|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
25-279 |
1.91e-156 |
|
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: 437.03 E-value: 1.91e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPY-KGLIIATKGGLVRTGP 103
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYpDDVVIATKGGLVRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYFPV 183
Cdd:cd19088 81 GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 184 VSVQNLFNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGTILDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSK 263
Cdd:cd19088 161 VSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSS 240
|
250
....*....|....*.
gi 19113480 264 VDHLEENVKAAGIQLS 279
Cdd:cd19088 241 VEHLEENLAAAGLRLS 256
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
22-288 |
7.27e-91 |
|
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: 272.82 E-value: 7.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 22 DMVVNRMGFGAMRVTGDgiWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYK--GLIIATKGGLV 99
Cdd:COG0667 10 GLKVSRLGLGTMTFGGP--WGGVDEAEA-IAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPrdDVVIATKVGRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 100 RtGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEA-- 177
Cdd:COG0667 87 M-GPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRAla 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 178 --EQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA---KPGTI----------------------- 228
Cdd:COG0667 166 iaEGLPPIVAVQNEYSLLDRSAEEeLLPAARELGVGVLAYSPLAGGLLTgkyRRGATfpegdraatnfvqgylternlal 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113480 229 ---LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:COG0667 246 vdaLRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDA 308
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
11-287 |
2.85e-85 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 257.59 E-value: 2.85e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 11 DASQAGTVKVGDMVVNRMGFGAMRVTGDGIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPY-KG 89
Cdd:PRK10376 3 TIMSSGTFTLGGRSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYpDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 90 LIIATKGGLVRTGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLhRI--DPKVPRKD----QFSEIAAMKKEGLIRH 163
Cdd:PRK10376 83 LTIVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNL-RLmgDGHGPAEGsieePLTVLAELQRQGLVRH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 164 VGLSEVTVDDIKEAEQYFPVVSVQNLFNLVNRKNEKVLEYCEQKGIAFIPWYPLAsGALAKPGTILDAVSKDLDRSTSQI 243
Cdd:PRK10376 162 IGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARDGIAYVPFFPLG-GFTPLQSSTLSDVAASLGATPMQV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19113480 244 ALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:PRK10376 241 ALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELD 284
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
28-288 |
2.51e-79 |
|
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: 242.60 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 28 MGFGAMRVTGDgiWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG----LIIATKgglVRTGP 103
Cdd:pfam00248 1 IGLGTWQLGGG--WGPISKEEA-LEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVkrdkVVIATK---VPDGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQ--YF 181
Cdd:pfam00248 75 GPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTkgKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 182 PVVSVQNLFNLVN-RKNEKVLEYCEQKGIAFIPWYPLASGALAKPGT--------------------------ILDAVSK 234
Cdd:pfam00248 155 PIVAVQVEYNLLRrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTrdpdkgpgerrrllkkgtplnlealeALEEIAK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19113480 235 DLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:pfam00248 235 EHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDE 288
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-287 |
1.37e-75 |
|
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: 233.19 E-value: 1.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 22 DMVVNRMGFGAMRVTGDgiWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG-LIIATKGGLVR 100
Cdd:cd19084 1 DLKVSRIGLGTWAIGGT--WWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDdVVIATKCGLRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQY 180
Cdd:cd19084 79 DGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 FPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA---KPGTI---------------------------L 229
Cdd:cd19084 159 GPIVSLQPPYSMLEREIEEeLLPYCRENGIGVLPYGPLAQGLLTgkyKKEPTfppddrrsrfpffrgenfeknleivdkL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113480 230 DAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19084 239 KEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
22-289 |
2.43e-68 |
|
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: 214.79 E-value: 2.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 22 DMVVNRMGFGAMRVT-GDGiwdEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG-LIIATKGGlV 99
Cdd:cd19078 1 GLEVSAIGLGCMGMShGYG---PPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDqVVIATKFG-F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 100 RTGPNEWHPCG---APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKE 176
Cdd:cd19078 77 KIDGGKPGPLGldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 177 AEQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA---KPGT------------------------- 227
Cdd:cd19078 157 AHAVCPVTAVQSEYSMMWREPEKeVLPTLEELGIGFVPFSPLGKGFLTgkiDENTkfdegddraslprftpealeanqal 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113480 228 --ILDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEE 289
Cdd:cd19078 237 vdLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDA 300
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
27-272 |
3.22e-67 |
|
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: 209.68 E-value: 3.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDGiwdepkDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG---LIIATKGGLvRTGP 103
Cdd:cd06660 2 RLGLGTMTFGGDG------DEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNrddVVIATKGGH-PPGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQY--- 180
Cdd:cd06660 75 DPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYaka 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 ---FPVVSVQNLFNLVNRK--NEKVLEYCEQKGIAFIPWYPLASGAlakpgtildavskdldrstSQIALSWVLQRSPVM 255
Cdd:cd06660 155 hglPGFAAVQPQYSLLDRSpmEEELLDWAEENGLPLLAYSPLARGP-------------------AQLALAWLLSQPFVT 215
|
250
....*....|....*..
gi 19113480 256 LPIPGTSKVDHLEENVK 272
Cdd:cd06660 216 VPIVGARSPEQLEENLA 232
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-286 |
2.22e-66 |
|
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: 209.76 E-value: 2.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 17 TVKVGD--MVVNRMGFGAMRVTGDGiwdEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALY-PYKGLIIA 93
Cdd:cd19076 2 TRKLGTqgLEVSALGLGCMGMSAFY---GPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKdRRDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 94 TKGGLVRT-GPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVD 172
Cdd:cd19076 79 TKFGIVRDpGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 173 DIKEAEQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLA----SGALAKPGTI------------------- 228
Cdd:cd19076 159 TIRRAHAVHPITAVQSEYSLWTRDIEDeVLPTCRELGIGFVAYSPLGrgflTGAIKSPEDLpeddfrrnnprfqgenfdk 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113480 229 -------LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKL 286
Cdd:cd19076 239 nlklvekLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
25-287 |
3.10e-57 |
|
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: 185.13 E-value: 3.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYK--GLIIATKgglvrtg 102
Cdd:cd19072 4 VPVLGLGTWGIGGGMSKDYSDDKKA-IEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDreDLFITTK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 103 PNEWHpcGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYF- 181
Cdd:cd19072 76 VSPDH--LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 182 --PVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGAL--AKPGTILDAVSKDLDRSTSQIALSWVLQRsPVML 256
Cdd:cd19072 154 kgPIVANQVEYNLFDREEESgLLPYCQKNGIAIIAYSPLEKGKLsnAKGSPLLDEIAKKYGKTPAQIALNWLISK-PNVI 232
|
250 260 270
....*....|....*....|....*....|.
gi 19113480 257 PIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19072 233 AIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
25-273 |
5.99e-57 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 183.45 E-value: 5.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDgiWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALypyKG----LIIATKGGLVR 100
Cdd:cd19086 3 VSEIGFGTWGLGGD--WWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKAL---KGrrdkVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQ-FSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQ 179
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDElFEALEKLKQEGKIRAYGVSVGDPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 180 YFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALAkpGTIldavskdldrstSQIALSWVLQRSPVMLPI 258
Cdd:cd19086 158 RGGIDVVQVIYNLLDQRPEEeLFPLAEEHGVGVIARVPLASGLLT--GKL------------AQAALRFILSHPAVSTVI 223
|
250
....*....|....*
gi 19113480 259 PGTSKVDHLEENVKA 273
Cdd:cd19086 224 PGARSPEQVEENAAA 238
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
17-287 |
1.90e-56 |
|
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: 184.54 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 17 TVKVG--DMVVNRMGFGAMRVTGDGIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYK--GLII 92
Cdd:cd19083 1 KVKLGksDIDVNPIGLGTNAVGGHNLYPNLDEEEG-KDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNrnEVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 93 ATKGGLvRTGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVD 172
Cdd:cd19083 80 ATKGAH-KFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 173 DIKEAEQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA-----------------KPGTILDAVSK 234
Cdd:cd19083 159 QLKEANKDGYVDVLQGEYNLLQREAEEdILPYCVENNISFIPYFPLASGLLAgkytkdtkfpdndlrndKPLFKGERFSE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113480 235 DLDR-------------STSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19083 239 NLDKvdklksiadekgvTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFID 304
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
25-292 |
3.51e-53 |
|
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: 175.47 E-value: 3.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIWdEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALypyKG----LIIATKGGLVR 100
Cdd:cd19085 1 VSRLGLGCWQFGGGYWW-GDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKAL---KGrrddVVIATKVSPDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEwhpcgapkfLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQY 180
Cdd:cd19085 77 LTPED---------VRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 FPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA----------------------KPGTI--------- 228
Cdd:cd19085 148 GRIDSNQLPYNLLWRAIEYeILPFCREHGIGVLAYSPLAQGLLTgkfssaedfppgdartrlfrhfEPGAEeetfealek 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113480 229 LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEEGKS 292
Cdd:cd19085 228 LKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-288 |
3.63e-52 |
|
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: 173.24 E-value: 3.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDG--IWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALypyKGL----IIATKGGLVR 100
Cdd:cd19102 3 TIGLGTWAIGGGGwgGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRAL---KGLrdrpIVATKCGLLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQY 180
Cdd:cd19102 80 DEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 FPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA---KPGTI---------------------------- 228
Cdd:cd19102 160 HPIASLQPPYSLLRRGIEAeILPFCAEHGIGVIVYSPMQSGLLTgkmTPERVaslpaddwrrrspffqepnlarnlalvd 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113480 229 -LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19102 240 aLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEA 300
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
18-281 |
6.60e-52 |
|
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: 172.77 E-value: 6.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 18 VKVG--DMVVNRMGFGAMR--VTGDGIWDEpkDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG---L 90
Cdd:cd19079 3 VRLGnsGLKVSRLCLGCMSfgDPKWRPWVL--DEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPrdeV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 91 IIATKGGL-VRTGPNewhPCG-APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSE 168
Cdd:cd19079 81 VIATKVYFpMGDGPN---GRGlSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 169 ------VTVDDIKEAEQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALAKP---------------- 225
Cdd:cd19079 158 myawqfAKALHLAEKNGWTKFVSMQNHYNLLYREEEReMIPLCEEEGIGVIPWSPLARGRLARPwgdtterrrsttdtak 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113480 226 ----------GTILDAV---SKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19079 238 lkydyfteadKEIVDRVeevAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEE 306
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
25-287 |
8.39e-51 |
|
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: 169.73 E-value: 8.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGdgiWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSEN---LLREAL--YP--YKGLIIATKGG 97
Cdd:cd19077 5 VGPIGLGLMGLTW---RPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFrkYPeyADKVVLSVKGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 98 LVRTGpneWHPCGAPKFLRQEVLMSMRRLG-VKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKE 176
Cdd:cd19077 82 LDPDT---LRPDGSPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 177 AEQYFPVVSVQNLFNLVNRKNEK--VLEYCEQKGIAFIPWYPLA----SGALAKPGTI-LDAVSKDLDR----------- 238
Cdd:cd19077 159 AHAVHPIAAVEVEYSLFSREIEEngVLETCAELGIPIIAYSPLGrgllTGRIKSLADIpEGDFRRHLDRfngenfeknlk 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113480 239 --------------STSQIALSWVLQRS-PVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19077 239 lvdalqelaekkgcTPAQLALAWILAQSgPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
22-287 |
6.56e-47 |
|
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: 159.69 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 22 DMVVNRMGFGAMrVTGDGIwdepkDKEACIATLKRLPELNINFIDTADSYGPEV-------SENLLREALYPYKG---LI 91
Cdd:cd19081 6 GLSVSPLCLGTM-VFGWTA-----DEETSFALLDAFVDAGGNFIDTADVYSAWVpgnaggeSETIIGRWLKSRGKrdrVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 92 IATKGGLvRTGPNewHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTV 171
Cdd:cd19081 80 IATKVGF-PMGPN--GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 172 DDIKEAEQ------YFPVVSVQNLFNLVNRKN-EK-VLEYCEQKGIAFIPWYPLASGAL-------AKPG---------- 226
Cdd:cd19081 157 WRLQEALElsrqhgLPRYVSLQPEYNLVDRESfEGeLLPLCREEGIGVIPYSPLAGGFLtgkyrseADLPgstrrgeaak 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113480 227 -----------TILDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19081 237 rylnerglrilDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-281 |
1.94e-46 |
|
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: 158.98 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 17 TVKVG--DMVVNRMGFGAMRVtGDGIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALypyKGL---- 90
Cdd:cd19149 1 YRKLGksGIEASVIGLGTWAI-GGGPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAI---KGRrdkv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 91 IIATKGGLV--RTGPNEWHP--------CGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGL 160
Cdd:cd19149 77 VLATKCGLRwdREGGSFFFVrdgvtvykNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 161 IRHVGLSEVTVDDIKEAEQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGAL---AKPGTILDA----- 231
Cdd:cd19149 157 IRAIGASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKeLLPYCKKNNIAFQAYSPLEQGLLtgkITPDREFDAgdars 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113480 232 ------------VSKDLDR----------STSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19149 237 gipwfspenrekVLALLEKwkplcekygcTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAE 308
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
25-287 |
2.82e-46 |
|
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: 157.77 E-value: 2.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVtGDGIWDEPKD--KEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG---LIIATKgglv 99
Cdd:cd19093 2 VSPLGLGTWQW-GDRLWWGYGEygDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDrdeVVIATK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 100 rtgpneWHPcgAPKFLRQEVLM-----SMRRLGVKQIDLWQLHRIDPKVPRKDQFSE-IAAMKKEGLIRHVGLSEVTVDD 173
Cdd:cd19093 77 ------FAP--LPWRLTRRSVVkalkaSLERLGLDSIDLYQLHWPGPWYSQIEALMDgLADAVEEGLVRAVGVSNYSADQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 174 IKEAEQYF-----PVVSVQNLFNLVNRKNEK--VLEYCEQKGIAFIPWYPLASGALA--------KPGTI---------- 228
Cdd:cd19093 149 LRRAHKALkergvPLASNQVEYSLLYRDPEQngLLPACDELGITLIAYSPLAQGLLTgkyspenpPPGGRrrlfgrknle 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113480 229 --------LDAVSKDLDRSTSQIALSWVLQRSPVmlPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19093 229 kvqplldaLEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
19-281 |
1.24e-45 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 156.83 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 19 KVGDMVvNRMGFGAMRVTGdgIWDEPKDKEACIATLKRLPELNINFIDTADSYGPevSENLL----------REALYpyk 88
Cdd:cd19144 8 RNGPSV-PALGFGAMGLSA--FYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD--SEELIgrwfkqnpgkREKIF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 89 gliIATKGGLVRTGPN-EWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLS 167
Cdd:cd19144 80 ---LATKFGIEKNVETgEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 168 EVTVDDIKEAEQYFPVVSVQ---NLFNL-VNRKNEKVLEYCEQKGIAFIPWYPLASGALAkpGTI--------------- 228
Cdd:cd19144 157 ECSAETLRRAHAVHPIAAVQieySPFSLdIERPEIGVLDTCRELGVAIVAYSPLGRGFLT--GAIrspddfeegdfrrma 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 229 -----------------LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19144 235 prfqaenfpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEE 304
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-286 |
1.36e-45 |
|
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: 156.44 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 16 GTVKVGD--MVVNRMGFGAMRVTGDgiWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALypyKGLI-- 91
Cdd:cd19145 1 PRVKLGSqgLEVSAQGLGCMGLSGD--YGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKAL---KDGPre 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 92 ---IATKGGLVRTGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSE 168
Cdd:cd19145 76 kvqLATKFGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 169 VTVDDIKEAEQYFPVVSVQNLFNLVNRK-NEKVLEYCEQKGIAFIPWYPLASGALA-KPGTI------------------ 228
Cdd:cd19145 156 ASADTIRRAHAVHPITAVQLEWSLWTRDiEEEIIPTCRELGIGIVPYSPLGRGFFAgKAKLEellensdvrkshprfqge 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113480 229 -----------LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKL 286
Cdd:cd19145 236 nleknkvlyerVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
25-282 |
1.47e-42 |
|
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: 148.12 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIwdepkDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKG-GLVRT 101
Cdd:cd19074 4 VSELSLGTWLTFGGQV-----DDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALkgWPRESYVISTKVfWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 102 GPNEWhpcG-APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEA--- 177
Cdd:cd19074 79 GPNDR---GlSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAhdl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 178 ---EQYFPVVSVQNLFNLVNRKNE-KVLEYCEQKGIAFIPWYPLASGALA---KPGTILD-------------------- 230
Cdd:cd19074 156 arqFGLIPPVVEQPQYNMLWREIEeEVIPLCEKNGIGLVVWSPLAQGLLTgkyRDGIPPPsrsratdednrdkkrrlltd 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113480 231 ----------AVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEV 282
Cdd:cd19074 236 enlekvkklkPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPEV 297
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
29-274 |
9.13e-42 |
|
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: 145.01 E-value: 9.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 29 GFGAMRVTGdgIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKGGLvrtgpneW 106
Cdd:cd19096 4 GFGTMRLPE--SDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALkeGPREKFYLATKLPP-------W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 107 HPCGAPKFlRQEVLMSMRRLGVKQIDLWQLH-----RIDPKVPRKDQFSEIAAMKKEGLIRHVGLS-EVTVDDIKEAEQY 180
Cdd:cd19096 75 SVKSAEDF-RRILEESLKRLGVDYIDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFSfHDSPELLKEILDS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 FPVVSVQ---NLFNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGTILDAVSKDLDRSTSQIALSWVLQRSPVMLP 257
Cdd:cd19096 154 YDFDFVQlqyNYLDQENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTV 233
|
250
....*....|....*..
gi 19113480 258 IPGTSKVDHLEENVKAA 274
Cdd:cd19096 234 LSGMSTPEQLDENIAAA 250
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
25-288 |
9.47e-40 |
|
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: 141.17 E-value: 9.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDgiwdepKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALypyKG----LIIATKGGlVR 100
Cdd:cd19087 13 VSRLCLGTMNFGGR------TDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWI---AGrrddIVLATKVF-GP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPrkdqFSEI-AAMK---KEGLIRHVGLSE------VT 170
Cdd:cd19087 83 MGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTP----LEETlRALDdlvRQGKIRYIGVSNfaawqiAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 171 VDDIKEAEQYFPVVSVQNLFNLVNRKNE-KVLEYCEQKGIAFIPWYPLASGAL----------------------AKPGT 227
Cdd:cd19087 159 AQGIAARRGLLRFVSEQPMYNLLKRQAElEILPAARAYGLGVIPYSPLAGGLLtgkygkgkrpesgrlveraryqARYGL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113480 228 I--------LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19087 239 EeyrdiaerFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-281 |
1.02e-39 |
|
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: 140.38 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 21 GDMVVNRMGFGAMRvtgdgIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKGL----IIATKG 96
Cdd:cd19092 2 EGLEVSRLVLGCMR-----LADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLrekiEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 97 GLVRTGPNEWHPCG----APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVprkdQFSEIA----AMKKEGLIRHVGLSE 168
Cdd:cd19092 77 GIRLGDDPRPGRIKhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLM----DPEEVAeafdELVKSGKVRYFGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 169 VTVDDIKEAEQY--FPVVSVQNLFNLVNRKNEK--VLEYCEQKGIAFIPWYPLASGALAKPGT--------ILDAVSKDL 236
Cdd:cd19092 153 FTPSQIELLQSYldQPLVTNQIELSLLHTEAIDdgTLDYCQLLDITPMAWSPLGGGRLFGGFDerfqrlraALEELAEEY 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19113480 237 DRSTSQIALSWVLqRSPV-MLPIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19092 233 GVTIEAIALAWLL-RHPArIQPILGTTNPERIRSAVKALDIELTRE 277
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
24-288 |
1.54e-39 |
|
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: 140.83 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 24 VVNRMGFGAMRVTGDGIWDEPK---DKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG-LIIATKGGLv 99
Cdd:cd19091 12 KVSELALGTMTFGGGGGFFGAWggvDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRDdVLIATKVRG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 100 RTG--PNEwhpCGAPKF-LRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEV------T 170
Cdd:cd19091 91 RMGegPND---VGLSRHhIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFsawqimK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 171 VDDIKEAEQYFPVVSVQNLFNLVNRKNE-KVLEYCEQKGIAFIPWYPLASGAL---------AKPGTI------------ 228
Cdd:cd19091 168 ALGISERRGLARFVALQAYYSLLGRDLEhELMPLALDQGVGLLVWSPLAGGLLsgkyrrgqpAPEGSRlrrtgfdfppvd 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 229 ----------LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19091 248 rergydvvdaLREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDK 317
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
28-287 |
1.72e-39 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 139.24 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 28 MGFGAMRVTGDGIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKgglvrtgpnE 105
Cdd:cd19137 7 LGLGTWGIGGFLTPDYSRDEEM-VELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIkdFPREDLFIVTK---------V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 106 WhpcgaPKFLRQEVLM-----SMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQY 180
Cdd:cd19137 77 W-----PTNLRYDDLLrslqnSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 F--PVVSVQNLFNLVNRKNEK--VLEYCEQKGIAFIPWYPLASGALAKPGTiLDAVSKDLDRSTSQIALSWVLQRsPVML 256
Cdd:cd19137 152 SqtPIVCNQVKYNLEDRDPERdgLLEYCQKNGITVVAYSPLRRGLEKTNRT-LEEIAKNYGKTIAQIALAWLIQK-PNVV 229
|
250 260 270
....*....|....*....|....*....|.
gi 19113480 257 PIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19137 230 AIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
19-291 |
1.90e-38 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 139.18 E-value: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 19 KVGDMVvNRMGFGAMRVTGdgiwdepKDKEACIATLKRLPELNINFIDTADSYGPevSENLLREAL-YPYKGLIIATKgg 97
Cdd:COG1453 8 KTGLEV-SVLGFGGMRLPR-------KDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALkGPRDKVILATK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 98 lvrTGPNEWHPCGAPKFLRQevlmSMRRLGVKQIDLWQLHRID-----PKVPRKDQFSEIA-AMKKEGLIRHVGLS-EVT 170
Cdd:COG1453 76 ---LPPWVRDPEDMRKDLEE----SLKRLQTDYIDLYLIHGLNteedlEKVLKPGGALEALeKAKAEGKIRHIGFStHGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 171 VDDIKEA-EQY-FPVVSVQnlFNLVNRKN---EKVLEYCEQKGIAFIPWYPLASGALAKPgtiLDAVSKDLD--RSTSQI 243
Cdd:COG1453 149 LEVIKEAiDTGdFDFVQLQ--YNYLDQDNqagEEALEAAAEKGIGVIIMKPLKGGRLANP---PEKLVELLCppLSPAEW 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19113480 244 ALSWVLQRSPVMLPIPGTSKVDHLEENVKAA--GIQLSSEVFAKLDEEGK 291
Cdd:COG1453 224 ALRFLLSHPEVTTVLSGMSTPEQLDENLKTAdnLEPLTEEELAILERLAE 273
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
32-287 |
7.86e-38 |
|
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: 135.07 E-value: 7.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 32 AMRVTGDGIW---DEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKGLII---------ATKGGLV 99
Cdd:cd19138 10 KVPALGQGTWymgEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFlvskvlpsnASRQGTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 100 RTGPNewhpcgapkflrqevlmSMRRLGVKQIDLWQLH-RIDpkVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAE 178
Cdd:cd19138 90 RACER-----------------SLRRLGTDYLDLYLLHwRGG--VPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 QYF---PVVSVQNLFNLVNRKNE-KVLEYCEQKGIAFIPWYPLASGALAKPGTI----LDAVSKDLDRSTSQIALSWVLq 250
Cdd:cd19138 151 AVPgggNCAANQVLYNLGSRGIEyDLLPWCREHGVPVMAYSPLAQGGLLRRGLLenptLKEIAARHGATPAQVALAWVL- 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 19113480 251 RSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19138 230 RDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
27-273 |
1.53e-37 |
|
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: 133.90 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDgiWDEPkDKEACIATLKRLPELNINFIDTADSYGPevSENLLREALypyKGL-----IIATKGGLVRT 101
Cdd:cd19095 2 VLGLGTSGIGRV--WGVP-SEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRAL---AGLrrddlFIATKVGTHGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 102 GPNEWHpCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLS--EVTVDDIKEAEQ 179
Cdd:cd19095 74 GGRDRK-DFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSgdGEELEAAIASGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 180 yFPVVSVQnlFNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAK--PGTILDAVSKDLDR--------STSQIALSWVL 249
Cdd:cd19095 153 -FDVVQLP--YNVLDREEEELLPLAAEAGLGVIVNRPLANGRLRRrvRRRPLYADYARRPEfaaeiggaTWAQAALRFVL 229
|
250 260
....*....|....*....|....
gi 19113480 250 QRSPVMLPIPGTSKVDHLEENVKA 273
Cdd:cd19095 230 SHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
27-287 |
8.33e-36 |
|
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: 129.14 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDgiwdepKDKEACIATLK---RLpelninfIDTADSYG--PEVSEnLLREALYPYKGLIIATKgglVrt 101
Cdd:cd19071 3 LIGLGTYKLKPE------ETAEAVLAALEagyRH-------IDTAAAYGneAEVGE-AIRESGVPREELFITTK---L-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 102 gpneWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH------RIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIK 175
Cdd:cd19071 64 ----WPTDHGYERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 176 EAEQYF---PVVsVQNLFNLVNRkNEKVLEYCEQKGIAFIPWYPLASGA---LAKPgtILDAVSKDLDRSTSQIALSWVL 249
Cdd:cd19071 140 ELLAAArikPAV-NQIELHPYLQ-QKELVEFCKEHGIVVQAYSPLGRGRrplLDDP--VLKEIAKKYGKTPAQVLLRWAL 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 19113480 250 QRSpvMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19071 216 QRG--VVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
27-287 |
2.38e-34 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 125.55 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDgiwdepkdkeACIATLKRLPELNINFIDTADSYG--PEVSEnLLREALYPYKGLIIATKgglVrtgPN 104
Cdd:COG0656 7 ALGLGTWQLPGE----------EAAAAVRTALEAGYRHIDTAAMYGneEGVGE-AIAASGVPREELFVTTK---V---WN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 105 EWHpcGAPKFLR--QEvlmSMRRLGVKQIDLWQLHRidpkvPRKDQFSE-IAAM---KKEGLIRHVGLSEVTVDDIKEAE 178
Cdd:COG0656 70 DNH--GYDDTLAafEE---SLERLGLDYLDLYLIHW-----PGPGPYVEtWRALeelYEEGLIRAIGVSNFDPEHLEELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 QY---FPVVsVQNLFNLVNRkNEKVLEYCEQKGIAFIPWYPLASGALAK-PgtILDAVSKDLDRSTSQIALSWVLQRSpv 254
Cdd:COG0656 140 AEtgvKPAV-NQVELHPYLQ-QRELLAFCREHGIVVEAYSPLGRGKLLDdP--VLAEIAEKHGKTPAQVVLRWHLQRG-- 213
|
250 260 270
....*....|....*....|....*....|...
gi 19113480 255 MLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:COG0656 214 VVVIPKSVTPERIRENLDAFDFELSDEDMAAID 246
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-272 |
3.20e-34 |
|
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: 124.52 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGamrvtgdGIWDEPKDKEACIATLKRLPELNINFIDTADSYGpeVSENLLREALYPY-KGLIIATKGGlVRTgp 103
Cdd:cd19100 11 VSRLGFG-------GGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYG--DSEEKIGKALKGRrDKVFLATKTG-ARD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 newhpcgaPKFLRQEVLMSMRRLGVKQIDLWQLHRIDpkvpRKDQFSEIAA----------MKKEGLIRHVGLSEVTVDD 173
Cdd:cd19100 79 --------YEGAKRDLERSLKRLGTDYIDLYQLHAVD----TEEDLDQVFGpggalealleAKEEGKIRFIGISGHSPEV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 174 IKEAEQYFPVVSVQNLFNLVNRKN----EKVLEYCEQKGIAFIPWYPLASGALAKPgtildavskdlDRSTSQIALSWVL 249
Cdd:cd19100 147 LLRALETGEFDVVLFPINPAGDHIdsfrEELLPLAREKGVGVIAMKVLAGGRLLSG-----------DPLDPEQALRYAL 215
|
250 260
....*....|....*....|...
gi 19113480 250 QRSPVMLPIPGTSKVDHLEENVK 272
Cdd:cd19100 216 SLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
28-287 |
6.64e-34 |
|
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: 125.79 E-value: 6.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 28 MGFGAMRVTGdgiwdepKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG-LIIATKGGLVRTGPNEw 106
Cdd:cd19080 18 MTFGTEWGWG-------ADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDrIVLATKYTMNRRPGDP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 107 HPCG-APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEV------TVDDIKEAEQ 179
Cdd:cd19080 90 NAGGnHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTpawvvaRANTLAELRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 180 YFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGAL-----------------AKPGT------------IL 229
Cdd:cd19080 170 WSPFVALQIEYSLLERTPEReLLPMARALGLGVTPWSPLGGGLLtgkyqrgeegrageakgVTVGFgklternwaivdVV 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113480 230 DAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19080 250 AAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
59-274 |
2.86e-33 |
|
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: 123.43 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 59 ELNINFIDTADSYG----PEVSENLLREALYPYKG---LIIATKGGLvrtgPNEWHPCGA---PKFLRQEVLMSMRRLGV 128
Cdd:cd19082 28 ELGGNFIDTARVYGdwveRGASERVIGEWLKSRGNrdkVVIATKGGH----PDLEDMSRSrlsPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 129 KQIDLWQLHRIDPKVPrkdqFSEI----AAMKKEGLIRHVGLSEVTVDDIKEAEQY------FPVVSVQNLFNLVNRK-- 196
Cdd:cd19082 104 DYIDLYFLHRDDPSVP----VGEIvdtlNELVRAGKIRAFGASNWSTERIAEANAYakahglPGFAASSPQWSLARPNep 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 197 ----------NEKVLEYCEQKGIAFIPWYPLASGALAKPGT-----------------------ILDAVSKDLDRSTSQI 243
Cdd:cd19082 180 pwpgptlvamDEEMRAWHEENQLPVFAYSSQARGFFSKRAAggaeddselrrvyyseenferleRAKELAEEKGVSPTQI 259
|
250 260 270
....*....|....*....|....*....|.
gi 19113480 244 ALSWVLQRSPVMLPIPGTSKVDHLEENVKAA 274
Cdd:cd19082 260 ALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-274 |
3.83e-33 |
|
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: 122.31 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRvtgdgiwdepkDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKgglVRTG 102
Cdd:cd19105 13 VSRLGFGGGG-----------LPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALkgLRRDKVFLATK---ASPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 103 PNEWhpcgAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPkvPRKDQFSE--IAAM---KKEGLIRHVGLSE--VTVDDIK 175
Cdd:cd19105 79 LDKK----DKAELLKSVEESLKRLQTDYIDIYQLHGVDT--PEERLLNEelLEALeklKKEGKVRFIGFSThdNMAEVLQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 176 EA--EQYFPVVSVQnlFNLVNRKNE--KVLEYCEQKGIAFIPWYPLASGALAKpgtILDAVSKDLDRSTSQIALSWVLQR 251
Cdd:cd19105 153 AAieSGWFDVIMVA--YNFLNQPAEleEALAAAAEKGIGVVAMKTLAGGYLQP---ALLSVLKAKGFSLPQAALKWVLSN 227
|
250 260
....*....|....*....|...
gi 19113480 252 SPVMLPIPGTSKVDHLEENVKAA 274
Cdd:cd19105 228 PRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
22-287 |
3.97e-33 |
|
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: 123.57 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 22 DMVVNRMGFGAMRVTGDgIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG---LIIATKGGL 98
Cdd:cd19148 1 DLPVSRIALGTWAIGGW-MWGGTDEKEA-IETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKrdrVVIATKVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 99 vrtgpnEWHPCG------APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPrkdqFSEIA-AMKK---EGLIRHVGLSE 168
Cdd:cd19148 79 ------EWDEGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVP----IEETAeALKElldEGKIRAIGVSN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 169 VTVDDIKEAEQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGAL----------------------AKP 225
Cdd:cd19148 149 FSPEQMETFRKVAPLHTVQPPYNLFEREIEKdVLPYARKHNIVTLAYGALCRGLLsgkmtkdtkfegddlrrtdpkfQEP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113480 226 --GTILDAVSKdLD--------RSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19148 229 rfSQYLAAVEE-LDklaqerygKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
29-287 |
1.98e-32 |
|
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: 120.07 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 29 GFGAMRVTGDgiwdepkdkeACIATLKRLPELNINFIDTADSYG--PEVSENLlREALYPYKGLIIATKgglvrtgpnEW 106
Cdd:cd19073 5 GLGTWQLRGD----------DCANAVKEALELGYRHIDTAEIYNneAEVGEAI-AESGVPREDLFITTK---------VW 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 107 HPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYFPVVSV 186
Cdd:cd19073 65 RDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 187 QNLFN----LVNRkneKVLEYCEQKGIAFIPWYPLASGALAKPGTILDaVSKDLDRSTSQIALSWVLQRSpvMLPIPGTS 262
Cdd:cd19073 145 VNQVEfhpfLYQA---ELLEYCRENDIVITAYSPLARGEVLRDPVIQE-IAEKYDKTPAQVALRWLVQKG--IVVIPKAS 218
|
250 260
....*....|....*....|....*
gi 19113480 263 KVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19073 219 SEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
27-283 |
8.14e-31 |
|
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: 116.88 E-value: 8.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGdgIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPevSENLLREAL--YPYKGLIIATKGGlvrtgpn 104
Cdd:cd19090 2 ALGLGTAGLGG--VFGGVDDDEA-VATIRAALDLGINYIDTAPAYGD--SEERLGLALaeLPREPLVLSTKVG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 105 eWHPCGAPKF----LRQEVLMSMRRLGVKQIDLWQLHriDPKVPRKDQ-------FSEIAAMKKEGLIRHVGLSEVTVDD 173
Cdd:cd19090 70 -RLPEDTADYsadrVRRSVEESLERLGRDRIDLLMIH--DPERVPWVDilapggaLEALLELKEEGLIKHIGLGGGPPDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 174 IKEA--EQYFPVVSVQNLFNLVNRKN-EKVLEYCEQKGIAFIPWYPLASGALAK---------PGTILD----------A 231
Cdd:cd19090 147 LRRAieTGDFDVVLTANRYTLLDQSAaDELLPAAARHGVGVINASPLGMGLLAGrppervrytYRWLSPelldrakrlyE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19113480 232 VSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVF 283
Cdd:cd19090 227 LCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
30-288 |
3.44e-30 |
|
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: 115.73 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 30 FGAMRVTGDGiwdEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKGLIIATKgglVRTGpneWHPC 109
Cdd:cd19075 5 LGTMTFGSQG---RFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERGFKIDTK---ANPG---VGGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 110 GAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKE-----AEQYFPVV 184
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEiveicKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 185 SV-QNLFNLVNRKNE-KVLEYCEQKGIAFIPWYPLASGALAKPGT----------------------------------- 227
Cdd:cd19075 156 TVyQGMYNAITRQVEtELFPCLRKLGIRFYAYSPLAGGFLTGKYKysedkagggrfdpnnalgklyrdrywkpsyfeale 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113480 228 ILDAVSKDLDRSTSQIALSWVLQRSPVMLP-----IPGTSKVDHLEENVKA--AGiQLSSEVFAKLDE 288
Cdd:cd19075 236 KVEEAAEKEGISLAEAALRWLYHHSALDGEkgdgvILGASSLEQLEENLAAleKG-PLPEEVVKAIDE 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-275 |
1.57e-29 |
|
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: 113.58 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 46 DKEACIATLKRLPELNINFIDTADSY--------GPEvSENLLREALYPYKG---LIIATKGGLVRTGPNEWH--PCG-A 111
Cdd:cd19752 15 DEETSFAILDRYVAAGGNFLDTANNYafwteggvGGE-SERLIGRWLKDRGNrddVVIATKVGAGPRDPDGGPesPEGlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 112 PKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTV------DDIKEAEQYFPVVS 185
Cdd:cd19752 94 AETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAwrleraRQIARQQGWAEFSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 186 VQNLFNLVNRK-----------NEKVLEYCEQKG-IAFIPWYPLASGALAKPG----------------TILDAVSKDLD 237
Cdd:cd19752 174 IQQRHSYLRPRpgadfgvqrivTDELLDYASSRPdLTLLAYSPLLSGAYTRPDrplpeqydgpdsdarlAVLEEVAGELG 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 19113480 238 RSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAG 275
Cdd:cd19752 254 ATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
39-274 |
3.86e-29 |
|
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: 113.12 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 39 GIWDEPKDK---EACIATLKRLPELNINFIDTADSYGP------EVSENLLREALYPYKG-LIIATKGGLvRTGPNEWHP 108
Cdd:cd19089 17 GLWHNFGDYtspEEARELLRTAFDLGITHFDLANNYGPppgsaeENFGRILKRDLRPYRDeLVISTKAGY-GMWPGPYGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 109 CGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEA-----EQYFPV 183
Cdd:cd19089 96 GGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAiallrELGVPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 184 VSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA--------------------KPGTI----------LDAV 232
Cdd:cd19089 176 IIHQPRYSLLDRWAEDgLLEVLEEAGIGFIAFSPLAQGLLTdkylngippdsrraaeskflTEEALtpekleqlrkLNKI 255
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19113480 233 SKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAA 274
Cdd:cd19089 256 AAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
25-288 |
6.07e-29 |
|
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: 113.04 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRvtgdgiWDEPKDKEACIATLKRLPELNINFIDTADSYG-PEVSE----------NLLREalypyKG---- 89
Cdd:cd19094 1 VSEICLGTMT------WGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvPPSPEtqgrteeiigSWLKK-----KGnrdk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 90 LIIATK--GglvRTGPNEWHPCGAPKFLRQEVLM----SMRRLGVKQIDLWQLH---RIDP---------------KVPR 145
Cdd:cd19094 70 VVLATKvaG---PGEGITWPRGGGTRLDRENIREavegSLKRLGTDYIDLYQLHwpdRYTPlfgggyytepseeedSVSF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 146 KDQFSEIAAMKKEGLIRHVGLSEVT----VDDIKEAEQ--YFPVVSVQNLFNLVNRKNEKVL-EYCEQKGIAFIPWYPLA 218
Cdd:cd19094 147 EEQLEALGELVKAGKIRHIGLSNETpwgvMKFLELAEQlgLPRIVSIQNPYSLLNRNFEEGLaEACHRENVGLLAYSPLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 219 SGAL---------AKPGTILD----------------------AVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHL 267
Cdd:cd19094 227 GGVLtgkyldgaaRPEGGRLNlfpgymaryrspqaleavaeyvKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQL 306
|
330 340
....*....|....*....|.
gi 19113480 268 EENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19094 307 KENIDAFDVPLSDELLAEIDA 327
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
18-288 |
9.80e-29 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 110.81 E-value: 9.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 18 VKVGDMVVNRMGFGAMRVTGdgiwdepkdkEACIATLKRLPELNINFIDTADSYGPE--VSENLlREALYPYKGLIIATK 95
Cdd:cd19140 1 VTVNGVRIPALGLGTYPLTG----------EECTRAVEHALELGYRHIDTAQMYGNEaqVGEAI-AASGVPRDELFLTTK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 96 gglvrtgpnEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIK 175
Cdd:cd19140 70 ---------VWPDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 176 EAEQY--FPVVSVQNLFN--LVNRkneKVLEYCEQKGIAFIPWYPLASGALAKPGTILDaVSKDLDRSTSQIALSWVLQR 251
Cdd:cd19140 141 EAVELseAPLFTNQVEYHpyLDQR---KLLDAAREHGIALTAYSPLARGEVLKDPVLQE-IGRKHGKTPAQVALRWLLQQ 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 19113480 252 SPVMLpIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19140 217 EGVAA-IPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-288 |
5.54e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 110.05 E-value: 5.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGdgIWDEPKDKEaCIATLKRLPELNINFIDTADSYGPEVSENLLREAL-YPYKGLIIATKGGLVRTGP 103
Cdd:cd19104 12 VSELTFGGGGIGG--LMGRTTREE-QIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALkGLPAGPYITTKVRLDPDDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEwhpcgAPKFLRQEVLMSMRRLGVKQIDLWQLH-RI---DPKVPRK-------DQFSEIAA----MKKEGLIRHVGLSE 168
Cdd:cd19104 89 GD-----IGGQIERSVEKSLKRLKRDSVDLLQLHnRIgdeRDKPVGGtlsttdvLGLGGVADaferLRSEGKIRFIGITG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 169 V-TVDDIKEAEQYFPVVSVQNLFNLVN-------------RKNEKVLEYCEQKGIAFIPWYPLASGALAK--------PG 226
Cdd:cd19104 164 LgNPPAIRELLDSGKFDAVQVYYNLLNpsaaearprgwsaQDYGGIIDAAAEHGVGVMGIRVLAAGALTTsldrgreaPP 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113480 227 TILDAVSKDLDR-------------STSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGI-QLSSEVFAKLDE 288
Cdd:cd19104 244 TSDSDVAIDFRRaaafralarewgeTLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAgPLPAENLARLEA 319
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
59-291 |
6.97e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 109.35 E-value: 6.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 59 ELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATK--GGLVRTGPNEwhpcgapkfLRQEVLMSMRRLGVKQIDLW 134
Cdd:cd19103 43 AAGLNLWDTAAVYGMGASEKILGEFLkrYPREDYIISTKftPQIAGQSADP---------VADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 135 QLHriDP-KVPRkdQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQY-----FPVVSVQNLFNLVNRKNEK--VLEYCEQ 206
Cdd:cd19103 114 WIH--NPaDVER--WTPELIPLLKSGKVKHVGVSNHNLAEIKRANEIlakagVSLSAVQNHYSLLYRSSEEagILDYCKE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 207 KGIAFIPWYPLASGALAKPGT---------------------------ILDAVSKDLDRSTSQIALSWVLQRSpvMLPIP 259
Cdd:cd19103 190 NGITFFAYMVLEQGALSGKYDtkhplpegsgraetynpllpqleeltaVMAEIGAKHGASIAQVAIAWAIAKG--TTPII 267
|
250 260 270
....*....|....*....|....*....|..
gi 19113480 260 GTSKVDHLEENVKAAGIQLSSEVFAKLDEEGK 291
Cdd:cd19103 268 GVTKPHHVEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
48-273 |
5.30e-26 |
|
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: 104.79 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 48 EACIATLKRLPELNINFIDTADSYGPEV---SEN---LLREALYPYKG-LIIATKGGLVR-TGP-NEWhpcGAPKFLRQE 118
Cdd:cd19151 30 ENSRAMLRRAFDLGITHFDLANNYGPPPgsaEENfgrILKEDLKPYRDeLIISTKAGYTMwPGPyGDW---GSKKYLIAS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 119 VLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYF-----PVVSVQNLFNLV 193
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILkdlgtPCLIHQPKYSMF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 194 NRKNEK-VLEYCEQKGIAFIPWYPLASGAL--------------AKPGTI----------------LDAVSKDLDRSTSQ 242
Cdd:cd19151 187 NRWVEEgLLDVLEEEGIGCIAFSPLAQGLLtdrylngipedsraAKGSSFlkpeqiteeklakvrrLNEIAQARGQKLAQ 266
|
250 260 270
....*....|....*....|....*....|.
gi 19113480 243 IALSWVLQRSPVMLPIPGTSKVDHLEENVKA 273
Cdd:cd19151 267 MALAWVLRNKRVTSVLIGASKPSQIEDAVGA 297
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
52-287 |
1.09e-25 |
|
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: 102.79 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 52 ATLKRLPELNINFIDTADSYGPEVSENL-LREALYPYKGLIIATKgglvrtgpnEWHP-CGAPKfLRQEVLMSMRRLGVK 129
Cdd:cd19135 30 AVVYALKECGYRHIDTAKRYGCEELLGKaIKESGVPREDLFLTTK---------LWPSdYGYES-TKQAFEASLKRLGVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 130 QIDLWQLHRIDPKVPRKDQFSEIA----AMK---KEGLIRHVGLSEVTVDDIKEAEQYFPVVSV--QNLFNLVNRKnEKV 200
Cdd:cd19135 100 YLDLYLLHWPDCPSSGKNVKETRAetwrALEelyDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHvnQVEFHPFQNP-VEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 201 LEYCEQKGIAFIPWYPLASG-ALAKPgtILDAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLS 279
Cdd:cd19135 179 IEYCRDNNIVFEGYCPLAKGkALEEP--TVTELAKKYQKTPAQILIRWSIQNGVVT--IPKSTKEERIKENCQVFDFSLS 254
|
....*...
gi 19113480 280 SEVFAKLD 287
Cdd:cd19135 255 EEDMATLD 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
27-291 |
2.68e-25 |
|
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: 101.93 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGamrvTGDGIWDEPKDK--EACIATLKRLPELNINFIDTADSYGPEVS-ENLLREALYPYKGLIIATKgglvrTGP 103
Cdd:cd19120 6 AIAFG----TGTAWYKSGDDDiqRDLVDSVKLALKAGFRHIDTAEMYGNEKEvGEALKESGVPREDLFITTK-----VSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEWHPCGApkfLRQevlmSMRRLGVKQIDLWQLH---RIDPKVPRKDQF-SEIAAMKKEGLIRHVGLSEVTVDDIKE--- 176
Cdd:cd19120 77 GIKDPREA---LRK----SLAKLGVDYVDLYLIHspfFAKEGGPTLAEAwAELEALKDAGLVRSIGVSNFRIEDLEElld 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 177 AEQYFPVVSvQNLFN-LVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPG---TILDAVSKDLDRSTSQIALSWVLQRS 252
Cdd:cd19120 150 TAKIKPAVN-QIEFHpYLYPQQPALLEYCREHGIVVSAYSPLSPLTRDAGGpldPVLEKIAEKYGVTPAQVLLRWALQKG 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 19113480 253 PVmlPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEEGK 291
Cdd:cd19120 229 IV--VVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGK 265
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-288 |
2.74e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 102.67 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 45 KDKEACIATLKRLPELNINFIDTADSYGPevSENLLREALYPYKG-------LIIATKggLVrTGPNEWHPcgAPKFLRQ 117
Cdd:cd19101 20 RDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRRerdaaddVQIHTK--WV-PDPGELTM--TRAYVEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 118 EVLMSMRRLGVKQIDLWQLHRIDPKVPRkdqFSEIA----AMKKEGLIRHVGLSEVTVDDIKEA-EQYFPVVSVQNLFNL 192
Cdd:cd19101 93 AIDRSLKRLGVDRLDLVQFHWWDYSDPG---YLDAAkhlaELQEEGKIRHLGLTNFDTERLREIlDAGVPIVSNQVQYSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 193 VNRKNEK-VLEYCEQKGIAFIPWYPLASGALA-------KPGTI-----------------------------LDAVSKD 235
Cdd:cd19101 170 LDRRPENgMAALCEDHGIKLLAYGTLAGGLLSekylgvpEPTGPaletrslqkyklmidewggwdlfqellrtLKAIADK 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19113480 236 LDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19101 250 HGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-272 |
4.96e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 102.01 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 23 MVVNRMGFGAMRVTGDGIWDEpKDKEACIATLKrlpeLNINFIDTADSYGPEVSE----NLLREALYPYK----GLIIAT 94
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDE-EYREALKAALD----SGINVIDTAINYRGGRSErligKALRELIEKGGikrdEVVIVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 95 KGGLVRTG-------------------------PNEWHpCGAPKFLRQEVLMSMRRLGVKQIDLWQLH---RIDPKVPRK 146
Cdd:cd19099 76 KAGYIPGDgdeplrplkyleeklgrglidvadsAGLRH-CISPAYLEDQIERSLKRLGLDTIDLYLLHnpeEQLLELGEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 147 DQFSEIAA-------MKKEGLIRHVGLS-----------------EVTVDDIKEAEQY---FPVV---------SVQNLF 190
Cdd:cd19099 155 EFYDRLEEafealeeAVAEGKIRYYGIStwdgfrappalpghlslEKLVAAAEEVGGDnhhFKVIqlplnllepEALTEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 191 NLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGTILDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEEN 270
Cdd:cd19099 235 NTVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGMRRPEHVDEN 314
|
..
gi 19113480 271 VK 272
Cdd:cd19099 315 LA 316
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
27-288 |
9.01e-25 |
|
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: 99.74 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDgiwdepkdkeACIATLKRLPELNINFIDTADSYGPE--VSENLlREALYPYKGLIIATKGGLVRTGPN 104
Cdd:cd19139 3 AFGLGTFRLKDD----------VVIDSVRTALELGYRHIDTAQIYDNEaaVGQAI-AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 105 EWHPCgapkfLRQevlmSMRRLGVKQIDLWQLH--RIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYF- 181
Cdd:cd19139 72 KLLPS-----LEE----SLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 182 --PVVSVQNLFN--LVNRkneKVLEYCEQKGIAFIPWYPLASG-ALAKPgtILDAVSKDLDRSTSQIALSWVLQRSpvML 256
Cdd:cd19139 143 agAIATNQIELSpyLQNR---KLVAHCKQHGIHVTSYMTLAYGkVLDDP--VLAAIAERHGATPAQIALAWAMARG--YA 215
|
250 260 270
....*....|....*....|....*....|..
gi 19113480 257 PIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19139 216 VIPSSTKREHLRSNLLALDLTLDADDMAAIAA 247
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
52-288 |
1.17e-24 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 101.60 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 52 ATLKRLPELNINFIDTADSYGP---EVSEN---LLREALYPYKG-LIIATKGGLvRTGPNEWHPCGAPKFLRQEVLMSMR 124
Cdd:PRK09912 47 AILRKAFDLGITHFDLANNYGPppgSAEENfgrLLREDFAAYRDeLIISTKAGY-DMWPGPYGSGGSRKYLLASLDQSLK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 125 RLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEA-----EQYFPVVSVQNLFNLVNRKNEK 199
Cdd:PRK09912 126 RMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMvellrEWKIPLLIHQPSYNLLNRWVDK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 200 --VLEYCEQKGIAFIPWYPLASGALA--------------KPGT-------------------ILDAVSKDLDRSTSQIA 244
Cdd:PRK09912 206 sgLLDTLQNNGVGCIAFTPLAQGLLTgkylngipqdsrmhREGNkvrgltpkmlteanlnslrLLNEMAQQRGQSMAQMA 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19113480 245 LSWVLQRSPVMLPIPGTSKVDHLEENVKA-AGIQLSSEVFAKLDE 288
Cdd:PRK09912 286 LSWLLKDERVTSVLIGASRAEQLEENVQAlNNLTFSTEELAQIDQ 330
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
29-287 |
5.36e-24 |
|
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: 98.09 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 29 GFGAMRVtgdgiwdepKDKEACIATLKRLPELNINFIDTADSYGPEVS-ENLLREALYPY----KGLIIATKgglvrTGP 103
Cdd:cd19136 5 GLGTFRL---------RGEEEVRQAVDAALKAGYRLIDTASVYRNEADiGKALRDLLPKYglsrEDIFITSK-----LAP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEWHPCGApkflRQEVLMSMRRLGVKQIDLWQLH-----RIDPKVP-----RKDQFSEIAAMKKEGLIRHVGLSEVTVDD 173
Cdd:cd19136 71 KDQGYEKA----RAACLGSLERLGTDYLDLYLIHwpgvqGLKPSDPrnaelRRESWRALEDLYKEGKLRAIGVSNYTVRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 174 IKEAEQYFPVVSVQNLFNLVNR-KNEKVLEYCEQKGIAFIPWYPLASGALA--KPGTILdAVSKDLDRSTSQIALSWVLQ 250
Cdd:cd19136 147 LEELLKYCEVPPAVNQVEFHPHlVQKELLKFCKDHGIHLQAYSSLGSGDLRllEDPTVL-AIAKKYGRTPAQVLLRWALQ 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 19113480 251 RSPVMlpIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19136 226 QGIGV--IPKSTNPERIAENIKVFDFELSEEDMAELN 260
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
22-281 |
4.95e-23 |
|
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: 96.08 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 22 DMVVNRMGFGAMRVTGdgIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKGGlv 99
Cdd:cd19163 10 GLKVSKLGFGASPLGG--VFGPVDEEEA-IRTVHEALDSGINYIDTAPWYGQGRSETVLGKALkgIPRDSYYLATKVG-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 100 RTGPNEwhpcgAPKF------LRQEVLMSMRRLGVKQIDLWQLHRIDpKVPRKDQ-FSE-IAAM---KKEGLIRHVGLSE 168
Cdd:cd19163 85 RYGLDP-----DKMFdfsaerITKSVEESLKRLGLDYIDIIQVHDIE-FAPSLDQiLNEtLPALqklKEEGKVRFIGITG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 169 VTVDDIKE-AEQYFPVVSV---QNLFNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAK-------PGT--ILDAVSK- 234
Cdd:cd19163 159 YPLDVLKEvLERSPVKIDTvlsYCHYTLNDTSLLELLPFFKEKGVGVINASPLSMGLLTErgppdwhPASpeIKEACAKa 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113480 235 ---------DLdrstSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19163 239 aaycksrgvDI----SKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
52-273 |
6.73e-23 |
|
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: 95.98 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 52 ATLKRLPELNINFIDTADSYGP---EVSEN---LLREALYPYKG-LIIATKGGL-VRTGP-NEWhpcGAPKFLRQEVLMS 122
Cdd:cd19150 34 AILRTAFDLGITHFDLANNYGPppgSAEENfgrILREDFAGYRDeLIISTKAGYdMWPGPyGEW---GSRKYLLASLDQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 123 MRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEA-----EQYFPVVSVQNLFNLVNRKN 197
Cdd:cd19150 111 LKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAaailrELGTPLLIHQPSYNMLNRWV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 198 EK--VLEYCEQKGIAFIPWYPLASGAL--------------AKPGTI---------------LDAVSKDLDRSTSQIALS 246
Cdd:cd19150 191 EEsgLLDTLQELGVGCIAFTPLAQGLLtdkylngipegsraSKERSLspkmlteanlnsiraLNEIAQKRGQSLAQMALA 270
|
250 260
....*....|....*....|....*..
gi 19113480 247 WVLQRSPVMLPIPGTSKVDHLEENVKA 273
Cdd:cd19150 271 WVLRDGRVTSALIGASRPEQLEENVGA 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-276 |
1.13e-22 |
|
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: 94.52 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 44 PKDKEAcIATLKRLPELNINFIDTADSYGpeVSENLLREALYPYKGLIIATKgglvrTGPNEWHPCGAPKFLRQEVLMSM 123
Cdd:cd19097 23 PSEKEA-KKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKRLDKFKIITK-----LPPLKEDKKEDEAAIEASVEASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 124 RRLGVKQIDLWQLHRI-DPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYFPVVSVQNLFNLVNR--KNEKV 200
Cdd:cd19097 95 KRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLPFNILDQrfLKSGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 201 LEYCEQKGIAF-----------------IPWYPL-ASGALAKpgtiLDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTS 262
Cdd:cd19097 175 LAKLKKKGIEIharsvflqglllmepdkLPAKFApAKPLLKK----LHELAKKLGLSPLELALGFVLSLPEIDKIVVGVD 250
|
250
....*....|....
gi 19113480 263 KVDHLEENVKAAGI 276
Cdd:cd19097 251 SLEQLKEIIAAFKK 264
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
31-281 |
2.91e-22 |
|
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: 94.80 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 31 GAMRVtGDGiWDE---PKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG---LIIATK--GGLVRTG 102
Cdd:cd19146 17 GAMSF-GEA-WKSmmgECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNrdeMVLATKytTGYRRGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 103 PNEW---HPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQ 179
Cdd:cd19146 95 PIKIksnYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 180 Y------FPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA-----------------------KPGTIL 229
Cdd:cd19146 175 YarahglTQFVVYQGHWSAAFRDFERdILPMCEAEGMALAPWGVLGQGQFRteeefkrrgrsgrkggpqtekerKVSEKL 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19113480 230 DAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19146 255 EKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDE 306
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
23-291 |
6.40e-20 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 87.00 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 23 MVVNRMGFGAMRVTGDgiwdepkdkeACIATLKRLPELNINFIDTADSYGPE--VSEnLLREALYPYKGLIIATKGGLVR 100
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQ----------VVIDSVKTALELGYRAIDTAQIYDNEaaVGQ-AIAESGVPRDELFITTKIWIDN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCgapkfLRQevlmSMRRLGVKQIDLWQLHRIDPK--VPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAe 178
Cdd:PRK11172 70 LAKDKLIPS-----LKE----SLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 qyFPVVSVQNLFN--------LVNRKnekVLEYCEQKGIAFIPWYPLASG-ALAKPgtILDAVSKDLDRSTSQIALSWVL 249
Cdd:PRK11172 140 --IAAVGAENIATnqielspyLQNRK---VVAFAKEHGIHVTSYMTLAYGkVLKDP--VIARIAAKHNATPAQVILAWAM 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19113480 250 QRSpvMLPIPGTSKVDHLEENVKAAGIQLSSE---VFAKLDEEGK 291
Cdd:PRK11172 213 QLG--YSVIPSSTKRENLASNLLAQDLQLDAEdmaAIAALDRNGR 255
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
46-288 |
9.35e-19 |
|
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: 84.57 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 46 DKEACIATLKRLPELNINFIDTADSYGPEVSE----NLLREALYPYKGLIIATK--GGLVRTGPNEwhpcgapKFLRQEV 119
Cdd:cd19143 29 DVDEAKECMKAAYDAGVNFFDNAEVYANGQSEeimgQAIKELGWPRSDYVVSTKifWGGGGPPPND-------RGLSRKH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 120 LM-----SMRRLGVKQIDLWQLHRIDPKVPrkdqFSEIA-AMK---KEGLIRHVGLSEVTVDDIKEA----EQYF---PV 183
Cdd:cd19143 102 IVegtkaSLKRLQLDYVDLVFCHRPDPATP----IEETVrAMNdliDQGKAFYWGTSEWSAQQIEEAheiaDRLGlipPV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 184 VSvQNLFNLVNRknEKV-LEY---CEQKGIAFIPWYPLASGAL--------------AKPGTI----------------- 228
Cdd:cd19143 178 ME-QPQYNLFHR--ERVeVEYaplYEKYGLGTTTWSPLASGLLtgkynngipegsrlALPGYEwlkdrkeelgqekiekv 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113480 229 --LDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGI--QLSSEVFAKLDE 288
Cdd:cd19143 255 rkLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlpKLTPEVMEKIEA 318
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
37-287 |
1.32e-16 |
|
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: 77.80 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 37 GDGIWDEPkDKEACIATLKRLpELNINFIDTADSYGPEVS-ENLLREALYPYKGLIIATKgglvrtgpnEWHPCGAPKFL 115
Cdd:cd19131 14 GLGVWQVS-NDEAASAVREAL-EVGYRSIDTAAIYGNEEGvGKAIRASGVPREELFITTK---------LWNSDQGYDST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 116 RQEVLMSMRRLGVKQIDLWQLHRidpKVPRKDQFSE----IAAMKKEGLIRHVGLSEVTVDD----IKEAEqyfpVVSVQ 187
Cdd:cd19131 83 LRAFDESLRKLGLDYVDLYLIHW---PVPAQDKYVEtwkaLIELKKEGRVKSIGVSNFTIEHlqrlIDETG----VVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 188 NLFNLVNRKNEKVL-EYCEQKGIAFIPWYPLASG-ALAKPgtILDAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVD 265
Cdd:cd19131 156 NQIELHPRFQQRELrAFHAKHGIQTESWSPLGQGgLLSDP--VIGEIAEKHGKTPAQVVIRWHLQNGLVV--IPKSVTPS 231
|
250 260
....*....|....*....|....*
gi 19113480 266 HLEENVKAAGIQLSSE---VFAKLD 287
Cdd:cd19131 232 RIAENFDVFDFELDADdmqAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
65-287 |
1.96e-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: 77.31 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYGPE--VSENLlREALYPYKGLIIATKggLvrtgPNEWHPCGAPKFLRQEvlmSMRRLGVKQIDLWQLHRIDPK 142
Cdd:cd19132 37 LDTAFNYENEgaVGEAV-RRSGVPREELFVTTK--L----PGRHHGYEEALRTIEE---SLYRLGLDYVDLYLIHWPNPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 143 VPRK-DQFSEIAAMKKEGLIRHVGLSEVT---VDDIKEAEQYFPVVSVQNLFNLVNRknEKVLEYCEQKGIAFIPWYPLA 218
Cdd:cd19132 107 RDLYvEAWQALIEAREEGLVRSIGVSNFLpehLDRLIDETGVTPAVNQIELHPYFPQ--AEQRAYHREHGIVTQSWSPLG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113480 219 SGA--LAKPgtILDAVSKDLDRSTSQIALSWVLQRSpvMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19132 185 RGSglLDEP--VIKAIAEKHGKTPAQVVLRWHVQLG--VVPIPKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
33-292 |
1.59e-15 |
|
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: 75.23 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWDEPKDKeaCIATLKRLPELNINFIDTADSYGPE-----VSENLLREALYPYKGLIIATKGglvrtgPNEWH 107
Cdd:cd19111 4 MPVIGLGTYQSPPEE--VRAAVDYALFVGYRHIDTALSYQNEkaigeALKWWLKNGKLKREEVFITTKL------PPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 108 pcgAPKFLRQEVLMSMRRLGVKQIDLWQLH-------------RIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDI 174
Cdd:cd19111 76 ---EFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 175 KEAEQY--FPVVSVQNLFNLVNRKNEKVlEYCEQKGIAFIPWYPLASGALA-------KPGTILD----AVSKDLDRSTS 241
Cdd:cd19111 153 NKILAYakVKPSNLQLECHAYLQQRELR-KFCNKKNIVVTAYAPLGSPGRAnqslwpdQPDLLEDptvlAIAKELDKTPA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 19113480 242 QIALSWVLQRSPVmlPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEEGKS 292
Cdd:cd19111 232 QVLLRFVLQRGTG--VLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRN 280
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
25-273 |
3.03e-15 |
|
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: 74.49 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAmrVTGDGIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREAL----YPYKGLIIATKGGLVR 100
Cdd:cd19153 12 VSPVGLGT--AALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALaalqVPRSSYTVATKVGRYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWhpcgAPKFLRQEVLMSMRRLGVKQIDLWQLHRI-----DPKVprKDQFSEIAAMKKEGLIRHVGLSEVTVDDIK 175
Cdd:cd19153 90 DSEFDY----SAERVRASVATSLERLHTTYLDVVYLHDIefvdyDTLV--DEALPALRTLKDEGVIKRIGIAGYPLDTLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 176 EAEQYFPVVSVQNL-----FNLVNRKNEKVLEYCEQ-KGIAFI----------------PWYPlASGAL----AKPGTIL 229
Cdd:cd19153 164 RATRRCSPGSLDAVlsychLTLQDARLESDAPGLVRgAGPHVInasplsmglltsqgppPWHP-ASGELrhyaAAADAVC 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19113480 230 DAVSKDLDRSTSQIALSWVLQRSPVMLpipGTSKVDHLEENVKA 273
Cdd:cd19153 243 ASVEASLPDLALQYSLAAHAGVGTVLL---GPSSLAQLRSMLAA 283
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
33-287 |
5.11e-15 |
|
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: 73.35 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWdEPKDKEACIATLKRLpELNINFIDTADSYGPEVS-ENLLREALYPYKGLIIATKgglvrtgpnEWHPCGA 111
Cdd:cd19134 11 MPVIGLGVG-ELSDDEAERSVSAAL-EAGYRLIDTAAAYGNEAAvGRAIAASGIPRGELFVTTK---------LATPDQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 112 PKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRK-DQFSEIAAMKKEGLIRHVGLSEVT---VDDIKEAEQYFPVVSVQ 187
Cdd:cd19134 80 FTASQAACRASLERLGLDYVDLYLIHWPAGREGKYvDSWGGLMKLREEGLARSIGVSNFTaehLENLIDLTFFTPAVNQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 188 NLFNLVNRknEKVLEYCEQKGIAFIPWYPLASGALAKPGTILdAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHL 267
Cdd:cd19134 160 ELHPLLNQ--AELRKVNAQHGIVTQAYSPLGVGRLLDNPAVT-AIAAAHGRTPAQVLLRWSLQLGNVV--ISRSSNPERI 234
|
250 260
....*....|....*....|
gi 19113480 268 EENVKAAGIQLSSEVFAKLD 287
Cdd:cd19134 235 ASNLDVFDFELTADHMDALD 254
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
12-287 |
1.38e-14 |
|
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: 72.94 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 12 ASQAGtVKVGDMVVNRMGFGAMRVTGDGiwdePKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKG-- 89
Cdd:cd19147 3 SKTAG-IRVSPLILGAMSIGDAWSGFMG----SMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 90 -LIIATKGGLVRTG-----PNEWHPCGAPK-FLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIR 162
Cdd:cd19147 78 qIVIATKFTTDYKAyevgkGKAVNYCGNHKrSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 163 HVGLSEVTVDDIKEAEQY------FPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALAKPGTILD----- 230
Cdd:cd19147 158 YLGVSDTPAWVVSAANYYatahgkTPFSVYQGRWNVLNRDFERdIIPMARHFGMALAPWDVLGGGKFQSKKAVEErkkng 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 231 -----------------AVSKDLDR--------STSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAK 285
Cdd:cd19147 238 eglrsfvggteqtpeevKISEALEKvaeehgteSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEY 317
|
..
gi 19113480 286 LD 287
Cdd:cd19147 318 LE 319
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
54-281 |
1.44e-14 |
|
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: 72.69 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 54 LKRLPELNINFIDTADSYGPevSENLLREAL------YPYKGLIIATKGGlvRTGPNEWHPcgAPKFLRQEVLMSMRRLG 127
Cdd:cd19164 40 VRRALELGIRAFDTSPYYGP--SEIILGRALkalrdeFPRDTYFIITKVG--RYGPDDFDY--SPEWIRASVERSLRRLH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 128 VKQIDLWQLHRI----DPKVprKDQFSEIAAMKKEGLIRHVGLSEVTVD---DIKEAEQYFPVVSVQNL-----FNLVNR 195
Cdd:cd19164 114 TDYLDLVYLHDVefvaDEEV--LEALKELFKLKDEGKIRNVGISGYPLPvllRLAELARTTAGRPLDAVlsychYTLQNT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 196 KNEKVLEYCEQKG-IAFI-----------------PWYPlAS----GALAKPGTILDAVSKDLDRSTSQIALSWVLQRSP 253
Cdd:cd19164 192 TLLAYIPKFLAAAgVKVVlnasplsmgllrsqgppEWHP-ASpelrAAAAKAAEYCQAKGTDLADVALRYALREWGGEGP 270
|
250 260
....*....|....*....|....*...
gi 19113480 254 VMLpipGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19164 271 TVV---GCSNVDELEEAVEAYWSVLAGA 295
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
122-288 |
6.91e-14 |
|
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: 70.11 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 122 SMRRLGVKQIDLWQLHRidpkvPRKDQFSE----IAAMKKEGLIRHVGLSEVTVDDIKEAEQYFPVVSVQNLFNLVNRKN 197
Cdd:cd19157 90 SLERLGLDYLDLYLIHW-----PVKGKYKEtwkaLEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHPRLT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 198 EK-VLEYCEQKGIAFIPWYPLASGALAKPGTILDaVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGI 276
Cdd:cd19157 165 QKeLRDYCKKQGIQLEAWSPLMQGQLLDNPVLKE-IAEKYNKSVAQVILRWDLQNGVVT--IPKSIKEHRIIENADVFDF 241
|
170
....*....|..
gi 19113480 277 QLSSEVFAKLDE 288
Cdd:cd19157 242 ELSQEDMDKIDA 253
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
29-287 |
1.24e-13 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 69.14 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 29 GFGAMRVTGDGIwdepkDKEACIATLK---RLpelninfIDTADSYGPEVS-ENLLREALYPYKGLIIATKGGLVRTGPN 104
Cdd:cd19133 13 GFGVFQIPDPEE-----CERAVLEAIKagyRL-------IDTAAAYGNEEAvGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 105 ewhpcGAPK-FLRqevlmSMRRLGVKQIDLWQLHRidpkvPRKDQFSEIAAM---KKEGLIRHVGLSEVTVD---DIKEA 177
Cdd:cd19133 81 -----KAKKaFER-----SLKRLGLDYLDLYLIHQ-----PFGDVYGAWRAMeelYKEGKIRAIGVSNFYPDrlvDLILH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 178 EQYFPVVSvQNLFNLVNRKNEkVLEYCEQKGIAFIPWYPLASG---ALAKPgtILDAVSKDLDRSTSQIALSWVLQRSPV 254
Cdd:cd19133 146 NEVKPAVN-QIETHPFNQQIE-AVEFLKKYGVQIEAWGPFAEGrnnLFENP--VLTEIAEKYGKSVAQVILRWLIQRGIV 221
|
250 260 270
....*....|....*....|....*....|...
gi 19113480 255 MlpIPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19133 222 V--IPKSVRPERIAENFDIFDFELSDEDMEAIA 252
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
25-293 |
1.63e-13 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 69.81 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAM---RVTGdgiwdePKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREAL----YPYKGLIIATKGG 97
Cdd:PLN02587 11 VSSVGFGASplgSVFG------PVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALkalgIPREKYVVSTKCG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 98 LVRTGPNewhpCGAPKFLRQeVLMSMRRLGVKQIDLWQLHRIDpkVPRKDQF-SE----IAAMKKEGLIRHVGLSEVTVD 172
Cdd:PLN02587 85 RYGEGFD----FSAERVTKS-VDESLARLQLDYVDILHCHDIE--FGSLDQIvNEtipaLQKLKESGKVRFIGITGLPLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 173 DIKEAEQYFPVVSVQNL-----FNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGT---------------ILDAV 232
Cdd:PLN02587 158 IFTYVLDRVPPGTVDVIlsychYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTENGPpewhpappelksacaAAATH 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113480 233 SKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAgIQLSSevfAKLDEEGKSE 293
Cdd:PLN02587 238 CKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAA-TELET---SGIDEELLSE 294
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
27-286 |
3.49e-13 |
|
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: 68.54 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTGDGIWDEpkdkEACIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKGGLVRTGPN 104
Cdd:cd19162 2 RLGLGAASLGNLARAGE----DEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALarHPRAEYVVSTKVGRLLEPGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 105 EWHPCGAPK-------FLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRK--DQFSEIAAMKKEGLIRHVGLSEVTVDDIK 175
Cdd:cd19162 78 AGRPAGADRrfdfsadGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQAltDAFPALEELRAEGVVGAIGVGVTDWAALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 176 EAEQYFP--VVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALAK-------------PGTILD------AVS 233
Cdd:cd19162 158 RAARRADvdVVMVAGRYTLLDRRAATeLLPLCAAKGVAVVAAGVFNSGILATddpagdrydyrpaTPEVLArarrlaAVC 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19113480 234 KDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKL 286
Cdd:cd19162 238 RRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAEFWAEL 290
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
27-281 |
4.28e-13 |
|
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: 67.93 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVTgdgiwdEPKDKEACIATLKrlpeLNINFIDTADSYGPE-----VSENLLREALYPYKGLIIATKgglvrt 101
Cdd:cd19128 3 RLGFGTYKIT------ESESKEAVKNAIK----AGYRHIDCAYYYGNEafigiAFSEIFKDGGVKREDLFITSK------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 102 gpnEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH-------------------RIDPKVPRKDQFSEIAAMKKEGLIR 162
Cdd:cd19128 67 ---LWPTMHQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 163 HVGLSEVTVDDIKEAEQYFPVVSVQNLFNL-VNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGTI-----LDAVSKDL 236
Cdd:cd19128 144 NIGVSNYSTKLLTDLLNYCKIKPFMNQIEChPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTFlndseLKALATKY 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19113480 237 DRSTSQIALSWVLQRSPVMLP-IPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19128 224 NTTPPQVIIAWHLQKWPKNYSvIPKSANKSRCQQNFDINDLALTKE 269
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
45-288 |
5.55e-13 |
|
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: 68.08 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 45 KDKEACIATLKRLPELNINFIDTADSYG--PEVSE---NLLREALYPYKGLIIATKGGlvrtgpNEWHPcgapkflRQEV 119
Cdd:cd19116 22 KDDEGVRQAVKHAIEAGYRHIDTAYLYGneAEVGEairEKIAEGVVKREDLFITTKLW------NSYHE-------REQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 120 L----MSMRRLGVKQIDLWQLH-------RIDPKVPRKDQFSEIA------AM---KKEGLIRHVGLSEVTvddikeAEQ 179
Cdd:cd19116 89 EpalrESLKRLGLDYVDLYLIHwpvafkeNNDSESNGDGSLSDIDyletwrGMedlVKLGLTRSIGVSNFN------SEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 180 YFPVVSVQNLFNLVNR-------KNEKVLEYCEQKGI---AFIPW-YPLASGALAKPGTI----LDAVSKDLDRSTSQIA 244
Cdd:cd19116 163 INRLLSNCNIKPAVNQievhptlTQEKLVAYCQSNGIvvmAYSPFgRLVPRGQTNPPPRLddptLVAIAKKYGKTTAQIV 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19113480 245 LSWVLQRSPVmlPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19116 243 LRYLIDRGVV--PIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
33-287 |
9.69e-13 |
|
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: 66.69 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWDEPKDKEACIATLKRLpELNINFIDTADSYGPEVSE-NLLREALYPYKGLIIATKgglvrtgpnEWHPCGA 111
Cdd:cd19126 9 MPWLGLGVFQTPDGDETERAVQTAL-ENGYRSIDTAAIYKNEEGVgEAIRESGVPREELFVTTK---------LWNDDQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 112 PKFLRQEVLMSMRRLGVKQIDLWQLHRidpkvPRKDQFSEI-AAMKK---EGLIRHVGLSEVTVDDIKEAEQYFPVVSVQ 187
Cdd:cd19126 79 ARRTEDAFQESLDRLGLDYVDLYLIHW-----PGKDKFIDTwKALEKlyaSGKVKAIGVSNFQEHHLEELLAHADVVPAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 188 NLFNLVNR-KNEKVLEYCEQKGIAFIPWYPLASGALAKPGTiLDAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDH 266
Cdd:cd19126 154 NQVEFHPYlTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPV-LAAIGEKYGKSAAQVVLRWDIQHGVVT--IPKSVHASR 230
|
250 260
....*....|....*....|.
gi 19113480 267 LEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19126 231 IKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
27-287 |
1.24e-12 |
|
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: 66.47 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 27 RMGFGAMRVtgdgiwdEPKDKEACIATLKrlpELNINFIDTADSYGPE--VSENLLREALyPYKGLIIATKGGLVRTGPN 104
Cdd:cd19130 12 QLGYGVFKV-------PPADTQRAVATAL---EVGYRHIDTAAIYGNEegVGAAIAASGI-PRDELFVTTKLWNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 105 EwhpcgapkfLRQEVLMSMRRLGVKQIDLWQLHRidpKVPRKDQFSEI-AAMKK---EGLIRHVGLSEVTVDDIKEAEQY 180
Cdd:cd19130 81 E---------PAAAFAESLAKLGLDQVDLYLVHW---PTPAAGNYVHTwEAMIElraAGRTRSIGVSNFLPPHLERIVAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 181 FPVVSVQNLFNLVNR-KNEKVLEYCEQKGIAFIPWYPLASGAL--AKPGTILDAVSkdlDRSTSQIALSWVLQRSPVMlp 257
Cdd:cd19130 149 TGVVPAVNQIELHPAyQQRTIRDWAQAHDVKIEAWSPLGQGKLlgDPPVGAIAAAH---GKTPAQIVLRWHLQKGHVV-- 223
|
250 260 270
....*....|....*....|....*....|
gi 19113480 258 IPGTSKVDHLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19130 224 FPKSVRRERMEDNLDVFDFDLTDTEIAAID 253
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
51-286 |
1.42e-12 |
|
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: 66.97 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 51 IATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKGGLV--------RTGPNEWHPcGAP-------- 112
Cdd:cd19161 23 DATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLreKPRDEFVLSTKVGRLlkparegsVPDPNGFVD-PLPfeivydys 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 113 --KFLRQeVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQ------------FSEIAAMKKEGLIRHVGLSEVTVDDIKEAE 178
Cdd:cd19161 102 ydGIMRS-FEDSLQRLGLNRIDILYVHDIGVYTHGDRKerhhfaqlmsggFKALEELKKAGVIKAFGLGVNEVQICLEAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 QYFPV--VSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALA---KPGTILD--AVSKDLDRSTSQI------- 243
Cdd:cd19161 181 DEADLdcFLLAGRYSLLDQSAEEeFLPRCEQRGTSLVIGGVFNSGILAtgtKSGAKFNygDAPAEIISRVMEIekicday 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19113480 244 -------ALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKL 286
Cdd:cd19161 261 nvplaaaALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEELWQAL 310
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
106-291 |
5.06e-12 |
|
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: 65.12 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 106 WHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH-----RIDPKVPRKDQ----FSEI------AAM---KKEGLIRHVGLS 167
Cdd:cd19123 79 WNNSHAPEDVLPALEKTLADLQLDYLDLYLMHwpvalKKGVGFPESGEdllsLSPIpledtwRAMeelVDKGLCRHIGVS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 168 EVTV---DDIKEAEQYFPVVSVQNLFNLVNRKneKVLEYCEQKGIAFIPWYPLASG-------ALAKPGTILDAVSKDLD 237
Cdd:cd19123 159 NFSVkklEDLLATARIKPAVNQVELHPYLQQP--ELLAFCRDNGIHLTAYSPLGSGdrpaamkAEGEPVLLEDPVINKIA 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113480 238 R----STSQIALSWVLQRSPVMLPIPGTSKvdHLEENVKAAGIQLSSEVFAKLDEEGK 291
Cdd:cd19123 237 EkhgaSPAQVLIAWAIQRGTVVIPKSVNPE--RIQQNLEAAEVELDASDMATIAALDR 292
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
33-293 |
6.09e-12 |
|
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: 64.46 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWDEPKDKEACIATLKRLpELNINFIDTADSYGPEVSENL-LREALYPYKGLIIATKgglvrtgpnEWHPCGA 111
Cdd:cd19156 9 MPRLGLGVWRVQDGAEAENAVKWAI-EAGYRHIDTAAIYKNEEGVGQgIRESGVPREEVFVTTK---------LWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 112 PKFLRQEVLMSMRRLGVKQIDLWQLHRidpkvPRKDQFSE----IAAMKKEGLIRHVGLSEVTVDDIKEAEQYFPVVSVQ 187
Cdd:cd19156 79 YESTLAAFEESLEKLGLDYVDLYLIHW-----PVKGKFKDtwkaFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 188 NLFNLVNRKNEKVL-EYCEQKGIAFIPWYPLASGALAKpGTILDAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDH 266
Cdd:cd19156 154 NQIELHPLLTQEPLrKFCKEKNIAVEAWSPLGQGKLLS-NPVLKAIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEER 230
|
250 260
....*....|....*....|....*..
gi 19113480 267 LEENVKAAGIQLSSEVFAKLDEEGKSE 293
Cdd:cd19156 231 IQENFDVFDFELTAEEIRQIDGLNTDH 257
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
65-297 |
7.69e-12 |
|
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: 64.67 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYGPE-----VSENLLREALYPYKGLIIATKgglvrtgpnEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH-- 137
Cdd:cd19125 41 IDCAAIYGNEkeigkALKKLFEDGVVKREDLFITSK---------LWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHwp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 138 ---RIDPKVPRKDQFSEI------AAMKK---EGLIRHVGLSEVTVDDIKEaeqyfpVVSVQNLFNLVNR-------KNE 198
Cdd:cd19125 112 vrlKKGAHMPEPEEVLPPdipstwKAMEKlvdSGKVRAIGVSNFSVKKLED------LLAVARVPPAVNQvechpgwQQD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 199 KVLEYCEQKGIAFIPWYPLASgalakPGT-----------ILDAVSKDLDRSTSQIALSWVLQRSPVMLpiPGTSKVDHL 267
Cdd:cd19125 186 KLHEFCKSKGIHLSAYSPLGS-----PGTtwvkknvlkdpIVTKVAEKLGKTPAQVALRWGLQRGTSVL--PKSTNEERI 258
|
250 260 270
....*....|....*....|....*....|
gi 19113480 268 EENVKAAGIQLSSEVFAKLDEegkSEDAKR 297
Cdd:cd19125 259 KENIDVFDWSIPEEDFAKFSS---IEQQRR 285
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
62-288 |
7.87e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 62.18 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 62 INFIDTADSYG----PE---VSENLLREALYPYKG---LIIATK-GGLVRTGPNEWHPCGA--PKFLRQEVLMSMRRLGV 128
Cdd:PRK10625 44 INLIDVAEMYPvpprPEtqgLTETYIGNWLAKRGSrekLIIASKvSGPSRNNDKGIRPNQAldRKNIREALHDSLKRLQT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 129 KQIDLWQLH-----------------RIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVT----VDDIKEAEQY-FP-VVS 185
Cdd:PRK10625 124 DYLDLYQVHwpqrptncfgklgyswtDSAPAVSLLETLDALAEQQRAGKIRYIGVSNETafgvMRYLHLAEKHdLPrIVT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 186 VQNLFNLVNRKNEKVL-EYCEQKGIAFIPWYPLASGAL-------AKPG----TILD------------------AVSKD 235
Cdd:PRK10625 204 IQNPYSLLNRSFEVGLaEVSQYEGVELLAYSCLAFGTLtgkylngAKPAgarnTLFSrftrysgeqtqkavaayvDIAKR 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19113480 236 LDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:PRK10625 284 HGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHLTLSEEVLAEIEA 336
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
106-288 |
1.32e-10 |
|
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: 60.89 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 106 WHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH---------RIDPKVPRKDQFSEIA---------------AMKKEGLI 161
Cdd:cd19118 75 WNNSHRPEYVEPALDDTLKELGLDYLDLYLIHwpvafkptgDLNPLTAVPTNGGEVDldlsvslvdtwkamvELKKTGKV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 162 RHVGLSEVTVDDIK---EAEQYFPVVsvqnlfNLVNRK----NEKVLEYCEQKGIAFIPWYPLASGALAKPGTI----LD 230
Cdd:cd19118 155 KSIGVSNFSIDHLQaiiEETGVVPAV------NQIEAHplllQDELVDYCKSKNIHITAYSPLGNNLAGLPLLVqhpeVK 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113480 231 AVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAagIQLSSEVFAKLDE 288
Cdd:cd19118 229 AIAAKLGKTPAQVLIAWGIQRGHSV--IPKSVTPSRIRSNFEQ--VELSDDEFNAVTA 282
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
65-257 |
3.92e-10 |
|
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: 59.71 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYG--PEVSENLlREALYPYKG-----LIIATKgglvrtgpnEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH 137
Cdd:cd19106 37 IDCAAVYGneQEVGEAL-KEKVGPGKAvpredLFVTSK---------LWNTKHHPEDVEPALRKTLKDLQLDYLDLYLIH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 138 ------RIDPKVPRKD----QFSEI------AAMKK---EGLIRHVGLSEVT---VDDIKEAEQYFPVV-SVQNLFNLVN 194
Cdd:cd19106 107 wpyafeRGDNPFPKNPdgtiRYDSThyketwKAMEKlvdKGLVKAIGLSNFNsrqIDDILSVARIKPAVlQVECHPYLAQ 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113480 195 rknEKVLEYCEQKGIAFIPWYPLASG--ALAKPG--TILD-----AVSKDLDRSTSQIALSWVLQRSPVMLP 257
Cdd:cd19106 187 ---NELIAHCKARGLVVTAYSPLGSPdrPWAKPDepVLLEepkvkALAKKYNKSPAQILLRWQVQRGVVVIP 255
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
26-274 |
4.93e-09 |
|
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: 56.46 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 26 NRMGFGAmrVTGDGIWDEPKDKEAcIATLKRLPELNINFIDTADSYGPEVSENLLREAL--YPYKGLIIATKGGLVRTGP 103
Cdd:cd19152 1 PKLGFGT--APLGNLYEAVSDEEA-KATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALreLGREDYVISTKVGRLLVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 104 NEWHPCGAPKFL------------RQEVLMSMR----RLGVKQIDLWQLHRIDPKVPR-----------KDQFSEIAAMK 156
Cdd:cd19152 78 QEVEPTFEPGFWnplpfdavfdysYDGILRSIEdslqRLGLSRIDLLSIHDPDEDLAGaesdehfaqaiKGAFRALEELR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 157 KEGLIRHVGLSEVTVDDIKEA--EQYFPVVSVQNLFNLVNRKNEK-VLEYCEQKGIAFIPWYPLASGALAKPGTILDAVS 233
Cdd:cd19152 158 EEGVIKAIGLGVNDWEVILRIleEADLDWVMLAGRYTLLDHSAAReLLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEY 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19113480 234 KDLDR------------------STSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAA 274
Cdd:cd19152 238 GPAPPeliarrdriealceqhgvSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
139-281 |
1.45e-08 |
|
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: 54.80 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 139 IDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTV---DDIKEAEQYFPVVSVQNLFNLVNRknEKVLEYCEQKGIAFIPWY 215
Cdd:cd19112 132 IDVTISLETTWHAMEKLVSAGLVRSIGISNYDIfltRDCLAYSKIKPAVNQIETHPYFQR--DSLVKFCQKHGISVTAHT 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113480 216 PLASGA-----------LAKPgtILDAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19112 210 PLGGAAanaewfgsvspLDDP--VLKDLAKKYGKSAAQIVLRWGIQRNTAV--IPKSSKPERLKENIDVFDFQLSKE 282
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
65-288 |
2.71e-08 |
|
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: 53.95 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYGPE--VSENLLREALyPYKGLIIATKGGLVRTGPNEwhpcgapkfLRQEVLMSMRRLGVKQIDLWQLHRidpk 142
Cdd:cd19127 39 IDTAAAYGNEreVGEGIRRSGV-DRSDIFVTTKLWISDYGYDK---------ALRGFDASLRRLGLDYVDLYLLHW---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 143 vPRKDQFSE-IAAMK------KEGLIRHVGLSEVTVDDIKEAEQYFPVVSVQNLFNL-VNRKNEKVLEYCEQKGIAFIPW 214
Cdd:cd19127 105 -PVPNDFDRtIQAYKalekllAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVELhPYFSQKDLRAFHRRLGIVTQAW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 215 YPL-------ASGALAKPGTILDAVSKDL----DRSTSQIALSWVLQRSpvMLPIPGTSKVDHLEENVKAAGIQLSSEVF 283
Cdd:cd19127 184 SPIggvmrygASGPTGPGDVLQDPTITGLaekyGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFDFALSAEDM 261
|
....*
gi 19113480 284 AKLDE 288
Cdd:cd19127 262 AAIDA 266
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
25-289 |
3.08e-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: 54.01 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIWDEPKDkeaciATLKRLPELNINFIDTADSYGPEVSE----NLLREALYPYKGLIIATKGgLVR 100
Cdd:cd19142 13 VSNVGLGTWSTFSTAISEEQAE-----EIVTLAYENGINYFDTSDAFTSGQAEtelgRILKKKGWKRSSYIVSTKI-YWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEwhpCG-APKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEA-- 177
Cdd:cd19142 87 YGSEE---RGlSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAfs 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 178 --EQY--FPVVSVQNLFNLVNRknEKV----LEYCEQKGIAFIPWYPLASG--------------------ALAKPG--- 226
Cdd:cd19142 164 iaRQFncPTPICEQSEYHMFCR--EKMelymPELYNKVGVGLITWSPLSLGldpgiseetrrlvtklsfksSKYKVGsdg 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113480 227 --------------TILDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAagIQLSSEVFAKLDEE 289
Cdd:cd19142 242 ngiheetrrashklRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNS--LQLLPKLNSAVMEE 316
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
47-288 |
4.57e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 53.50 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 47 KEACIATLKRLPELNINFIDTADSYGpEVSENL---LREALYPYKGLIIATKGGLVRTGpnEWHPCGAP--------KFL 115
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSYG-RAEEFLgswLRSRNIAPDAVFVGSKWGYTYTA--DWQVDAAVhevkdhslARL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 116 RQEVLMSMRRLGvKQIDLWQLHR--IDPKVPR-KDQFSEIAAMKKEGliRHVGLS--------------EVTVDDIKeae 178
Cdd:cd19098 111 LKQWEETRSLLG-KHLDLYQIHSatLESGVLEdADVLAALAELKAEG--VKIGLSlsgpqqaetlrralEIEIDGAR--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 qyfPVVSVQNLFNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGTI---------LDAVSKDLDRSTSQIALSWVL 249
Cdd:cd19098 185 ---LFDSVQATWNLLEQSAGEALEEAHEAGMGVIVKEALANGRLTDRNPSpelaplmavLKAVADRLGVTPDALALAAVL 261
|
250 260 270
....*....|....*....|....*....|....*....
gi 19113480 250 QRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19098 262 AQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALAD 300
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
25-273 |
8.11e-08 |
|
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: 52.83 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIWDEPKDKEACIATlkrlpELNINFIDTADSYGPEVSE----NLLREALYPYKGLIIATKggLVR 100
Cdd:cd19141 12 VSCLGLGTWVTFGSQISDEVAEELVTLAY-----ENGINLFDTAEVYAAGKAEivlgKILKKKGWRRSSYVITTK--IFW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKE---- 176
Cdd:cd19141 85 GGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEaysv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 177 AEQY--FPVVSVQNLFNLVNR-KNEKVLEYCEQK-GIAFIPWYPLASGALAKP--------------------GTILD-- 230
Cdd:cd19141 165 ARQFnlIPPIVEQAEYHLFQReKVEMQLPELFHKiGVGAMTWSPLACGILSGKyddgvpeysraslkgyqwlkEKILSee 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19113480 231 ------------AVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKA 273
Cdd:cd19141 245 grrqqaklkelqIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQA 299
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
25-287 |
8.69e-08 |
|
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: 52.68 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 25 VNRMGFGAMRVTGDGIWDEPKDKEACIATlkrlpELNINFIDTADSYGPEVSE----NLLREALYPYKGLIIATKggLVR 100
Cdd:cd19160 15 VSCLGLGTWVTFGSQISDETAEDLLTVAY-----EHGVNLFDTAEVYAAGKAErtlgNILKSKGWRRSSYVVTTK--IYW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 101 TGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKE---- 176
Cdd:cd19160 88 GGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEaysv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 177 AEQY--FPVVSVQNLFNLVNRknEKV----LEYCEQKGIAFIPWYPLASGALAKP--GTILDA----------------- 231
Cdd:cd19160 168 ARQFnlIPPVCEQAEYHLFQR--EKVemqlPELYHKIGVGSVTWSPLACGLITGKydGRVPDTcraavkgyqwlkekvqs 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113480 232 ---------------VSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGI--QLSSEVFAKLD 287
Cdd:cd19160 246 eegkkqqakvkelhpIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTPQTVMEID 318
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
65-291 |
9.47e-08 |
|
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: 52.50 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYGPE--VSENLlREALYPYKGLIIATKGGlvrtgpNEWHPcgapkflRQEVLM--SMRRLGVKQIDLWQLHRID 140
Cdd:cd19117 44 IDTAAIYGNEeeVGQGI-KDSGVPREEIFITTKLW------CTWHR-------RVEEALdqSLKKLGLDYVDLYLMHWPV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 141 PKVPRKDQF---------------------SEIAAMKKEGLIRHVGLSEVTVDDIKE--AEQYFPVVSVQNLFNL-VNRK 196
Cdd:cd19117 110 PLDPDGNDFlfkkddgtkdhepdwdfiktwELMQKLPATGKVKAIGVSNFSIKNLEKllASPSAKIVPAVNQIELhPLLP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 197 NEKVLEYCEQKGIAFIPWYPLAS--GALAKPGTILDaVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSkvDHLEENVKAa 274
Cdd:cd19117 190 QPKLVDFCKSKGIHATAYSPLGStnAPLLKEPVIIK-IAKKHGKTPAQVIISWGLQRGYSVLPKSVTP--SRIESNFKL- 265
|
250
....*....|....*..
gi 19113480 275 gIQLSSEVFAKLDEEGK 291
Cdd:cd19117 266 -FTLSDEEFKEIDELHK 281
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
122-270 |
1.18e-07 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 52.07 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 122 SMRRLGVKQIDLWQLH---------RIDPK-----------VPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIK---EAE 178
Cdd:cd19129 89 SLKRLQLDYLDLYLIHtpfafqpgdEQDPRdangnviyddgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLReifEAA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 QYFP-VVSVQNLFNLvnrKNEKVLEYCEQKGIAFIPWYPLASGalAKPGTILD----AVSKDLDRSTSQIALSWVLQRSP 253
Cdd:cd19129 169 RIKPaVVQVESHPYL---PEWELLDFCKNHGIVLQAFAPLGHG--MEPKLLEDpvitAIARRVNKTPAQVLLAWAIQRGT 243
|
170
....*....|....*..
gi 19113480 254 VMLPIPGTSkvDHLEEN 270
Cdd:cd19129 244 ALLTTSKTP--SRIREN 258
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
122-291 |
1.71e-07 |
|
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: 51.47 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 122 SMRRLGVKQIDLWQLH---------RIDPKVPRKDQF-----------SEIAAMKK---EGLIRHVGLSEVTVDDIKEAE 178
Cdd:cd19122 95 SLKNLKLDYIDLFLVHwpiaaekndQRSPKLGPDGKYvilkdltenpePTWRAMEEiyeSGKAKAIGVSNWTIPGLKKLL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 179 QYFPVVSVQNLFNLVN-RKNEKVLEYCEQKGIAFIPWYPLAS-------GALAKPGTILDAVSKDLDRSTSQIALSWVLQ 250
Cdd:cd19122 175 SFAKVKPHVNQIEIHPfLPNEELVDYCFSNDILPEAYSPLGSqnqvpstGERVSENPTLNEVAEKGGYSLAQVLIAWGLR 254
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19113480 251 RSPVMLPIPGTSKvdHLEENVKAagIQLSSEVFAKLDEEGK 291
Cdd:cd19122 255 RGYVVLPKSSTPS--RIESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
65-288 |
1.41e-06 |
|
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: 48.95 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYGPE-----VSENLLREALYPYKGLIIATKGGLVRTGPNEWHPCgapkfLRQevlmSMRRLGVKQIDLWQLH-- 137
Cdd:cd19154 42 IDTAFLYQNEeaigeALAELLEEGVVKREDLFITTKLWTHEHAPEDVEEA-----LRE----SLKKLQLEYVDLYLIHap 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 138 --------RIDPKVPRKDQFSEI------AAMKK---EGLIRHVGLSEVTVDDIKE--AEQYFPVVSVQNLFNLVNRKNE 198
Cdd:cd19154 113 aafkddegESGTMENGMSIHDAVdvedvwRGMEKvydEGLTKAIGVSNFNNDQIQRilDNARVKPHNNQVECHLYFPQKE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 199 KVlEYCEQKGIAFIPWYPLAS---------GALAKPGTILD-----AVSKDLDRSTSQIALSWVLQRSpvMLPIPGTSKV 264
Cdd:cd19154 193 LV-EFCKKHNISVTSYATLGSpgranftksTGVSPAPNLLQdpivkAIAEKHGKTPAQVLLRYLLQRG--IAVIPKSATP 269
|
250 260
....*....|....*....|....
gi 19113480 265 DHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19154 270 SRIKENFNIFDFSLSEEDMATLEE 293
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
33-288 |
1.35e-05 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 45.72 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWDEPKDKEACIATLKRLPELNINFIDTADSYGpevSENLLREALYpykgliIATKGGLVRT----------G 102
Cdd:cd19124 5 MPVIGMGTASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALA------EALRLGLVKSrdelfvtsklW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 103 PNEWHPCGAPKFLRQevlmSMRRLGVKQIDLWQLH---RIDPKV----PRKDQF------SEIAAM---KKEGLIRHVGL 166
Cdd:cd19124 76 CSDAHPDLVLPALKK----SLRNLQLEYVDLYLIHwpvSLKPGKfsfpIEEEDFlpfdikGVWEAMeecQRLGLTKAIGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 167 SEVTVDDIKEAEQYF---PVVSvQNLFNLVNRKnEKVLEYCEQKGIAFIPWYPL-ASGALAKPGTILD-AVSKDL----D 237
Cdd:cd19124 152 SNFSCKKLQELLSFAtipPAVN-QVEMNPAWQQ-KKLREFCKANGIHVTAYSPLgAPGTKWGSNAVMEsDVLKEIaaakG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 19113480 238 RSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19124 230 KTVAQVSLRWVYEQGVSL--VVKSFNKERMKQNLDIFDWELTEEDLEKISE 278
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
106-293 |
1.85e-05 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 45.56 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 106 WHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRI------DPKVPRKDQ-------------FSEIAAMKKEGLIRHVGL 166
Cdd:cd19109 75 WNTCHPPELVRPTLERTLKVLQLDYVDLYIIEMPmafkpgDEIYPRDENgkwlyhktnlcatWEALEACKDAGLVKSIGV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 167 S-------EVTVDdiKEAEQYFPV---VSVQNLFNlvnrkNEKVLEYCEQKGIAFIPWYPLASGALAK----------PG 226
Cdd:cd19109 155 SnfnrrqlELILN--KPGLKHKPVsnqVECHPYFT-----QPKLLEFCQQHDIVIVAYSPLGTCRDPIwvnvssppllED 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113480 227 TILDAVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEEGKSE 293
Cdd:cd19109 228 PLLNSIGKKYNKTAAQVVLRFNIQRGVVV--IPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNV 292
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
33-293 |
3.88e-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: 44.44 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWD-EPKDKEACIATLKrlpELNINFIDTADSYGPEVS-ENLLREALYPYK----GLIIATKggLVRTGpNEW 106
Cdd:cd19155 12 MPVVGLGTWQsSPEEIETAVDTAL---EAGYRHIDTAYVYRNEAAiGNVLKKWIDSGKvkreELFIVTK--LPPGG-NRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 107 HpcGAPKFLRQevlmSMRRLGVKQIDLW---------------------QLHRIDPKVPRKDQFSEIAAMKKEGLIRHVG 165
Cdd:cd19155 86 E--KVEKFLLK----SLEKLQLDYVDLYlihfpvgslskeddsgkldptGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 166 LSEVTVDDIKEAEQYFPVVSVQNLFNLVNRKNEKVL-EYCEQKGIAFIPWYPLASGALAK--------PGTILD------ 230
Cdd:cd19155 160 LSNFNREQMARILKNARIKPANLQVELHVYLQQKDLvDFCSTHSITVTAYAPLGSPGAAHfspgtgspSGSSPDllqdpv 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113480 231 --AVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEEGKSE 293
Cdd:cd19155 240 vkAIAERHGKSPAQVLLRWLMQRGVVV--IPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNI 302
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
158-286 |
4.18e-05 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 44.33 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 158 EGLIRHVGLSEVTVDDI-----KEAEQYFPVVSVQNLFNLVNRknEKVLEYCEQKGIAFIPWYPLASG--ALAKPG--TI 228
Cdd:cd19107 142 EGLVKAIGVSNFNHLQIerilnKPGLKYKPAVNQIECHPYLTQ--EKLIQYCQSKGIVVTAYSPLGSPdrPWAKPEdpSL 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113480 229 LD-----AVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSEVFAKL 286
Cdd:cd19107 220 LEdpkikEIAAKHNKTTAQVLIRFPIQRNLVV--IPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
65-288 |
1.36e-04 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 42.93 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 65 IDTADSYGPEVS-----ENLLREALYPYKGLIIATKgglvrtgpnEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH-- 137
Cdd:cd19114 34 IDGALLYGNEAEvgrgiRKAIQEGLVKREDLFIVTK---------LWNNFHGKDHVREAFDRQLKDYGLDYIDLYLIHfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 138 ----RIDP-------------------KVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYF---PVVSVQNLFN 191
Cdd:cd19114 105 ipaaYVDPaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYAkikPAVLQIEHHP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 192 LVNRknEKVLEYCEQKGIAFIPWYPLASGALAK------------PGTILDAVSKDLDRSTSQIALSWVLQRSPVMlpIP 259
Cdd:cd19114 185 YLQQ--KRLIDWAKKQGIQITAYSSFGNAVYTKvtkhlkhftnllEHPVVKKLADKHKRDTGQVLLRWAVQRNITV--IP 260
|
250 260
....*....|....*....|....*....
gi 19113480 260 GTSKVDHLEENVKAAGIQLSSEVFAKLDE 288
Cdd:cd19114 261 KSVNVERMKTNLDITSYKLDEEDMEALYE 289
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
122-288 |
1.58e-04 |
|
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: 42.52 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 122 SMRRLGVKQIDLWQLH--------RIDPKVPRK--------------DQFSEIAAMKKEGLIRHVGLSEVTvddIKEAEQ 179
Cdd:cd19121 92 SLKSLGLDYVDLYLVHwpvllnpnGNHDLFPTLpdgsrdldwdwnhvDTWKQMEKVLKTGKTKAIGVSNYS---IPYLEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 180 YFPVVSVQNLFNLVNRK----NEKVLEYCEQKGIAFIPWYPLAS--GALAKPGTILdAVSKDLDRSTSQIALSWVLQRSP 253
Cdd:cd19121 169 LLKHATVVPAVNQVENHpylpQQELVDFCKEKGILIEAYSPLGStgSPLISDEPVV-EIAKKHNVGPGTVLISYQVARGA 247
|
170 180 190
....*....|....*....|....*....|....*
gi 19113480 254 VMlpIPGTSKVDHLEENVKAagIQLSSEVFAKLDE 288
Cdd:cd19121 248 VV--LPKSVTPDRIKSNLEI--IDLDDEDMNKLND 278
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
199-287 |
2.35e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 42.22 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 199 KVLEYCEQKGIAFIPWYPLASGA------------LAKPgtILDAVSKDLDRSTSQIALSWVLQRSPVMLpipGTS-KVD 265
Cdd:cd19108 196 KLLDFCKSKDIVLVAYSALGSQRdkewvdqnspvlLEDP--VLCALAKKHKRTPALIALRYQLQRGVVVL---AKSfNEK 270
|
90 100
....*....|....*....|..
gi 19113480 266 HLEENVKAAGIQLSSEVFAKLD 287
Cdd:cd19108 271 RIKENLQVFEFQLTSEDMKALD 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
106-281 |
3.74e-04 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 41.48 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 106 WHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLH---------------RIDPKVPRKDQFSEI-AAMKK---EGLIRHVGL 166
Cdd:cd19110 71 WCTCHKKSLVKTACTRSLKALKLNYLDLYLIHwpmgfkpgepdlpldRSGMVIPSDTDFLDTwEAMEDlviEGLVKNIGV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 167 SEVTVDDI-----KEAEQYFPVVSVQNLFNLVNRKneKVLEYCEQKGIAFIPWYPLASGALAKP---GTILDAVSKDLDR 238
Cdd:cd19110 151 SNFNHEQLerllnKPGLRVKPVTNQIECHPYLTQK--KLISFCQSRNVSVTAYRPLGGSCEGVDlidDPVIQRIAKKHGK 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19113480 239 STSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSE 281
Cdd:cd19110 229 SPAQILIRFQIQRNVIV--IPKSVTPSRIKENIQVFDFELTEH 269
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
33-289 |
4.30e-04 |
|
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: 41.28 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 33 MRVTGDGIWDepKDKEACIATLKRLPELNINFIDTADSYG--PEVSENL---LREALYPYKGLIIATKgglvrtgpnEWH 107
Cdd:cd19113 11 MPSVGFGCWK--LDNATAADQIYQAIKAGYRLFDGAEDYGneKEVGEGVnraIDEGLVKREELFLTSK---------LWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 108 PCGAPKFLRQEVLMSMRRLGVKQIDLWQLH--------RIDPKVP------RKDQFSE-----------IAAMKKEGLIR 162
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvPIEEKYPpgfycgDGDNFVYedvpildtwkaLEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 163 HVGLSEVT----VDDIKEAEQYFPVVSVQNLFNLVNrknEKVLEYCEQKGIA------FIP--WYPLASGALAKPGTILD 230
Cdd:cd19113 160 SIGVSNFPgaliLDLLRGATIKPAVLQIEHHPYLQQ---PKLIEYAQKAGITitayssFGPqsFVELNQGRALNTPTLFE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113480 231 -----AVSKDLDRSTSQIALSWVLQRSPVMlpIPGTSKVDHLEENVKAAGIQLSSEVF---AKLDEE 289
Cdd:cd19113 237 hdtikSIAAKHNKTPAQVLLRWATQRGIAV--IPKSNLPERLLQNLSVNDFDLTKEDFeeiAKLDIG 301
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
108-290 |
4.26e-03 |
|
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: 38.25 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 108 PCGAPKFLRQEVLMSMRRLGVKQIDLWQlhridpkvprkdQFSEIaamKKEGLIRHVGLSEVTVDDIKEAEQYFPVVSVQ 187
Cdd:cd19119 121 DSGKPFTPVNDDGKTRYAASGDHITTYK------------QLEKI---YLDGRAKAIGVSNYSIVYLERLIKECKVVPAV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113480 188 NLFNLVNRKNEKVL-EYCEQKGIAFIPWYPLAS-GALAKPGTILDAVSKDLDRSTSQIALSW-VLQRSPVmlpIPGTSKV 264
Cdd:cd19119 186 NQVELHPHLPQMDLrDFCFKHGILVTAYSPLGShGAPNLKNPLVKKIAEKYNVSTGDILISYhVRQGVIV---LPKSLKP 262
|
170 180
....*....|....*....|....*.
gi 19113480 265 DHLEENVKAAGiqLSSEVFAKLDEEG 290
Cdd:cd19119 263 VRIVSNGKIVS--LTKEDLQKLDDIG 286
|
|
| |
