|
Name |
Accession |
Description |
Interval |
E-value |
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
3-298 |
3.08e-172 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 478.49 E-value: 3.08e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 3 ERILMAPQGPTFSRLVMGYWRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVT 82
Cdd:COG4989 2 KRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 83 KCGI-ATTAKPENVIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFT 161
Cdd:COG4989 82 KCGIrLPSEARDNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 162 PAQFSLLQSRLPFTLATNQVEISPVHQPLLLDGTLDLLQQLRIRPMAWSCLGGGRLFS--DESFAPLRAELHQVAEETGA 239
Cdd:COG4989 162 PSQFELLQSALDQPLVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGgfDEQFPRLRAALDELAEKYGV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 240 qTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAALGYDVP 298
Cdd:COG4989 242 -SPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREEWYELYEAARGHEVP 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-292 |
1.09e-159 |
|
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: 446.23 E-value: 1.09e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 9 PQGPTFSRLVMGYWRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIAT 88
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 89 T-AKPENVIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSL 167
Cdd:cd19092 81 GdDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 168 LQSRLPFTLATNQVEISPVHQPLLLDGTLDLLQQLRIRPMAWSCLGGGRLFS--DESFAPLRAELHQVAEETGAqTIEQV 245
Cdd:cd19092 161 LQSYLDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGgfDERFQRLRAALEELAEEYGV-TIEAI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495142658 246 VYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAA 292
Cdd:cd19092 240 ALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYEIYEAA 286
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
11-298 |
9.87e-53 |
|
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: 174.98 E-value: 9.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLVMGYWRL--MEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlaPHLRDKMEIVTKCGIAT 88
Cdd:COG0667 10 GLKVSRLGLGTMTFggPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVIATKVGRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 89 TAKPENVIGHyiteRAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLL 168
Cdd:COG0667 88 GPGPNGRGLS----REHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 169 QSRLPFT--LATNQVEISPVHQpLLLDGTLDLLQQLRIRPMAWSCLGGGRL------------------------FSDES 222
Cdd:COG0667 164 LAIAEGLppIVAVQNEYSLLDR-SAEEELLPAARELGVGVLAYSPLAGGLLtgkyrrgatfpegdraatnfvqgyLTERN 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142658 223 FAPLRAeLHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAALGYDVP 298
Cdd:COG0667 243 LALVDA-LRAIAAEHGV-TPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAAVPAP 316
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-274 |
1.50e-52 |
|
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: 171.93 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRLMeWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlAPHLRDKMEIVTKCGiattAKPEN 94
Cdd:cd06660 1 SRLGLGTMTFG-GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLK-GRGNRDDVVIATKGG----HPPGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 95 VIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPF 174
Cdd:cd06660 75 DPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 175 T----LATNQVEISPVHQPLLLDGTLDLLQQLRIRPMAWSCLGGGrlfsdesfaplraelhqvaeetgaqtIEQVVYAWV 250
Cdd:cd06660 155 HglpgFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------PAQLALAWL 208
|
250 260
....*....|....*....|....
gi 495142658 251 MRLPSRPLPIIGSGKIDRVKSAVG 274
Cdd:cd06660 209 LSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-292 |
1.68e-50 |
|
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: 168.26 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 17 LVMGYWRL--MEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPEN 94
Cdd:pfam00248 1 IGLGTWQLggGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 95 VighyitERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPF 174
Cdd:pfam00248 81 G------SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 175 TLATNQVEISPVhQPLLLDGTLDLLQQLRIRPMAWSCLGGGRL--------------------FSDESFAPLRAELHQVA 234
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLtgkytrdpdkgpgerrrllkKGTPLNLEALEALEEIA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 235 EETGaQTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAA 292
Cdd:pfam00248 234 KEHG-VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-289 |
1.98e-42 |
|
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: 147.67 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLVMGYWRL---MEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGIa 87
Cdd:cd19084 1 DLKVSRIGLGTWAIggtWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALK---GRRDDVVIATKCGL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 88 ttaKPEN-VIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFS 166
Cdd:cd19084 77 ---RWDGgKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 167 LLQSRLPFtlATNQVEISPVHQpLLLDGTLDLLQQLRIRPMAWSCLGGGRL---------------------FSDESFA- 224
Cdd:cd19084 154 EARKYGPI--VSLQPPYSMLER-EIEEELLPYCRENGIGVLPYGPLAQGLLtgkykkeptfppddrrsrfpfFRGENFEk 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142658 225 --PLRAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIR 289
Cdd:cd19084 231 nlEIVDKLKEIAEKYGK-SLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
42-295 |
6.59e-39 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 137.11 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKcgIATT-AKPENVIghyiterahivQSAENSLRHLHTD 120
Cdd:COG0656 28 LEAGYRHIDTAAMYGN---EEGVGEAIAASGVPREELFVTTK--VWNDnHGYDDTL-----------AAFEESLERLGLD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 121 VLDLLLIHRP--DPLMDAdeiAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPVHQPllldgtldl 198
Cdd:COG0656 92 YLDLYLIHWPgpGPYVET---WRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 199 lQQLR-------IRPMAWSCLGGGRLFSDEsfaplraELHQVAEETGAqTIEQVVYAWVMRLPSRPLPiiGSGKIDRVKS 271
Cdd:COG0656 160 -RELLafcrehgIVVEAYSPLGRGKLLDDP-------VLAEIAEKHGK-TPAQVVLRWHLQRGVVVIP--KSVTPERIRE 228
|
250 260
....*....|....*....|....
gi 495142658 272 AVGALSIEMSRQQWFRIRKAALGY 295
Cdd:COG0656 229 NLDAFDFELSDEDMAAIDALDRGE 252
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-289 |
4.11e-35 |
|
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: 127.35 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 13 TFSRLVMGYWRLME-WNYSARELVGFIEQ---HLELGITTVDHADIYGNYQCEAAFGEALRlaPHLRDKMEIVTKCGIaT 88
Cdd:cd19072 3 EVPVLGLGTWGIGGgMSKDYSDDKKAIEAlryAIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFITTKVSP-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 89 TAKPENVIghyiterahivQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLL 168
Cdd:cd19072 80 HLKYDDVI-----------KAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 169 QSRL-PFTLATNQVEISPVHQpLLLDGTLDLLQQLRIRPMAWSCLGGGRLfsdeSFAPLRAELHQVAEETGAqTIEQVVY 247
Cdd:cd19072 149 QSYLkKGPIVANQVEYNLFDR-EEESGLLPYCQKNGIAIIAYSPLEKGKL----SNAKGSPLLDEIAKKYGK-TPAQIAL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 495142658 248 AWVMRLPsRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIR 289
Cdd:cd19072 223 NWLISKP-NVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
27-284 |
3.82e-34 |
|
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: 124.52 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGiATTAKPENVIghyiterahi 106
Cdd:cd19071 9 YKLKPEETAEAVLAALEAGYRHIDTAAAYGN---EAEVGEAIRESGVPREELFITTKLW-PTDHGYERVR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 107 vQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIA------EAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQ 180
Cdd:cd19071 75 -EALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEarletwRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 181 VEISPVHQPllldgtldllQQLR-------IRPMAWSCLGGGR--LFSDEsfaplraELHQVAEETGAqTIEQVVYAWVM 251
Cdd:cd19071 154 IELHPYLQQ----------KELVefckehgIVVQAYSPLGRGRrpLLDDP-------VLKEIAKKYGK-TPAQVLLRWAL 215
|
250 260 270
....*....|....*....|....*....|...
gi 495142658 252 RLPSRPLPiiGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19071 216 QRGVVVIP--KSSNPERIKENLDVFDFELSEED 246
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
11-281 |
5.08e-34 |
|
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: 125.77 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLV---MGY----WRlmEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALR-LAPhlRDKMEIVT 82
Cdd:cd19079 9 GLKVSRLClgcMSFgdpkWR--PWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKeFAP--RDEVVIAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 83 KCGIATTAKPENvighYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTP 162
Cdd:cd19079 85 KVYFPMGDGPNG----RGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 163 AQF------SLLQSRLPFTLATNQV---------EISPVhqpllldgtldlLQQLRIRPMAWSCLGGGRL---------- 217
Cdd:cd19079 161 WQFakalhlAEKNGWTKFVSMQNHYnllyreeerEMIPL------------CEEEGIGVIPWSPLARGRLarpwgdtter 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142658 218 -------------FSDESFAPLRAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19079 229 rrsttdtaklkydYFTEADKEIVDRVEEVAKERGV-SMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLS 304
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-288 |
3.96e-32 |
|
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: 119.66 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 9 PQGPTFSRLVMGYWRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKcgiat 88
Cdd:cd19138 6 PDGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIR---GRRDKVFLVSK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 89 tAKPENvighyiTERAHIVQSAENSLRHLHTDVLDLLLIHRPD--PLmdaDEIAEAFLELHKSGKVRHFGVSNFTPAQFS 166
Cdd:cd19138 78 -VLPSN------ASRQGTVRACERSLRRLGTDYLDLYLLHWRGgvPL---AETVAAMEELKKEGKIRAWGVSNFDTDDME 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 167 LLQsRLPF--TLATNQVEISPVHQ-------PllldgtldLLQQLRIRPMAWSCLGGGRLFSDESFAplRAELHQVAEET 237
Cdd:cd19138 148 ELW-AVPGggNCAANQVLYNLGSRgieydllP--------WCREHGVPVMAYSPLAQGGLLRRGLLE--NPTLKEIAARH 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495142658 238 GAqTIEQVVYAWVMRLPSrPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRI 288
Cdd:cd19138 217 GA-TPAQVALAWVLRDGN-VIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
42-281 |
8.18e-32 |
|
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: 118.47 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRLAPhlrDKMEIVTKCGIA-TTAKPENVIGHyiteRAHIVQSAENSLRHLHTD 120
Cdd:cd19088 34 LELGVNFIDTADSYGPDVNERLIAEALHPYP---DDVVIATKGGLVrTGPGWWGPDGS----PEYLRQAVEASLRRLGLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 121 VLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQfsLLQSRLPFTLATNQVEISPVHQplLLDGTLDLLQ 200
Cdd:cd19088 107 RIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQ--IEEARAIVRIVSVQNRYNLANR--DDEGVLDYCE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 201 QLRIRPMAWSCLGGGRLfsdesfAPLRAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEM 280
Cdd:cd19088 183 AAGIAFIPWFPLGGGDL------AQPGGLLAEVAARLGA-TPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRL 255
|
.
gi 495142658 281 S 281
Cdd:cd19088 256 S 256
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
42-277 |
2.82e-31 |
|
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: 118.04 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNY----QCEAAFGEALRlAPHLRDKMEIVTKCGIATTAKPEnviGHYITERAhIVQSAENSLRHL 117
Cdd:cd19082 27 VELGGNFIDTARVYGDWvergASERVIGEWLK-SRGNRDKVVIATKGGHPDLEDMS---RSRLSPED-IRADLEESLERL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 118 HTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPA----------------------QFSLLQSRLPFT 175
Cdd:cd19082 102 GTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTEriaeanayakahglpgfaasspQWSLARPNEPPW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 176 LATNQVEISPvhqpllldGTLDLLQQLRIRPMAWSCLGGG------------------RLFSDESFAplRAE-LHQVAEE 236
Cdd:cd19082 182 PGPTLVAMDE--------EMRAWHEENQLPVFAYSSQARGffskraaggaeddselrrVYYSEENFE--RLErAKELAEE 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495142658 237 TGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALS 277
Cdd:cd19082 252 KGV-SPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
15-281 |
2.85e-31 |
|
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: 118.07 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRL----MEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGiatta 90
Cdd:cd19085 2 SRLGLGCWQFgggyWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALK---GRRDDVVIATKVS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 91 kPENvighyiTERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQS 170
Cdd:cd19085 74 -PDN------LTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 171 RLPFTlaTNQV-----------EISPVhqpllldgtldlLQQLRIRPMAWSCLG----GGRLFSDESFAP---------- 225
Cdd:cd19085 147 AGRID--SNQLpynllwraieyEILPF------------CREHGIGVLAYSPLAqgllTGKFSSAEDFPPgdartrlfrh 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142658 226 -----------LRAELHQVAEETGaQTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19085 213 fepgaeeetfeALEKLKEIADELG-VTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELS 278
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
18-291 |
2.96e-31 |
|
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: 118.10 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 18 VMGywrlMEWNYSA----RELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALrlAPhLRDKMEIVTKCGIaTTAKPE 93
Cdd:cd19078 11 CMG----MSHGYGPppdkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEAL--KP-FRDQVVIATKFGF-KIDGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 94 NVIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQF-------- 165
Cdd:cd19078 83 PGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIrrahavcp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 166 -SLLQSRLPFTLATNQVEISPVhqpllldgtldlLQQLRIRPMAWSCLGGGRL---------------------FSDESF 223
Cdd:cd19078 163 vTAVQSEYSMMWREPEKEVLPT------------LEELGIGFVPFSPLGKGFLtgkidentkfdegddraslprFTPEAL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142658 224 A---PLRAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKA 291
Cdd:cd19078 231 EanqALVDLLKEFAEEKGA-TPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDA 300
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
19-289 |
3.12e-31 |
|
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: 116.60 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 19 MGYWRLmewnySARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKcgIATTA-KPENVIg 97
Cdd:cd19073 6 LGTWQL-----RGDDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTK--VWRDHlRPEDLK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 98 hyiterahivQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLA 177
Cdd:cd19073 75 ----------KSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 178 TNQVEISPVHQPlllDGTLDLLQQLRIRPMAWSCLGGGRLFSDEsfaplraELHQVAEETGAqTIEQVVYAWVMRLPSRP 257
Cdd:cd19073 145 VNQVEFHPFLYQ---AELLEYCRENDIVITAYSPLARGEVLRDP-------VIQEIAEKYDK-TPAQVALRWLVQKGIVV 213
|
250 260 270
....*....|....*....|....*....|..
gi 495142658 258 LPiiGSGKIDRVKSAVGALSIEMSRQQWFRIR 289
Cdd:cd19073 214 IP--KASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
27-252 |
1.37e-30 |
|
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: 115.43 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPEnvighyiterahI 106
Cdd:cd19140 16 YPLTGEECTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKVWPDNYSPDD------------F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 107 VQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPV 186
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142658 187 HQPlllDGTLDLLQQLRIRPMAWSCLGGGRLFSDESFAPLrAELHqvaeetgAQTIEQVVYAWVMR 252
Cdd:cd19140 161 LDQ---RKLLDAAREHGIALTAYSPLARGEVLKDPVLQEI-GRKH-------GKTPAQVALRWLLQ 215
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
31-284 |
1.43e-30 |
|
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: 116.94 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 31 ARELVGFIeqhLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGIATTAKPeNVIGhyiTERAHIVQSA 110
Cdd:cd19091 41 ADRLVDIA---LDAGINFFDTADVYSEGESEEILGKALK---GRRDDVLIATKVRGRMGEGP-NDVG---LSRHHIIRAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 111 ENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQS---RLPFT-LATNQV----- 181
Cdd:cd19091 111 EASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGiseRRGLArFVALQAyysll 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 182 ------EISPVhqpllldgtlDLLQQLRIrpMAWSCLGGGRL-------------------------FSDESFAPLRAEL 230
Cdd:cd19091 191 grdlehELMPL----------ALDQGVGL--LVWSPLAGGLLsgkyrrgqpapegsrlrrtgfdfppVDRERGYDVVDAL 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 495142658 231 HQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19091 259 REIAKETGA-TPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEE 311
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-292 |
2.24e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 113.15 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 20 GYWRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGIATTAkpENVIGHY 99
Cdd:cd19102 14 GGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK---GLRDRPIVATKCGLLWDE--EGRIRRS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 100 ITeRAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPftLATN 179
Cdd:cd19102 89 LK-PASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHP--IASL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 180 QVEISPVHQPLLLDGTLDLLQQlRIRPMAWSCLGGG-----------------------RLFSDESFAP---LRAELHQV 233
Cdd:cd19102 166 QPPYSLLRRGIEAEILPFCAEH-GIGVIVYSPMQSGlltgkmtpervaslpaddwrrrsPFFQEPNLARnlaLVDALRPI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 234 AEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAA 292
Cdd:cd19102 245 AERHGR-TVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
15-289 |
3.28e-29 |
|
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: 112.71 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYW-----RLMEWN-YSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHlRDKMEIVTKcgIAT 88
Cdd:cd19093 3 SPLGLGTWqwgdrLWWGYGeYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGD-RDEVVIATK--FAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 89 TakpenvigHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDP-LMDADEIAEAFLELHKSGKVRHFGVSNFTPAQF-- 165
Cdd:cd19093 80 L--------PWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLrr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 166 ---SLLQSRLPftLATNQVEISPVHQPLLLDGTLDLLQQLRIRPMAWSCLGGGRL-----------------FSDESF-- 223
Cdd:cd19093 152 ahkALKERGVP--LASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLtgkyspenpppggrrrlFGRKNLek 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142658 224 -APLRAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKidRVKSAVGALSIEMSRQQWFRIR 289
Cdd:cd19093 230 vQPLLDALEEIAEKYGK-TPAQVALNWLIAKGVVPIPGAKNAE--QAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
15-180 |
5.79e-29 |
|
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: 112.40 E-value: 5.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRLMEWNYSA---RELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHlRDKMEIVTKCGIATTak 91
Cdd:cd19148 5 SRIALGTWAIGGWMWGGtdeKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGK-RDRVVIATKVGLEWD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 92 pENVIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSR 171
Cdd:cd19148 82 -EGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKV 160
|
....*....
gi 495142658 172 LPftLATNQ 180
Cdd:cd19148 161 AP--LHTVQ 167
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
10-281 |
7.73e-29 |
|
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: 111.92 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 10 QGPTFSRL---VMGywrlMEWNYSAR---ELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTK 83
Cdd:cd19076 8 QGLEVSALglgCMG----MSAFYGPAdeeESIATLHRALELGVTFLDTADMYGPGTNEELLGKALK---DRRDEVVIATK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 84 CGIATTAKPENVI--GhyitERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFT 161
Cdd:cd19076 81 FGIVRDPGSGFRGvdG----RPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 162 PAQF---------SLLQSRlpFTLATNQVE--ISPVhqpllldgtldlLQQLRIRPMAWSCLGGGRL------------- 217
Cdd:cd19076 157 ADTIrrahavhpiTAVQSE--YSLWTRDIEdeVLPT------------CRELGIGFVAYSPLGRGFLtgaikspedlped 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142658 218 --------FSDESFA---PLRAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19076 223 dfrrnnprFQGENFDknlKLVEKLEAIAAEKGC-TPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLT 296
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
42-281 |
9.19e-29 |
|
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: 111.90 E-value: 9.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALrlAPHlRDKMEIVTKCGIATTAKPeNVIGhyiTERAHIVQSAENSLRHLHTDV 121
Cdd:cd19087 40 LDAGINFFDTADVYGGGRSEEIIGRWI--AGR-RDDIVLATKVFGPMGDDP-NDRG---LSRRHIRRAVEASLRRLQTDY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQ---------------FSLLQSrlPFTLATNQ--VEIS 184
Cdd:cd19087 113 IDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQiakaqgiaarrgllrFVSEQP--MYNLLKRQaeLEIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 185 PVhqpllldgtldlLQQLRIRPMAWSCLGGGRL------------------------FSDESFAPLRAELHQVAEETGaQ 240
Cdd:cd19087 191 PA------------ARAYGLGVIPYSPLAGGLLtgkygkgkrpesgrlveraryqarYGLEEYRDIAERFEALAAEAG-L 257
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495142658 241 TIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19087 258 TPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLT 298
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-284 |
2.23e-28 |
|
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: 109.58 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLVMGYWRL---MEWNYSA-RELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKcgi 86
Cdd:cd19137 1 GEKIPALGLGTWGIggfLTPDYSRdEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP--REDLFIVTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 87 attAKPENVighyitERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFS 166
Cdd:cd19137 76 ---VWPTNL------RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 167 LLQSRLPFTLATNQVEISPVHQPLLLDGTLDLLQQLRIRPMAWSCLgggrlfsDESFAPLRAELHQVAEETGAqTIEQVV 246
Cdd:cd19137 147 EAISKSQTPIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPL-------RRGLEKTNRTLEEIAKNYGK-TIAQIA 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 495142658 247 YAWVMRLPSrPLPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19137 219 LAWLIQKPN-VVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
11-288 |
2.47e-28 |
|
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: 110.77 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLVMGYWRLMEW---NYSARELVGFIEqhleLGITTVDHADIYGNYQCEAAFGEALR-----LAPHL-RDKMEIV 81
Cdd:cd19081 6 GLSVSPLCLGTMVFGWTadeETSFALLDAFVD----AGGNFIDTADVYSAWVPGNAGGESETiigrwLKSRGkRDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 82 TKCGIATTAkpenviGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFT 161
Cdd:cd19081 82 TKVGFPMGP------NGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 162 PAQF--SLLQSR----LPFTLAtnQVEISPVHQPLLLDGTLDLLQQLRIRPMAWSCLGGG-------------------- 215
Cdd:cd19081 156 AWRLqeALELSRqhglPRYVSL--QPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrge 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142658 216 ---RLFSDESFAPLrAELHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRI 288
Cdd:cd19081 234 aakRYLNERGLRIL-DALDEVAAEHGA-TPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-284 |
2.48e-27 |
|
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: 108.08 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGIATTAKPENVIGHYiteRAHIVQSAENSLRHLHTDV 121
Cdd:cd19080 41 VEAGGNFIDTANNYTNGTSERLLGEFIA---GNRDRIVLATKYTMNRRPGDPNAGGNH---RKNLRRSVEASLRRLQTDY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNfTPA----------------QFSLLQsrLPFTLA--TNQVEI 183
Cdd:cd19080 115 IDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISD-TPAwvvarantlaelrgwsPFVALQ--IEYSLLerTPEREL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 184 SPVhqpllldgtldlLQQLRIRPMAWSCLGGGRL------------------------FSDESFApLRAELHQVAEETGA 239
Cdd:cd19080 192 LPM------------ARALGLGVTPWSPLGGGLLtgkyqrgeegrageakgvtvgfgkLTERNWA-IVDVVAAVAEELGR 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495142658 240 qTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19080 259 -SAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQ 302
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
42-293 |
4.01e-27 |
|
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: 105.90 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPEnvighyiterahIVQSAENSLRHLHTDV 121
Cdd:cd19139 24 LELGYRHIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWIDNLSKDK------------LLPSLEESLEKLRTDY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPDP--LMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRL-PFTLATNQVEISPVHQpllLDGTLDL 198
Cdd:cd19139 89 VDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVgAGAIATNQIELSPYLQ---NRKLVAH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 199 LQQLRIRPMAWSCLGGGRLFSDESFAplraelhQVAEETGAqTIEQVVYAWVMRLPSRPLPiiGSGKIDRVKSAVGALSI 278
Cdd:cd19139 166 CKQHGIHVTSYMTLAYGKVLDDPVLA-------AIAERHGA-TPAQIALAWAMARGYAVIP--SSTKREHLRSNLLALDL 235
|
250
....*....|....*
gi 495142658 279 EMSRQQWFRIrkAAL 293
Cdd:cd19139 236 TLDADDMAAI--AAL 248
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
27-249 |
1.44e-26 |
|
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: 104.76 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTakpenviGHYITERAHi 106
Cdd:cd19131 18 WQVSNDEAASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTKLWNSDQ-------GYDSTLRAF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 107 vqsaENSLRHLHTDVLDLLLIHRPDPLMDA-DEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISP 185
Cdd:cd19131 87 ----DESLRKLGLDYVDLYLIHWPVPAQDKyVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIELHP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142658 186 VHQpllLDGTLDLLQQLRIRPMAWSCLGGGRLFSDESfaplraeLHQVAEETGAqTIEQVVYAW 249
Cdd:cd19131 163 RFQ---QRELRAFHAKHGIQTESWSPLGQGGLLSDPV-------IGEIAEKHGK-TPAQVVIRW 215
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-295 |
6.53e-26 |
|
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: 103.08 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 22 WRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKcgiattakpenvighYIT 101
Cdd:cd19120 15 WYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTK---------------VSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 102 ERAHIVQSAENSLRHLHTDVLDLLLIHRP----DPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQF-SLLQSRlPFTL 176
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLeELLDTA-KIKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 177 ATNQVEISPvHQPLLLDGTLDLLQQLRIRPMAWSCLGGGRLFSDEsfaPLRAELHQVAEETGAqTIEQVVYAWVmrLPSR 256
Cdd:cd19120 156 AVNQIEFHP-YLYPQQPALLEYCREHGIVVSAYSPLSPLTRDAGG---PLDPVLEKIAEKYGV-TPAQVLLRWA--LQKG 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 495142658 257 PLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAALGY 295
Cdd:cd19120 229 IVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQK 267
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-259 |
1.25e-24 |
|
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: 99.65 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLVMGYWRLMewnysARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKcgiatta 90
Cdd:cd19132 4 GTQIPAIGFGTYPLK-----GDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTK------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 91 kpenvighyITERAH----IVQSAENSLRHLHTDVLDLLLIHRPDPLMDA-DEIAEAFLELHKSGKVRHFGVSNFTPAQF 165
Cdd:cd19132 69 ---------LPGRHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNPSRDLyVEAWQALIEAREEGLVRSIGVSNFLPEHL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 166 SLLQSRLPFTLATNQVEISPVHQpllLDGTLDLLQQLRIRPMAWSCLGGG-RLFSDESFAplraelhQVAEETGAqTIEQ 244
Cdd:cd19132 140 DRLIDETGVTPAVNQIELHPYFP---QAEQRAYHREHGIVTQSWSPLGRGsGLLDEPVIK-------AIAEKHGK-TPAQ 208
|
250
....*....|....*
gi 495142658 245 VVYAWVMRLPSRPLP 259
Cdd:cd19132 209 VVLRWHVQLGVVPIP 223
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
42-281 |
1.78e-24 |
|
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: 99.97 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRlaPHLRDKMEIVTKCGIATTAKPEnvigHYITERAHIVQSAENSLRHLHTDV 121
Cdd:cd19074 32 YDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGPGPN----DRGLSRKHIFESIHASLKRLQLDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQF----SLLQSRLPFTLATNQVEISPVHQPLLLDGTLD 197
Cdd:cd19074 106 VDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIaeahDLARQFGLIPPVVEQPQYNMLWREIEEEVIPL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 198 LLQQlRIRPMAWSCLGGG----------------------------RLFSDESFAPLRaELHQVAEETGAqTIEQVVYAW 249
Cdd:cd19074 186 CEKN-GIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrRLLTDENLEKVK-KLKPIADELGL-TLAQLALAW 262
|
250 260 270
....*....|....*....|....*....|..
gi 495142658 250 VMRLPSRPLPIIGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19074 263 CLRNPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-158 |
1.99e-24 |
|
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: 98.70 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRL---MEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGiaTTAK 91
Cdd:cd19086 4 SEIGFGTWGLggdWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALK---GRRDKVVIATKFG--NRFD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 92 PENVIGHYiTERAHIVQSAENSLRHLHTDVLDLLLIHRP-DPLMDADEIAEAFLELHKSGKVRHFGVS 158
Cdd:cd19086 79 GGPERPQD-FSPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVS 145
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-158 |
5.20e-24 |
|
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: 97.66 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 29 YSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKCgiattakpenVIGHYITERAHIVQ 108
Cdd:cd19105 22 GLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLR--RDKVFLATKA----------SPRLDKKDKAELLK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 495142658 109 SAENSLRHLHTDVLDLLLIHR---PDPLMDADEIAEAFLELHKSGKVRHFGVS 158
Cdd:cd19105 90 SVEESLKRLQTDYIDIYQLHGvdtPEERLLNEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
42-298 |
8.42e-24 |
|
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: 98.67 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYqcEAAFGEALRLAPHLRDKMEIVTKCGIatTAKPENVIGHYITERAHIVQSAENSLRHLHTDV 121
Cdd:cd19144 44 FELGCTFWDTADIYGDS--EELIGRWFKQNPGKREKIFLATKFGI--EKNVETGEYSVDGSPEYVKKACETSLKRLGVDY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAqfSLLQSRLPFTLATNQVEISP----VHQPllLDGTLD 197
Cdd:cd19144 120 IDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAE--TLRRAHAVHPIAAVQIEYSPfsldIERP--EIGVLD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 198 LLQQLRIRPMAWSCLG----GGRLFSDESFAP--------------------LRAELHQVAEETGAqTIEQVVYAWVMRL 253
Cdd:cd19144 196 TCRELGVAIVAYSPLGrgflTGAIRSPDDFEEgdfrrmaprfqaenfpknleLVDKIKAIAKKKNV-TAGQLTLAWLLAQ 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495142658 254 PSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAALGYDVP 298
Cdd:cd19144 275 GDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEVV 319
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
18-275 |
1.16e-23 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 96.92 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 18 VMGYWRlMEWNYSARELVGFIEQHLELGITTVDHADIYGNyqCEAAFGEALrlAPHLRDKMEIVTKCGiattAKPENVIG 97
Cdd:cd19095 7 TSGIGR-VWGVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRAL--AGLRRDDLFIATKVG----THGEGGRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 98 HYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAqfsllqsrLPFTLA 177
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE--------LEAAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 178 TN-----QVEISPVHQpllldgtldllQQLRIRPMAWSC---------LGGGRLFSDESFAPLRAELHQV---AEETGAQ 240
Cdd:cd19095 150 SGvfdvvQLPYNVLDR-----------EEEELLPLAAEAglgvivnrpLANGRLRRRVRRRPLYADYARRpefAAEIGGA 218
|
250 260 270
....*....|....*....|....*....|....*
gi 495142658 241 TIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGA 275
Cdd:cd19095 219 TWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
42-293 |
1.25e-23 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 97.02 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTAKpenvighyiterAHIVQSAENSLRHLHTDV 121
Cdd:PRK11172 26 LELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWIDNLAK------------DKLIPSLKESLQKLRTDY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPDP--LMDADEIAEAFLELHKSGKVRHFGVSNFTPAqfsLLQSRL----PFTLATNQVEISPVHQpllLDGT 195
Cdd:PRK11172 91 VDLTLIHWPSPndEVSVEEFMQALLEAKKQGLTREIGISNFTIA---LMKQAIaavgAENIATNQIELSPYLQ---NRKV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 196 LDLLQQLRIRPMAWSCLGGGRLFSDESFAplraelhQVAEETGAqTIEQVVYAWVMRLPSRPLPiiGSGKIDRVKSAVGA 275
Cdd:PRK11172 165 VAFAKEHGIHVTSYMTLAYGKVLKDPVIA-------RIAAKHNA-TPAQVILAWAMQLGYSVIP--SSTKRENLASNLLA 234
|
250
....*....|....*...
gi 495142658 276 LSIEMSRQQWFRIrkAAL 293
Cdd:PRK11172 235 QDLQLDAEDMAAI--AAL 250
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-290 |
1.89e-23 |
|
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: 97.73 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRL---MEWNYS-ARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGI---- 86
Cdd:cd19149 12 SVIGLGTWAIgggPWWGGSdDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIK---GRRDKVVLATKCGLrwdr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 87 ATTAKPENVIGHYI---TERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPA 163
Cdd:cd19149 89 EGGSFFFVRDGVTVyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 164 QF---------SLLQSR------------LPFTlATNQVEI---SPVHQPLLLDgtldllqqlRIRPMAWSCLGGGR--- 216
Cdd:cd19149 169 QIkeyvkagqlDIIQEKysmldrgiekelLPYC-KKNNIAFqaySPLEQGLLTG---------KITPDREFDAGDARsgi 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 217 -LFSDESFAPLRAELHQ---VAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRK 290
Cdd:cd19149 239 pWFSPENREKVLALLEKwkpLCEKYGC-TLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-277 |
2.22e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 97.02 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNY-------QCEAAFGEALRlAPHLRDKMEIVTKCGIATTAKPENVIGHYITERAHIVQSA 110
Cdd:cd19752 23 LDRYVAAGGNFLDTANNYAFWteggvggESERLIGRWLK-DRGNRDDVVIATKVGAGPRDPDGGPESPEGLSAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 111 ENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTP----------------------AQFSLL 168
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAwrlerarqiarqqgwaefsaiqQRHSYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 169 QSRLPFTLATnQVEISPVHQpllldgtldllQQLRIRP----MAWSCLGGG------RLFSD-----ESFAPLRAeLHQV 233
Cdd:cd19752 182 RPRPGADFGV-QRIVTDELL-----------DYASSRPdltlLAYSPLLSGaytrpdRPLPEqydgpDSDARLAV-LEEV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 495142658 234 AEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALS 277
Cdd:cd19752 249 AGELGA-TPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
32-281 |
7.92e-22 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 92.87 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 32 RELVgfiEQHLELGITTVDHADIYGNYQCEAAFGEALRLaphlRDKMEIVtkcgIATTAKPENVIGHYI--TERAHIVQS 109
Cdd:cd19083 36 KDLV---REALDNGVNLLDTAFIYGLGRSEELVGEVLKE----YNRNEVV----IATKGAHKFGGDGSVlnNSPEFLRSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 110 AENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFT----------------PAQFSLLQSR-- 171
Cdd:cd19083 105 VEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSleqlkeankdgyvdvlQGEYNLLQREae 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 172 ---LPFTlATNQVEISPVHqpllldgtldllqqlrirPMAWSCLgGGRLFSDESFAP--LRAE----------------- 229
Cdd:cd19083 185 ediLPYC-VENNISFIPYF------------------PLASGLL-AGKYTKDTKFPDndLRNDkplfkgerfsenldkvd 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495142658 230 -LHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19083 245 kLKSIADEKGV-TVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLT 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-276 |
4.67e-21 |
|
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: 90.78 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRLMEWNYSARELVGFIEQHLELGITtvdHADIYGNY-----QCEAAFGEALRLA-PHLRDKMEIVTKCGIAT 88
Cdd:cd19089 12 PAISLGLWHNFGDYTSPEEARELLRTAFDLGIT---HFDLANNYgpppgSAEENFGRILKRDlRPYRDELVISTKAGYGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 89 TAKPenvIGHYiTERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQF--- 165
Cdd:cd19089 89 WPGP---YGDG-GSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKArra 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 166 -SLLQSR-LPFtlATNQVEISpVHQPLLLDGTLDLLQQLRIRPMAWSCLGGGRL--------------------FSDESF 223
Cdd:cd19089 165 iALLRELgVPL--IIHQPRYS-LLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLtdkylngippdsrraaeskfLTEEAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142658 224 APLRAE----LHQVAEETGaQTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGAL 276
Cdd:cd19089 242 TPEKLEqlrkLNKIAAKRG-QSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
42-249 |
1.18e-20 |
|
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: 88.79 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIAttakpenvigHYITERAHivQSAENSLRHLHTDV 121
Cdd:cd19133 33 IKAGYRLIDTAAAYGN---EEAVGRAIKKSGIPREELFITTKLWIQ----------DAGYEKAK--KAFERSLKRLGLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRPdpLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPVHQpllLDGTLDLLQQ 201
Cdd:cd19133 98 LDLYLIHQP--FGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHPFNQ---QIEAVEFLKK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495142658 202 LRIRPMAWSCLGGGR--LFSDESFAPLrAELHQvaeetgaQTIEQVVYAW 249
Cdd:cd19133 173 YGVQIEAWGPFAEGRnnLFENPVLTEI-AEKYG-------KSVAQVILRW 214
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
43-284 |
3.19e-19 |
|
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: 86.03 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 43 ELGITTVDHADIYGNYQCEAAFGEALRLApHLRDKMEIVTKCGIATTA------KPENVIGHYitERAHIVqSAENSLRH 116
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSETWIGEWMKSR-KNRDQIVIATKFTTDYKAyevgkgKAVNYCGNH--KRSLHV-SVRDSLRK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 117 LHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNfTPA----------------QFSLLQSRLPFTLATNQ 180
Cdd:cd19147 121 LQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSD-TPAwvvsaanyyatahgktPFSVYQGRWNVLNRDFE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 181 VEISPVhqpllldgtldllqqLRIRPMA---WSCLGGGRLFSDESFAPLRAE-----------------------LHQVA 234
Cdd:cd19147 200 RDIIPM---------------ARHFGMAlapWDVLGGGKFQSKKAVEERKKNgeglrsfvggteqtpeevkiseaLEKVA 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495142658 235 EETGAQTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19147 265 EEHGTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEE 314
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-164 |
2.93e-18 |
|
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: 82.99 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 16 RLVMGywrLMEWNYSAR--------ELVGFIeqhLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRdkmeIVTKC--G 85
Cdd:cd19075 2 KIILG---TMTFGSQGRfttaeaaaELLDAF---LERGHTEIDTARVYPDGTSEELLGELGLGERGFK----IDTKAnpG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 86 IATTAKPENVIghyiterahivQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQ 164
Cdd:cd19075 72 VGGGLSPENVR-----------KQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWE 139
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
31-277 |
7.16e-18 |
|
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: 82.07 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 31 ARELvgfIEQHLELGITtvdHADIYGNY-----QCEAAFGEALR--LAPHlRDKMEIVTKCGIATTAKPENVIGhyitER 103
Cdd:cd19151 32 SRAM---LRRAFDLGIT---HFDLANNYgpppgSAEENFGRILKedLKPY-RDELIISTKAGYTMWPGPYGDWG----SK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 104 AHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQ----FSLLQSrlpftLATN 179
Cdd:cd19151 101 KYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEareaAAILKD-----LGTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 180 QVeispVHQPL-------LLDGTLDLLQQLRIRPMAWSCLGGG--------------RLFSDESFapLRAE--------- 229
Cdd:cd19151 176 CL----IHQPKysmfnrwVEEGLLDVLEEEGIGCIAFSPLAQGlltdrylngipedsRAAKGSSF--LKPEqiteeklak 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495142658 230 ---LHQVAEETGaQTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALS 277
Cdd:cd19151 250 vrrLNEIAQARG-QKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-163 |
7.46e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 80.60 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 11 GPTFSRLVMGYWRLMEwnYSARELVGFIEQHLELGITTVDHADIYGNyqCEAAFGEALRlapHLRDKMEIVTKCGiATTA 90
Cdd:cd19100 8 GLKVSRLGFGGGPLGR--LSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALK---GRRDKVFLATKTG-ARDY 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 91 KpenvighyiTERAHIvqsaENSLRHLHTDVLDLLLIH------RPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPA 163
Cdd:cd19100 80 E---------GAKRDL----ERSLKRLGTDYIDLYQLHavdteeDLDQVFGPGGALEALLEAKEEGKIRFIGISGHSPE 145
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
30-249 |
1.07e-17 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 80.91 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 30 SARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPEnvighyiTERAHivqs 109
Cdd:cd19127 20 PPEETADAVATALADGYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWISDYGYDK-------ALRGF---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 110 aENSLRHLHTDVLDLLLIHRPDPlMDADEIAEAFLELHK---SGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPV 186
Cdd:cd19127 86 -DASLRRLGLDYVDLYLLHWPVP-NDFDRTIQAYKALEKllaEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVELHPY 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 187 H-QPllldGTLDLLQQLRIRPMAWSCLGGGRLFSDE-SFAPLRAELHQV----AEETGAqTIEQVVYAW 249
Cdd:cd19127 164 FsQK----DLRAFHRRLGIVTQAWSPIGGVMRYGASgPTGPGDVLQDPTitglAEKYGK-TPAQIVLRW 227
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-158 |
3.27e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 80.39 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRlapHLRDKMEIVTKCGIATTAkPENVIGhyiteraHIVQSAENSLRHLHTDV 121
Cdd:cd19104 42 LDLGINFFDTAPSYGDGKSEENLGRALK---GLPAGPYITTKVRLDPDD-LGDIGG-------QIERSVEKSLKRLKRDS 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 495142658 122 LDLLLIH------RPDPL---------MDADEIAEAFLELHKSGKVRHFGVS 158
Cdd:cd19104 111 VDLLQLHnrigdeRDKPVggtlsttdvLGLGGVADAFERLRSEGKIRFIGIT 162
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
42-281 |
1.47e-16 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 77.48 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATtakpenvighyitERAHIVQSA-ENSLRHLHTD 120
Cdd:cd19126 33 LENGYRSIDTAAIYKN---EEGVGEAIRESGVPREELFVTTKLWNDD-------------QRARRTEDAfQESLDRLGLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 121 VLDLLLIHRPDPlmdaDEIAE---AFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPVHQpllldgtld 197
Cdd:cd19126 97 YVDLYLIHWPGK----DKFIDtwkALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPYLT--------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 198 lLQQLR-------IRPMAWSCLGGGRLFSDESFAplraelhQVAEETGaQTIEQVVYAWVMRLPSRPLPiiGSGKIDRVK 270
Cdd:cd19126 164 -QKELRgyckskgIVVEAWSPLGQGGLLSNPVLA-------AIGEKYG-KSAAQVVLRWDIQHGVVTIP--KSVHASRIK 232
|
250
....*....|.
gi 495142658 271 SAVGALSIEMS 281
Cdd:cd19126 233 ENADIFDFELS 243
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
38-249 |
1.53e-16 |
|
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: 77.64 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGiATTAKPENVIghyiterahivQSAENSLRHL 117
Cdd:cd19130 29 VATALEVGYRHIDTAAIYGN---EEGVGAAIAASGIPRDELFVTTKLW-NDRHDGDEPA-----------AAFAESLAKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 118 HTDVLDLLLIHRPDPLMDA-DEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPVHQpllLDGTL 196
Cdd:cd19130 94 GLDQVDLYLVHWPTPAAGNyVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQ---QRTIR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142658 197 DLLQQLRIRPMAWSCLGGGRLFSDESFAPLrAELHqvaeetgAQTIEQVVYAW 249
Cdd:cd19130 171 DWAQAHDVKIEAWSPLGQGKLLGDPPVGAI-AAAH-------GKTPAQIVLRW 215
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-284 |
4.38e-16 |
|
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: 76.70 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 4 RILMAPQGPTFSRLVMGYWRLMEWnYSA----RELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKME 79
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGD-YGApkpeEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGP--REKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 80 IVTKCGIATtakPENVIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSN 159
Cdd:cd19145 79 LATKFGIHE---IGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 160 FTP-------AQFSLLQSRLPFTLATNQVE--ISPVhqpllldgtldlLQQLRIRPMAWSCLG------GGRLFSDESFA 224
Cdd:cd19145 156 ASAdtirrahAVHPITAVQLEWSLWTRDIEeeIIPT------------CRELGIGIVPYSPLGrgffagKAKLEELLENS 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 225 PLRAEL------------------HQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19145 224 DVRKSHprfqgenleknkvlyervEALAKKKGC-TPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKED 300
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-174 |
6.67e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 75.64 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 30 SARELVGFIEQHLELGITTVDHADIYGNyqCEAAFGEALRLAPHLRdkmeIVTKCGIATTAKPENvighyiteRAHIVQS 109
Cdd:cd19097 24 SEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKRLDKFK----IITKLPPLKEDKKED--------EAAIEAS 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142658 110 AENSLRHLHTDVLDLLLIHRP-DPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPF 174
Cdd:cd19097 90 VEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKI 155
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
27-249 |
1.92e-15 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 74.72 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPEnvighyiterahi 106
Cdd:PRK11565 23 WQASNEEVITAIHKALEVGYRSIDTAAIYKN---EEGVGKALKEASVAREELFITTKLWNDDHKRPR------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 107 vQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIA-EAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISP 185
Cdd:PRK11565 87 -EALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAwKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142658 186 VHQpllldgtldlLQQLR-------IRPMAWSCL--GGGRLFSDEsfaplraELHQVAEETGaQTIEQVVYAW 249
Cdd:PRK11565 166 LMQ----------QRQLHawnathkIQTESWSPLaqGGKGVFDQK-------VIRDLADKYG-KTPAQIVIRW 220
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-184 |
2.22e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 74.94 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 13 TFSRLVMGYWRLME-WNYSARE--LVGFIEQHLELGITTVDHADIYGNyqCEAAFGEALRLaphLRDKMEIVTKCGIATT 89
Cdd:cd19101 1 TISRVINGMWQLSGgHGGIRDEdaAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKR---LRRERDAADDVQIHTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 90 AKPEnvIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDA-DEIAEAFLELHKSGKVRHFGVSNF-TPAQFSL 167
Cdd:cd19101 76 WVPD--PGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGyLDAAKHLAELQEEGKIRHLGLTNFdTERLREI 153
|
170
....*....|....*..
gi 495142658 168 LQSRLPftLATNQVEIS 184
Cdd:cd19101 154 LDAGVP--IVSNQVQYS 168
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
42-284 |
2.51e-15 |
|
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: 74.58 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAF---GEALRLAPHLRDKMEIVTK-CGIATTAKPEnvighyiTERAHIVQSAENSLRHL 117
Cdd:cd19077 35 LDAGSNLWNGGEFYGPPDPHANLkllARFFRKYPEYADKVVLSVKgGLDPDTLRPD-------GSPEAVRKSIENILRAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 118 -HTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTpAQfSLLQSRLPFTLATNQVEISPVHQPLLLDGTL 196
Cdd:cd19077 108 gGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVS-AE-TIRRAHAVHPIAAVEVEYSLFSREIEENGVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 197 DLLQQLRIRPMAWSCLGGGRL---------------------FSDESFA---PLRAELHQVAEETGAqTIEQVVYAWVMR 252
Cdd:cd19077 186 ETCAELGIPIIAYSPLGRGLLtgriksladipegdfrrhldrFNGENFEknlKLVDALQELAEKKGC-TPAQLALAWILA 264
|
250 260 270
....*....|....*....|....*....|....
gi 495142658 253 LpSRP--LPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19077 265 Q-SGPkiIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
38-253 |
4.19e-15 |
|
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: 73.43 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNyqcEAAFGEALR-LAPHLRDKME---IVTKCGiattakPENVIGhyitERAHivQSAENS 113
Cdd:cd19136 21 VDAALKAGYRLIDTASVYRN---EADIGKALRdLLPKYGLSREdifITSKLA------PKDQGY----EKAR--AACLGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 114 LRHLHTDVLDLLLIHRPDP-LMDADEIA---------EAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEI 183
Cdd:cd19136 86 LERLGTDYLDLYLIHWPGVqGLKPSDPRnaelrreswRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAVNQVEF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 184 SP-VHQpllldgtldllQQLR-------IRPMAWSCLGGGRLFSDESFAPLraelhQVAEETGaQTIEQVVYAWVMRL 253
Cdd:cd19136 166 HPhLVQ-----------KELLkfckdhgIHLQAYSSLGSGDLRLLEDPTVL-----AIAKKYG-RTPAQVLLRWALQQ 226
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-158 |
2.48e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 71.97 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 13 TFSRLVMGYWRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALR----LAPHLRDKMEIVTKCG--- 85
Cdd:cd19099 2 TLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRelieKGGIKRDEVVIVTKAGyip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 86 ------------IATTAKPENVIGHYITERAH------IVQSAENSLRHLHTDVLDLLLIHRP-------DPLMDADEIA 140
Cdd:cd19099 82 gdgdeplrplkyLEEKLGRGLIDVADSAGLRHcispayLEDQIERSLKRLGLDTIDLYLLHNPeeqllelGEEEFYDRLE 161
|
170 180
....*....|....*....|.
gi 495142658 141 EAFLELHK---SGKVRHFGVS 158
Cdd:cd19099 162 EAFEALEEavaEGKIRYYGIS 182
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
16-249 |
2.58e-14 |
|
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: 71.39 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 16 RLVMGYWRLMEWNysarELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATTakpenv 95
Cdd:cd19156 11 RLGLGVWRVQDGA----EAENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIRESGVPREEVFVTTKLWNSDQ------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 96 iGHYITerahiVQSAENSLRHLHTDVLDLLLIHRP--DPLMDAdeiAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLP 173
Cdd:cd19156 78 -GYEST-----LAAFEESLEKLGLDYVDLYLIHWPvkGKFKDT---WKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142658 174 FTLATNQVEISPVHQpllLDGTLDLLQQLRIRPMAWSCLGGGRLFSDesfaplrAELHQVAEETGaQTIEQVVYAW 249
Cdd:cd19156 149 VAPMVNQIELHPLLT---QEPLRKFCKEKNIAVEAWSPLGQGKLLSN-------PVLKAIGKKYG-KSAAQVIIRW 213
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
31-164 |
2.79e-14 |
|
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: 71.86 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 31 ARELvgfIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPENVIGhyiTERAHIVQSA 110
Cdd:cd19143 33 AKEC---MKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPPPNDRG---LSRKHIVEGT 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 495142658 111 ENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQ 164
Cdd:cd19143 107 KASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
27-284 |
5.84e-14 |
|
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: 70.27 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKcgiatTAKPENviGHYITERAhi 106
Cdd:cd19134 19 GELSDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTK-----LATPDQ--GFTASQAA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 107 vqsAENSLRHLHTDVLDLLLIHRPDPlmDADEIAEAF---LELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEI 183
Cdd:cd19134 87 ---CRASLERLGLDYVDLYLIHWPAG--REGKYVDSWgglMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 184 SPVhqpLLLDGTLDLLQQLRIRPMAWSCLGGGRLFSDEsfaplraELHQVAEETGaQTIEQVVYAWVMRLPSRPLPiiGS 263
Cdd:cd19134 162 HPL---LNQAELRKVNAQHGIVTQAYSPLGVGRLLDNP-------AVTAIAAAHG-RTPAQVLLRWSLQLGNVVIS--RS 228
|
250 260
....*....|....*....|.
gi 495142658 264 GKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19134 229 SNPERIASNLDVFDFELTADH 249
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
27-281 |
6.16e-14 |
|
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: 70.60 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRlapHLRDKMEIVTKCGIATTAKPenVIGHyitERAHI 106
Cdd:cd19111 12 YQSPPEEVRAAVDYALFVGYRHIDTALSYQN---EKAIGEALK---WWLKNGKLKREEVFITTKLP--PVYL---EFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 107 VQSAENSLRHLHTDVLDLLLIHRP-------DPLM------DADEIAEAFLELHKSGKVRHFGVSNFTPAQFS--LLQSR 171
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPcgfvnkkDKGErelassDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINkiLAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 172 LPftLATNQVEISPVHQpllLDGTLDLLQQLRIRPMAWSCLGG-GRL-FSDESFAPLRAE---LHQVAEETGaQTIEQVV 246
Cdd:cd19111 161 VK--PSNLQLECHAYLQ---QRELRKFCNKKNIVVTAYAPLGSpGRAnQSLWPDQPDLLEdptVLAIAKELD-KTPAQVL 234
|
250 260 270
....*....|....*....|....*....|....*
gi 495142658 247 YAWVMRLPSRPLPiiGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19111 235 LRFVLQRGTGVLP--KSTNKERIEENFEVFDFELT 267
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
31-288 |
7.21e-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: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 31 ARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCGIATtakpenvIGHYITERAHivqsa 110
Cdd:cd19157 23 GSEVVNAVKTALKNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKVWNAD-------QGYDSTLKAF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 111 ENSLRHLHTDVLDLLLIHRPDPLMDAdEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPvhqpl 190
Cdd:cd19157 88 EASLERLGLDYLDLYLIHWPVKGKYK-ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHP----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 191 lldgtLDLLQQLR-------IRPMAWSCLGGGRLFSDESfaplraeLHQVAEETGaQTIEQVVYAWvmRLPSRPLPIIGS 263
Cdd:cd19157 162 -----RLTQKELRdyckkqgIQLEAWSPLMQGQLLDNPV-------LKEIAEKYN-KSVAQVILRW--DLQNGVVTIPKS 226
|
250 260
....*....|....*....|....*
gi 495142658 264 GKIDRVKSAVGALSIEMSRQQWFRI 288
Cdd:cd19157 227 IKEHRIIENADVFDFELSQEDMDKI 251
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
42-251 |
1.05e-13 |
|
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: 69.60 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPHL-----RDKMEIVTK--CGIAttakpenvighyitERAHIVQSAENSL 114
Cdd:cd19124 30 IEVGYRHFDTAAAYGT---EEALGEALAEALRLglvksRDELFVTSKlwCSDA--------------HPDLVLPALKKSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 115 RHLHTDVLDLLLIHRP---------------DPL-MDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLAT 178
Cdd:cd19124 93 RNLQLEYVDLYLIHWPvslkpgkfsfpieeeDFLpFDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFATIPPAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 179 NQVEISPVHQpllldgtldlLQQLR-------IRPMAWSCLGGGRLF--SDESFAplRAELHQVAEETGAqTIEQVVYAW 249
Cdd:cd19124 173 NQVEMNPAWQ----------QKKLRefckangIHVTAYSPLGAPGTKwgSNAVME--SDVLKEIAAAKGK-TVAQVSLRW 239
|
..
gi 495142658 250 VM 251
Cdd:cd19124 240 VY 241
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-292 |
1.82e-13 |
|
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: 69.28 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKC--GIATTaKPENVIghyiterahivQSAENSLRHLHT 119
Cdd:cd19103 42 MAAGLNLWDTAAVYGMGASEKILGEFLKRYP--REDYIISTKFtpQIAGQ-SADPVA-----------DMLEGSLARLGT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 120 DVLDLLLIHRPdplMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLP---FTLATNQVEISPVHQPLLLDGTL 196
Cdd:cd19103 108 DYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAkagVSLSAVQNHYSLLYRSSEEAGIL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 197 DLLQQLRIRPMAWSCL-----------------GGGRLFSDESFAPLRAELHQVAEETGAQ---TIEQVVYAWVmrLPSR 256
Cdd:cd19103 185 DYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETYNPLLPQLEELTAVMAEIGAKhgaSIAQVAIAWA--IAKG 262
|
250 260 270
....*....|....*....|....*....|....*.
gi 495142658 257 PLPIIGSGKIDRVKSAVGALSIEMSRQQWFRIRKAA 292
Cdd:cd19103 263 TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLA 298
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
43-189 |
4.31e-13 |
|
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: 67.73 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 43 ELGITTVDHADIYGnyqCEAAFGEALRLAPHLRDKMEIVTKCGiattakPenviGHYITERAhiVQSAENSLRHLHTDVL 122
Cdd:cd19135 37 ECGYRHIDTAKRYG---CEELLGKAIKESGVPREDLFLTTKLW------P----SDYGYEST--KQAFEASLKRLGVDYL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142658 123 DLLLIHRPDPLMDADEIAE-------AFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISPVHQP 189
Cdd:cd19135 102 DLYLLHWPDCPSSGKNVKEtraetwrALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNP 175
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-162 |
4.75e-13 |
|
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: 68.36 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIY-----GNYQ--CEAAFGEALRLAPhLRDKMEIVTKcgIATTAKPENVIGHYIT--ERAHIVQSAEN 112
Cdd:cd19094 28 FDEGVNFIDTAEMYpvppsPETQgrTEEIIGSWLKKKG-NRDKVVLATK--VAGPGEGITWPRGGGTrlDRENIREAVEG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 113 SLRHLHTDVLDLLLIHRPD---PLMDA---------------DEIAEAFLELHKSGKVRHFGVSNFTP 162
Cdd:cd19094 105 SLKRLGTDYIDLYQLHWPDrytPLFGGgyytepseeedsvsfEEQLEALGELVKAGKIRHIGLSNETP 172
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
49-284 |
5.41e-13 |
|
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: 68.22 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 49 VDHADIYGNYQCEAAFGE--ALRlapHLRDKMEIVTKCGIA-TTAKPENVIGHYI-TERAHIVQSAENSLRHLHTDVLDL 124
Cdd:cd19146 52 IDTANNYQGEESERWVGEwmASR---GNRDEMVLATKYTTGyRRGGPIKIKSNYQgNHAKSLRLSVEASLKKLQTSYIDI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 125 LLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNfTPA----------------QFSLLQSRLPFTLATNQVEISPVHQ 188
Cdd:cd19146 129 LYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSD-TPAwvvskanayarahgltQFVVYQGHWSAAFRDFERDILPMCE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 189 pllldgtldlLQQLRIRPmaWSCLGGGRLFSDESFA-----------------PLRAELHQVAEETGAqTIEQVVYAWVM 251
Cdd:cd19146 208 ----------AEGMALAP--WGVLGQGQFRTEEEFKrrgrsgrkggpqtekerKVSEKLEKVAEEKGT-AITSVALAYVM 274
|
250 260 270
....*....|....*....|....*....|...
gi 495142658 252 RLPSRPLPIIGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19146 275 HKAPYVFPIVGGRKVEHLKGNIEALGISLSDEE 307
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-158 |
6.04e-13 |
|
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: 67.20 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 15 SRLVMGYWRL-MEWNYSARE--LVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKCGIATTAK 91
Cdd:cd19096 1 SVLGFGTMRLpESDDDSIDEekAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGP--REKFYLATKLPPWSVKS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142658 92 PENVighyiteRAHIvqsaENSLRHLHTDVLDLLLIH---RPD--PLMDADEIAEAFLELHKSGKVRHFGVS 158
Cdd:cd19096 79 AEDF-------RRIL----EESLKRLGVDYIDFYLLHglnSPEwlEKARKGGLLEFLEKAKKEGLIRHIGFS 139
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
35-161 |
1.03e-12 |
|
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: 66.92 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 35 VGFIEQHLELGITTVDHADIYGNyqCEAAFGEALR-LAP-HLRDKMEIVTKCGiattakpenvigHYITE-----RAHIV 107
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGP--SEIILGRALKaLRDeFPRDTYFIITKVG------------RYGPDdfdysPEWIR 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 108 QSAENSLRHLHTDVLDLLLIHrpD-PLMDADEIAEAFLELHK---SGKVRHFGVSNFT 161
Cdd:cd19164 103 ASVERSLRRLHTDYLDLVYLH--DvEFVADEEVLEALKELFKlkdEGKIRNVGISGYP 158
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
27-281 |
1.13e-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: 67.05 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyQCE--AAFGEALRLAPHLRDKMEIVTKCGiATTAKPENVIGhyitera 104
Cdd:cd19123 20 WKSKPGEVGQAVKQALEAGYRHIDCAAIYGN-EAEigAALAEVFKEGKVKREDLWITSKLW-NNSHAPEDVLP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 105 hivqSAENSLRHLHTDVLDLLLIHRP--------------DPLMDADEIAE----AFLELHKSGKVRHFGVSNFTPAQFS 166
Cdd:cd19123 91 ----ALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgeDLLSLSPIPLEdtwrAMEELVDKGLCRHIGVSNFSVKKLE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 167 LL--QSRLPftLATNQVEISPVHQpllldgtldlLQQLR-------IRPMAWSCLGGG---RLFSDESFAPLRAE--LHQ 232
Cdd:cd19123 167 DLlaTARIK--PAVNQVELHPYLQ----------QPELLafcrdngIHLTAYSPLGSGdrpAAMKAEGEPVLLEDpvINK 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495142658 233 VAEETGAqTIEQVVYAWVMRLPSRPLPiiGSGKIDRVKSAVGALSIEMS 281
Cdd:cd19123 235 IAEKHGA-SPAQVLIAWAIQRGTVVIP--KSVNPERIQQNLEAAEVELD 280
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
42-158 |
2.43e-12 |
|
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: 65.65 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqCEAAFGEALRLAPhlRDKMEIVTKCGiattAKPEnviGHYITERAHIVQSAENSLRHLHTDV 121
Cdd:cd19090 30 LDLGINYIDTAPAYGD--SEERLGLALAELP--REPLVLSTKVG----RLPE---DTADYSADRVRRSVEESLERLGRDR 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495142658 122 LDLLLIHRPDPLMDADEIA-----EAFLELHKSGKVRHFGVS 158
Cdd:cd19090 99 IDLLMIHDPERVPWVDILApggalEALLELKEEGLIKHIGLG 140
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
38-158 |
2.77e-12 |
|
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: 65.65 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKCGIATTAKPENVigHYITERahIVQSAENSLRHL 117
Cdd:cd19163 39 VHEALDSGINYIDTAPWYGQGRSETVLGKALKGIP--RDSYYLATKVGRYGLDPDKMF--DFSAER--ITKSVEESLKRL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 495142658 118 HTDVLDLLLIHRPD--PLMD--ADEIAEAFLELHKSGKVRHFGVS 158
Cdd:cd19163 113 GLDYIDIIQVHDIEfaPSLDqiLNETLPALQKLKEEGKVRFIGIT 157
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
42-276 |
3.07e-12 |
|
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: 65.94 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITtvdHADIYGNY-----QCEAAFGEALR--LAPHlRDKMEIVTKCGIATTAKPENVIGhyitERAHIVQSAENSL 114
Cdd:cd19150 40 FDLGIT---HFDLANNYgpppgSAEENFGRILRedFAGY-RDELIISTKAGYDMWPGPYGEWG----SRKYLLASLDQSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 115 RHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPA---QFSLLQSRLPFTLATNQVEISPVHQPLL 191
Cdd:cd19150 112 KRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPErtrEAAAILRELGTPLLIHQPSYNMLNRWVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 192 LDGTLDLLQQLRIRPMAWSCLGGGRL------------------------FSDESFAPLRAeLHQVAEETGaQTIEQVVY 247
Cdd:cd19150 192 ESGLLDTLQELGVGCIAFTPLAQGLLtdkylngipegsraskerslspkmLTEANLNSIRA-LNEIAQKRG-QSLAQMAL 269
|
250 260
....*....|....*....|....*....
gi 495142658 248 AWVMRLPSRPLPIIGSGKIDRVKSAVGAL 276
Cdd:cd19150 270 AWVLRDGRVTSALIGASRPEQLEENVGAL 298
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
27-237 |
2.14e-11 |
|
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: 62.93 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHL---RDKMEIVTKCGIATTAKPENVIghyiter 103
Cdd:cd19121 20 WQAKAGEVKAAVAHALKIGYRHIDGALCYQN---EDEVGEGIKEAIAGgvkREDLFVTTKLWSTYHRRVELCL------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 104 ahivqsaENSLRHLHTDVLDLLLIHRP--------DPLM------------DADEIAE-AFLE-LHKSGKVRHFGVSNFT 161
Cdd:cd19121 90 -------DRSLKSLGLDYVDLYLVHWPvllnpngnHDLFptlpdgsrdldwDWNHVDTwKQMEkVLKTGKTKAIGVSNYS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 162 PAQFSLLQSRLPFTLATNQVEISPvHQPLLLDGTLDLLQQlrIRPMAWSCLG--GGRLFSDESFAPLrAELHQVAEET 237
Cdd:cd19121 163 IPYLEELLKHATVVPAVNQVENHP-YLPQQELVDFCKEKG--ILIEAYSPLGstGSPLISDEPVVEI-AKKHNVGPGT 236
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
42-281 |
4.72e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 62.29 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRlaPHlRDKMEIVTKCGIATTAKpenviGHYIT--ERAHIVQSAENSLRHLHT 119
Cdd:PRK10376 50 VALGVNHIDTSDFYGPHVTNQLIREALH--PY-PDDLTIVTKVGARRGED-----GSWLPafSPAELRRAVHDNLRNLGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 120 DVLDLL------LIHRPDPlmdaDEIAEAF---LELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEIspVHQPL 190
Cdd:PRK10376 122 DVLDVVnlrlmgDGHGPAE----GSIEEPLtvlAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNL--AHRAD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 191 LLDGTLDLLQQLRIRPmaWSCLGGgrlfsdesFAPLRAE-LHQVAEETGAqTIEQVVYAWVMRLPSRPLPIIGSGKIDRV 269
Cdd:PRK10376 196 DALIDALARDGIAYVP--FFPLGG--------FTPLQSStLSDVAASLGA-TPMQVALAWLLQRSPNILLIPGTSSVAHL 264
|
250
....*....|..
gi 495142658 270 KSAVGALSIEMS 281
Cdd:PRK10376 265 RENLAAAELVLS 276
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
38-285 |
6.59e-11 |
|
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: 61.59 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPH----LRDKMEIVTK--CgiaTTAKPENVIGhyiterahivqSAE 111
Cdd:cd19125 30 VKTAIKEGYRHIDCAAIYGN---EKEIGKALKKLFEdgvvKREDLFITSKlwC---TDHAPEDVPP-----------ALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 112 NSLRHLHTDVLDLLLIHRP------DPLMDADEIAE--------AFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLA 177
Cdd:cd19125 93 KTLKDLQLDYLDLYLIHWPvrlkkgAHMPEPEEVLPpdipstwkAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARVPPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 178 TNQVEISPVHQpllLDGTLDLLQQLRIRPMAWSCLGggrlfSDESFAPLRAELH-----QVAEETGaQTIEQVVYAWVMR 252
Cdd:cd19125 173 VNQVECHPGWQ---QDKLHEFCKSKGIHLSAYSPLG-----SPGTTWVKKNVLKdpivtKVAEKLG-KTPAQVALRWGLQ 243
|
250 260 270
....*....|....*....|....*....|...
gi 495142658 253 LPSRPLPiiGSGKIDRVKSAVGALSIEMSRQQW 285
Cdd:cd19125 244 RGTSVLP--KSTNEERIKENIDVFDWSIPEEDF 274
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
38-249 |
8.86e-11 |
|
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: 61.36 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPHLRDKMEIVTKCgiattakpenvighYITERAHIVQSAENSLRHL 117
Cdd:cd19117 33 VEAALKAGYRHIDTAAIYGN---EEEVGQGIKDSGVPREEIFITTKL--------------WCTWHRRVEEALDQSLKKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 118 HTDVLDLLLIHRPDPLMDADEIA---------------------EAFLELHKSGKVRHFGVSNF-TPAQFSLLQSRL-PF 174
Cdd:cd19117 96 GLDYVDLYLMHWPVPLDPDGNDFlfkkddgtkdhepdwdfiktwELMQKLPATGKVKAIGVSNFsIKNLEKLLASPSaKI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142658 175 TLATNQVEISPVH-QPllldGTLDLLQQLRIRPMAWSCLGggrlfsdESFAPLRAE--LHQVAEETGAQTiEQVVYAW 249
Cdd:cd19117 176 VPAVNQIELHPLLpQP----KLVDFCKSKGIHATAYSPLG-------STNAPLLKEpvIIKIAKKHGKTP-AQVIISW 241
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
33-160 |
2.62e-10 |
|
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: 59.86 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 33 ELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIATTakpenviGHYITERAHIVQSAEN 112
Cdd:cd19153 34 EAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRD-------SEFDYSAERVRASVAT 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 495142658 113 SLRHLHTDVLDLLLIHR---PDPLMDADEIAEAFLELHKSGKVRHFGVSNF 160
Cdd:cd19153 107 SLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
38-249 |
3.55e-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: 59.35 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNyqcEAAFGEALRlapHLRDKMEIVTKCGIATTAKPENViGHyitERAHIVQSAENSLRHL 117
Cdd:cd19118 26 VKIALKAGYRHLDLAKVYQN---QHEVGQALK---ELLKEEPGVKREDLFITSKLWNN-SH---RPEYVEPALDDTLKEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 118 HTDVLDLLLIHRP------------------DPLMDAD------EIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLP 173
Cdd:cd19118 96 GLDYLDLYLIHWPvafkptgdlnpltavptnGGEVDLDlsvslvDTWKAMVELKKTGKVKSIGVSNFSIDHLQAIIEETG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 174 FTLATNQVEISP-VHQPllldGTLDLLQQLRIRPMAWSCLGGGRLfsdeSFAPL--RAELHQVAEETGaQTIEQVVYAW 249
Cdd:cd19118 176 VVPAVNQIEAHPlLLQD----ELVDYCKSKNIHITAYSPLGNNLA----GLPLLvqHPEVKAIAAKLG-KTPAQVLIAW 245
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
19-284 |
3.79e-10 |
|
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: 59.81 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 19 MGYWRLmewnySARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAphlrDKMEIVTKCGIATTAKPENvigh 98
Cdd:cd19112 16 LGVWRM-----EPGEIKELILNAIKIGYRHFDCAADYKN---EKEVGEALAEA----FKTGLVKREDLFITTKLWN---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 99 yiTERAHIVQSAENSLRHLHTDVLDLLLIHRP-----------DPLMDADEIAEAFL------------ELHKSGKVRHF 155
Cdd:cd19112 80 --SDHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttGSALGEDGVLDIDVtislettwhameKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 156 GVSNFTP--AQFSLLQSRL-PftlATNQVEISPVHQpllLDGTLDLLQQLRIRPMAWSCLGGGRLFSDE--SFAPLRAE- 229
Cdd:cd19112 158 GISNYDIflTRDCLAYSKIkP---AVNQIETHPYFQ---RDSLVKFCQKHGISVTAHTPLGGAAANAEWfgSVSPLDDPv 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 495142658 230 LHQVAEETGaQTIEQVVYAWVMRLPSRPLPiiGSGKIDRVKSAVGALSIEMSRQQ 284
Cdd:cd19112 232 LKDLAKKYG-KSAAQIVLRWGIQRNTAVIP--KSSKPERLKENIDVFDFQLSKED 283
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
17-290 |
4.67e-10 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 59.62 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 17 LVMGYWRLMEWNYSARELVGFIEQHLELGITTVDHADIYGNY--QCEAAFGEALR--LAPHlRDKMEIVTKCGIATTAKP 92
Cdd:PRK09912 28 LSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPpgSAEENFGRLLRedFAAY-RDELIISTKAGYDMWPGP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 93 ENVIGhyitERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFS-----L 167
Cdd:PRK09912 107 YGSGG----SRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQkmvelL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 168 LQSRLPFTlatnqveispVHQPLLLDGTLDLLQQ-------------LRIRPMAWSCLGGG------------------- 215
Cdd:PRK09912 183 REWKIPLL----------IHQPSYNLLNRWVDKSglldtlqnngvgcIAFTPLAQGLLTGKylngipqdsrmhregnkvr 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 216 ----RLFSDESFAPLRAeLHQVAEETGaQTIEQVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALS-IEMSRQQWFRIRK 290
Cdd:PRK09912 253 gltpKMLTEANLNSLRL-LNEMAQQRG-QSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNnLTFSTEELAQIDQ 330
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
38-166 |
5.69e-09 |
|
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: 56.32 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKcgIATTAKPEnviGHYITeRAHIVQSAENSLRHL 117
Cdd:cd19142 37 VTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTK--IYWSYGSE---ERGLS-RKHIIESVRASLRRL 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 495142658 118 HTDVLDLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQFS 166
Cdd:cd19142 111 QLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
42-185 |
6.29e-09 |
|
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: 55.75 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRLAPhlrdKMEIVTKCGIATTAKpenVIGHYiTERAHIVQSAENSLRHLHTDV 121
Cdd:cd19116 35 IEAGYRHIDTAYLYGN---EAEVGEAIREKI----AEGVVKREDLFITTK---LWNSY-HEREQVEPALRESLKRLGLDY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 122 LDLLLIHRP------------DPLMDAD----EIAEAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVEISP 185
Cdd:cd19116 104 VDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCNIKPAVNQIEVHP 183
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
51-292 |
9.02e-09 |
|
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: 55.32 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 51 HADIYGNYQCEAAFGEALR--LA--PHL-RDKMEIVTKcgiattakpenvIGHYITERAHIVQSAENSLRHLHTDVLDLL 125
Cdd:cd19122 40 HLDCAWFYLNEDEVGDAVRdfLKenPSVkREDLFICTK------------VWNHLHEPEDVKWSIDNSLKNLKLDYIDLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 126 LIHRP---------DPLMDAD-------EIAE-------AFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATNQVE 182
Cdd:cd19122 108 LVHWPiaaekndqrSPKLGPDgkyvilkDLTEnpeptwrAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 183 ISPVhQPLLLDGTLDLLQQlrIRPMAWSCLGggrlfsDESFAPLRAE-------LHQVAEETGaQTIEQVVYAWVMRLPS 255
Cdd:cd19122 188 IHPF-LPNEELVDYCFSND--ILPEAYSPLG------SQNQVPSTGErvsenptLNEVAEKGG-YSLAQVLIAWGLRRGY 257
|
250 260 270
....*....|....*....|....*....|....*..
gi 495142658 256 RPLPiiGSGKIDRVKSAVGalSIEMSRQQWFRIRKAA 292
Cdd:cd19122 258 VVLP--KSSTPSRIESNFK--SIELSDEDFEAINQVA 290
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
38-249 |
9.77e-09 |
|
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: 55.22 E-value: 9.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNYQ-CEAAFGEALRLAPHLRDKMEIVTKCGiATTAKPENVighyiterahiVQSAENSLRH 116
Cdd:cd19128 20 VKNAIKAGYRHIDCAYYYGNEAfIGIAFSEIFKDGGVKREDLFITSKLW-PTMHQPENV-----------KEQLLITLQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 117 LHTDVLDLLLIHRP---DPLMDAD----------------EIAEAFLELHKSGKVRHFGVSNFTPAqfsLLQSRL----- 172
Cdd:cd19128 88 LQLEYLDLFLIHWPlafDMDTDGDprddnqiqslskkpleDTWRAMEQCVDEKLTKNIGVSNYSTK---LLTDLLnycki 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142658 173 -PFtlaTNQVEISPVHQPLLLDGTLDllqQLRIRPMAWSCLGGGrlFSDESFAPLR-AELHQVAEETGaQTIEQVVYAW 249
Cdd:cd19128 165 kPF---MNQIECHPYFQNDKLIKFCI---ENNIHVTAYRPLGGS--YGDGNLTFLNdSELKALATKYN-TTPPQVIIAW 234
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
42-173 |
2.13e-08 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 54.40 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGiattakpeNVIGHYITERAHIVQSAENSLRHLHTDV 121
Cdd:PLN02587 41 FRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKCG--------RYGEGFDFSAERVTKSVDESLARLQLDY 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 495142658 122 LDLLLIHRPDpLMDADEIAE----AFLELHKSGKVRHFGVSNFTPAQFSLLQSRLP 173
Cdd:PLN02587 113 VDILHCHDIE-FGSLDQIVNetipALQKLKESGKVRFIGITGLPLAIFTYVLDRVP 167
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
27-249 |
4.92e-08 |
|
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: 53.18 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALrlAPHL------RDKMEIVTKCGIATTAkpenvighyi 100
Cdd:cd19154 20 WQSKGAEGITAVRTALKAGYRLIDTAFLYQN---EEAIGEAL--AELLeegvvkREDLFITTKLWTHEHA---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 101 teRAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDAD-------------------EIAEAFLELHKSGKVRHFGVSNFT 161
Cdd:cd19154 85 --PEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEgesgtmengmsihdavdveDVWRGMEKVYDEGLTKAIGVSNFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 162 PAQFSLLQSRLPFTLATNQVEISPVHQpllLDGTLDLLQQLRIRPMAWSCLGG-GRLFSDES--FAPLRAELH-----QV 233
Cdd:cd19154 163 NDQIQRILDNARVKPHNNQVECHLYFP---QKELVEFCKKHNISVTSYATLGSpGRANFTKStgVSPAPNLLQdpivkAI 239
|
250
....*....|....*.
gi 495142658 234 AEETGaQTIEQVVYAW 249
Cdd:cd19154 240 AEKHG-KTPAQVLLRY 254
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
43-278 |
7.14e-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: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 43 ELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKcgIATTAKPENVIGhyiTERAHIVQSAENSLRHLHTDVL 122
Cdd:cd19141 41 ENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK--IFWGGKAETERG---LSRKHIIEGLKASLERLQLEYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 123 DLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPA----------QFSLlqsrLPFTLatNQVEISPVHQPLLL 192
Cdd:cd19141 116 DIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMeimeaysvarQFNL----IPPIV--EQAEYHLFQREKVE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 193 DGTLDLLQQLRIRPMAWSCLGGG--------------------------RLFSDES---FAPLRaELHQVAEETGAqTIE 243
Cdd:cd19141 190 MQLPELFHKIGVGAMTWSPLACGilsgkyddgvpeysraslkgyqwlkeKILSEEGrrqQAKLK-ELQIIADRLGC-TLP 267
|
250 260 270
....*....|....*....|....*....|....*
gi 495142658 244 QVVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSI 278
Cdd:cd19141 268 QLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
43-278 |
1.13e-07 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 52.39 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 43 ELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPENVIghyitERAHIVQSAENSLRHLHTDVL 122
Cdd:cd19158 42 DNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGL-----SRKHIIEGLKASLERLQLEYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 123 DLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQ----FSLLQSRLPFTLATNQVEISPVHQPLLLDGTLDL 198
Cdd:cd19158 117 DVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEimeaYSVARQFNLIPPICEQAEYHMFQREKVEVQLPEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 199 LQQLRIRPMAWSCLGGG--------------------------RLFSDESF---APLRaELHQVAEETGAqTIEQVVYAW 249
Cdd:cd19158 197 FHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEGRrqqAKLK-ELQAIAERLGC-TLPQLAIAW 274
|
250 260
....*....|....*....|....*....
gi 495142658 250 VMRLPSRPLPIIGSGKIDRVKSAVGALSI 278
Cdd:cd19158 275 CLRNEGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
43-278 |
1.18e-07 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 52.35 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 43 ELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPENVIghyitERAHIVQSAENSLRHLHTDVL 122
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGL-----SRKHIIEGLKGSLQRLQLEYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 123 DLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPAQ----FSLLQSRLPFTLATNQVEISPVHQPLLLDGTLDL 198
Cdd:cd19159 117 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEimeaYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 199 LQQLRIRPMAWSCLGGGRL-------FSDESFAPLRA---------------------ELHQVAEETGAqTIEQVVYAWV 250
Cdd:cd19159 197 YHKIGVGAMTWSPLACGIIsgkygngVPESSRASLKCyqwlkerivseegrkqqnklkDLSPIAERLGC-TLPQLAVAWC 275
|
250 260
....*....|....*....|....*...
gi 495142658 251 MRLPSRPLPIIGSGKIDRVKSAVGALSI 278
Cdd:cd19159 276 LRNEGVSSVLLGSSTPEQLIENLGAIQV 303
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
38-157 |
1.69e-07 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 51.46 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKCGIATTAKPE----NVIGHYITERAHIVQ----- 108
Cdd:cd19152 26 LVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQEveptFEPGFWNPLPFDAVFdysyd 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142658 109 ----SAENSLRHLHTDVLDLLLIHRPDPLMDADE--------IAEAFLELHK---SGKVRHFGV 157
Cdd:cd19152 104 gilrSIEDSLQRLGLSRIDLLSIHDPDEDLAGAEsdehfaqaIKGAFRALEElreEGVIKAIGL 167
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
51-185 |
7.64e-07 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 49.42 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 51 HADIYGNYQCEAAFGEALRlapHLRDKMEIvtkcgiattaKPENVighYITERA------HIVQSAENSLRHLHTDVLDL 124
Cdd:cd19119 43 HIDTAYAYETEDFVGEAIK---RAIDDGSI----------KREEL---FITTKVwptfydEVERSLDESLKALGLDYVDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 125 LLIHRPDPLM-DADEIAEAFL------------------------ELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLATN 179
Cdd:cd19119 107 LLVHWPVCFEkDSDDSGKPFTpvnddgktryaasgdhittykqleKIYLDGRAKAIGVSNYSIVYLERLIKECKVVPAVN 186
|
....*.
gi 495142658 180 QVEISP 185
Cdd:cd19119 187 QVELHP 192
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
43-278 |
9.35e-07 |
|
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: 49.60 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 43 ELGITTVDHADIYGNYQCEAAFGEALRLAPHLRDKMEIVTKCGIATTAKPENVIghyitERAHIVQSAENSLRHLHTDVL 122
Cdd:cd19160 44 EHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIYWGGQAETERGL-----SRKHIIEGLRGSLDRLQLEYV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 123 DLLLIHRPDPLMDADEIAEAFLELHKSGKVRHFGVSNFTPA----------QFSLLQSrlpftlATNQVEISPVHQPLLL 192
Cdd:cd19160 119 DIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMeimeaysvarQFNLIPP------VCEQAEYHLFQREKVE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 193 DGTLDLLQQLRIRPMAWSCLGGGRLFS-------DESFAPLRA---------------------ELHQVAEETGAqTIEQ 244
Cdd:cd19160 193 MQLPELYHKIGVGSVTWSPLACGLITGkydgrvpDTCRAAVKGyqwlkekvqseegkkqqakvkELHPIADRLGC-TVAQ 271
|
250 260 270
....*....|....*....|....*....|....
gi 495142658 245 VVYAWVMRLPSRPLPIIGSGKIDRVKSAVGALSI 278
Cdd:cd19160 272 LAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQV 305
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
30-156 |
2.04e-06 |
|
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: 48.48 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 30 SARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALRLAPhlRDKMEIVTKCGIATTAKPENVIG------------ 97
Cdd:cd19161 18 SNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKVGRLLKPAREGSVPdpngfvdplpfe 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142658 98 -HYITERAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDADEIA------------EAFLELHKSGKVRHFG 156
Cdd:cd19161 96 iVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKErhhfaqlmsggfKALEELKKAGVIKAFG 167
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
75-162 |
3.88e-06 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 47.54 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 75 RDKMEIVTKCGIATTAKPENVIGHYITERAHIVQSAENSLRHLHTDVLDLLLIHRPD-----------------PLMDAD 137
Cdd:PRK10625 79 REKLIIASKVSGPSRNNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPAVSLL 158
|
90 100
....*....|....*....|....*
gi 495142658 138 EIAEAFLELHKSGKVRHFGVSNFTP 162
Cdd:PRK10625 159 ETLDALAEQQRAGKIRYIGVSNETA 183
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
27-182 |
6.85e-06 |
|
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: 46.75 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALR----LAPHLRDKMEIVTKCgiattakPEnvighyITE 102
Cdd:cd19155 20 WQSSPEEIETAVDTALEAGYRHIDTAYVYRN---EAAIGNVLKkwidSGKVKREELFIVTKL-------PP------GGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 103 RAHIVQSA-ENSLRHLHTDVLDLLLIHRP---------------------DPLMDADEIAEAFLELHKSGKVRHFGVSNF 160
Cdd:cd19155 84 RREKVEKFlLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180
....*....|....*....|..
gi 495142658 161 TPAQFSLLQSRLPFTLATNQVE 182
Cdd:cd19155 164 NREQMARILKNARIKPANLQVE 185
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
42-185 |
1.36e-05 |
|
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: 45.84 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALR--LAPHL---RDKMEIVTKCGiATTAKPENVIGhyiterahivqSAENSLRH 116
Cdd:cd19106 30 LDAGYRHIDCAAVYGN---EQEVGEALKekVGPGKavpREDLFVTSKLW-NTKHHPEDVEP-----------ALRKTLKD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 117 LHTDVLDLLLIHRP--------------DPLMDADEIA-----EAFLELHKSGKVRHFGVSNFTPAQFSLLQSRLPFTLA 177
Cdd:cd19106 95 LQLDYLDLYLIHWPyafergdnpfpknpDGTIRYDSTHyketwKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVARIKPA 174
|
....*...
gi 495142658 178 TNQVEISP 185
Cdd:cd19106 175 VLQVECHP 182
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
105-185 |
3.09e-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: 44.72 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 105 HIVQSA-ENSLRHLHTDVLDLLLIHRPDPLMDADEIA-------------------EAFLELHKSGKVRHFGVSNFTPAQ 164
Cdd:cd19107 78 GLVKGAcQKTLSDLKLDYLDLYLIHWPTGFKPGKELFpldesgnvipsdttfldtwEAMEELVDEGLVKAIGVSNFNHLQ 157
|
90 100
....*....|....*....|...
gi 495142658 165 FSLLQSR--LPFTLATNQVEISP 185
Cdd:cd19107 158 IERILNKpgLKYKPAVNQIECHP 180
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
30-158 |
4.37e-05 |
|
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: 44.27 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 30 SARELVGFIEQHLELGITTVDHADIYGNYQCEAAFGEALrlAPHLRDKMEIVTKCGIATTAKPENVIGHYITE----RAH 105
Cdd:cd19162 17 GEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAAL--ARHPRAEYVVSTKVGRLLEPGAAGRPAGADRRfdfsADG 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 495142658 106 IVQSAENSLRHLHTDVLDLLLIHRPDPLMDA--DEIAEAFLELHKSGKVRHFGVS 158
Cdd:cd19162 95 IRRSIEASLERLGLDRLDLVFLHDPDRHLLQalTDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
24-185 |
9.65e-05 |
|
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: 43.41 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 24 LMEWNYSARELVGFIEQHLELGITTVDHADIYGNyQCEAAFG--EALRLAPHLRDKMEIVTKCGIATTAKPenvighyit 101
Cdd:cd19110 9 LGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHN-ESEVGAGirEKIKEGVVRREDLFIVSKLWCTCHKKS--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 102 erahIVQSA-ENSLRHLHTDVLDLLLIHRP------DPLMDADEIA-------------EAFLELHKSGKVRHFGVSNFT 161
Cdd:cd19110 79 ----LVKTAcTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRSGmvipsdtdfldtwEAMEDLVIEGLVKNIGVSNFN 154
|
170 180
....*....|....*....|....*.
gi 495142658 162 PAQFSLLQSR--LPFTLATNQVEISP 185
Cdd:cd19110 155 HEQLERLLNKpgLRVKPVTNQIECHP 180
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
38-185 |
1.08e-04 |
|
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: 43.25 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 38 IEQHLELGITTVDHADIYGNyqcEAAFGEALRlaPHLRD---KMEIVTKCG--IATTAKPEnvighyiterahIVQSA-E 111
Cdd:cd19109 27 VKVAIDTGYRHIDGAYIYQN---EHEVGQAIR--EKIAEgkvKREDIFYCGklWNTCHPPE------------LVRPTlE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 112 NSLRHLHTDVLDLLLIHRPDPLMDADEIA-------------------EAFLELHKSGKVRHFGVSNFTPAQFSLLQSR- 171
Cdd:cd19109 90 RTLKVLQLDYVDLYIIEMPMAFKPGDEIYprdengkwlyhktnlcatwEALEACKDAGLVKSIGVSNFNRRQLELILNKp 169
|
170
....*....|....*
gi 495142658 172 -LPFTLATNQVEISP 185
Cdd:cd19109 170 gLKHKPVSNQVECHP 184
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
42-185 |
2.44e-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: 41.83 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 42 LELGITTVDHADIYGNyqcEAAFGEALRlaphlrDKMEivtkcgiATTAKPENVIghYITE------RAHIVQSA-ENSL 114
Cdd:cd19108 37 IDAGFRHIDSAYLYQN---EEEVGQAIR------SKIA-------DGTVKREDIF--YTSKlwctfhRPELVRPAlEKSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 115 RHLHTDVLDLLLIHRPDPLMDADEIA-------------------EAFLELHKSGKVRHFGVSNFTPAQFSLLQSR--LP 173
Cdd:cd19108 99 KKLQLDYVDLYLIHFPVALKPGEELFpkdengklifdtvdlcatwEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKpgLK 178
|
170
....*....|..
gi 495142658 174 FTLATNQVEISP 185
Cdd:cd19108 179 YKPVCNQVECHP 190
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
27-280 |
7.04e-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: 40.62 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 27 WNYSARELVGFIEQHLELGITTVDHADIYGNyqcEAAFGEALRLAPH----LRDKMEIVTKCGIATTAKpenvighyite 102
Cdd:cd19114 12 AKIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKAIQeglvKREDLFIVTKLWNNFHGK----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 103 rAHIVQSAENSLRHLHTDVLDLLLIHRPDPLMDAD----------------------EIAEAFLELHK---SGKVRHFGV 157
Cdd:cd19114 78 -DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaenypflwkdkelkkfpleqsPMQECWREMEKlvdAGLVRNIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142658 158 SNFTPAQFSLLQSRLPFTLATNQVEISPvHQPLLLDGTLDLLQQLRIrpMAWSCLGGGRLF----SDESFAPL--RAELH 231
Cdd:cd19114 157 ANFNVQLILDLLTYAKIKPAVLQIEHHP-YLQQKRLIDWAKKQGIQI--TAYSSFGNAVYTkvtkHLKHFTNLleHPVVK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495142658 232 QVAEETGAQTiEQVVYAWVMRlpsRPLPII-GSGKIDRVKSAVGALSIEM 280
Cdd:cd19114 234 KLADKHKRDT-GQVLLRWAVQ---RNITVIpKSVNVERMKTNLDITSYKL 279
|
|
| |
