCAAALTWLasvefatEQQKPSVEGLAIQYALdaqKEHHNVVTTMV-VGSMGEAEV 312
Cdd:cd19164 233 PELRAAAAKAAEYC-------QAKGTDLADVALRYAL---REWGGEGPTVVgCSNVDELEE 283
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
14-345 |
7.75e-60 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 195.38 E-value: 7.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGGLYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQTPRHEYYLATKVGRYR 91
Cdd:PLN02587 11 VSSVGFGASPLGSVFGPVSEED---AIASVREAFRLGINFFDTSPYYGGtlSEKVLGKALKALGIPREKYVVSTKCGRYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 92 SDkhpngeFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDD 171
Cdd:PLN02587 88 EG------FDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIPALQKLKESGKVRFIGITGLPLAIFTY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 172 IVQRSPR-PLQVVQSYSHLTLQNDALLTkaaswhakgntvspihrrvLLKHYVLPGIVVINAAPLSMGLLTSRGPPAWHP 250
Cdd:PLN02587 162 VLDRVPPgTVDVILSYCHYSLNDSSLED-------------------LLPYLKSKGVGVISASPLAMGLLTENGPPEWHP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 251 ASSALRASCAAAltwlasVEFATEQQKpSVEGLAIQYALdaqkeHHNVVTTMVVGSMGEAEVLSSIRARDNPSLLSKAH- 329
Cdd:PLN02587 223 APPELKSACAAA------ATHCKEKGK-NISKLALQYSL-----SNKDISTTLVGMNSVQQVEENVAAATELETSGIDEe 290
|
330
....*....|....*..
gi 698810080 330 -IAKFRQLLGHSYNESW 345
Cdd:PLN02587 291 lLSEVEAILAPVKNKTW 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-257 |
1.87e-45 |
|
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: 156.95 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNNAEDVVGQALRRVqtPRHEYYLATKVGRyrsdkHP 96
Cdd:cd19090 3 LGLGTAGLGGVFGGVDDDE---AVATIRAALDLGINYIDTAPAYGDSEERLGLALAEL--PREPLVLSTKVGR-----LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 97 NGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVLHE--AIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19090 73 EDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggALEALLELKEEGLIKHIGLGGGPPDLLRRAIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 175 RSprPLQVVQSYSHLTLQN-DALLTKAAswHAKGNTVSpihrrvllkhyvlpgivVINAAPLSMGLLTSRGP------PA 247
Cdd:cd19090 153 TG--DFDVVLTANRYTLLDqSAADELLP--AAARHGVG-----------------VINASPLGMGLLAGRPPervrytYR 211
|
250
....*....|
gi 698810080 248 WHPASSALRA 257
Cdd:cd19090 212 WLSPELLDRA 221
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-337 |
7.61e-45 |
|
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: 155.55 E-value: 7.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQTPRHEYYLATKVGRYRSDK 94
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEE---ALEALRAALEAGINFIDTAEVYGDgkSEELLGEALKDYPVKRDKVVIATKVPDGDGPW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HpngeFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:pfam00248 78 P----SGGSKENIRKSLEESLKRLGTDYIDLYYLHW---PDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 175 RSPRPLQVVQ-SYSHLTLQNDALLTKAASWHakgntvspihrrvllkhyvlpGIVVINAAPLSMGLLTSR-------GPP 246
Cdd:pfam00248 151 KGKIPIVAVQvEYNLLRRRQEEELLEYCKKN---------------------GIPLIAYSPLGGGLLTGKytrdpdkGPG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 247 AWHPassALRASCAAALTWLASVEFATEQQKPSVEGLAIQYALDAQKehhnvVTTMVVGSMGEAEVLSSIRARDNPslLS 326
Cdd:pfam00248 210 ERRR---LLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPG-----VTIPIPGASNPEQLEDNLGALEFP--LS 279
|
330
....*....|.
gi 698810080 327 KAHIAKFRQLL 337
Cdd:pfam00248 280 DEEVARIDELL 290
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
11-337 |
9.24e-42 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 148.40 E-value: 9.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTG--VNGVALGSVGLGGLYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtPRHEYYLATK 86
Cdd:COG0667 8 RSGlkVSRLGLGTMTFGGPWGGVDEAE---AIAILDAALDAGINFFDTADVYGPgrSEELLGEALKGR--PRDDVVIATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 87 VGRYRSDkHPNGeFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVefvDRDTVLHEAIPALAELQAEGVIKLIGICGYPL 166
Cdd:COG0667 83 VGRRMGP-GPNG-RGLSREHIRRAVEASLRRLGTDYIDLYQLHRP---DPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 167 DVLDDI--VQRSPRPLQVVQsyshltlqndalltkaaswhakgNTVSPIHRRVLlkHYVLP-----GIVVINAAPLSMGL 239
Cdd:COG0667 158 EQLRRAlaIAEGLPPIVAVQ-----------------------NEYSLLDRSAE--EELLPaarelGVGVLAYSPLAGGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 240 LTSR-GPPAWHPASSALRASCAAALTWLASV-------EFATEQQKPSVEgLAIQYALdaqkeHHNVVTTMVVGSMGEAE 311
Cdd:COG0667 213 LTGKyRRGATFPEGDRAATNFVQGYLTERNLalvdalrAIAAEHGVTPAQ-LALAWLL-----AQPGVTSVIPGARSPEQ 286
|
330 340
....*....|....*....|....*.
gi 698810080 312 VLSSIRARDNPslLSKAHIAKFRQLL 337
Cdd:COG0667 287 LEENLAAADLE--LSAEDLAALDAAL 310
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-326 |
5.65e-36 |
|
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: 132.10 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQdlPGEAVtiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRvqTPRHEYYLATKVGRYRSDK 94
Cdd:cd19162 3 LGLGAASLGNLAR--AGEDE--AAATLDAAWDAGIRYFDTAPLYGLglSERRLGAALAR--HPRAEYVVSTKVGRLLEPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HPNGE------FDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEfVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDV 168
Cdd:cd19162 77 AAGRPagadrrFDFSADGIRRSIEASLERLGLDRLDLVFLHDPD-RHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 169 LDDIVQRSprPLQVVQSYSHLTLQNDALLTkaaswhakgntvspihrrVLLKHYVLPGIVVINAAPLSMGLLTSRGPPA- 247
Cdd:cd19162 156 LLRAARRA--DVDVVMVAGRYTLLDRRAAT------------------ELLPLCAAKGVAVVAAGVFNSGILATDDPAGd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 248 ---WHPASS-------ALRASCAAALTWLASVefateqqkpsveglAIQYALdaqkeHHNVVTTMVVGSMGEAEVlssir 317
Cdd:cd19162 216 rydYRPATPevlararRLAAVCRRYGVPLPAA--------------ALQFPL-----RHPAVASVVVGAASPAEL----- 271
|
....*....
gi 698810080 318 aRDNPSLLS 326
Cdd:cd19162 272 -RDNLALLR 279
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
19-318 |
6.95e-36 |
|
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: 130.82 E-value: 6.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 19 LGSVGLGGLyQDLPGEAVTIAVetFETAFPRGVRLIDTAPWYNNAEDVVGQALRRVQtpRHEYYLATKVGRYRSDkhPNG 98
Cdd:cd19095 5 LGTSGIGRV-WGVPSEAEAARL--LNTALDLGINLIDTAPAYGRSEERLGRALAGLR--RDDLFIATKVGTHGEG--GRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 99 EFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPlDVLDDIVQRSpr 178
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLH---GPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG-EELEAAIASG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 179 PLQVVQ-SYSHLTLQNDALLTKAAswhAKGntvspihrrvllkhyvlPGIVVInaAPLSMGLLTSRGPPawhpasSALRA 257
Cdd:cd19095 152 VFDVVQlPYNVLDREEEELLPLAA---EAG-----------------LGVIVN--RPLANGRLRRRVRR------RPLYA 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698810080 258 SCAAALTWLASVEFATEQQkpsvegLAIQYALDaqkehHNVVTTMVVGSMGEAEVLSSIRA 318
Cdd:cd19095 204 DYARRPEFAAEIGGATWAQ------AALRFVLS-----HPGVSSAIVGTTNPEHLEENLAA 253
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
15-227 |
1.11e-31 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 119.77 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQdLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgryrsdk 94
Cdd:COG0656 1 NGVEIPALGLG-TWQ-LPGEEAAAAVRT---ALEAGYRHIDTAAMYGN-EEGVGEAIAASGVPREELFVTTKV------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 hPNGefDYSRSRIRQSVQDSLAKLGTTYLDVVYLH---DVEFVdrdtvlhEAIPALAELQAEGVIKLIGICGYPLDVLDD 171
Cdd:COG0656 68 -WND--NHGYDDTLAAFEESLERLGLDYLDLYLIHwpgPGPYV-------ETWRALEELYEEGLIRAIGVSNFDPEHLEE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 172 IVQRSPRPLQVVQSYSHLTLQNDALLtkaaSWHAKGNTV----SPIHRRVLLKHYVLPGI 227
Cdd:COG0656 138 LLAETGVKPAVNQVELHPYLQQRELL----AFCREHGIVveaySPLGRGKLLDDPVLAEI 193
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-318 |
1.17e-31 |
|
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: 121.28 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtPRHEYYLATKVGRY---- 90
Cdd:cd19161 3 LGLGTAGLGNLYTAVSNAD---ADATLDAAWDSGIRYFDTAPMYGHglAEHRLGDFLREK--PRDEFVLSTKVGRLlkpa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 RSDKHPNG-----------EFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFV---DRDTVLHEA------IPALAEL 150
Cdd:cd19161 78 REGSVPDPngfvdplpfeiVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYthgDRKERHHFAqlmsggFKALEEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 151 QAEGVIKLIGICGYPLDVLDDIVQRSPRPLQVV-QSYSHL-TLQNDALLTKAaswhakgntvspiHRRvllkhyvlpGIV 228
Cdd:cd19161 158 KKAGVIKAFGLGVNEVQICLEALDEADLDCFLLaGRYSLLdQSAEEEFLPRC-------------EQR---------GTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 229 VINAAPLSMGLLTSRGPPAWH------PAS-----SALRASCAAALTWLASVefateqqkpsveglAIQYALdaqkeHHN 297
Cdd:cd19161 216 LVIGGVFNSGILATGTKSGAKfnygdaPAEiisrvMEIEKICDAYNVPLAAA--------------ALQFPL-----RHP 276
|
330 340
....*....|....*....|.
gi 698810080 298 VVTTMVVGSMGEAEVLSSIRA 318
Cdd:cd19161 277 AVASVLTGARNPAQLRQNVEA 297
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-312 |
1.01e-29 |
|
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: 115.78 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtPRHEYYLATKVGRYRSDK 94
Cdd:cd19152 3 LGFGTAPLGNLYEAVSDEE---AKATLVAAWDLGIRYFDTAPWYGAglSEERLGAALREL--GREDYVISTKVGRLLVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 ---HPNGE------------FDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVE--------FVDRDTVLHEAIPALAELQ 151
Cdd:cd19152 78 qevEPTFEpgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDedlagaesDEHFAQAIKGAFRALEELR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 152 AEGVIKLIGICGYPLDVLDDIVQRSprplqvvqsyshltlQNDALLTkAASWHakgntvspihrrvLLKHY----VLP-- 225
Cdd:cd19152 158 EEGVIKAIGLGVNDWEVILRILEEA---------------DLDWVML-AGRYT-------------LLDHSaareLLPec 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 226 ---GIVVINAAPLSMGLLTSRGPPAWH---PASSALRAscaaaltWLASVEFATEQQKPSVEGLAIQYALDaqkehHNVV 299
Cdd:cd19152 209 ekrGVKVVNAGPFNSGFLAGGDNFDYYeygPAPPELIA-------RRDRIEALCEQHGVSLAAAALQFALA-----PPAV 276
|
330
....*....|...
gi 698810080 300 TTMVVGSMGEAEV 312
Cdd:cd19152 277 ASVAPGASSPERV 289
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-318 |
1.82e-29 |
|
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: 113.34 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGlyqDLPGEAV-TIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRvqtPRHEYYLATKVGrYRSD 93
Cdd:cd19086 6 IGFGTWGLGG---DWWGDVDdAEAIRALRAALDLGINFFDTADVYGDghSERLLGKALKG---RRDKVVIATKFG-NRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 KHPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLH--DVEFVDRDtvlhEAIPALAELQAEGVIKLIGICGYPLDVLDD 171
Cdd:cd19086 79 GGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnpPDEVLDND----ELFEALEKLKQEGKIRAYGVSVGDPEEALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 172 IVQRspRPLQVVQSYSHLTLQN--DALLTKAAswhakgntvspihrrvllKHyvlpGIVVINAAPLSMGLLTSRgppawh 249
Cdd:cd19086 155 ALRR--GGIDVVQVIYNLLDQRpeEELFPLAE------------------EH----GVGVIARVPLASGLLTGK------ 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 698810080 250 passalrascaaaltwLAsvefateqqkpsveGLAIQYALDaqkehHNVVTTMVVGSMGEAEVLSSIRA 318
Cdd:cd19086 205 ----------------LA--------------QAALRFILS-----HPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
22-206 |
1.81e-28 |
|
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: 110.69 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 22 VGLGGLYQDLPGEAVTiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQtPRHEYYLATKVGryrsdkHPNGE 99
Cdd:cd06660 3 LGLGTMTFGGDGDEEE-AFALLDAALEAGGNFFDTADVYGDgrSERLLGRWLKGRG-NRDDVVIATKGG------HPPGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 100 ----FDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQR 175
Cdd:cd06660 75 dpsrSRLSPEHIRRDLEESLRRLGTDYIDLYYLH---RDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAY 151
|
170 180 190
....*....|....*....|....*....|....*
gi 698810080 176 SPR----PLQVVQSYSHLtLQNDALLTKAASWHAK 206
Cdd:cd06660 152 AKAhglpGFAAVQPQYSL-LDRSPMEEELLDWAEE 185
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-240 |
4.19e-28 |
|
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: 109.88 E-value: 4.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTGVNgvaLGSVGLGGLYQDLPGEAVtiAVETFETAFPRGVRLIDTAPWYNNAEDVVGQALRRvqtPRHEYYLATKVGry 90
Cdd:cd19100 6 RTGLK---VSRLGFGGGPLGRLSQEE--AAAIIRRALDLGINYFDTAPSYGDSEEKIGKALKG---RRDKVFLATKTG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 rsdkhpngefDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFV-DRDTVL--HEAIPALAELQAEGVIKLIGICGYPLD 167
Cdd:cd19100 76 ----------ARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEeDLDQVFgpGGALEALLEAKEEGKIRFIGISGHSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 168 VLDDIVQRspRPLQVVQ-SYSHLTLQND----ALLTKAaswHAKGNTVS---PIHRRVLLK----------HYVL--PGI 227
Cdd:cd19100 146 VLLRALET--GEFDVVLfPINPAGDHIDsfreELLPLA---REKGVGVIamkVLAGGRLLSgdpldpeqalRYALslPPV 220
|
250
....*....|...
gi 698810080 228 VVINAAPLSMGLL 240
Cdd:cd19100 221 DVVIVGMDSPEEL 233
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-332 |
9.13e-27 |
|
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: 107.61 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQDLPGEAVTIavETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtpRHEYYLATKVGrYRSDK 94
Cdd:cd19084 7 IGLGTWAIGGTWWGEVDDQESI--EAIKAAIDLGINFFDTAPVYGFghSEEILGKALKGR---RDDVVIATKCG-LRWDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19084 81 GKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIH---WPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 175 RSprPLQVVQS-YShltlqndaLLTKAAswhakgntvspihRRVLLKHYVLPGIVVINAAPLSMGLLTSRGPPAWHPASS 253
Cdd:cd19084 158 YG--PIVSLQPpYS--------MLEREI-------------EEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 254 ALRAS--------------CAAALTwlasvEFATEQQKPSVEgLAIQYALDaqkehHNVVTTMVVGSMGEAEVLSSIRAR 319
Cdd:cd19084 215 DRRSRfpffrgenfeknleIVDKLK-----EIAEKYGKSLAQ-LAIAWTLA-----QPGVTSAIVGAKNPEQLEENAGAL 283
|
330
....*....|...
gi 698810080 320 DnpSLLSKAHIAK 332
Cdd:cd19084 284 D--WELTEEELKE 294
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-320 |
1.49e-26 |
|
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: 106.90 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGG----LYQDlpgEAVTIAveTFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtpRHEYYLATKV 87
Cdd:cd19085 1 VSRLGLGCWQFGGgywwGDQD---DEESIA--TIHAALDAGINFFDTAEAYGDghSEEVLGKALKGR---RDDVVIATKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 88 GryrsdkhPNgefDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLD 167
Cdd:cd19085 73 S-------PD---NLTPEDVRKSCERSLKRLGTDYIDLYQIH---WPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 168 VLDDIVQRSprPLQVVQ-SYShltlqndaLLtkaasWhakgntvspihRRVLlkHYVLP-----GIVVINAAPLSMGLLT 241
Cdd:cd19085 140 QLEEALDAG--RIDSNQlPYN--------LL-----W-----------RAIE--YEILPfcrehGIGVLAYSPLAQGLLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 242 SRGPPAWHPASSALRASC---------AAALTWLASVE-FATEQQKPSVEgLAIQYALdaqkeHHNVVTTMVVGSMGEAE 311
Cdd:cd19085 192 GKFSSAEDFPPGDARTRLfrhfepgaeEETFEALEKLKeIADELGVTMAQ-LALAWVL-----QQPGVTSVIVGARNPEQ 265
|
....*....
gi 698810080 312 VLSSIRARD 320
Cdd:cd19085 266 LEENAAAVD 274
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
14-227 |
5.82e-25 |
|
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: 101.57 E-value: 5.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGgLYQdLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgryrsd 93
Cdd:cd19140 3 VNGVRIPALGLG-TYP-LTGEECTRAVEH---ALELGYRHIDTAQMYGN-EAQVGEAIAASGVPRDELFLTTKV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 kHPNgefDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19140 71 -WPD---NYSPDDFLASVEESLRKLRTDYVDLLLLH---WPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 698810080 174 QRSPRPLQVVQSYSHLTLQNDALLtKAASWHakGNTV---SPIHRRVLLKHYVLPGI 227
Cdd:cd19140 144 ELSEAPLFTNQVEYHPYLDQRKLL-DAAREH--GIALtaySPLARGEVLKDPVLQEI 197
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
21-197 |
7.90e-25 |
|
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: 101.40 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 21 SVGLG--GLYQDLPGEAVTIAVETfetafprGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgryrsdkHPNg 98
Cdd:cd19071 3 LIGLGtyKLKPEETAEAVLAALEA-------GYRHIDTAAAYGN-EAEVGEAIRESGVPREELFITTKL-------WPT- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 99 efDYSRSRIRQSVQDSLAKLGTTYLDVVYLH---DVEFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQR 175
Cdd:cd19071 67 --DHGYERVREALEESLKDLGLDYLDLYLIHwpvPGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAA 144
|
170 180
....*....|....*....|..
gi 698810080 176 SPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19071 145 ARIKPAVNQIELHPYLQQKELV 166
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
19-227 |
3.54e-24 |
|
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: 99.27 E-value: 3.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 19 LGSVGLGGLyqDLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgrYRSDKHPNg 98
Cdd:cd19073 1 IPALGLGTW--QLRGDDCANAVKE---ALELGYRHIDTAEIYNN-EAEVGEAIAESGVPREDLFITTKV--WRDHLRPE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 99 efdysrsRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQRSPR 178
Cdd:cd19073 72 -------DLKKSVDRSLEKLGTDYVDLLLIH---WPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 698810080 179 PLQVVQSYSHLTLQNDALLTKAASWHAKGNTVSPIHRRVLLKHYVLPGI 227
Cdd:cd19073 142 PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGEVLRDPVIQEI 190
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-207 |
7.50e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 95.73 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTGVNgvaLGSVGLGGlyqdlpGEAVTIAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRVqtPRHEYYLATKVg 88
Cdd:cd19105 8 KTGLK---VSRLGFGG------GGLPRESPELLRRALDLGINYFDTAEGYgnGNSEEIIGEALKGL--RRDKVFLATKA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 89 RYRSDKhpngefdYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVLHEAIPALAELQAEGVIKLIGIC--GYPL 166
Cdd:cd19105 76 SPRLDK-------KDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALEKLKKEGKVRFIGFSthDNMA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 698810080 167 DVLDDIVQrsPRPLQVVQ-SYSHLTLQN--DALLTKAaswHAKG 207
Cdd:cd19105 149 EVLQAAIE--SGWFDVIMvAYNFLNQPAelEEALAAA---AEKG 187
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
5-243 |
7.07e-22 |
|
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: 94.41 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 5 TDVQAFRTGvngvaLGSVGLGG--LYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRVQtpRHE 80
Cdd:cd19083 7 SDIDVNPIG-----LGTNAVGGhnLYPNLDEEE---GKDLVREALDNGVNLLDTAFIYglGRSEELVGEVLKEYN--RNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 81 YYLATKVGRYRSDKhpNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIG 160
Cdd:cd19083 77 VVIATKGAHKFGGD--GSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIH---FPDGETPKAEAVGALQELKDEGKIRAIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 161 ICGYPLDVLDDIVQRSprPLQVVQSYSHLtLQNDALLTkaaswhakgntvspihrrvLLKHYVLPGIVVINAAPLSMGLL 240
Cdd:cd19083 152 VSNFSLEQLKEANKDG--YVDVLQGEYNL-LQREAEED-------------------ILPYCVENNISFIPYFPLASGLL 209
|
...
gi 698810080 241 TSR 243
Cdd:cd19083 210 AGK 212
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
17-184 |
1.35e-21 |
|
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: 93.53 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGlyQDLPGEAVTIAVETFETAFPRGVRLIDTAPWYN--NAEDVVGQALRRVqTPRHEYYLATKVGRyrsDK 94
Cdd:cd19148 7 IALGTWAIGG--WMWGGTDEKEAIETIHKALDLGINLIDTAPVYGfgLSEEIVGKALKEY-GKRDRVVIATKVGL---EW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HPNGEF--DYSRSRIRQSVQDSLAKLGTTYLDvvyLHDVEFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDI 172
Cdd:cd19148 81 DEGGEVvrNSSPARIRKEVEDSLRRLQTDYID---LYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETF 157
|
170
....*....|..
gi 698810080 173 vqRSPRPLQVVQ 184
Cdd:cd19148 158 --RKVAPLHTVQ 167
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-257 |
2.41e-21 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 93.11 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGG--LYQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYN--NAEDVVGQALRRVqtpRHEYYLATKVG-RYR 91
Cdd:cd19149 14 IGLGTWAIGGgpWWGGSDDNE---SIRTIHAALDLGINLIDTAPAYGfgHSEEIVGKAIKGR---RDKVVLATKCGlRWD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 92 SDKhpnGEFDY-----------SRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIG 160
Cdd:cd19149 88 REG---GSFFFvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTH---WQDVETPIEETMEALEELKRQGKIRAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 161 ICGYPLDVLDDIVQRSprPLQVVQS-YSHLtlqndalltkaasWHAKGNTVSPIHRrvllKHyvlpGIVVINAAPLSMGL 239
Cdd:cd19149 162 ASNVSVEQIKEYVKAG--QLDIIQEkYSML-------------DRGIEKELLPYCK----KN----NIAFQAYSPLEQGL 218
|
250
....*....|....*...
gi 698810080 240 LTSRGPPAWHPASSALRA 257
Cdd:cd19149 219 LTGKITPDREFDAGDARS 236
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-184 |
5.55e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 91.05 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 18 ALGSVGLGGLY-----QDLPGEAVtiAVETFETAFPRGVRLIDTAPWYNNAEDVVGQALRRVQTPRheyyLATKVgryrs 92
Cdd:cd19097 4 ALGTAQFGLDYgiankSGKPSEKE--AKKILEYALKAGINTLDTAPAYGDSEKVLGKFLKRLDKFK----IITKL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 93 dKHPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEfvDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDI 172
Cdd:cd19097 73 -PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPD--DLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKA 149
|
170
....*....|..
gi 698810080 173 VQRSprPLQVVQ 184
Cdd:cd19097 150 LESF--KIDIIQ 159
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-324 |
7.64e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 88.86 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 10 FRTG--VNGVALGSVGLGGLYqdLPGEAVTiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtpRHEYYLAT 85
Cdd:cd19104 6 GRTGlkVSELTFGGGGIGGLM--GRTTREE-QIAAVRRALDLGINFFDTAPSYGDgkSEENLGRALKGL---PAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 86 KVGRyrsdkhPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLH----DVEFVDRDTVLH--------EAIPALAELQAE 153
Cdd:cd19104 80 KVRL------DPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigDERDKPVGGTLSttdvlglgGVADAFERLRSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 154 GVIKLIGICGypLDVLDDI--VQRSPRPlQVVQSYSHltlqndaLLTKAASWHAKGNTVSPIHRRVlLKHYVLPGIVVIN 231
Cdd:cd19104 154 GKIRFIGITG--LGNPPAIreLLDSGKF-DAVQVYYN-------LLNPSAAEARPRGWSAQDYGGI-IDAAAEHGVGVMG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 232 AAPLSMGLLTS---RGPPAWHPASSALRASC--AAALTWLASVEFATEQQkpsvegLAIQYALDaqkehHNVVTTMVVGS 306
Cdd:cd19104 223 IRVLAAGALTTsldRGREAPPTSDSDVAIDFrrAAAFRALAREWGETLAQ------LAHRFALS-----NPGVSTVLVGV 291
|
330
....*....|....*...
gi 698810080 307 MGEAEVLSSIRARDNPSL 324
Cdd:cd19104 292 KNREELEEAVAAEAAGPL 309
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
15-227 |
1.80e-19 |
|
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: 86.66 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTIAVETFETafprGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrsdk 94
Cdd:cd19131 6 DGNTIPQLGLG-VWQVSNDEAASAVREALEV----GYRSIDTAAIYGN-EEGVGKAIRASGVPREELFITTKLW------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 hpNGEFDYSRSriRQSVQDSLAKLGTTYLDVVYLH-DVEFVDRDTvlhEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19131 74 --NSDQGYDST--LRAFDESLRKLGLDYVDLYLIHwPVPAQDKYV---ETWKALIELKKEGRVKSIGVSNFTIEHLQRLI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 698810080 174 QRSPRPLQVVQSYSHLTLQNDALltkaASWHAKGNTV----SPIHRRVLLKHYVLPGI 227
Cdd:cd19131 147 DETGVVPVVNQIELHPRFQQREL----RAFHAKHGIQteswSPLGQGGLLSDPVIGEI 200
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-337 |
3.26e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 86.57 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 39 AVETFETAFPRGVRLIDTAPWYN--NAEDVVGQALRRVqtpRHEYYLATKVGR-YRSDKHPNGefDYSRSRIRQSVQDSL 115
Cdd:cd19102 28 SIAAIRAALDLGINWIDTAAVYGlgHSEEVVGRALKGL---RDRPIVATKCGLlWDEEGRIRR--SLKPASIRAECEASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 116 AKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIvqRSPRPLQVVQ-SYSHLtlqnd 194
Cdd:cd19102 103 RRLGVDVIDLYQIH---WPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRC--QAIHPIASLQpPYSLL----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 195 alltkaaswhakgntvspihRRVLLKHyVLP-----GIVVINAAPLSMGLLT--------SRGPPAWHPASSALRAscAA 261
Cdd:cd19102 173 --------------------RRGIEAE-ILPfcaehGIGVIVYSPMQSGLLTgkmtpervASLPADDWRRRSPFFQ--EP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 262 ALTW-LASVE----FAtEQQKPSVEGLAIQYALdaqkeHHNVVTTMVVGSMGEAEVLSSIRARDnpSLLSKAHIAKFRQL 336
Cdd:cd19102 230 NLARnLALVDalrpIA-ERHGRTVAQLAIAWVL-----RRPEVTSAIVGARRPDQIDETVGAAD--LRLTPEELAEIEAL 301
|
.
gi 698810080 337 L 337
Cdd:cd19102 302 L 302
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
13-161 |
3.68e-19 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 86.50 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 13 GVNGVALGSVGLG--GLYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRvqtPRHEYYLATKVG 88
Cdd:cd19076 6 GTQGLEVSALGLGcmGMSAFYGPADEEESIATLHRALELGVTFLDTADMYgpGTNEELLGKALKD---RRDEVVIATKFG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 698810080 89 RYRSDKHPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGI 161
Cdd:cd19076 83 IVRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHR---VDPNVPIEETVGAMAELVEEGKVRYIGL 152
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-243 |
1.53e-18 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 84.57 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 16 GVALGSVGLGGLYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtPRHEYYLATKVgRYRSD 93
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqAEEVLGKALKGW--PRESYVISTKV-FWPTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 KHPNgEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19074 78 PGPN-DRGLSRKHIFESIHASLKRLQLDYVDIYYCHR---YDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 698810080 174 ----QRSPRPLQVVQS-YSHLtlqndalltkaasWHAKGNTVSPIHRRVllkhyvlpGIVVINAAPLSMGLLTSR 243
Cdd:cd19074 154 dlarQFGLIPPVVEQPqYNML-------------WREIEEEVIPLCEKN--------GIGLVVWSPLAQGLLTGK 207
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
11-161 |
3.68e-18 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 83.79 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTGVNGVALGSVGLGGL-YQDLPGEAVTIAVET----FETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqTPRHEYYL 83
Cdd:cd19079 4 RLGNSGLKVSRLCLGCMsFGDPKWRPWVLDEEEsrpiIKRALDLGINFFDTANVYSGgaSEEILGRALKEF-APRDEVVI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 698810080 84 ATKVgRYRSDKHPNGEfDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGI 161
Cdd:cd19079 83 ATKV-YFPMGDGPNGR-GLSRKHIMAEVDASLKRLGTDYIDLYQIHR---WDYETPIEETLEALHDVVKSGKVRYIGA 155
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
21-331 |
5.30e-18 |
|
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: 83.46 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 21 SVGLGGL--YQDLPGEAVTIavetFETAFPRGVRLIDTAPWYN----NAEDVVGQALRRVQTP-RHEYYLATKVGrYRSD 93
Cdd:cd19089 15 SLGLWHNfgDYTSPEEAREL----LRTAFDLGITHFDLANNYGpppgSAEENFGRILKRDLRPyRDELVISTKAG-YGMW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 KHPNGEFDySRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLD--- 170
Cdd:cd19089 90 PGPYGDGG-SRKYLLASLDQSLKRMGLDYVDIFYHHR---YDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARrai 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 171 DIVQRSPRPLQVVQ-SYSHLTLQN-DALLTKAASWhakgntvspihrrvllkhyvlpGIVVINAAPLSMGLLT---SRGP 245
Cdd:cd19089 166 ALLRELGVPLIIHQpRYSLLDRWAeDGLLEVLEEA----------------------GIGFIAFSPLAQGLLTdkyLNGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 246 PawhPASSALRAScaaalTWLASVEFATEQQKP-------------SVEGLAIQYALdaqkeHHNVVTTMVVGSMGEAEV 312
Cdd:cd19089 224 P---PDSRRAAES-----KFLTEEALTPEKLEQlrklnkiaakrgqSLAQLALSWVL-----RDPRVTSVLIGASSPSQL 290
|
330
....*....|....*....
gi 698810080 313 LSSIRARDNPSlLSKAHIA 331
Cdd:cd19089 291 EDNVAALKNLD-FSEEELA 308
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
15-173 |
6.25e-18 |
|
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: 82.24 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQdLPGEAVTiaVETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgrYRSDk 94
Cdd:cd19133 5 NGVEMPILGFG-VFQ-IPDPEEC--ERAVLEAIKAGYRLIDTAAAYGN-EEAVGRAIKKSGIPREELFITTKL--WIQD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 hpngefdYSRSRIRQSVQDSLAKLGTTYLDVVYLH----DVefvdrdtvlHEAIPALAELQAEGVIKLIGICGYPLDVLD 170
Cdd:cd19133 77 -------AGYEKAKKAFERSLKRLGLDYLDLYLIHqpfgDV---------YGAWRAMEELYKEGKIRAIGVSNFYPDRLV 140
|
...
gi 698810080 171 DIV 173
Cdd:cd19133 141 DLI 143
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
15-176 |
4.96e-17 |
|
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: 80.14 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTiAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgrYRSDk 94
Cdd:cd19127 5 NGVEMPALGLG-VFQTPPEETAD-AVAT---ALADGYRLIDTAAAYGN-EREVGEGIRRSGVDRSDIFVTTKL--WISD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 hpngefdYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRD-TVlhEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19127 76 -------YGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDrTI--QAYKALEKLLAEGRVRAIGVSNFTPEHLERLI 146
|
...
gi 698810080 174 QRS 176
Cdd:cd19127 147 DAT 149
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
19-169 |
1.02e-16 |
|
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: 78.81 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 19 LGSVGLGGLYQDLPGEAVTiAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtPRHEYYLATKVgryrSDKHp 96
Cdd:cd19072 9 LGTWGIGGGMSKDYSDDKK-AIEALRYAIELGINLIDTAEMYGGghAEELVGKAIKGF--DREDLFITTKV----SPDH- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 698810080 97 ngefdYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVL 169
Cdd:cd19072 81 -----LKYDDVIKAAKESLKRLGTDYIDLYLIH---WPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEEL 145
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
16-174 |
2.77e-16 |
|
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: 77.70 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 16 GVALGSVGLGgLYQdLPGEAvtiAVETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKV-GRYrsdk 94
Cdd:cd19132 4 GTQIPAIGFG-TYP-LKGDE---GVEAVVAALQAGYRLLDTAFNYEN-EGAVGEAVRRSGVPREELFVTTKLpGRH---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HPngefdysRSRIRQSVQDSLAKLGTTYLDVVYLH-DVEFVDRDTvlhEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19132 74 HG-------YEEALRTIEESLYRLGLDYVDLYLIHwPNPSRDLYV---EAWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
.
gi 698810080 174 Q 174
Cdd:cd19132 144 D 144
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-165 |
3.68e-16 |
|
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: 78.04 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTG--VNGVALGSVGLGG---LYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtpRHEYYL 83
Cdd:cd19091 8 RSGlkVSELALGTMTFGGgggFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEgeSEEILGKALKGR---RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 84 ATKVgRYRSDKHPNgEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICG 163
Cdd:cd19091 85 ATKV-RGRMGEGPN-DVGLSRHHIIRAVEASLKRLGTDYIDLYQLHG---FDALTPLEETLRALDDLVRQGKVRYIGVSN 159
|
..
gi 698810080 164 YP 165
Cdd:cd19091 160 FS 161
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
15-227 |
3.72e-16 |
|
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: 77.09 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgrYRSDK 94
Cdd:cd19126 5 NGTRMPWLGLG-VFQTPDGDETERAVQT---ALENGYRSIDTAAIYKN-EEGVGEAIRESGVPREELFVTTKL--WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HPNgefdysrsRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLhEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19126 78 RAR--------RTEDAFQESLDRLGLDYVDLYLIH---WPGKDKFI-DTWKALEKLYASGKVKAIGVSNFQEHHLEELLA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 698810080 175 RSPRPLQVVQSYSHLTLQNDALLTKAASWHAKGNTVSPIHRRVLLKHYVLPGI 227
Cdd:cd19126 146 HADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAI 198
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
14-187 |
4.18e-16 |
|
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: 77.66 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGGLYQDLPGEAVtiAVETFETAFPRGVRLIDTA----PWYNnaEDVVGQALrrvQTPRHEYYLATKVG- 88
Cdd:cd19078 4 VSAIGLGCMGMSHGYGPPPDKEE--MIELIRKAVELGITFFDTAevygPYTN--EELVGEAL---KPFRDQVVIATKFGf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 89 RYRSDKHPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICgyplDV 168
Cdd:cd19078 77 KIDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHR---VDPNVPIEEVAGTMKELIKEGKIRHWGLS----EA 149
|
170 180
....*....|....*....|..
gi 698810080 169 LDDIVQRSPR--PLQVVQS-YS 187
Cdd:cd19078 150 GVETIRRAHAvcPVTAVQSeYS 171
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-243 |
1.09e-15 |
|
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: 77.10 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 1 MPTSTdVQAFRTGVNGVALGSVGLGGLYQDLPGEAVTIAVetFETAFPRGVRLIDTAPWYNNAEDVVGQALRRVQTPRHE 80
Cdd:cd19144 1 IPTRT-LGRNGPSVPALGFGAMGLSAFYGPPKPDEERFAV--LDAAFELGCTFWDTADIYGDSEELIGRWFKQNPGKREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 81 YYLATKVGRYR----SDKHPNGEFDYsrsrIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVI 156
Cdd:cd19144 78 IFLATKFGIEKnvetGEYSVDGSPEY----VKKACETSLKRLGVDYIDLYYQHR---VDGKTPIEKTVAAMAELVQEGKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 157 KLIGICgyplDVLDDIVQR--SPRPLQVVQ-SYSHLTL---QNDALLTKAAswhakgntvspihrRVLlkhyvlpGIVVI 230
Cdd:cd19144 151 KHIGLS----ECSAETLRRahAVHPIAAVQiEYSPFSLdieRPEIGVLDTC--------------REL-------GVAIV 205
|
250
....*....|...
gi 698810080 231 NAAPLSMGLLTSR 243
Cdd:cd19144 206 AYSPLGRGFLTGA 218
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
27-197 |
2.05e-15 |
|
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: 75.35 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 27 LYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGRYRSDkhpngefdysrsr 106
Cdd:cd19120 15 WYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGN-EKEVGEALKESGVPREDLFITTKVSPGIKD------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 107 IRQSVQDSLAKLGTTYLDVVYLHDVEFVD-RDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQRSPRPLQV--V 183
Cdd:cd19120 81 PREALRKSLAKLGVDYVDLYLIHSPFFAKeGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAVnqI 160
|
170
....*....|....
gi 698810080 184 QSYSHLTLQNDALL 197
Cdd:cd19120 161 EFHPYLYPQQPALL 174
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
15-184 |
3.34e-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: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGV-----ALGSVGLGGLYQdlpgEAVTIAVETFetafprGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgr 89
Cdd:cd19135 9 NGVempilGLGTSHSGGYSH----EAVVYALKEC------GYRHIDTAKRYGC-EELLGKAIKESGVPREDLFLTTKL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 90 yrsdkHPNgefDYSRSRIRQSVQDSLAKLGTTYLDVVYLH----DVEFVDRDTVLHEAIPALAELQAEGVIKLIGICGYP 165
Cdd:cd19135 76 -----WPS---DYGYESTKQAFEASLKRLGVDYLDLYLLHwpdcPSSGKNVKETRAETWRALEELYDEGLCRAIGVSNFL 147
|
170
....*....|....*....
gi 698810080 166 LDVLDDIVQRSPRPLQVVQ 184
Cdd:cd19135 148 IEHLEQLLEDCSVVPHVNQ 166
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-167 |
5.50e-15 |
|
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: 73.79 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGGLYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRrvqtPRHE-YYLATKVGRY 90
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYgpDVNERLIAEALH----PYPDdVVIATKGGLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 RS---DKHPNGEFDYsrsrIRQSVQDSLAKLGTTYLDVVYLHDVefvDRDTVLHEAIPALAELQAEGVIKLIGICGYPLD 167
Cdd:cd19088 77 RTgpgWWGPDGSPEY----LRQAVEASLRRLGLDRIDLYQLHRI---DPKVPFEEQLGALAELQDEGLIRHIGLSNVTVA 149
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-256 |
6.90e-15 |
|
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: 73.36 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 23 GLGGL-YQDLPGEAVTI--AVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtPRHEYYLATKVgryrsdkhPN 97
Cdd:cd19096 4 GFGTMrLPESDDDSIDEekAIEMIRYAIDAGINYFDTAYGYGGgkSEEILGEALKEG--PREKFYLATKL--------PP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 98 GEFDySRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHE-----AIPALAELQAEGVIKLIGI--CGYPlDVLD 170
Cdd:cd19096 74 WSVK-SAEDFRRILEESLKRLGVDYIDFYLLHG---LNSPEWLEKarkggLLEFLEKAKKEGLIRHIGFsfHDSP-ELLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 171 DIVqrSPRPLQVVQ-SYSHL---TLQNDALLTKAASwhaKGNtvspihrrvllkhyvlpGIVVINaaPLSMGLLTSRGPP 246
Cdd:cd19096 149 EIL--DSYDFDFVQlQYNYLdqeNQAGRPGIEYAAK---KGM-----------------GVIIME--PLKGGGLANNPPE 204
|
250
....*....|....*...
gi 698810080 247 A--------WHPASSALR 256
Cdd:cd19096 205 AlailcgapLSPAEWALR 222
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-174 |
7.26e-15 |
|
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: 74.13 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 16 GVALGSVGLGGLYQDLPGEAVTIAVETFetaFPRGVRLIDTAPWYNN--AEDVVGQALRrvqtPRHEYYLATKVgryrsd 93
Cdd:cd19075 2 KIILGTMTFGSQGRFTTAEAAAELLDAF---LERGHTEIDTARVYPDgtSEELLGELGL----GERGFKIDTKA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 kHPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19075 69 -NPGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLH---APDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIV 144
|
.
gi 698810080 174 Q 174
Cdd:cd19075 145 E 145
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
11-160 |
1.06e-14 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 73.76 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTG--VNGVALGSVGLGGLyqdlPGEAVTIAVetFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVqtpRHEYYLATK 86
Cdd:cd19087 8 RTGlkVSRLCLGTMNFGGR----TDEETSFAI--MDRALDAGINFFDTADVYGGgrSEEIIGRWIAGR---RDDIVLATK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 698810080 87 VGrYRSDKHPNgEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIG 160
Cdd:cd19087 79 VF-GPMGDDPN-DRGLSRRHIRRAVEASLRRLQTDYIDLYQMHH---FDRDTPLEETLRALDDLVRQGKIRYIG 147
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
33-162 |
3.48e-14 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 72.60 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 33 GEAVTI--AVETFETAFPRGVRLIDTA-----PW----YNNAEDVVGQALRRvQTPRHEYYLATKV-GRYRSDKHPNGEF 100
Cdd:cd19094 12 GEQNTEaeAHEQLDYAFDEGVNFIDTAemypvPPspetQGRTEEIIGSWLKK-KGNRDKVVLATKVaGPGEGITWPRGGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 101 -DYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLH------------EAIP------ALAELQAEGVIKLIGI 161
Cdd:cd19094 91 tRLDRENIREAVEGSLKRLGTDYIDLYQLHW---PDRYTPLFgggyytepseeeDSVSfeeqleALGELVKAGKIRHIGL 167
|
.
gi 698810080 162 C 162
Cdd:cd19094 168 S 168
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
39-160 |
4.35e-14 |
|
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: 71.82 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 39 AVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQTPRHEYYLATKVG-RYRSDKHPN--GEFDYSRSRIRQSVQD 113
Cdd:cd19092 26 LLSLIEAALELGITTFDHADIYGGgkCEELFGEALALNPGLREKIEIQTKCGiRLGDDPRPGriKHYDTSKEHILASVEG 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 698810080 114 SLAKLGTTYLDVVYLHdvefvdR-DTVLH--EAIPALAELQAEGVIKLIG 160
Cdd:cd19092 106 SLKRLGTDYLDLLLLH------RpDPLMDpeEVAEAFDELVKSGKVRYFG 149
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-161 |
4.79e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 71.97 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGGLYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRV----QTPRHEYYLATKVG-- 88
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGgrSERLIGKALRELiekgGIKRDEVVIVTKAGyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 89 -------------------RYRSDKH--PNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVE----------FVDRd 137
Cdd:cd19099 81 pgdgdeplrplkyleeklgRGLIDVAdsAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEeqllelgeeeFYDR- 159
|
170 180
....*....|....*....|....
gi 698810080 138 tvLHEAIPALAELQAEGVIKLIGI 161
Cdd:cd19099 160 --LEEAFEALEEAVAEGKIRYYGI 181
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
31-174 |
9.47e-14 |
|
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: 70.07 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 31 LPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrsdkhpngEFDYSRSRIRQS 110
Cdd:cd19139 11 LKDDVVIDSVRT---ALELGYRHIDTAQIYDN-EAAVGQAIAESGVPRDELFITTKIW----------IDNLSKDKLLPS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 698810080 111 VQDSLAKLGTTYLDVVYLH-----DVEFVDrdtvlhEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHwpspnDEVPVE------EYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
15-174 |
1.87e-13 |
|
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: 69.73 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrsdk 94
Cdd:cd19157 6 NGVKMPWLGLG-VFKVEEGSEVVNAVKT---ALKNGYRSIDTAAIYGN-EEGVGKGIKESGIPREELFITSKVW------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 hpNGEFDYSRSriRQSVQDSLAKLGTTYLDVVYLHdvefVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19157 75 --NADQGYDST--LKAFEASLERLGLDYLDLYLIH----WPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLA 146
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
22-230 |
3.94e-13 |
|
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: 68.43 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 22 VGLGgLYQdLPGEAvtIAVETFETAFPRGVRLIDTAPWYNNAEDVvGQALRRV----QTPRHEYYLATKVGRYrsdkhpn 97
Cdd:cd19136 4 LGLG-TFR-LRGEE--EVRQAVDAALKAGYRLIDTASVYRNEADI-GKALRDLlpkyGLSREDIFITSKLAPK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 98 gefDYSRSRIRQSVQDSLAKLGTTYLDVVYLH--DVEFVDRDTVLHEAI-----PALAELQAEGVIKLIGICGYPLDVLD 170
Cdd:cd19136 72 ---DQGYEKARAACLGSLERLGTDYLDLYLIHwpGVQGLKPSDPRNAELrreswRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 171 DIVQRS---PRPLQV---------------------VQSYSHLTLQNDALLT----KAASWHAKgntVSPIHrrVLLKHY 222
Cdd:cd19136 149 ELLKYCevpPAVNQVefhphlvqkellkfckdhgihLQAYSSLGSGDLRLLEdptvLAIAKKYG---RTPAQ--VLLRWA 223
|
....*...
gi 698810080 223 VLPGIVVI 230
Cdd:cd19136 224 LQQGIGVI 231
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
17-196 |
4.45e-13 |
|
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: 68.37 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGG-LYQDLPGEAVtiAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRVqtPRHEYYLATKVgryrsd 93
Cdd:cd19137 7 LGLGTWGIGGfLTPDYSRDEE--MVELLKTAIELGYTHIDTAEMYggGHTEELVGKAIKDF--PREDLFIVTKV------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 KHPNgefdYSRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIV 173
Cdd:cd19137 77 WPTN----LRYDDLLRSLQNSLRRLDTDYIDLYLIH---WPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAI 149
|
170 180
....*....|....*....|....*..
gi 698810080 174 QRSPRPLQVVQS----YSHLTLQNDAL 196
Cdd:cd19137 150 SKSQTPIVCNQVkynlEDRDPERDGLL 176
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
21-161 |
8.48e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 67.74 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 21 SVGLGGLyqDLPGEAVtiaVETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrSDKhpngef 100
Cdd:PRK11172 5 AFGLGTF--RLKDQVV---IDSVKTALELGYRAIDTAQIYDN-EAAVGQAIAESGVPRDELFITTKIW---IDN------ 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 698810080 101 dYSRSRIRQSVQDSLAKLGTTYLDVVYLH------DVEfvdrdtvLHEAIPALAELQAEGVIKLIGI 161
Cdd:PRK11172 70 -LAKDKLIPSLKESLQKLRTDYVDLTLIHwpspndEVS-------VEEFMQALLEAKKQGLTREIGI 128
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
23-164 |
2.13e-12 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 66.63 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 23 GLGgLYQDLPGEAVTIAVETFETafprGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVgrYRSDKHpngefdy 102
Cdd:PRK11565 19 GLG-VWQASNEEVITAIHKALEV----GYRSIDTAAIYKN-EEGVGKALKEASVAREELFITTKL--WNDDHK------- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 698810080 103 srsRIRQSVQDSLAKLGTTYLDVvYLHDVEFVDRDTVLhEAIPALAELQAEGVIKLIGICGY 164
Cdd:PRK11565 84 ---RPREALEESLKKLQLDYVDL-YLMHWPVPAIDHYV-EAWKGMIELQKEGLIKSIGVCNF 140
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
50-187 |
2.26e-12 |
|
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: 66.85 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 50 GVRLIDTAPWYNN---------AEDVVGQALRRvQTPRHEYYLATKVGRYRSDKHPngefDYSRSRIRQSVQDSLAKLGT 120
Cdd:cd19081 39 GGNFIDTADVYSAwvpgnaggeSETIIGRWLKS-RGKRDRVVIATKVGFPMGPNGP----GLSRKHIRRAVEASLRRLQT 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 698810080 121 TYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQRS-----PRPLQVVQSYS 187
Cdd:cd19081 114 DYIDLYQAH---WDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSrqhglPRYVSLQPEYN 182
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
22-233 |
2.93e-12 |
|
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: 66.03 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 22 VGLGGLYQDLPGEAVTIAVETfetafprGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrsdkHPNGEFD 101
Cdd:cd19134 16 LGVGELSDDEAERSVSAALEA-------GYRLIDTAAAYGN-EAAVGRAIAASGIPRGELFVTTKLA------TPDQGFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 102 YSRSRIRQsvqdSLAKLGTTYLDVVYLH-----DVEFVDrdtvlheAIPALAELQAEGVIKLIGICGYPLDVLDDIVQRS 176
Cdd:cd19134 82 ASQAACRA----SLERLGLDYVDLYLIHwpagrEGKYVD-------SWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 698810080 177 PRPLQVVQSYSHLTLQNDALLTKAASWHAKGNTVSPIHRRVLLKHyvlPGIVVINAA 233
Cdd:cd19134 151 FFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDN---PAVTAIAAA 204
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
39-241 |
3.08e-12 |
|
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: 66.48 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 39 AVETFETAFPRGVRLIDTAPWYN--NAEDVVGQALRRVQtPRHEYYLATKVGRYRSDKhpngefdySRSRIRQSVQDSLA 116
Cdd:cd19093 28 LQAAFDAALEAGVNLFDTAEVYGtgRSERLLGRFLKELG-DRDEVVIATKFAPLPWRL--------TRRSVVKALKASLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 117 KLGTTYLDVVYLHDVEFVDR--DTVLHeaipALAELQAEGVIKLIGICGYPLDVLDDIVQRSPR---PLQVVQ-SYShlt 190
Cdd:cd19093 99 RLGLDSIDLYQLHWPGPWYSqiEALMD----GLADAVEEGLVRAVGVSNYSADQLRRAHKALKErgvPLASNQvEYS--- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 698810080 191 lqndaLLtkaaswhakgntvspihRRVLLKHYVLP-----GIVVINAAPLSMGLLT 241
Cdd:cd19093 172 -----LL-----------------YRDPEQNGLLPacdelGITLIAYSPLAQGLLT 205
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-189 |
3.95e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 66.20 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 50 GVRLIDTAPWYN---------NAEDVVGQALRRvQTPRHEYYLATKVG-RYRSDKHPNGEFD-YSRSRIRQSVQDSLAKL 118
Cdd:cd19752 30 GGNFLDTANNYAfwteggvggESERLIGRWLKD-RGNRDDVVIATKVGaGPRDPDGGPESPEgLSAETIEQEIDKSLRRL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 698810080 119 GTTYLDVVYLHdVEfvDRDTVLHEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQRS-----PRPLQVVQSYSHL 189
Cdd:cd19752 109 GTDYIDLYYAH-VD--DRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIArqqgwAEFSAIQQRHSYL 181
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-255 |
1.49e-11 |
|
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: 64.36 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQdLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRvqtprheyYLATKVGRyRSD- 93
Cdd:cd19154 8 NGVKMPLIGLG-TWQ-SKGAEGITAVRT---ALKAGYRLIDTAFLYQN-EEAIGEALAE--------LLEEGVVK-REDl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 ----KHPNGEfdYSRSRIRQSVQDSLAKLGTTYLDVVYLH------DVEFVDRDTVLHEAIP----------ALAELQAE 153
Cdd:cd19154 73 fittKLWTHE--HAPEDVEEALRESLKKLQLEYVDLYLIHapaafkDDEGESGTMENGMSIHdavdvedvwrGMEKVYDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 154 GVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNdalltkaaswhakgntvsPIHRRVLLKHyvlpGIVVINAA 233
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQ------------------KELVEFCKKH----NISVTSYA 208
|
250 260
....*....|....*....|...
gi 698810080 234 PL-SMGLLTSRGPPAWHPASSAL 255
Cdd:cd19154 209 TLgSPGRANFTKSTGVSPAPNLL 231
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
14-161 |
1.59e-11 |
|
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: 64.38 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGGLYQDLPGEAVTIAVetFETAFPRGVRLIDTAPWY--NNAEDVVGQALRrvQTPRHEYYLATKVG-RY 90
Cdd:cd19145 12 VSAQGLGCMGLSGDYGAPKPEEEGIAL--IHHAFNSGVTFLDTSDIYgpNTNEVLLGKALK--DGPREKVQLATKFGiHE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 698810080 91 RSDKHP--NGEFDYsrsrIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGI 161
Cdd:cd19145 88 IGGSGVevRGDPAY----VRAACEASLKRLDVDYIDLYYQHR---IDTTVPIEITMGELKKLVEEGKIKYIGL 153
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-174 |
2.57e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 63.77 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 39 AVETFETAFPRGVRLIDTAPWYNNAEDVVGQALRRVqtpRHEYYLATKVGRYRSDKHPNGEFDYSRSRIRQSVQDSLAKL 118
Cdd:cd19101 25 AVRAMAAYVDAGLTTFDCADIYGPAEELIGEFRKRL---RRERDAADDVQIHTKWVPDPGELTMTRAYVEAAIDRSLKRL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 698810080 119 GTTYLDVVYLHDVEFVDRDTVlhEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19101 102 GVDRLDLVQFHWWDYSDPGYL--DAAKHLAELQEEGKIRHLGLTNFDTERLREILD 155
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
15-197 |
5.02e-11 |
|
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: 62.68 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRV----QTPRHEYYLATKVGry 90
Cdd:cd19116 7 DGNEIPAIALG-TWKLKDDEGVRQAVKH---AIEAGYRHIDTAYLYGN-EAEVGEAIREKiaegVVKREDLFITTKLW-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 rSDKHpngefdySRSRIRQSVQDSLAKLGTTYLDVVYLH---DVEFVDRDTVLHEAIP----------ALAELQAEGVIK 157
Cdd:cd19116 80 -NSYH-------EREQVEPALRESLKRLGLDYVDLYLIHwpvAFKENNDSESNGDGSLsdidyletwrGMEDLVKLGLTR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 698810080 158 LIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19116 152 SIGVSNFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLV 191
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-160 |
5.44e-11 |
|
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: 62.57 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALGSVGLGglyQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNN------AEDVVGQAL--RRVqtpRHEYYLATKVG 88
Cdd:cd19082 3 IVLGTADFG---TRIDEEE---AFALLDAFVELGGNFIDTARVYGDwvergaSERVIGEWLksRGN---RDKVVIATKGG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 698810080 89 ryrsdkHPNGEfDYSRSR-----IRQSVQDSLAKLGTTYLDVVYLH-DvefvDRDTVLHEAIPALAELQAEGVIKLIG 160
Cdd:cd19082 74 ------HPDLE-DMSRSRlspedIRADLEESLERLGTDYIDLYFLHrD----DPSVPVGEIVDTLNELVRAGKIRAFG 140
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
15-227 |
5.81e-11 |
|
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: 62.15 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrsdk 94
Cdd:cd19156 5 NGVEMPRLGLG-VWRVQDGAEAENAVKW---AIEAGYRHIDTAAIYKN-EEGVGQGIRESGVPREEVFVTTKLW------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 hpNGEFDYSRSriRQSVQDSLAKLGTTYLDVVYLH---DVEFVDrdtvlheAIPALAELQAEGVIKLIGICGYPLDVLDD 171
Cdd:cd19156 74 --NSDQGYEST--LAAFEESLEKLGLDYVDLYLIHwpvKGKFKD-------TWKAFEKLYKEKKVRAIGVSNFHEHHLEE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 698810080 172 IVQRSPRPLQVVQSYSHLTLQNDALLTKAASWHAKGNTVSPIHRRVLLKHYVLPGI 227
Cdd:cd19156 143 LLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAI 198
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
36-154 |
9.48e-11 |
|
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: 62.23 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 36 VTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQTPRHEYYLATKVGRYRSDKHPNGEfDYSRSRIRQSVQD 113
Cdd:cd19143 30 VDEAKECMKAAYDAGVNFFDNAEVYANgqSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPPPNDR-GLSRKHIVEGTKA 108
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 698810080 114 SLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEG 154
Cdd:cd19143 109 SLKRLQLDYVDLVFCHR---PDPATPIEETVRAMNDLIDQG 146
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
40-161 |
1.10e-10 |
|
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: 61.50 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 40 VETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRrvqTPRHEYYLATKVgrYRSDKhpngefdySRSRIRQSVQDSLAK 117
Cdd:cd19138 32 IEALRAGIDLGMTLIDTAEMYGDggSEELVGEAIR---GRRDKVFLVSKV--LPSNA--------SRQGTVRACERSLRR 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 698810080 118 LGTTYLDVVYLHdvefvDRDTV-LHEAIPALAELQAEGVIKLIGI 161
Cdd:cd19138 99 LGTDYLDLYLLH-----WRGGVpLAETVAAMEELKKEGKIRAWGV 138
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
15-228 |
3.09e-10 |
|
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: 59.92 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVtiavETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrSDK 94
Cdd:cd19130 6 DGNSIPQLGYG-VFKVPPADTQ----RAVATALEVGYRHIDTAAIYGN-EEGVGAAIAASGIPRDELFVTTKLW---NDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 95 HpngefdySRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVlhEAIPALAELQAEGVIKLIGICGYPLDVLDDIVQ 174
Cdd:cd19130 77 H-------DGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYV--HTWEAMIELRAAGRTRSIGVSNFLPPHLERIVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 175 RSPRPLQVVQSYSHLTLQN---------------------------DALLTKAASWHakGNTVSPIHRRVLLK--HYVLP 225
Cdd:cd19130 148 ATGVVPAVNQIELHPAYQQrtirdwaqahdvkieawsplgqgkllgDPPVGAIAAAH--GKTPAQIVLRWHLQkgHVVFP 225
|
...
gi 698810080 226 GIV 228
Cdd:cd19130 226 KSV 228
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
11-321 |
3.33e-10 |
|
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: 60.55 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTGVNGVALGSVGLGgLYQDLpGEAVTIAV--ETFETAFPRGVRLIDTA----PWYNNAEDVVGQALRRVQTP-RHEYYL 83
Cdd:cd19150 4 RCGKSGLKLPALSLG-LWHNF-GDDTPLETqrAILRTAFDLGITHFDLAnnygPPPGSAEENFGRILREDFAGyRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 84 ATKVGrYRSDKHPNGEFDySRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICG 163
Cdd:cd19150 82 STKAG-YDMWPGPYGEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHR---FDPDTPLEETMGALDHAVRSGKALYVGISS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 164 Y---PLDVLDDIVQRSPRPLQVVQ-SYSHLTlqndalltkaaSWhakgntvspIHRRVLLKHYVLPGIVVINAAPLSMGL 239
Cdd:cd19150 157 YspeRTREAAAILRELGTPLLIHQpSYNMLN-----------RW---------VEESGLLDTLQELGVGCIAFTPLAQGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 240 LTSR---GPPAwhpassALRASCAAALtwlaSVEFATEQQKPSVEGL-AI---------QYALdAQKEHHNVVTTMVVGS 306
Cdd:cd19150 217 LTDKylnGIPE------GSRASKERSL----SPKMLTEANLNSIRALnEIaqkrgqslaQMAL-AWVLRDGRVTSALIGA 285
|
330
....*....|....*
gi 698810080 307 MGEAEVLSSIRARDN 321
Cdd:cd19150 286 SRPEQLEENVGALDN 300
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
39-165 |
9.15e-10 |
|
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: 59.16 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 39 AVETFETAFPRGVRLIDTAPWYNN--AEDVVGQAlrrVQTPRHEYYLATKVGRYRSDKHPN--GEfdySRSRIRQSVQDS 114
Cdd:cd19080 33 ARAMFDAYVEAGGNFIDTANNYTNgtSERLLGEF---IAGNRDRIVLATKYTMNRRPGDPNagGN---HRKNLRRSVEAS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 698810080 115 LAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGYP 165
Cdd:cd19080 107 LRRLQTDYIDLLYVH---AWDFTTPVEEVMRALDDLVRAGKVLYVGISDTP 154
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
15-197 |
1.50e-09 |
|
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: 58.19 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEaVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVqtprheyyLATKVGRYRSD- 93
Cdd:cd19118 3 TGNKIPAIGLG-TWQAEPGE-VGAAVKI---ALKAGYRHLDLAKVYQN-QHEVGQALKEL--------LKEEPGVKREDl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 94 ----KHPNGefDYSRSRIRQSVQDSLAKLGTTYLDVVYLH-DVEF--------------------VDRDTVLHEAIPALA 148
Cdd:cd19118 69 fitsKLWNN--SHRPEYVEPALDDTLKELGLDYLDLYLIHwPVAFkptgdlnpltavptnggevdLDLSVSLVDTWKAMV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 698810080 149 ELQAEGVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19118 147 ELKKTGKVKSIGVSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELV 195
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-189 |
6.30e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 56.57 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 17 VALG--SVGLGGLYQD-LPGEAVTIA--VETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRvqTPRHEYYLATKVGr 89
Cdd:cd19103 7 IALGtwSWGSGGAGGDqVFGNHLDEDtlKAVFDKAMAAGLNLWDTAAVYgmGASEKILGEFLKR--YPREDYIISTKFT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 90 yrsdkhPNGEfDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTvlheaiPALAELQAEGVIKLIGICGYPLDVL 169
Cdd:cd19103 84 ------PQIA-GQSADPVADMLEGSLARLGTDYIDIYWIHNPADVERWT------PELIPLLKSGKVKHVGVSNHNLAEI 150
|
170 180
....*....|....*....|....
gi 698810080 170 ---DDIVQRSPRPLQVVQS-YSHL 189
Cdd:cd19103 151 kraNEILAKAGVSLSAVQNhYSLL 174
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
15-129 |
9.62e-09 |
|
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: 55.97 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEaVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTPRHEYYLATKVGryrSDK 94
Cdd:cd19117 10 TGAEIPAVGLG-TWQSKPNE-VAKAVEA---ALKAGYRHIDTAAIYGN-EEEVGQGIKDSGVPREEIFITTKLW---CTW 80
|
90 100 110
....*....|....*....|....*....|....*
gi 698810080 95 HpngefdysrSRIRQSVQDSLAKLGTTYLDVVYLH 129
Cdd:cd19117 81 H---------RRVEEALDQSLKKLGLDYVDLYLMH 106
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-129 |
7.08e-08 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 53.62 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 13 GVNGVALGSVGLGGLYQDLPGEAVTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQALRRVQTPRHEYYLATKV-GR 89
Cdd:cd19142 7 GKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqAETELGRILKKKGWKRSSYIVSTKIyWS 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 698810080 90 YRSDkhpngEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLH 129
Cdd:cd19142 87 YGSE-----ERGLSRKHIIESVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
15-231 |
8.18e-08 |
|
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: 52.92 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEaVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQT---PRHEYYLATKVGRyr 91
Cdd:cd19121 8 TGASIPAVGLG-TWQAKAGE-VKAAVAH---ALKIGYRHIDGALCYQN-EDEVGEGIKEAIAggvKREDLFVTTKLWS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 92 sdkhpngefDYSRsRIRQSVQDSLAKLGTTYLDVVYLH-DVEFVDRDTvlHEAIPALAE--------------------L 150
Cdd:cd19121 80 ---------TYHR-RVELCLDRSLKSLGLDYVDLYLVHwPVLLNPNGN--HDLFPTLPDgsrdldwdwnhvdtwkqmekV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 151 QAEGVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL--TKAASWHAK-----GNTVSPIHR-----RVL 218
Cdd:cd19121 148 LKTGKTKAIGVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVdfCKEKGILIEaysplGSTGSPLISdepvvEIA 227
|
250
....*....|...
gi 698810080 219 LKHYVLPGIVVIN 231
Cdd:cd19121 228 KKHNVGPGTVLIS 240
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
15-162 |
9.77e-08 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 53.01 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLG--GL---YQDLPGEAvtiAVETFETAFPRGVRLIDTAPWYNNAE-----DVVGQALRRVQTPRHEYYLA 84
Cdd:cd19077 1 NGKLVGPIGLGlmGLtwrPNPTPDEE---AFETMKAALDAGSNLWNGGEFYGPPDphanlKLLARFFRKYPEYADKVVLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 85 TKVGRYRSDKHPNGefdySRSRIRQSVQDSLAKLGTT-YLDVvylhdveF----VDRDTVLHEAIPALAELQAEGVIKLI 159
Cdd:cd19077 78 VKGGLDPDTLRPDG----SPEAVRKSIENILRALGGTkKIDI-------FeparVDPNVPIEETIKALKELVKEGKIRGI 146
|
...
gi 698810080 160 GIC 162
Cdd:cd19077 147 GLS 149
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
14-165 |
1.04e-07 |
|
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: 52.90 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGGLYQDLPGE-AVTIAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQ--ALRRVqtpRHEYYLATKVG 88
Cdd:cd19147 10 VSPLILGAMSIGDAWSGFMGSmDKEQAFELLDAFYEAGGNFIDTANNYQDeqSETWIGEwmKSRKN---RDQIVIATKFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 89 ----RYRSDKHPNGEF--DYSRSrIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGIC 162
Cdd:cd19147 87 tdykAYEVGKGKAVNYcgNHKRS-LHVSVRDSLRKLQTDWIDILYVH---WWDYTTSIEEVMDSLHILVQQGKVLYLGVS 162
|
...
gi 698810080 163 GYP 165
Cdd:cd19147 163 DTP 165
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
16-196 |
1.51e-07 |
|
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: 52.35 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 16 GVALGSVGLGgLYQDLPGEaVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRVQTP----RHEYYLATKVgrYR 91
Cdd:cd19125 8 GAKIPAVGLG-TWQADPGV-VGNAVKT---AIKEGYRHIDCAAIYGN-EKEIGKALKKLFEDgvvkREDLFITSKL--WC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 92 SDKHPngefdysrSRIRQSVQDSLAKLGTTYLDVVYLH-------DVEFVDRDTVLHEAIP----ALAELQAEGVIKLIG 160
Cdd:cd19125 80 TDHAP--------EDVPPALEKTLKDLQLDYLDLYLIHwpvrlkkGAHMPEPEEVLPPDIPstwkAMEKLVDSGKVRAIG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 698810080 161 ICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDAL 196
Cdd:cd19125 152 VSNFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKL 187
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-196 |
1.98e-07 |
|
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: 51.73 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 16 GVALGSVGLGgLYQdLPGEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRV----QTPRHEYYLATKVGRYr 91
Cdd:cd19111 1 GFPMPVIGLG-TYQ-SPPEEVRAAVDY---ALFVGYRHIDTALSYQN-EKAIGEALKWWlkngKLKREEVFITTKLPPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 92 sdkhpngefDYSRSRIRQSVQDSLAKLGTTYLDVVYLH-DVEFVDRD---------TVLHEAIPALAELQAEGVIKLIGI 161
Cdd:cd19111 74 ---------YLEFKDTEKSLEKSLENLKLPYVDLYLIHhPCGFVNKKdkgerelasSDVTSVWRAMEALVSEGKVKSIGL 144
|
170 180 190
....*....|....*....|....*....|....*
gi 698810080 162 CGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDAL 196
Cdd:cd19111 145 SNFNPRQINKILAYAKVKPSNLQLECHAYLQQREL 179
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
15-197 |
2.24e-07 |
|
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: 51.62 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEaVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRR-----VQTPRHEYYLATKVgr 89
Cdd:cd19106 3 TGQKMPLIGLG-TWKSKPGQ-VKAAVKY---ALDAGYRHIDCAAVYGN-EQEVGEALKEkvgpgKAVPREDLFVTSKL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 90 YRSDKHPngefdysrSRIRQSVQDSLAKLGTTYLDVVYLH--------DVEFV--DRDTVLHEAIP------ALAELQAE 153
Cdd:cd19106 75 WNTKHHP--------EDVEPALRKTLKDLQLDYLDLYLIHwpyafergDNPFPknPDGTIRYDSTHyketwkAMEKLVDK 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 698810080 154 GVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19106 147 GLVKAIGLSNFNSRQIDDILSVARIKPAVLQVECHPYLAQNELI 190
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
11-167 |
3.57e-07 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 51.25 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTGVNGVALGSVGLGgLYQDLPGeavtiaVETFE-------TAFPRGVRLIDTApwyNN-------AEDVVGQALRR-VQ 75
Cdd:cd19151 4 RCGRSGLKLPAISLG-LWHNFGD------VDRYEnsramlrRAFDLGITHFDLA---NNygpppgsAEENFGRILKEdLK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 76 TPRHEYYLATKVGRYRSDKhPNGEFDySRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGV 155
Cdd:cd19151 74 PYRDELIISTKAGYTMWPG-PYGDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHR---PDPETPLEETMGALDQIVRQGK 148
|
170
....*....|..
gi 698810080 156 IKLIGICGYPLD 167
Cdd:cd19151 149 ALYVGISNYPPE 160
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
46-243 |
5.77e-07 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 50.76 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 46 AFPRGVRLIDTAPWYN----NAEDVVGQALRRVQTP-RHEYYLATKVGrYRSDKHPNGEfDYSRSRIRQSVQDSLAKLGT 120
Cdd:PRK09912 52 AFDLGITHFDLANNYGpppgSAEENFGRLLREDFAAyRDELIISTKAG-YDMWPGPYGS-GGSRKYLLASLDQSLKRMGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 121 TYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGVIKLIGICGYPLD---VLDDIVQRSPRPLQVVQ-SYSHLTlqndal 196
Cdd:PRK09912 130 EYVDIFYSHR---VDENTPMEETASALAHAVQSGKALYVGISSYSPErtqKMVELLREWKIPLLIHQpSYNLLN------ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 698810080 197 ltkaaSWHAKGNTVSPIHRRvllkhyvlpGIVVINAAPLSMGLLTSR 243
Cdd:PRK09912 201 -----RWVDKSGLLDTLQNN---------GVGCIAFTPLAQGLLTGK 233
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
26-197 |
5.83e-07 |
|
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: 50.21 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 26 GLYQDLPGEAVtiavETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRV----QTPRHEYYLATKVGRYrsdkhpngefD 101
Cdd:cd19128 7 GTYKITESESK----EAVKNAIKAGYRHIDCAYYYGN-EAFIGIAFSEIfkdgGVKREDLFITSKLWPT----------M 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 102 YSRSRIRQSVQDSLAKLGTTYLDVVYLHDVEFVDRDTVLHEAIP----------------ALAELQAEGVIKLIGICGYP 165
Cdd:cd19128 72 HQPENVKEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDnqiqslskkpledtwrAMEQCVDEKLTKNIGVSNYS 151
|
170 180 190
....*....|....*....|....*....|...
gi 698810080 166 LDVLDDIVQRSP-RPLqVVQSYSHLTLQNDALL 197
Cdd:cd19128 152 TKLLTDLLNYCKiKPF-MNQIECHPYFQNDKLI 183
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
14-165 |
6.64e-07 |
|
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: 50.50 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGSVGLGGLYQDLPGEAVT-IAVETFETAFPRGVRLIDTAPWYNN--AEDVVGQ--ALRRVqtpRHEYYLATKVG 88
Cdd:cd19146 11 VSPLCLGAMSFGEAWKSMMGECDKeTAFKLLDAFYEQGGNFIDTANNYQGeeSERWVGEwmASRGN---RDEMVLATKYT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 89 -RYRSDKHPNGEFDY---SRSRIRQSVQDSLAKLGTTYLDVVYLHdveFVDRDTVLHEAIPALAELQAEGVIKLIGICGY 164
Cdd:cd19146 88 tGYRRGGPIKIKSNYqgnHAKSLRLSVEASLKKLQTSYIDILYVH---WWDYTTSIPELMQSLNHLVAAGKVLYLGVSDT 164
|
.
gi 698810080 165 P 165
Cdd:cd19146 165 P 165
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
46-161 |
1.37e-06 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 49.47 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 46 AFPRGVRLIDTAPWY---------NNAEDVVGQALRRvQTPRHEYYLATKV-GRYRSDKH---PNGEFDysRSRIRQSVQ 112
Cdd:PRK10625 39 AVAQGINLIDVAEMYpvpprpetqGLTETYIGNWLAK-RGSREKLIIASKVsGPSRNNDKgirPNQALD--RKNIREALH 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 698810080 113 DSLAKLGTTYLDVVYLH------------DVEFVDRDTV--LHEAIPALAELQAEGVIKLIGI 161
Cdd:PRK10625 116 DSLKRLQTDYLDLYQVHwpqrptncfgklGYSWTDSAPAvsLLETLDALAEQQRAGKIRYIGV 178
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
50-161 |
2.01e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.81 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 50 GVRLIDTAPWYnnAEDVVGQALRRVQTP-RHEYYLATKVGRYRSDkhpNGEF--DYSRSRIRQSVQDSLAKLGTTYLDVV 126
Cdd:PRK10376 53 GVNHIDTSDFY--GPHVTNQLIREALHPyPDDLTIVTKVGARRGE---DGSWlpAFSPAELRRAVHDNLRNLGLDVLDVV 127
|
90 100 110
....*....|....*....|....*....|....*...
gi 698810080 127 YL---HDVeFVDRDTVLHEAIPALAELQAEGVIKLIGI 161
Cdd:PRK10376 128 NLrlmGDG-HGPAEGSIEEPLTVLAELQRQGLVRHIGL 164
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
15-129 |
2.66e-06 |
|
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: 48.26 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGGLyqdLPGEAVTIAVETFETAFPRGVRLIDTApWYNNAEDVVGQALRRV----QTPRHEYYLATKVGRY 90
Cdd:cd19119 8 TGASIPALGLGTA---SPHEDRAEVKEAVEAAIKEGYRHIDTA-YAYETEDFVGEAIKRAiddgSIKREELFITTKVWPT 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 698810080 91 RSDkhpngefdysrsRIRQSVQDSLAKLGTTYLDVVYLH 129
Cdd:cd19119 84 FYD------------EVERSLDESLKALGLDYVDLLLVH 110
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-161 |
8.44e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 46.95 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 46 AFPRGVRLIDTAPWYNNAEDVVGQALRRVQTPRHEYYLATKVG-RY----RSDKHPNGEFDYSRSRIRQSVQDSLAKLGt 120
Cdd:cd19098 44 AWAAGVRYFDAARSYGRAEEFLGSWLRSRNIAPDAVFVGSKWGyTYtadwQVDAAVHEVKDHSLARLLKQWEETRSLLG- 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 698810080 121 TYLDVVYLHDVEF---VDRDTVLHEaipALAELQAEGVikLIGI 161
Cdd:cd19098 123 KHLDLYQIHSATLesgVLEDADVLA---ALAELKAEGV--KIGL 161
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|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
11-197 |
1.62e-05 |
|
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: 46.08 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 11 RTGVNGVALGSVGLGGLYQD-LPGEAVTIAVETFETafprGVRLIDTApWYNNAEDVVGQALR-----RVQTPRHEYYLA 84
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFANEgAKGETYAAVTKALDV----GYRHLDCA-WFYLNEDEVGDAVRdflkeNPSVKREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 85 TKVGRYRsdkhpngefdYSRSRIRQSVQDSLAKLGTTYLDVVYLH-----------------DVEFVDRDTVLHEAIP-- 145
Cdd:cd19122 76 TKVWNHL----------HEPEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaekndqrspklgpDGKYVILKDLTENPEPtw 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 698810080 146 -ALAELQAEGVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19122 146 rAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELV 198
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|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
14-127 |
3.74e-05 |
|
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: 45.13 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGS-VGLGG-LYQDLPGEAVTIAVETfetafprGVRLIDTAPWY--NNAEDVVGQALRRVQTPRHEYYLATKV-- 87
Cdd:cd19141 12 VSCLGLGTwVTFGSqISDEVAEELVTLAYEN-------GINLFDTAEVYaaGKAEIVLGKILKKKGWRRSSYVITTKIfw 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 698810080 88 -GRYRSDKhpngefDYSRSRIRQSVQDSLAKLGTTYLDVVY 127
Cdd:cd19141 85 gGKAETER------GLSRKHIIEGLKASLERLQLEYVDIVF 119
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| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
15-182 |
3.94e-05 |
|
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: 44.82 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPgEAVTIAVETfetAFPRGVRLIDTAPWYNNaEDVVGQALRRV----QTPRHEYYLATKVGRY 90
Cdd:cd19155 8 NGEKMPVVGLG-TWQSSP-EEIETAVDT---ALEAGYRHIDTAYVYRN-EAAIGNVLKKWidsgKVKREELFIVTKLPPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 RSDKHpngefdysrsRIRQSVQDSLAKLGTTYLDVVYLH-----------------DVEFVDRDTVLHEAIPALAELQAE 153
Cdd:cd19155 82 GNRRE----------KVEKFLLKSLEKLQLDYVDLYLIHfpvgslskeddsgkldpTGEHKQDYTTDLLDIWKAMEAQVD 151
|
170 180 190
....*....|....*....|....*....|...
gi 698810080 154 -GVIKLIGICGYPLDVLDDIVQRS---PRPLQV 182
Cdd:cd19155 152 qGLTRSIGLSNFNREQMARILKNArikPANLQV 184
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|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
15-197 |
4.99e-05 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 44.74 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGGLYQDlpgeaVTIAVETFETAFPRGVRLIDTAPWYNNaEDVVGQALRRV----QTPRHEYYLATKVgrY 90
Cdd:cd19113 7 SGYKMPSVGFGCWKLD-----NATAADQIYQAIKAGYRLFDGAEDYGN-EKEVGEGVNRAidegLVKREELFLTSKL--W 78
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 RSDKHPNgefdysrsRIRQSVQDSLAKLGTTYLDVVYLH---DVEFV-------------DRDTVLHEAIP------ALA 148
Cdd:cd19113 79 NNFHDPK--------NVETALNKTLSDLKLDYVDLFLIHfpiAFKFVpieekyppgfycgDGDNFVYEDVPildtwkALE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 698810080 149 ELQAEGVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19113 151 KLVDAGKIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLI 199
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|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
15-198 |
5.02e-04 |
|
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: 41.63 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGE---AVTIAVETfetafprGVRLIDTAPWYNNaEDVVGQALRRVQTP----RHEYYLATKV 87
Cdd:cd19123 8 NGDLIPALGLG-TWKSKPGEvgqAVKQALEA-------GYRHIDCAAIYGN-EAEIGAALAEVFKEgkvkREDLWITSKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 88 grYRSDKHPNGefdysrsrIRQSVQDSLAKLGTTYLD-------VVYLHDVEFVDR--DTVLHEAIP------ALAELQA 152
Cdd:cd19123 79 --WNNSHAPED--------VLPALEKTLADLQLDYLDlylmhwpVALKKGVGFPESgeDLLSLSPIPledtwrAMEELVD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 698810080 153 EGVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALLT 198
Cdd:cd19123 149 KGLCRHIGVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLA 194
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| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
14-155 |
6.85e-04 |
|
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: 41.18 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 14 VNGVALGS-VGLGGLYQDlpgeavTIAVETFETAFPRGVRLIDTAPWY--NNAEDVVGQALRRVQTPRHEYYLATKVgrY 90
Cdd:cd19159 13 VSCLGLGTwVTFGGQISD------EVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKL--Y 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 698810080 91 RSDKhPNGEFDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGV 155
Cdd:cd19159 85 WGGK-AETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGM 145
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| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
15-197 |
8.42e-04 |
|
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: 40.93 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 15 NGVALGSVGLGgLYQDLPGEAVTIAVEtfetAFPRGVRLIDTAPWYNNaEDVVGQALRRV----QTPRHEYYLATKVgrY 90
Cdd:cd19112 7 SGHKMPVIGLG-VWRMEPGEIKELILN----AIKIGYRHFDCAADYKN-EKEVGEALAEAfktgLVKREDLFITTKL--W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 91 RSDkhpngefdysRSRIRQSVQDSLAKLGTTYLDVVYLH--------------------DVEFVDRDTVLHEAIPALAEL 150
Cdd:cd19112 79 NSD----------HGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedGVLDIDVTISLETTWHAMEKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 698810080 151 QAEGVIKLIGICGYPLDVLDDIVQRSPRPLQVVQSYSHLTLQNDALL 197
Cdd:cd19112 149 VSAGLVRSIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLV 195
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|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-127 |
1.31e-03 |
|
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: 40.35 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 12 TGVNGVALGSVGLG----GLyqdlpGEAVT----IAVETFET----AFPRGVRLIDTAPWY--NNAEDVVGQALRRVQTP 77
Cdd:cd19160 1 TGMKYRNLGKSGLRvsclGL-----GTWVTfgsqISDETAEDlltvAYEHGVNLFDTAEVYaaGKAERTLGNILKSKGWR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 698810080 78 RHEYYLATKV---GRYRSDKhpngefDYSRSRIRQSVQDSLAKLGTTYLDVVY 127
Cdd:cd19160 76 RSSYVVTTKIywgGQAETER------GLSRKHIIEGLRGSLDRLQLEYVDIVF 122
|
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| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
13-155 |
2.76e-03 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 39.30 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698810080 13 GVNGVALGSVGLGgLYQDLPGEAVTIAVETFET-AFPRGVRLIDTAPWY--NNAEDVVGQALRRVQTPRHEYYLATKV-- 87
Cdd:cd19158 7 GKSGLRVSCLGLG-TWVTFGGQITDEMAEHLMTlAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVITTKIfw 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 698810080 88 -GRYRSDKhpngefDYSRSRIRQSVQDSLAKLGTTYLDVVYLHDvefVDRDTVLHEAIPALAELQAEGV 155
Cdd:cd19158 86 gGKAETER------GLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGM 145
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