|
Name |
Accession |
Description |
Interval |
E-value |
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-296 |
0e+00 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 506.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 1 MERVQL-ADNLSFSRVIYGCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIV 79
Cdd:COG4989 1 MKRIKLgASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 80 TKCGIKLPSK---YGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNF 156
Cdd:COG4989 81 TKCGIRLPSEardNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 157 KRSQLSMLESYLPFPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDRAVRLRDTLEQVRGELG 236
Cdd:COG4989 161 TPSQFELLQSALDQPLVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRAALDELAEKYG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 237 AeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAILQSSMGHDVP 296
Cdd:COG4989 241 V-SPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREEWYELYEAARGHEVP 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
7-290 |
5.99e-163 |
|
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: 454.32 E-value: 5.99e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 7 ADNLSFSRVIYGCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKCGIKL 86
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 87 PS---KYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSM 163
Cdd:cd19092 81 GDdprPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 164 LESYLPFPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDRAVRLRDTLEQVRGELGAeTIDEV 243
Cdd:cd19092 161 LQSYLDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRAALEELAEEYGV-TIEAI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 737525220 244 LYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAILQSS 290
Cdd:cd19092 240 ALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYEIYEAA 286
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-283 |
1.62e-64 |
|
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: 205.03 E-value: 1.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 1 MERVQL-ADNLSFSRVIYGCWRLAD--WGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPSLRSQIE 77
Cdd:COG0667 1 MEYRRLgRSGLKVSRLGLGTMTFGGpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEAL--KGRPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 78 IVTKCGIKL-PSKYGmklYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNF 156
Cdd:COG0667 79 IATKVGRRMgPGPNG---RGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 157 KRSQL--SMLESYLPFPLVTNQIEVSAYRLEnLEDGTVDLCLEKRMPPMVWSPLAGG---------AIFSADD------- 218
Cdd:COG0667 156 SAEQLrrALAIAEGLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGlltgkyrrgATFPEGDraatnfv 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 219 -----DRAVRLRDTLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQW 283
Cdd:COG0667 235 qgyltERNLALVDALRAIAAEHGV-TPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDL 303
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
9-286 |
3.49e-62 |
|
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: 198.52 E-value: 3.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRL--ADWGYSARQ-LLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTlkpSLRSQIEIVTKCGIK 85
Cdd:cd19084 1 DLKVSRIGLGTWAIggTWWGEVDDQeSIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALK---GRRDDVVIATKCGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 86 lPSKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLE 165
Cdd:cd19084 78 -WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 166 SYlpFPLVTNQIEVSAYRlENLEDGTVDLCLEKRMPPMVWSPLAGG---------AIFSADDDRA-------------VR 223
Cdd:cd19084 157 KY--GPIVSLQPPYSMLE-REIEEELLPYCRENGIGVLPYGPLAQGlltgkykkePTFPPDDRRSrfpffrgenfeknLE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737525220 224 LRDTLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19084 234 IVDKLKEIAEKYGK-SLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
13-272 |
5.01e-59 |
|
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: 188.50 E-value: 5.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLaDWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPsLRSQIEIVTKCGIklPSKYGM 92
Cdd:cd06660 1 SRLGLGTMTF-GGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGGH--PPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 KLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLP--- 169
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 170 -FPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAIfsadddravrlrdtleqvrgelgaetidEVLYAWL 248
Cdd:cd06660 157 lPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGPA----------------------------QLALAWL 208
|
250 260
....*....|....*....|....
gi 737525220 249 FAHPARMMPIVGSGKQERIERAVR 272
Cdd:cd06660 209 LSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-286 |
1.37e-58 |
|
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: 189.06 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 15 VIYGCWRLAD--WGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKCGIKLpskyGM 92
Cdd:pfam00248 1 IGLGTWQLGGgwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGD----GP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 KLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPL 172
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 173 VTNQIEVSAYRlENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDD------------------RAVRLRDTLEQVRGE 234
Cdd:pfam00248 157 VAVQVEYNLLR-RRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRdpdkgpgerrrllkkgtpLNLEALEALEEIAKE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 737525220 235 LGaETIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:pfam00248 236 HG-VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-281 |
4.29e-48 |
|
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: 161.99 E-value: 4.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLAD---WGYSARQ-LLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTlkpSLRSQIEIVTKCGIKlps 88
Cdd:cd19085 2 SRLGLGCWQFGGgywWGDQDDEeSIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALK---GRRDDVVIATKVSPD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 89 kygmklyDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYL 168
Cdd:cd19085 76 -------NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 169 PFplVTNQIevsAYRL--ENLEDGTVDLCLEKRMPPMVWSPLAGG---------AIFSADDDR--------------AVR 223
Cdd:cd19085 149 RI--DSNQL---PYNLlwRAIEYEILPFCREHGIGVLAYSPLAQGlltgkfssaEDFPPGDARtrlfrhfepgaeeeTFE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 224 LRDTLEQVRGELGaETIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19085 224 ALEKLKEIADELG-VTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPS 280
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-282 |
3.76e-44 |
|
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: 150.84 E-value: 3.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRLADW---GYSARQL-LSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPSLRSQIEIVTKCgi 84
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGmskDYSDDKKaIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 85 kLPSKYGmklydtsKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSML 164
Cdd:cd19072 77 -SPDHLK-------YDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 165 ESYL-PFPLVTNQIEvsaYRLEN--LEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDRavrlrdTLEQVRGELGAeTID 241
Cdd:cd19072 149 QSYLkKGPIVANQVE---YNLFDreEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSP------LLDEIAKKYGK-TPA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 737525220 242 EVLYAWLFAHPaRMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19072 219 QIALNWLISKP-NVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
9-286 |
4.16e-43 |
|
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: 149.31 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRLAdWGYSA----RQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPsLRSQIEIVTKCGI 84
Cdd:cd19078 1 GLEVSAIGLGCMGMS-HGYGPppdkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEAL--KP-FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 85 KL-PSKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSnfkrsqlSM 163
Cdd:cd19078 77 KIdGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-------EA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 164 LESYLP-----FPLVTNQIEVSAYRLENlEDGTVDLCLEKRMPPMVWSPLA----GGAI-----FSADDDRAV------- 222
Cdd:cd19078 150 GVETIRrahavCPVTAVQSEYSMMWREP-EKEVLPTLEELGIGFVPFSPLGkgflTGKIdentkFDEGDDRASlprftpe 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 223 ------RLRDTLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19078 229 aleanqALVDLLKEFAEEKGA-TPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
10-281 |
6.47e-43 |
|
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: 149.27 E-value: 6.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 10 LSFSRVIYGCWRLAD-----WGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTlKPSLRSQIEIVTKCGi 84
Cdd:cd19079 10 LKVSRLCLGCMSFGDpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALK-EFAPRDEVVIATKVY- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 85 kLPSKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNF------KR 158
Cdd:cd19079 88 -FPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMyawqfaKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 159 SQLSMLESYLPFPLVTNQIEVsAYRLENLEdgTVDLCLEKRMPPMVWSPLAGG-----------------------AIFS 215
Cdd:cd19079 167 LHLAEKNGWTKFVSMQNHYNL-LYREEERE--MIPLCEEEGIGVIPWSPLARGrlarpwgdtterrrsttdtaklkYDYF 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737525220 216 ADDDRAVRLRdtLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19079 244 TEADKEIVDR--VEEVAKERGV-SMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEE 306
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
13-273 |
4.64e-39 |
|
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: 136.84 E-value: 4.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLA-DWG--YSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlkPSLRSQIEIVTKCGIKLPSK 89
Cdd:cd19086 4 SEIGFGTWGLGgDWWgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKAL---KGRRDKVVIATKFGNRFDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 90 YGMKlYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRP-DPFMNPEEVAEAFCQLKADGKVRYFGVSnfkrsqLSMLESYL 168
Cdd:cd19086 81 PERP-QDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVS------VGDPEEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 169 PF----PLVTNQIEVSAYRLENlEDGTVDLCLEKRMPPMVWSPLAGGaIFSadddravrlrdtleqvrGELGaetidEVL 244
Cdd:cd19086 154 AAlrrgGIDVVQVIYNLLDQRP-EEELFPLAEEHGVGVIARVPLASG-LLT-----------------GKLA-----QAA 209
|
250 260
....*....|....*....|....*....
gi 737525220 245 YAWLFAHPARMMPIVGSGKQERIERAVRA 273
Cdd:cd19086 210 LRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-281 |
6.25e-39 |
|
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: 138.49 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 10 LSFSRVIYGCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPSLRSQIEIVTKC--GIKlP 87
Cdd:cd19074 2 LKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKAL--KGWPRESYVISTKVfwPTG-P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 88 SKYGMKLydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQL----SM 163
Cdd:cd19074 79 GPNDRGL---SRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIaeahDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 164 LESYLPFPLVTNQIEVSAYRLEnLEDGTVDLCLEKRMPPMVWSPLAGG-----------------AIFSADDDRAVRL-- 224
Cdd:cd19074 156 ARQFGLIPPVVEQPQYNMLWRE-IEEEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsrATDEDNRDKKRRLlt 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737525220 225 RDTLEQVR------GELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19074 235 DENLEKVKklkpiaDELGL-TLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
35-282 |
3.89e-38 |
|
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: 136.97 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 35 LIEFCLERGITTFDHADIYGNYTCESRFGDALTLKpslRSQIEIVTKCGIKLPSkyGMKLYDTSKDHIIASVEQSLRNFR 114
Cdd:cd19091 44 LVDIALDAGINFFDTADVYSEGESEEILGKALKGR---RDDVLIATKVRGRMGE--GPNDVGLSRHHIIRAVEASLKRLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 115 TDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQ----LSMLESYLPFPLVTNQIEvsaYRLEN--LE 188
Cdd:cd19091 119 TDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQimkaLGISERRGLARFVALQAY---YSLLGrdLE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 189 DGTVDLCLEKRMPPMVWSPLAGGaIFSA------------------------DDDRAVRLRDTLEQVRGELGAeTIDEVL 244
Cdd:cd19091 196 HELMPLALDQGVGLLVWSPLAGG-LLSGkyrrgqpapegsrlrrtgfdfppvDRERGYDVVDALREIAKETGA-TPAQVA 273
|
250 260 270
....*....|....*....|....*....|....*...
gi 737525220 245 YAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19091 274 LAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEE 311
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
13-273 |
4.27e-37 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 132.36 E-value: 4.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRL--ADWGYSARQLLSLIEFCLERGITTFDHADIYGNytCESRFGDALtlKPSLRSQIEIVTKCGIklPSKY 90
Cdd:cd19095 1 SVLGLGTSGIgrVWGVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRAL--AGLRRDDLFIATKVGT--HGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 91 GMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFkrsqlsmlESYLPF 170
Cdd:cd19095 75 GRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGD--------GEELEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 171 PLVTNQ---IEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSAddDRAVRLRDTLEQVRG---ELGAETIDEVL 244
Cdd:cd19095 147 AIASGVfdvVQLPYNVLDREEEELLPLAAEAGLGVIVNRPLANGRLRRR--VRRRPLYADYARRPEfaaEIGGATWAQAA 224
|
250 260
....*....|....*....|....*....
gi 737525220 245 YAWLFAHPARMMPIVGSGKQERIERAVRA 273
Cdd:cd19095 225 LRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
17-286 |
6.52e-37 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 132.10 E-value: 6.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 17 YGCWRLADwgysaRQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgiklpskygmkLY- 95
Cdd:COG0656 10 LGTWQLPG-----EEAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAASGVPREELFVTTK------------VWn 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 96 -DTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPfMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVT 174
Cdd:COG0656 70 dNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGP-GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 175 NQIEVSAYRlenLEDGTVDLCLEKRMPPMVWSPLAGGAIFsaDDdravrlrDTLEQVRGELGAeTIDEVLYAWLFAHpaR 254
Cdd:COG0656 149 NQVELHPYL---QQRELLAFCREHGIVVEAYSPLGRGKLL--DD-------PVLAEIAEKHGK-TPAQVVLRWHLQR--G 213
|
250 260 270
....*....|....*....|....*....|..
gi 737525220 255 MMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:COG0656 214 VVVIPKSVTPERIRENLDAFDFELSDEDMAAI 245
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-279 |
4.09e-36 |
|
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: 130.03 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLA---DWGYSA--RQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPSlRSQIEIVTKCGIkLP 87
Cdd:cd19088 2 SRLGYGAMRLTgpgIWGPPAdrEEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEAL--HPY-PDDVVIATKGGL-VR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 88 SKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESY 167
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 168 lpFPLVTNQievSAYRLENLED-GTVDLCLEKRMPPMVWSPLAGGAIfsadddrAVRLRDtLEQVRGELGAeTIDEVLYA 246
Cdd:cd19088 158 --VRIVSVQ---NRYNLANRDDeGVLDYCEAAGIAFIPWFPLGGGDL-------AQPGGL-LAEVAARLGA-TPAQVALA 223
|
250 260 270
....*....|....*....|....*....|...
gi 737525220 247 WLFAHPARMMPIVGSGKQERIERAVRALSFSLS 279
Cdd:cd19088 224 WLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-282 |
7.65e-36 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 129.14 E-value: 7.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 14 RVIYGCWRLADwgysaRQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgikLPSKygmk 93
Cdd:cd19071 3 LIGLGTYKLKP-----EETAEAVLAALEAGYRHIDTAAAYGN---EAEVGEAIRESGVPREELFITTK----LWPT---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 94 lyDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNP------EEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESY 167
Cdd:cd19071 67 --DHGYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGgskearLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 168 LPFPLVTNQIEVSAYrleNLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDdravrlrDTLEQVRGELGAeTIDEVLYAW 247
Cdd:cd19071 145 ARIKPAVNQIELHPY---LQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDD-------PVLKEIAKKYGK-TPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*
gi 737525220 248 LFAHpaRMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19071 214 ALQR--GVVVIPKSSNPERIKENLDVFDFELSEED 246
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
48-283 |
1.06e-35 |
|
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: 130.03 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 48 DHADIYGNYTCESRFGDALT-----LKPSL-RSQIEIVTKCGI-KLPSKYGmklydTSKDHIIASVEQSLRNFRTDYIDV 120
Cdd:cd19081 44 DTADVYSAWVPGNAGGESETiigrwLKSRGkRDRVVIATKVGFpMGPNGPG-----LSRKHIRRAVEASLRRLQTDYIDL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 121 LLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQL------SMLESYLPFplVTNQIEVSAYRLENLEDGTVDL 194
Cdd:cd19081 119 YQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLqealelSRQHGLPRY--VSLQPEYNLVDRESFEGELLPL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 195 CLEKRMPPMVWSPLAGG--------------------AIFSADDDRAVRLRDTLEQVRGELGAeTIDEVLYAWLFAHPAR 254
Cdd:cd19081 197 CREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeAAKRYLNERGLRILDALDEVAAEHGA-TPAQVALAWLLARPGV 275
|
250 260
....*....|....*....|....*....
gi 737525220 255 MMPIVGSGKQERIERAVRALSFSLSREQW 283
Cdd:cd19081 276 TAPIAGARTVEQLEDLLAAAGLRLTDEEV 304
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-283 |
4.27e-35 |
|
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: 128.11 E-value: 4.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLAD---WGYSAR---QLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPsLRSQIEIVTKcgikl 86
Cdd:cd19093 3 SPLGLGTWQWGDrlwWGYGEYgdeDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 87 pskYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNP-EEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLE 165
Cdd:cd19093 77 ---FAPLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQiEALMDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 166 SYLP---FPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAI---FSADD-----DRAVR----------L 224
Cdd:cd19093 154 KALKergVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLtgkYSPENpppggRRRLFgrknlekvqpL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 737525220 225 RDTLEQVRGELGAeTIDEVLYAWLFAHPArmMPIVGSGKQERIERAVRALSFSLSREQW 283
Cdd:cd19093 234 LDALEEIAEKYGK-TPAQVALNWLIAKGV--VPIPGAKNAEQAEENAGALGWRLSEEEV 289
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
13-281 |
8.96e-35 |
|
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: 127.77 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLADW----GYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTlkpSLRSQIEIVTKCGI---- 84
Cdd:cd19149 12 SVIGLGTWAIGGGpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIK---GRRDKVVLATKCGLrwdr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 85 ----KLPSKYGMKLY-DTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRS 159
Cdd:cd19149 89 eggsFFFVRDGVTVYkNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 160 QLSMLESYlpFPLVTNQIEVSAYRLEnLEDGTVDLCLEKRMPPMVWSPLAGG---------AIFSADDDRAVR---LRDT 227
Cdd:cd19149 169 QIKEYVKA--GQLDIIQEKYSMLDRG-IEKELLPYCKKNNIAFQAYSPLEQGlltgkitpdREFDAGDARSGIpwfSPEN 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737525220 228 LEQVRGELGAE---------TIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19149 246 REKVLALLEKWkplcekygcTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAE 308
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
39-282 |
3.34e-34 |
|
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: 126.15 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 39 CLERGITTFDHADIYGNYTCESRFGDALTLKpslRSQIEIVTKCGiklpskygmklYDTSKD---------HIIASVEQS 109
Cdd:cd19087 39 ALDAGINFFDTADVYGGGRSEEIIGRWIAGR---RDDIVLATKVF-----------GPMGDDpndrglsrrHIRRAVEAS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 110 LRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNF------------KRSQLSMLESYLP-FPLVTNQ 176
Cdd:cd19087 105 LRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaARRGLLRFVSEQPmYNLLKRQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 177 IEVsayrlENLEdgtvdLCLEKRMPPMVWSPLAGGaIFS--------ADDDRAV------------RLRDTLEQ---VRG 233
Cdd:cd19087 185 AEL-----EILP-----AARAYGLGVIPYSPLAGG-LLTgkygkgkrPESGRLVeraryqarygleEYRDIAERfeaLAA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 737525220 234 ELGaETIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19087 254 EAG-LTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPEL 301
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
25-286 |
3.91e-34 |
|
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: 124.68 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 25 WGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCGIKlpskygmklyDTSKDHIIA 104
Cdd:cd19140 16 YPLTGEECTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKVWPD----------NYSPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 105 SVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAYrl 184
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPY-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 185 enLEDGTV-DLCLEKRMPPMVWSPLAGGAIfsadddravrLRDTLEQVRGELGAETIDEVLYAWLFAHPARMMpIVGSGK 263
Cdd:cd19140 161 --LDQRKLlDAAREHGIALTAYSPLARGEV----------LKDPVLQEIGRKHGKTPAQVALRWLLQQEGVAA-IPKATN 227
|
250 260
....*....|....*....|...
gi 737525220 264 QERIERAVRALSFSLSREQWFAI 286
Cdd:cd19140 228 PERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-286 |
1.13e-33 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 124.71 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLA--DWGYSA-----RQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTlkpSLRSQIEIVTKCGIk 85
Cdd:cd19102 2 TTIGLGTWAIGggGWGGGWgpqddRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK---GLRDRPIVATKCGL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 86 LPSKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLE 165
Cdd:cd19102 78 LWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 166 SYlpFPLVTNQIEVSAYRLEnLEDGTVDLCLEKRMPPMVWSPLAGG-----------AIFSADD-------------DRA 221
Cdd:cd19102 158 AI--HPIASLQPPYSLLRRG-IEAEILPFCAEHGIGVIVYSPMQSGlltgkmtpervASLPADDwrrrspffqepnlARN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737525220 222 VRLRDTLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19102 235 LALVDALRPIAERHGR-TVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEI 298
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
18-282 |
1.76e-33 |
|
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: 123.06 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 18 GCWRLADW---GYSA-RQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCgikLPSkygmk 93
Cdd:cd19137 10 GTWGIGGFltpDYSRdEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP--REDLFIVTKV---WPT----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 94 lyDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLV 173
Cdd:cd19137 80 --NLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 174 TNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGaifsadddrAVRLRDTLEQVRGELGAeTIDEVLYAWLFAHPa 253
Cdd:cd19137 158 CNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRG---------LEKTNRTLEEIAKNYGK-TIAQIALAWLIQKP- 226
|
250 260
....*....|....*....|....*....
gi 737525220 254 RMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19137 227 NVVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-281 |
4.97e-33 |
|
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: 123.09 E-value: 4.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 2 ERVQLADN-LSFSRVIYGCWRLAdWGYSAR---QLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlkPSLRSQIE 77
Cdd:cd19076 1 PTRKLGTQgLEVSALGLGCMGMS-AFYGPAdeeESIATLHRALELGVTFLDTADMYGPGTNEELLGKAL---KDRRDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 78 IVTKCGIKLPSKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFK 157
Cdd:cd19076 77 IATKFGIVRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 158 RSQLSMLESYLPFPLVtnQIEVSAYRLEnLEDGTVDLCLEKRMPPMVWSPLA----GGAIFSADD--------------- 218
Cdd:cd19076 157 ADTIRRAHAVHPITAV--QSEYSLWTRD-IEDEVLPTCRELGIGFVAYSPLGrgflTGAIKSPEDlpeddfrrnnprfqg 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737525220 219 ---DRAVRLRDTLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19076 234 enfDKNLKLVEKLEAIAAEKGC-TPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPE 298
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
18-286 |
1.37e-31 |
|
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: 118.12 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 18 GCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTlkpSLRSQIEIVTKCgikLPSkygmklyDT 97
Cdd:cd19138 17 GTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIR---GRRDKVFLVSKV---LPS-------NA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 98 SKDHIIASVEQSLRNFRTDYIDVLLIHRPD--PFmnpEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESyLPF--PLV 173
Cdd:cd19138 84 SRQGTVRACERSLRRLGTDYLDLYLLHWRGgvPL---AETVAAMEELKKEGKIRAWGVSNFDTDDMEELWA-VPGggNCA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 174 TNQIEvsaYRLEN--LEDGTVDLCLEKRMPPMVWSPLAGGAIFsaddDRAVRLRDTLEQVRGELGAeTIDEVLYAWLFAH 251
Cdd:cd19138 160 ANQVL---YNLGSrgIEYDLLPWCREHGVPVMAYSPLAQGGLL----RRGLLENPTLKEIAARHGA-TPAQVALAWVLRD 231
|
250 260 270
....*....|....*....|....*....|....*
gi 737525220 252 PArMMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19138 232 GN-VIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-154 |
2.79e-30 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 114.22 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCwrladwGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCGIKLPSKygm 92
Cdd:cd19105 14 SRLGFGG------GGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLR--RDKVFLATKASPRLDKK--- 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737525220 93 klydtSKDHIIASVEQSLRNFRTDYIDVLLIH---RPDPFMNPEEVAEAFCQLKADGKVRYFGVS 154
Cdd:cd19105 83 -----DKAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-282 |
7.59e-30 |
|
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: 113.87 E-value: 7.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 17 YGC---WRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgiklpskygmk 93
Cdd:cd19120 9 FGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTK------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 94 lYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRP----DPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQL-SMLESYL 168
Cdd:cd19120 74 -VSPGIKDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLeELLDTAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 169 PFPLVtNQIEVSAYrLENLEDGTVDLCLEKRMPPMVWSPLAGgaiFSADDDRAvrLRDTLEQVRGELGAETiDEVLYAWL 248
Cdd:cd19120 153 IKPAV-NQIEFHPY-LYPQQPALLEYCREHGIVVSAYSPLSP---LTRDAGGP--LDPVLEKIAEKYGVTP-AQVLLRWA 224
|
250 260 270
....*....|....*....|....*....|....
gi 737525220 249 FAHpaRMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19120 225 LQK--GIVVVTTSSKEERMKEYLEAFDFELTEEE 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-286 |
4.26e-29 |
|
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: 111.21 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 18 GCWRLADwgysaRQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCgikLPSKYgmklydt 97
Cdd:cd19073 7 GTWQLRG-----DDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTKV---WRDHL------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 98 SKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQI 177
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 178 EVSAYrLENLEdgTVDLCLEKRMPPMVWSPLAGGAIFsadDDRAVRlrdtleqvrgELGAE---TIDEVLYAWLFAHpaR 254
Cdd:cd19073 149 EFHPF-LYQAE--LLEYCRENDIVITAYSPLARGEVL---RDPVIQ----------EIAEKydkTPAQVALRWLVQK--G 210
|
250 260 270
....*....|....*....|....*....|..
gi 737525220 255 MMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19073 211 IVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
40-282 |
1.95e-28 |
|
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: 110.77 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNYTCESRFGDaltLKPSLRSQIEIVTKcgiklpskYGMklYDTSKD------H---IIASVEQSL 110
Cdd:cd19080 41 VEAGGNFIDTANNYTNGTSERLLGE---FIAGNRDRIVLATK--------YTM--NRRPGDpnaggnHrknLRRSVEASL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 111 RNFRTDYIDVLLIHRPDpFMNP-EEVAEAFCQLKADGKVRYFGVSNFKR---SQLSML-ESYLPFPLVTNQIEVS-AYRl 184
Cdd:cd19080 108 RRLQTDYIDLLYVHAWD-FTTPvEEVMRALDDLVRAGKVLYVGISDTPAwvvARANTLaELRGWSPFVALQIEYSlLER- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 185 eNLEDGTVDLCLEKRMPPMVWSPLAGG---------------------AIFSADDDRAVRLRDTLEQVRGELGAeTIDEV 243
Cdd:cd19080 186 -TPERELLPMARALGLGVTPWSPLGGGlltgkyqrgeegrageakgvtVGFGKLTERNWAIVDVVAAVAEELGR-SAAQV 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 737525220 244 LYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19080 264 ALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQ 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
71-275 |
6.90e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 108.96 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 71 SLRSQIEIVTKCGIKLPSKYGMK--LYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKV 148
Cdd:cd19752 64 GNRDDVVIATKVGAGPRDPDGGPesPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 149 RYFGVSNFK-----------RSQ-------LSMLESYL-PFPLVTNQIEVsayrleNLEDGTVDLC-LEKRMPPMVWSPL 208
Cdd:cd19752 144 RAIGASNFAawrlerarqiaRQQgwaefsaIQQRHSYLrPRPGADFGVQR------IVTDELLDYAsSRPDLTLLAYSPL 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 209 AGGAIfsADDDRAV-----------RLRdTLEQVRGELGAeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALS 275
Cdd:cd19752 218 LSGAY--TRPDRPLpeqydgpdsdaRLA-VLEEVAGELGA-TPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
40-275 |
1.30e-27 |
|
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: 108.41 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNY----TCESRFGDALTlKPSLRSQIEIVTKCGIklPSKYGMKLYDTSKDHIIASVEQSLRNFRT 115
Cdd:cd19082 27 VELGGNFIDTARVYGDWvergASERVIGEWLK-SRGNRDKVVIATKGGH--PDLEDMSRSRLSPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 116 DYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESY-----LPfPLVTNQIEVS--AYRLENLE 188
Cdd:cd19082 104 DYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYakahgLP-GFAASSPQWSlaRPNEPPWP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 189 DGTV--------DLCLEKRMPPMVWSPLAGGAiFS----ADDDRAVRLRDT---------LEQVRgELGAE---TIDEVL 244
Cdd:cd19082 183 GPTLvamdeemrAWHEENQLPVFAYSSQARGF-FSkraaGGAEDDSELRRVyyseenferLERAK-ELAEEkgvSPTQIA 260
|
250 260 270
....*....|....*....|....*....|.
gi 737525220 245 YAWLFAHPARMMPIVGSGKQERIERAVRALS 275
Cdd:cd19082 261 LAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
40-286 |
6.97e-27 |
|
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: 107.14 E-value: 6.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNYtcESRFGDALTLKPSLRSQIEIVTKCGIKLPSKYGMKLYDTSKDHIIASVEQSLRNFRTDYID 119
Cdd:cd19144 44 FELGCTFWDTADIYGDS--EELIGRWFKQNPGKREKIFLATKFGIEKNVETGEYSVDGSPEYVKKACETSLKRLGVDYID 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSnfKRSQLSMLESYLPFPLVTNQIEVSAYRL--ENLEDGTVDLCLE 197
Cdd:cd19144 122 LYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS--ECSAETLRRAHAVHPIAAVQIEYSPFSLdiERPEIGVLDTCRE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 198 KRMPPMVWSPLA----GGAIFSADD-------DRAVR-----------LRDTLEQVRGELGAeTIDEVLYAWLFAHPARM 255
Cdd:cd19144 200 LGVAIVAYSPLGrgflTGAIRSPDDfeegdfrRMAPRfqaenfpknleLVDKIKAIAKKKNV-TAGQLTLAWLLAQGDDI 278
|
250 260 270
....*....|....*....|....*....|.
gi 737525220 256 MPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19144 279 IPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-272 |
1.66e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 104.10 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLadWGYSARQLLSLIEFCLERGITTFDHADIYGNytCESRFGDALtlkPSLRSQIEIVTKCGiklpskygm 92
Cdd:cd19100 12 SRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKAL---KGRRDKVFLATKTG--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 klyDTSKDHIIASVEQSLRNFRTDYIDVLLIH------RPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQL-SMLE 165
Cdd:cd19100 76 ---ARDYEGAKRDLERSLKRLGTDYIDLYQLHavdteeDLDQVFGPGGALEALLEAKEEGKIRFIGISGHSPEVLlRALE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 166 SYLP----FPLvtNQIEvsaYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADddravrlrdtleqvrgelgAETID 241
Cdd:cd19100 153 TGEFdvvlFPI--NPAG---DHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGD-------------------PLDPE 208
|
250 260 270
....*....|....*....|....*....|.
gi 737525220 242 EVLyAWLFAHPARMMPIVGSGKQERIERAVR 272
Cdd:cd19100 209 QAL-RYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
13-220 |
1.01e-25 |
|
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: 103.54 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLADW---GYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSlRSQIEIVTKCGIKLPSK 89
Cdd:cd19148 5 SRIALGTWAIGGWmwgGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGK-RDRVVIATKVGLEWDEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 90 yGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLp 169
Cdd:cd19148 84 -GEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVA- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737525220 170 fPLVTNQievSAYRL--ENLEDGTVDLCLEKRMPPMVWSPLAGGAI---------FSADDDR 220
Cdd:cd19148 162 -PLHTVQ---PPYNLfeREIEKDVLPYARKHNIVTLAYGALCRGLLsgkmtkdtkFEGDDLR 219
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
35-275 |
3.87e-25 |
|
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: 102.10 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 35 LIEFCLERGITTFDHADIYGNY--TCESRFGDALT--LKPsLRSQIEIVTKCGIKL-PSKYGmklyD-TSKDHIIASVEQ 108
Cdd:cd19151 35 MLRRAFDLGITHFDLANNYGPPpgSAEENFGRILKedLKP-YRDELIISTKAGYTMwPGPYG----DwGSKKYLIASLDQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 109 SLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFK----RSQLSMLESyLPFPLVTNQIEVSAYRl 184
Cdd:cd19151 110 SLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPpeeaREAAAILKD-LGTPCLIHQPKYSMFN- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 185 ENLEDGTVDLCLEKRMPPMVWSPLAGGAIFS------ADDDRA-------------------VRLRDTLEQVRGelgaET 239
Cdd:cd19151 188 RWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDrylngiPEDSRAakgssflkpeqiteeklakVRRLNEIAQARG----QK 263
|
250 260 270
....*....|....*....|....*....|....*.
gi 737525220 240 IDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALS 275
Cdd:cd19151 264 LAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
34-274 |
8.52e-25 |
|
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: 101.18 E-value: 8.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 34 SLIEFCLERGITTFDHADIYGNY--TCESRFGDAL-TLKPSLRSQIEIVTKCGIKL-PSKYGMKlydTSKDHIIASVEQS 109
Cdd:cd19089 33 ELLRTAFDLGITHFDLANNYGPPpgSAEENFGRILkRDLRPYRDELVISTKAGYGMwPGPYGDG---GSRKYLLASLDQS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 110 LRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLP---FPLVTNQIEVSAYRLEN 186
Cdd:cd19089 110 LKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRelgVPLIIHQPRYSLLDRWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 187 lEDGTVDLCLEKRMPPMVWSPLAGGAIF------SADDDRAVRLR----------DTLEQVRG--ELGAE---TIDEVLY 245
Cdd:cd19089 190 -EDGLLEVLEEAGIGFIAFSPLAQGLLTdkylngIPPDSRRAAESkflteealtpEKLEQLRKlnKIAAKrgqSLAQLAL 268
|
250 260
....*....|....*....|....*....
gi 737525220 246 AWLFAHPARMMPIVGSGKQERIERAVRAL 274
Cdd:cd19089 269 SWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
40-286 |
9.55e-25 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 99.74 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgiklpskygMKLYDTSKDHIIASVEQSLRNFRTDYID 119
Cdd:cd19139 24 LELGYRHIDTAQIYDN---EAAVGQAIAESGVPRDELFITTK----------IWIDNLSKDKLLPSLEESLEKLRTDYVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRPDPF--MNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYL-PFPLVTNQIEVSAYrLENLEDgtVDLCL 196
Cdd:cd19139 91 LTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVgAGAIATNQIELSPY-LQNRKL--VAHCK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 197 EKRMPPMVWSPLAGGAIFsaDDdravrlrDTLEQVRGELGAeTIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSF 276
Cdd:cd19139 168 QHGIHVTSYMTLAYGKVL--DD-------PVLAAIAERHGA-TPAQIALAWAMARGYAVIP--SSTKREHLRSNLLALDL 235
|
250
....*....|
gi 737525220 277 SLSREQWFAI 286
Cdd:cd19139 236 TLDADDMAAI 245
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-275 |
3.62e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 100.28 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRLAdwGYSARQLLSLIEFCLERGITTFDHADIYGNytCESRFGDALtlkPSLRSQIEIVTKcgikLPS 88
Cdd:COG1453 10 GLEVSVLGFGGMRLP--RKDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKAL---KGPRDKVILATK----LPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 89 kygmklYDTSKDHIIASVEQSLRNFRTDYIDVLLIH---RPDPF---MNPEEVAEAFCQLKADGKVRYFGVSN------F 156
Cdd:COG1453 79 ------WVRDPEDMRKDLEESLKRLQTDYIDLYLIHglnTEEDLekvLKPGGALEALEKAKAEGKIRHIGFSThgslevI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 157 KRsqlsMLESYLpFPLVtnQIEVSaYRLENLEDGT--VDLCLEKRMPPMVWSPLAGGAIFSADDDRAVRLRDTLeqvrge 234
Cdd:COG1453 153 KE----AIDTGD-FDFV--QLQYN-YLDQDNQAGEeaLEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLCPPL------ 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 737525220 235 lgaeTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALS 275
Cdd:COG1453 219 ----SPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTAD 255
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
35-287 |
9.44e-23 |
|
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: 95.56 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 35 LIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPSLRSQIEIVTKCGIKLPSkyGMKLYDTSKDHIIASVEQSLRNFR 114
Cdd:cd19083 38 LVREALDNGVNLLDTAFIYGLGRSEELVGEVL--KEYNRNEVVIATKGAHKFGG--DGSVLNNSPEFLRSAVEKSLKRLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 115 TDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESylpfplvTNQIEV--SAYRLEN--LEDG 190
Cdd:cd19083 114 TDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEANK-------DGYVDVlqGEYNLLQreAEED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 191 TVDLCLEKRMPPMVWSPLAGGAI---------FSADDDRA-------------VRLRDTLEQVRGELGAETIDEVLyAWL 248
Cdd:cd19083 187 ILPYCVENNISFIPYFPLASGLLagkytkdtkFPDNDLRNdkplfkgerfsenLDKVDKLKSIADEKGVTVAHLAL-AWY 265
|
250 260 270
....*....|....*....|....*....|....*....
gi 737525220 249 FAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAIL 287
Cdd:cd19083 266 LTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFID 304
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
33-283 |
2.23e-22 |
|
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: 93.77 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 33 LSLIEFCLERGITTFDHADIYGNytCESRFGDALTLKPslRSQIEIVTKCGiKLPSKYgmklYDTSKDHIIASVEQSLRN 112
Cdd:cd19090 23 VATIRAALDLGINYIDTAPAYGD--SEERLGLALAELP--REPLVLSTKVG-RLPEDT----ADYSADRVRRSVEESLER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 113 FRTDYIDVLLIHRPDPF-----MNPEEVAEAFCQLKADGKVRYFGvsnfkrsqLSMLESYLPFPLV-TNQIEV--SAYRL 184
Cdd:cd19090 94 LGRDRIDLLMIHDPERVpwvdiLAPGGALEALLELKEEGLIKHIG--------LGGGPPDLLRRAIeTGDFDVvlTANRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 185 eNL-----EDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDRA--------VRLRDTLEQVRgELGAET---IDEVLYAWL 248
Cdd:cd19090 166 -TLldqsaADELLPAAARHGVGVINASPLGMGLLAGRPPERVrytyrwlsPELLDRAKRLY-ELCDEHgvpLPALALRFL 243
|
250 260 270
....*....|....*....|....*....|....*
gi 737525220 249 FAHPARMMPIVGSGKQERIERAVRALSFSLSREQW 283
Cdd:cd19090 244 LRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-282 |
2.86e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 94.25 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 10 LSFSRVIYGCWRLAD-WGYSARQ-LLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlkPSLRSQIEIVTKCGIKLP 87
Cdd:cd19104 10 LKVSELTFGGGGIGGlMGRTTREeQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRAL---KGLPAGPYITTKVRLDPD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 88 SKygmklyDTSKDHIIASVEQSLRNFRTDYIDVLLIH------RPDP---------FMNPEEVAEAFCQLKADGKVRYFG 152
Cdd:cd19104 87 DL------GDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigdeRDKPvggtlsttdVLGLGGVADAFERLRSEGKIRFIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 153 VSNFKRSQL--SMLESYLP--FPLVTNQIEVSA----YRLENLED--GTVDLCLEKRMPPMVWSPLAGGAI--------- 213
Cdd:cd19104 161 ITGLGNPPAirELLDSGKFdaVQVYYNLLNPSAaearPRGWSAQDygGIIDAAAEHGVGVMGIRVLAAGALttsldrgre 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 214 --------FSADDDRAVRLRDTLEQvrgelGAETIDEVlyAWLFAHPARMMP--IVGSGKQERIERAVRALSF-SLSREQ 282
Cdd:cd19104 241 apptsdsdVAIDFRRAAAFRALARE-----WGETLAQL--AHRFALSNPGVStvLVGVKNREELEEAVAAEAAgPLPAEN 313
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-154 |
3.99e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 92.98 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 28 SARQLLSLIEFCLERGITTFDHADIYGNytCESRFGDALTLKPSLRsqieIVTKCGIKLPSKygmklyDTSKDHIIASVE 107
Cdd:cd19097 24 SEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKRLDKFK----IITKLPPLKEDK------KEDEAAIEASVE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 737525220 108 QSLRNFRTDYIDVLLIHRP-DPFMNPEEVAEAFCQLKADGKVRYFGVS 154
Cdd:cd19097 92 ASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS 139
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-282 |
9.30e-22 |
|
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: 92.88 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 3 RVQL-ADNLSFSRVIYGCWRLADWgYSA----RQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPSLRSQIE 77
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGCMGLSGD-YGApkpeEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKAL--KDGPREKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 78 IVTKCGIKLPSKYGMKLYDTSkDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSnfK 157
Cdd:cd19145 79 LATKFGIHEIGGSGVEVRGDP-AYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLS--E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 158 RSQLSMLESYLPFPLVTNQIEVSAYRlENLEDGTVDLCLEKRMPPMVWSPL-----AGGAIFS---ADDDravrLRDTLE 229
Cdd:cd19145 156 ASADTIRRAHAVHPITAVQLEWSLWT-RDIEEEIIPTCRELGIGIVPYSPLgrgffAGKAKLEellENSD----VRKSHP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737525220 230 QVRGelgaETID--EVLY-------------------AWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19145 231 RFQG----ENLEknKVLYervealakkkgctpaqlalAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKED 300
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-281 |
2.09e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 91.50 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 11 SFSRVIYGCWRLAD-WGYSAR--QLLSLIEFCLERGITTFDHADIYGNytCESRFGDALTL---KPSLRSQIEIVTK-CG 83
Cdd:cd19101 1 TISRVINGMWQLSGgHGGIRDedAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRlrrERDAADDVQIHTKwVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 84 IklPSKYGMklydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDpFMNP--EEVAEAFCQLKADGKVRYFGVSNFKRSQL 161
Cdd:cd19101 79 D--PGELTM-----TRAYVEAAIDRSLKRLGVDRLDLVQFHWWD-YSDPgyLDAAKHLAELQEEGKIRHLGLTNFDTERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 162 S-MLESylPFPLVTNQIEVSAY--RLENledGTVDLCLEKRMPPMVWSPLAGGaiFSADD--DRAVRLRDTLEQVRGELG 236
Cdd:cd19101 151 ReILDA--GVPIVSNQVQYSLLdrRPEN---GMAALCEDHGIKLLAYGTLAGG--LLSEKylGVPEPTGPALETRSLQKY 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737525220 237 AETID---------EVLYA------------------WLFAHPARMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19101 224 KLMIDewggwdlfqELLRTlkaiadkhgvsianvavrWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDE 295
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-282 |
3.98e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 90.86 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNYTCESRFGDalTLKPSLRSQIEIVTKcgiklpskYGMKLYDTSKDHIIASVEQSLRNFRTDYID 119
Cdd:cd19103 42 MAAGLNLWDTAAVYGMGASEKILGE--FLKRYPREDYIISTK--------FTPQIAGQSADPVADMLEGSLARLGTDYID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRPdpfMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLP---FPLVTNQIEVSAYRLENLEDGTVDLCL 196
Cdd:cd19103 112 IYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAkagVSLSAVQNHYSLLYRSSEEAGILDYCK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 197 EKRMPPMVWSPLAGGAI---------FSADDDRAVRLRDTLEQVR------GELGAE---TIDEVLYAWLFAHPArmMPI 258
Cdd:cd19103 189 ENGITFFAYMVLEQGALsgkydtkhpLPEGSGRAETYNPLLPQLEeltavmAEIGAKhgaSIAQVAIAWAIAKGT--TPI 266
|
250 260
....*....|....*....|....
gi 737525220 259 VGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19103 267 IGVTKPHHVEDAARAASITLTDDE 290
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
40-154 |
5.36e-21 |
|
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: 90.41 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNytCESRFGDAL-TLKPSL-RSQIEIVTKCGiklpsKYGMKLYDTSKDHIIASVEQSLRNFRTDY 117
Cdd:cd19164 44 LELGIRAFDTSPYYGP--SEIILGRALkALRDEFpRDTYFIITKVG-----RYGPDDFDYSPEWIRASVERSLRRLHTDY 116
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 737525220 118 IDVLLIHrpD-PFMNPEEVAEAFC---QLKADGKVRYFGVS 154
Cdd:cd19164 117 LDLVYLH--DvEFVADEEVLEALKelfKLKDEGKIRNVGIS 155
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-286 |
3.17e-20 |
|
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: 87.71 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 6 LADNLSFSRVIYGCWRLadWGYSArqlLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgik 85
Cdd:cd19132 1 LNDGTQIPAIGFGTYPL--KGDEG---VEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTK---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 86 LPSKygmklyDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPE-EVAEAFCQLKADGKVRYFGVSNFKRSQLSML 164
Cdd:cd19132 69 LPGR------HHGYEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 165 ESYLPFPLVTNQIEVSAY--RLENLEdgtvdLCLEKRMPPMVWSPLAGGAIFSADddravrlrDTLEQVRGELGAeTIDE 242
Cdd:cd19132 143 IDETGVTPAVNQIELHPYfpQAEQRA-----YHREHGIVTQSWSPLGRGSGLLDE--------PVIKAIAEKHGK-TPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 737525220 243 VLYAWLFAHPArmMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19132 209 VVLRWHVQLGV--VPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-211 |
7.04e-20 |
|
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: 87.90 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 10 LSFSRVIYGCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKcgikLPSK 89
Cdd:cd19142 11 LRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTK----IYWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 90 YGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPfMNP-EEVAEAFCQLKADGKVRYFGVSNFkrSQLSMLESYL 168
Cdd:cd19142 87 YGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADP-MCPmEEVVRAMSYLIDNGLIMYWGTSRW--SPVEIMEAFS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 169 ---PFPLVTNQIEVSAYRLenledgtvdLCLEK---RMPP---------MVWSPLAGG 211
Cdd:cd19142 164 iarQFNCPTPICEQSEYHM---------FCREKmelYMPElynkvgvglITWSPLSLG 212
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
14-161 |
2.23e-19 |
|
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: 86.07 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 14 RVIYGCwrlADWGYSAR-----QLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRsqieIVTKcgikLPS 88
Cdd:cd19075 2 KIILGT---MTFGSQGRfttaeAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERGFK----IDTK----ANP 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737525220 89 KYGMKLydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQL 161
Cdd:cd19075 71 GVGGGL---SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEV 140
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
36-154 |
4.29e-19 |
|
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: 84.91 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 36 IEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCGiklpsKYG---MKLYDTSKDHIIASVEQSLRN 112
Cdd:cd19163 39 VHEALDSGINYIDTAPWYGQGRSETVLGKALKGIP--RDSYYLATKVG-----RYGldpDKMFDFSAERITKSVEESLKR 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 737525220 113 FRTDYIDVLLIHRPD--PFMNP--EEVAEAFCQLKADGKVRYFGVS 154
Cdd:cd19163 112 LGLDYIDIIQVHDIEfaPSLDQilNETLPALQKLKEEGKVRFIGIT 157
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
34-274 |
4.52e-19 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 85.34 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 34 SLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKC----GIKLPSKYGMklydtSKDHIIASVEQS 109
Cdd:cd19143 35 ECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIfwggGGPPPNDRGL-----SRKHIVEGTKAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 110 LRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSmlESY-------LPFPLVtNQIEVSAY 182
Cdd:cd19143 110 LKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIE--EAHeiadrlgLIPPVM-EQPQYNLF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 183 RLENLEDGTVDLCLEKRMPPMVWSPLAGGAI-------------FSADDDRAVRLR------DTLEQVRG------ELGA 237
Cdd:cd19143 187 HRERVEVEYAPLYEKYGLGTTTWSPLASGLLtgkynngipegsrLALPGYEWLKDRkeelgqEKIEKVRKlkpiaeELGC 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 737525220 238 eTIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRAL 274
Cdd:cd19143 267 -SLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKAL 302
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-282 |
7.21e-19 |
|
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: 83.91 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 1 MERVQLADNLSFSRVIYGCWRLAdwGYSARQLLSLIEFClerGITTFDHADIYGnytCESRFGDALTLKPSLRSQIEIVT 80
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTSHSG--GYSHEAVVYALKEC---GYRHIDTAKRYG---CEELLGKAIKESGVPREDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 81 KCgikLPSKYGmklYDTSKdhiiASVEQSLRNFRTDYIDVLLIHRPD---PFMNPEEVAE----AFCQLKADGKVRYFGV 153
Cdd:cd19135 74 KL---WPSDYG---YESTK----QAFEASLKRLGVDYLDLYLLHWPDcpsSGKNVKETRAetwrALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 154 SNFKRSQLSMLESYLPFPLVTNQIEVSAYrleNLEDGTVDLCLEKRMPPMVWSPLAGGAIfsadddravrLRD-TLEQVR 232
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVVPHVNQVEFHPF---QNPVELIEYCRDNNIVFEGYCPLAKGKA----------LEEpTVTELA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 737525220 233 GELGaETIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19135 211 KKYQ-KTPAQILIRWSIQNGVVTIP--KSTKEERIKENCQVFDFSLSEED 257
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
40-282 |
3.88e-18 |
|
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: 82.67 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNYTCESRF---GDALTLKPSLRSQIEIVTKCGIKlpskYGMKLYDTSKDHIIASVEQSLRNFR-T 115
Cdd:cd19077 35 LDAGSNLWNGGEFYGPPDPHANLkllARFFRKYPEYADKVVLSVKGGLD----PDTLRPDGSPEAVRKSIENILRALGgT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 116 DYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSmlESYLPFPLVTNQIEVSAYRLENLEDGTVDLC 195
Cdd:cd19077 111 KKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIR--RAHAVHPIAAVEVEYSLFSREIEENGVLETC 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 196 LEKRMPPMVWSPLA----GGAIFSADD--DRAVR----------LRDTLEQVRG--ELGAE---TIDEVLYAWLFA-HPA 253
Cdd:cd19077 189 AELGIPIIAYSPLGrgllTGRIKSLADipEGDFRrhldrfngenFEKNLKLVDAlqELAEKkgcTPAQLALAWILAqSGP 268
|
250 260
....*....|....*....|....*....
gi 737525220 254 RMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19077 269 KIIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
40-286 |
4.62e-18 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 81.99 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCGIklpSKYgmklydtSKDHIIASVEQSLRNFRTDYID 119
Cdd:PRK11172 26 LELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWI---DNL-------AKDKLIPSLKESLQKLRTDYVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRPDP--------FMnpEEVAEAfcqlKADGKVRYFGVSNFKRSQL-SMLESYLPFPLVTNQIEVSAYrLENLEdg 190
Cdd:PRK11172 93 LTLIHWPSPndevsveeFM--QALLEA----KKQGLTREIGISNFTIALMkQAIAAVGAENIATNQIELSPY-LQNRK-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 191 TVDLCLEKRMPPMVWSPLAGGAIfsadddravrLRD-TLEQVRGELGAeTIDEVLYAWLFAHPARMMPivGSGKQERIER 269
Cdd:PRK11172 164 VVAFAKEHGIHVTSYMTLAYGKV----------LKDpVIARIAAKHNA-TPAQVILAWAMQLGYSVIP--SSTKRENLAS 230
|
250
....*....|....*..
gi 737525220 270 AVRALSFSLSREQWFAI 286
Cdd:PRK11172 231 NLLAQDLQLDAEDMAAI 247
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
10-220 |
5.77e-18 |
|
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.
Pssm-ID: 213602 [Multi-domain] Cd Length: 317 Bit Score: 82.29 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 10 LSFSRVIYGCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKC--GIKLP 87
Cdd:TIGR01293 9 LRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTKIfwGGKAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 88 SKYGMklydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFkrSQLSMLESY 167
Cdd:TIGR01293 89 TERGL-----SRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRW--SSMEIMEAY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 737525220 168 L---PFPLVTNQIEVSAYRL---ENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDR 220
Cdd:TIGR01293 162 SvarQFNLIPPICEQAEYHMfqrEKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSG 220
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
13-275 |
8.45e-18 |
|
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: 80.68 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRL---ADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCGIKLpsk 89
Cdd:cd19096 1 SVLGFGTMRLpesDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGP--REKFYLATKLPPWS--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 90 ygmklyDTSKDHIIASVEQSLRNFRTDYIDVLLIH---RPD--PFMNPEEVAEAFCQLKADGKVRYFGVS------NFKR 158
Cdd:cd19096 76 ------VKSAEDFRRILEESLKRLGVDYIDFYLLHglnSPEwlEKARKGGLLEFLEKAKKEGLIRHIGFSfhdspeLLKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 159 sqlsMLESYlPFPLVTNQIEVSAYRLENLEDGtVDLCLEKRMPPMVWSPLAGGaifsadddravRLRDTLEQVRGELGAE 238
Cdd:cd19096 150 ----ILDSY-DFDFVQLQYNYLDQENQAGRPG-IEYAAKKGMGVIIMEPLKGG-----------GLANNPPEALAILCGA 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 737525220 239 --TIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALS 275
Cdd:cd19096 213 plSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
35-220 |
1.20e-17 |
|
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: 81.34 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 35 LIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKC--GIKLPSKYGMklydtSKDHIIASVEQSLRN 112
Cdd:cd19141 35 LVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIfwGGKAETERGL-----SRKHIIEGLKASLER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 113 FRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFkrSQLSMLESYL---PFPLVTNQIEVSAYRLENLED 189
Cdd:cd19141 110 LQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRW--SAMEIMEAYSvarQFNLIPPIVEQAEYHLFQREK 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 737525220 190 gtvdlcLEKRMP---------PMVWSPLAGGAIFSADDDR 220
Cdd:cd19141 188 ------VEMQLPelfhkigvgAMTWSPLACGILSGKYDDG 221
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
34-288 |
1.49e-17 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 81.57 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 34 SLIEFCLERGITTFDHADIYGNY--TCESRFGDALT--LKPsLRSQIEIVTKCGIKL-PSKYGMklyDTSKDHIIASVEQ 108
Cdd:PRK09912 47 AILRKAFDLGITHFDLANNYGPPpgSAEENFGRLLRedFAA-YRDELIISTKAGYDMwPGPYGS---GGSRKYLLASLDQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 109 SLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNF--KRSQ-LSMLESYLPFPLVTNQievSAYRLE 185
Cdd:PRK09912 123 SLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYspERTQkMVELLREWKIPLLIHQ---PSYNLL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 186 NL---EDGTVDLCLEKRMPPMVWSPLAGG----------------------------AIFSADDDRAVRLRDTLEQVRGe 234
Cdd:PRK09912 200 NRwvdKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKMLTEANLNSLRLLNEMAQQRG- 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 737525220 235 lgaETIDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALS-FSLSREQWFAILQ 288
Cdd:PRK09912 279 ---QSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNnLTFSTEELAQIDQ 330
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
40-282 |
1.19e-16 |
|
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: 77.67 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNytcESRFGDALT---LKPSL-RSQIEIVTKCGiklPSKYGmklYDTSKdhiiASVEQSLRNFRT 115
Cdd:cd19136 25 LKAGYRLIDTASVYRN---EADIGKALRdllPKYGLsREDIFITSKLA---PKDQG---YEKAR----AACLGSLERLGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 116 DYIDVLLIH-------RPDPFMNPE---EVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAYRLE 185
Cdd:cd19136 92 DYLDLYLIHwpgvqglKPSDPRNAElrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAVNQVEFHPHLVQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 186 N-LedgtVDLCLEKRMPPMVWSPLAGGAIFSADDDRAVRLRDTLeqvrgelgAETIDEVLYAWLFAHPARMMPivGSGKQ 264
Cdd:cd19136 172 KeL----LKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKY--------GRTPAQVLLRWALQQGIGVIP--KSTNP 237
|
250
....*....|....*...
gi 737525220 265 ERIERAVRALSFSLSREQ 282
Cdd:cd19136 238 ERIAENIKVFDFELSEED 255
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-293 |
1.95e-16 |
|
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: 77.17 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 4 VQLADNLSFSRVIYGCWRLADwgysARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcg 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD----GAEAENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIRESGVPREEVFVTTK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 84 iklpskygmkLYDTSK--DHIIASVEQSLRNFRTDYIDVLLIHRP--DPFMnpeEVAEAFCQLKADGKVRYFGVSNFKRS 159
Cdd:cd19156 72 ----------LWNSDQgyESTLAAFEESLEKLGLDYVDLYLIHWPvkGKFK---DTWKAFEKLYKEKKVRAIGVSNFHEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 160 QLS-MLESYLPFPLVtNQIEVsaYRLENLEDgTVDLCLEKRMPPMVWSPLAGGAIFSadddravrlrdtlEQVRGELGA- 237
Cdd:cd19156 139 HLEeLLKSCKVAPMV-NQIEL--HPLLTQEP-LRKFCKEKNIAVEAWSPLGQGKLLS-------------NPVLKAIGKk 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 238 --ETIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFSLSREQWFAILQSSMGH 293
Cdd:cd19156 202 ygKSAAQVIIRWDIQHGIITIP--KSVHEERIQENFDVFDFELTAEEIRQIDGLNTDH 257
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
9-213 |
2.13e-16 |
|
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: 78.16 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRLADWGYSARQLL-----SLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKC- 82
Cdd:cd19159 5 NLGKSGLRVSCLGLGTWVTFGGQISdevaeRLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 83 -GIKLPSKYGMklydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFkrSQL 161
Cdd:cd19159 85 wGGKAETERGL-----SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW--SAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 162 SMLESYLP------FPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAI 213
Cdd:cd19159 158 EIMEAYSVarqfnmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGII 215
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
9-213 |
2.43e-16 |
|
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: 77.82 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRLADWGYSARQLL-----SLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKC- 82
Cdd:cd19158 5 NLGKSGLRVSCLGLGTWVTFGGQITdemaeHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 83 -GIKLPSKYGMklydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFkrSQL 161
Cdd:cd19158 85 wGGKAETERGL-----SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW--SSM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 162 SMLESYLP------FPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAI 213
Cdd:cd19158 158 EIMEAYSVarqfnlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIV 215
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
9-220 |
3.17e-16 |
|
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: 77.72 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 9 NLSFSRVIYGCWRLADWGYSARQLL-----SLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKC- 82
Cdd:cd19160 7 NLGKSGLRVSCLGLGTWVTFGSQISdetaeDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 83 -GIKLPSKYGMklydtSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQL 161
Cdd:cd19160 87 wGGQAETERGL-----SRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737525220 162 ----SMLESYLPFPLVTNQIEVSAYRLENLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDR 220
Cdd:cd19160 162 meaySVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGR 224
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
48-282 |
4.61e-16 |
|
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: 76.79 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 48 DHADIYGNYTCESRFGDALTLKpSLRSQIEIVTKCGIKLpSKYGMKLYDT------SKDHIIASVEQSLRNFRTDYIDVL 121
Cdd:cd19147 52 DTANNYQDEQSETWIGEWMKSR-KNRDQIVIATKFTTDY-KAYEVGKGKAvnycgnHKRSLHVSVRDSLRKLQTDWIDIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 122 LIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESY------LPFPLVTNQIEVSAyrlENLEDGTVDLC 195
Cdd:cd19147 130 YVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYatahgkTPFSVYQGRWNVLN---RDFERDIIPMA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 196 LEKRMPPMVWSPLAGGAIFSAD---------------------DDRAVRLRDTLEQVRGELGAETIDEVLYAWLFAHPAR 254
Cdd:cd19147 207 RHFGMALAPWDVLGGGKFQSKKaveerkkngeglrsfvggteqTPEEVKISEALEKVAEEHGTESVTAIALAYVRSKAPN 286
|
250 260
....*....|....*....|....*...
gi 737525220 255 MMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19147 287 VFPLVGGRKIEHLKDNIEALSIKLTPEE 314
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
4-215 |
7.56e-16 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 75.49 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 4 VQLADNLSFSRVIYGCWRLADwgysaRQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcg 83
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSN-----DEAASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 84 iklpskygmkLYDTSKDHIIA--SVEQSLRNFRTDYIDVLLIHRPDP----FMnpeEVAEAFCQLKADGKVRYFGVSNFK 157
Cdd:cd19131 72 ----------LWNSDQGYDSTlrAFDESLRKLGLDYVDLYLIHWPVPaqdkYV---ETWKALIELKKEGRVKSIGVSNFT 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 737525220 158 RSQLSMLESYLPFPLVTNQIEVSAyRLENLEdgTVDLCLEKRMPPMVWSPLAGGAIFS 215
Cdd:cd19131 139 IEHLQRLIDETGVVPVVNQIELHP-RFQQRE--LRAFHAKHGIQTESWSPLGQGGLLS 193
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-154 |
1.34e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 75.43 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 10 LSFSRVIYGCWRLADWGYSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALT----LKPSLRSQIEIVTKCGI- 84
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRelieKGGIKRDEVVIVTKAGYi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 85 ---------------KLPSKYGMKLYDT-------SKDHIIASVEQSLRNFRTDYIDVLLIHrpdpfmNPEE-------- 134
Cdd:cd19099 81 pgdgdeplrplkyleEKLGRGLIDVADSaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLH------NPEEqllelgee 154
|
170 180
....*....|....*....|....*...
gi 737525220 135 -----VAEAFCQL---KADGKVRYFGVS 154
Cdd:cd19099 155 efydrLEEAFEALeeaVAEGKIRYYGIS 182
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-286 |
1.56e-15 |
|
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: 74.87 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 14 RVIYGCWRLADwgySARQllSLIEFCLERGITTFDHADIYGNytcESRFGDALTlkpslrsqiEIVTKCGIKLPSKY-GM 92
Cdd:cd19128 3 RLGFGTYKITE---SESK--EAVKNAIKAGYRHIDCAYYYGN---EAFIGIAFS---------EIFKDGGVKREDLFiTS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 KLYDT--SKDHIIASVEQSLRNFRTDYIDVLLIHRP---------DPFMNP----------EEVAEAFCQLKADGKVRYF 151
Cdd:cd19128 66 KLWPTmhQPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgDPRDDNqiqslskkplEDTWRAMEQCVDEKLTKNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 152 GVSNFKRSQLSMLESYLPFPLVTNQIEVSAYrLENleDGTVDLCLEKRMPPMVWSPLAGGaifSADDDRAVRLRDTLEQV 231
Cdd:cd19128 146 GVSNYSTKLLTDLLNYCKIKPFMNQIECHPY-FQN--DKLIKFCIENNIHVTAYRPLGGS---YGDGNLTFLNDSELKAL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 737525220 232 RGELGAeTIDEVLYAW-LFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19128 220 ATKYNT-TPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-281 |
2.21e-15 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 74.35 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 4 VQLADNLSFSRVIYGCWRLADwgysARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCg 83
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEE----GSEVVNAVKTALKNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 84 ikLPSKYGmklYDTSkdhiIASVEQSLRNFRTDYIDVLLIHRPDPFMNpEEVAEAFCQLKADGKVRYFGVSNFKRSQLSM 163
Cdd:cd19157 74 --WNADQG---YDST----LKAFEASLERLGLDYLDLYLIHWPVKGKY-KETWKALEKLYKDGRVRAIGVSNFQVHHLED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 164 LESYLPFPLVTNQIEVSAyRLENLEdgTVDLCLEKRMPPMVWSPLAGGAIFSadddravrlRDTLEQVrGELGAETIDEV 243
Cdd:cd19157 144 LLADAEIVPMVNQVEFHP-RLTQKE--LRDYCKKQGIQLEAWSPLMQGQLLD---------NPVLKEI-AEKYNKSVAQV 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 737525220 244 LYAWLFAHpaRMMPIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19157 211 ILRWDLQN--GVVTIPKSIKEHRIIENADVFDFELSQE 246
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
39-284 |
5.16e-15 |
|
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: 74.14 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 39 CLERGITTFDHADIY--------GNYTcESRFGDALTLKPSlRSQIEIVTK-CG----IKLPSKYGMKLydtSKDHIIAS 105
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetQGRT-EEIIGSWLKKKGN-RDKVVLATKvAGpgegITWPRGGGTRL---DRENIREA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 106 VEQSLRNFRTDYIDVLLIHRPD------------------PFMNPEEVAEAFCQLKADGKVRYFGVSN------FKRSQL 161
Cdd:cd19094 102 VEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvMKFLEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 162 SMLESYLPFPLVTNqievsAYRL--ENLEDGTVDLCLEKRMPPMVWSPLAGGAI---FSADDDRAVRLRDTL-----EQV 231
Cdd:cd19094 182 AEQLGLPRIVSIQN-----PYSLlnRNFEEGLAEACHRENVGLLAYSPLAGGVLtgkYLDGAARPEGGRLNLfpgymARY 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 737525220 232 RGELGAETIDEvlYAWLFahparmmpivgsgKQERIERAVRALSFSLSReqWF 284
Cdd:cd19094 257 RSPQALEAVAE--YVKLA-------------RKHGLSPAQLALAWVRSR--PF 292
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-290 |
6.30e-15 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 73.30 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDAL-------TLKpslRSQIEIVTKcgikLPSkYGMKL 94
Cdd:cd19111 9 LGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQN---EKAIGEALkwwlkngKLK---REEVFITTK----LPP-VYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 95 YDTSKdhiiaSVEQSLRNFRTDYIDVLLIHRPDPFMNP-------------EEVAEAFCQLKADGKVRYFGVSNFKRSQL 161
Cdd:cd19111 78 KDTEK-----SLEKSLENLKLPYVDLYLIHHPCGFVNKkdkgerelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 162 SMLESYLPFPLVTNQIEVSAYRLENledGTVDLCLEKRMPPMVWSPLA--GGAIFSADDDRAVRLRD-TLEQVRGELGaE 238
Cdd:cd19111 153 NKILAYAKVKPSNLQLECHAYLQQR---ELRKFCNKKNIVVTAYAPLGspGRANQSLWPDQPDLLEDpTVLAIAKELD-K 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 737525220 239 TIDEVLYAwlFAHPARMMPIVGSGKQERIERAVRALSFSLSREQwFAILQSS 290
Cdd:cd19111 229 TPAQVLLR--FVLQRGTGVLPKSTNKERIEENFEVFDFELTEEH-FKKLKTL 277
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
36-211 |
7.42e-15 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 73.34 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 36 IEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKCGiklpsKYGMKLYDTSKDHIIASVEQSLRNFRT 115
Cdd:cd19153 39 VAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVG-----RYRDSEFDYSAERVRASVATSLERLHT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 116 DYIDVLLIHR---PDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTnqiEVSAYRLENLEDGTv 192
Cdd:cd19153 114 TYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLD---AVLSYCHLTLQDAR- 189
|
170 180
....*....|....*....|....*...
gi 737525220 193 dlcLEKRMP-------PMVW--SPLAGG 211
Cdd:cd19153 190 ---LESDAPglvrgagPHVInaSPLSMG 214
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
40-274 |
8.63e-15 |
|
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: 73.26 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNY--TCESRFGDALT--LKPsLRSQIEIVTKCGIKL-PSKYGMKlydTSKDHIIASVEQSLRNFR 114
Cdd:cd19150 40 FDLGITHFDLANNYGPPpgSAEENFGRILRedFAG-YRDELIISTKAGYDMwPGPYGEW---GSRKYLLASLDQSLKRMG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 115 TDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNF---KRSQLSMLESYLPFPLVTNQievSAYRLENL---E 188
Cdd:cd19150 116 LDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYspeRTREAAAILRELGTPLLIHQ---PSYNMLNRwveE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 189 DGTVDLCLEKRMPPMVWSPLAGG------------------------AIFSADDDRAVRLRDTLEQVRGelgaETIDEVL 244
Cdd:cd19150 193 SGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsraskerslspKMLTEANLNSIRALNEIAQKRG----QSLAQMA 268
|
250 260 270
....*....|....*....|....*....|
gi 737525220 245 YAWLFAHPARMMPIVGSGKQERIERAVRAL 274
Cdd:cd19150 269 LAWVLRDGRVTSALIGASRPEQLEENVGAL 298
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
22-286 |
1.34e-14 |
|
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: 72.44 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALT--LKPSL--RSQIEIVTKcgiklpskygmkLYDT 97
Cdd:cd19123 17 LGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGN---EAEIGAALAevFKEGKvkREDLWITSK------------LWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 98 S--KDHIIASVEQSLRNFRTDYIDVLLIHRPDPF---------------MNPEEVAE---AFCQLKADGKVRYFGVSNFK 157
Cdd:cd19123 82 ShaPEDVLPALEKTLADLQLDYLDLYLMHWPVALkkgvgfpesgedllsLSPIPLEDtwrAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 158 RSQLSMLESYLPFPLVTNQIEVSAYrLENLEdgTVDLCLEKRMPPMVWSPLAGG----AIFSADDDRAvrLRD-TLEQVR 232
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPY-LQQPE--LLAFCRDNGIHLTAYSPLGSGdrpaAMKAEGEPVL--LEDpVINKIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 737525220 233 GELGAeTIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19123 237 EKHGA-SPAQVLIAWAIQRGTVVIP--KSVNPERIQQNLEAAEVELDASDMATI 287
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
40-286 |
1.52e-14 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 71.70 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgiklpskygMKLYDTSKDHIIASVEQSLRNFRTDYID 119
Cdd:cd19126 33 LENGYRSIDTAAIYKN---EEGVGEAIRESGVPREELFVTTK----------LWNDDQRARRTEDAFQESLDRLGLDYVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRP--DPFMnpeEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAYrLENLEdgTVDLCLE 197
Cdd:cd19126 100 LYLIHWPgkDKFI---DTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPY-LTQKE--LRGYCKS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 198 KRMPPMVWSPLAGGAIfsADDDRAVRLrdtleqvrGELGAETIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFS 277
Cdd:cd19126 174 KGIVVEAWSPLGQGGL--LSNPVLAAI--------GEKYGKSAAQVVLRWDIQHGVVTIP--KSVHASRIKENADIFDFE 241
|
....*....
gi 737525220 278 LSREQWFAI 286
Cdd:cd19126 242 LSEDDMTAI 250
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
3-286 |
1.59e-14 |
|
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: 71.87 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 3 RVQLADNLSFSRVIYGCWRLADwgysaRQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKC 82
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPP-----ADTQRAVATALEVGYRHIDTAAIYGN---EEGVGAAIAASGIPRDELFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 83 GIKlpskygmklyDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFM-NPEEVAEAFCQLKADGKVRYFGVSNFKRSQL 161
Cdd:cd19130 73 WND----------RHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAgNYVHTWEAMIELRAAGRTRSIGVSNFLPPHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 162 SMLESYLPFPLVTNQIEVSAYrLENLEdgTVDLCLEKRMPPMVWSPLAGGAIFsadDDRAVrlrdtleqvrGELGA---E 238
Cdd:cd19130 143 ERIVAATGVVPAVNQIELHPA-YQQRT--IRDWAQAHDVKIEAWSPLGQGKLL---GDPPV----------GAIAAahgK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 737525220 239 TIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19130 207 TPAQIVLRWHLQKGHVVFP--KSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-283 |
2.13e-14 |
|
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: 71.87 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLADwGY---SARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCGIKL--- 86
Cdd:cd19152 1 PKLGFGTAPLGN-LYeavSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLvpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 87 --PSKYGMKL----------YDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAE-----------AFCQLK 143
Cdd:cd19152 78 qeVEPTFEPGfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEhfaqaikgafrALEELR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 144 ADGKVRYFGV-SNFKRSQLSMLESYLP-FPLVTNQ---IEVSAyrlenlEDGTVDLCLEKRMPPMVWSP-----LAGGAI 213
Cdd:cd19152 158 EEGVIKAIGLgVNDWEVILRILEEADLdWVMLAGRytlLDHSA------ARELLPECEKRGVKVVNAGPfnsgfLAGGDN 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737525220 214 FSADDDR-----AVRLRDTLEQVrgelgAET----IDEVLYAWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQW 283
Cdd:cd19152 232 FDYYEYGpappeLIARRDRIEAL-----CEQhgvsLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAAFW 305
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
22-218 |
2.70e-14 |
|
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: 71.41 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALtlKPSL-----RSQIEIVTKCgiklpskygmklYD 96
Cdd:cd19121 17 LGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQN---EDEVGEGI--KEAIaggvkREDLFVTTKL------------WS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 97 TSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPfMNPEEVAEAFCQLK-----------------------ADGKVRYFGV 153
Cdd:cd19121 80 TYHRRVELCLDRSLKSLGLDYVDLYLVHWPVL-LNPNGNHDLFPTLPdgsrdldwdwnhvdtwkqmekvlKTGKTKAIGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 154 SNFkrsQLSMLESYLPFPLVT---NQIEVSAYrLENLEdgTVDLCLEKRMPPMVWSPL--AGGAIFSADD 218
Cdd:cd19121 159 SNY---SIPYLEELLKHATVVpavNQVENHPY-LPQQE--LVDFCKEKGILIEAYSPLgsTGSPLISDEP 222
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
45-288 |
4.42e-14 |
|
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: 71.11 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 45 TTFDHADIYGNYTCESRFGDA----LTLKPSL-RSQIEIVTKCGIKLpskygmklydTSKDHIIASVEQSLRNFRTDYID 119
Cdd:cd19122 36 VGYRHLDCAWFYLNEDEVGDAvrdfLKENPSVkREDLFICTKVWNHL----------HEPEDVKWSIDNSLKNLKLDYID 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRP-----------------------DPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQ 176
Cdd:cd19122 106 LFLVHWPiaaekndqrspklgpdgkyvilkDLTENPEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 177 IEVSAYrLENLEdgTVDLCLEKRMPPMVWSPLAGGAIFSADDDRaVRLRDTLEQVrGELGAETIDEVLYAWLFAHPARMM 256
Cdd:cd19122 186 IEIHPF-LPNEE--LVDYCFSNDILPEAYSPLGSQNQVPSTGER-VSENPTLNEV-AEKGGYSLAQVLIAWGLRRGYVVL 260
|
250 260 270
....*....|....*....|....*....|..
gi 737525220 257 PivGSGKQERIERAVRalSFSLSREQWFAILQ 288
Cdd:cd19122 261 P--KSSTPSRIESNFK--SIELSDEDFEAINQ 288
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
40-215 |
5.00e-14 |
|
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: 70.30 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 40 LERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCGIKlpskygmklyDTSKDHIIASVEQSLRNFRTDYID 119
Cdd:cd19133 33 IKAGYRLIDTAAAYGN---EEAVGRAIKKSGIPREELFITTKLWIQ----------DAGYEKAKKAFERSLKRLGLDYLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 120 VLLIHRpdPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLesyLPF----PLVtNQIEVSAYrleNLEDGTVDLC 195
Cdd:cd19133 100 LYLIHQ--PFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDL---ILHnevkPAV-NQIETHPF---NQQIEAVEFL 170
|
170 180
....*....|....*....|..
gi 737525220 196 LEKRMPPMVWSPLAGG--AIFS 215
Cdd:cd19133 171 KKYGVQIEAWGPFAEGrnNLFE 192
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
34-282 |
9.13e-14 |
|
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: 70.53 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 34 SLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPSlRSQIEIVTK--------CGIKLPSKYGmklyDTSKDHIIAS 105
Cdd:cd19146 39 KLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGN-RDEMVLATKyttgyrrgGPIKIKSNYQ----GNHAKSLRLS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 106 VEQSLRNFRTDYIDVLLIHRPDPFMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPF----PLVTNQIEVS- 180
Cdd:cd19146 114 VEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAhgltQFVVYQGHWSa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 181 AYRleNLEDGTVDLCLEKRMPPMVWSPLAGGAIFSADDDRA---------------VRLRDTLEQVRGELGAeTIDEVLY 245
Cdd:cd19146 194 AFR--DFERDILPMCEAEGMALAPWGVLGQGQFRTEEEFKRrgrsgrkggpqtekeRKVSEKLEKVAEEKGT-AITSVAL 270
|
250 260 270
....*....|....*....|....*....|....*..
gi 737525220 246 AWLFAHPARMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19146 271 AYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEE 307
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
28-286 |
9.27e-14 |
|
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: 69.74 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 28 SARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCGIklpSKYGmklydtsKDHIIASVE 107
Cdd:cd19127 20 PPEETADAVATALADGYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWI---SDYG-------YDKALRGFD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 108 QSLRNFRTDYIDVLLIHRPDP--FMNPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAY--- 182
Cdd:cd19127 87 ASLRRLGLDYVDLYLLHWPVPndFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVELHPYfsq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 183 ---RLENLEDGTVDLClekrmppmvWSPLAGGAIFSADDDRAVR--LRDTLEQVRGELGAETIDEVLYAWLFAHpaRMMP 257
Cdd:cd19127 167 kdlRAFHRRLGIVTQA---------WSPIGGVMRYGASGPTGPGdvLQDPTITGLAEKYGKTPAQIVLRWHLQN--GVSA 235
|
250 260
....*....|....*....|....*....
gi 737525220 258 IVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19127 236 IPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
93-281 |
1.01e-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: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 KLY--DTSKDHIIASVEQSLRNFRTDYIDVLLIH-----RPDPFMNP-----------EEVAEAFCQLKADGKVRYFGVS 154
Cdd:cd19124 73 KLWcsDAHPDLVLPALKKSLRNLQLEYVDLYLIHwpvslKPGKFSFPieeedflpfdiKGVWEAMEECQRLGLTKAIGVS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 155 NFKRSQLSMLESYLPFPLVTNQIEVS-AYRLENLedgtVDLCLEKRMPPMVWSPLAGGAIFSADDdrAVRLRDTLEQVRG 233
Cdd:cd19124 153 NFSCKKLQELLSFATIPPAVNQVEMNpAWQQKKL----REFCKANGIHVTAYSPLGAPGTKWGSN--AVMESDVLKEIAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 737525220 234 ELGAeTIDEVLYAWLFAHPARMmpIVGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19124 227 AKGK-TVAQVSLRWVYEQGVSL--VVKSFNKERMKQNLDIFDWELTEE 271
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
28-152 |
3.00e-13 |
|
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: 68.89 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 28 SARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCGIKL-PSKYGMKL------------ 94
Cdd:cd19161 18 SNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKVGRLLkPAREGSVPdpngfvdplpfe 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737525220 95 --YDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVA------------EAFCQLKADGKVRYFG 152
Cdd:cd19161 96 ivYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKErhhfaqlmsggfKALEELKKAGVIKAFG 167
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
43-196 |
1.81e-12 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 66.34 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 43 GITTFDHADIYGNYTCESRFGDALTLKPSLRSQIEIVTKCGiklpsKYGmKLYDTSKDHIIASVEQSLRNFRTDYIDVLL 122
Cdd:PLN02587 44 GINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKCG-----RYG-EGFDFSAERVTKSVDESLARLQLDYVDILH 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737525220 123 IH-----RPDPFMNpeEVAEAFCQLKADGKVRYFGVSNfkrsqlsmlesyLPFPLVTnqievsaYRLENLEDGTVDLCL 196
Cdd:PLN02587 118 CHdiefgSLDQIVN--ETIPALQKLKESGKVRFIGITG------------LPLAIFT-------YVLDRVPPGTVDVIL 175
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-154 |
1.88e-12 |
|
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: 66.23 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 13 SRVIYGCWRLADWG-YSARQLLSLIEFCLERGITTFDHADIYGNYTCESRFGDALTLKPslRSQIEIVTKCGIKL----- 86
Cdd:cd19162 1 PRLGLGAASLGNLArAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHP--RAEYVVSTKVGRLLepgaa 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737525220 87 -PSKYGMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNpEEVAEAF---CQLKADGKVRYFGVS 154
Cdd:cd19162 79 gRPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLL-QALTDAFpalEELRAEGVVGAIGVG 149
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
36-286 |
6.89e-12 |
|
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: 64.44 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 36 IEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgiklpskygmkLYDTSKDHIIASVEQSLRNFRT 115
Cdd:cd19117 33 VEAALKAGYRHIDTAAIYGN---EEEVGQGIKDSGVPREEIFITTK------------LWCTWHRRVEEALDQSLKKLGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 116 DYIDVLLIHRPDPFM---------------------NPEEVAEAFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLV- 173
Cdd:cd19117 98 DYVDLYLMHWPVPLDpdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 174 -TNQIEVSAYrleNLEDGTVDLCLEKRMPPMVWSPLAggaifSADddrAVRLRDTLEQVRGELGAETIDEVLYAWLFAHP 252
Cdd:cd19117 178 aVNQIELHPL---LPQPKLVDFCKSKGIHATAYSPLG-----STN---APLLKEPVIIKIAKKHGKTPAQVIISWGLQRG 246
|
250 260 270
....*....|....*....|....*....|....
gi 737525220 253 ARMMPivGSGKQERIERAVRAlsFSLSREQWFAI 286
Cdd:cd19117 247 YSVLP--KSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
36-286 |
2.87e-11 |
|
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: 62.81 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 36 IEFCLERGITTFDHADIYGNytcESRFGDALTlkpSLRSQIEIVTKCGIKLPSKygmkLYDTS--KDHIIASVEQSLRNF 113
Cdd:cd19118 26 VKIALKAGYRHLDLAKVYQN---QHEVGQALK---ELLKEEPGVKREDLFITSK----LWNNShrPEYVEPALDDTLKEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 114 RTDYIDVLLIHRPDPF-------------MNPEEVA-----------EAFCQLKADGKVRYFGVSNFKRSQL-SMLESYL 168
Cdd:cd19118 96 GLDYLDLYLIHWPVAFkptgdlnpltavpTNGGEVDldlsvslvdtwKAMVELKKTGKVKSIGVSNFSIDHLqAIIEETG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 169 PFPLVtNQIEVSAyRLenLEDGTVDLCLEKRMPPMVWSPLAGGAIfsadddRAVRL--RDTLEQVRGELGaETIDEVLYA 246
Cdd:cd19118 176 VVPAV-NQIEAHP-LL--LQDELVDYCKSKNIHITAYSPLGNNLA------GLPLLvqHPEVKAIAAKLG-KTPAQVLIA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 737525220 247 WlfAHPARMMPIVGSGKQERIERAVRalSFSLSREQWFAI 286
Cdd:cd19118 245 W--GIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAV 280
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
17-282 |
2.93e-11 |
|
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: 62.89 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 17 YGCWRLadwgySARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTL--KPSL--RSQIEIVTKcgiklpskygm 92
Cdd:cd19112 16 LGVWRM-----EPGEIKELILNAIKIGYRHFDCAADYKN---EKEVGEALAEafKTGLvkREDLFITTK----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 kLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRP-----------DPFMNPEEVAEAFC------------QLKADGKVR 149
Cdd:cd19112 77 -LWNSDHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttGSALGEDGVLDIDVtislettwhameKLVSAGLVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 150 YFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAYRlenLEDGTVDLCLEKRMPPMVWSPLAGGAifsADDDR--AVR-LRD 226
Cdd:cd19112 156 SIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYF---QRDSLVKFCQKHGISVTAHTPLGGAA---ANAEWfgSVSpLDD 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 737525220 227 TLEQVRGELGAETIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIP--KSSKPERLKENIDVFDFQLSKED 283
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
22-281 |
3.07e-11 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 62.81 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDAL-------TLKpslRSQIEIVTKcgikLPSKYgmkl 94
Cdd:cd19154 17 LGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQN---EEAIGEALaelleegVVK---REDLFITTK----LWTHE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 95 ydTSKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPE----------------EVAEAFCQLKA---DGKVRYFGVSN 155
Cdd:cd19154 83 --HAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEgesgtmengmsihdavDVEDVWRGMEKvydEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 156 FKRSQLSMLESYLPFPLVTNQIEVSAYrLENLEdgTVDLCLEKRMPPMVWSPLA--GGAIFSADDDRAVRLRDTLEQVRG 233
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLY-FPQKE--LVEFCKKHNISVTSYATLGspGRANFTKSTGVSPAPNLLQDPIVK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 737525220 234 ELGA---ETIDEVLYAWLFAHPARMMPivGSGKQERIERAVRALSFSLSRE 281
Cdd:cd19154 238 AIAEkhgKTPAQVLLRYLLQRGIAVIP--KSATPSRIKENFNIFDFSLSEE 286
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
22-178 |
1.05e-10 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKcgiklpskygmkLYDTSKDH 101
Cdd:PRK11565 20 LGVWQASNEEVITAIHKALEVGYRSIDTAAIYKN---EEGVGKALKEASVAREELFITTK------------LWNDDHKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 102 IIASVEQSLRNFRTDYIDVLLIHRPDPFMNpeEVAEAFCQ---LKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIE 178
Cdd:PRK11565 85 PREALEESLKKLQLDYVDLYLMHWPVPAID--HYVEAWKGmieLQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIE 162
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-282 |
1.97e-10 |
|
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: 60.37 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 3 RVQLADNLSFSRVIYGCWRLADwgysARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPSL----RSQIEI 78
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKD----DEGVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREKIAEgvvkREDLFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 79 VTKcgiklpskygmkLYDT--SKDHIIASVEQSLRNFRTDYIDVLLIHRP-------DPFMNPE---------EVAEAFC 140
Cdd:cd19116 75 TTK------------LWNSyhEREQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGME 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 141 QLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSayrLENLEDGTVDLCLEKRMPPMVWSPLaGGAIFSADDDR 220
Cdd:cd19116 143 DLVKLGLTRSIGVSNFNSEQINRLLSNCNIKPAVNQIEVH---PTLTQEKLVAYCQSNGIVVMAYSPF-GRLVPRGQTNP 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737525220 221 AVRLRDTLEQVRGELGAETIDEVLYAWLFAHpaRMMPIVGSGKQERIERAVRALSFSLSREQ 282
Cdd:cd19116 219 PPRLDDPTLVAIAKKYGKTTAQIVLRYLIDR--GVVPIPKSSNKKRIKENIDIFDFQLTPEE 278
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-286 |
7.50e-10 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 58.33 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 4 VQLADNLSFSRVIYGCWRLADwgYSARQLLSLiefCLERGITTFDHADIYGNytcESRFGDALTLKPSLRSQIEIVTKCG 83
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSD--DEAERSVSA---ALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 84 IklpSKYGmklYDTSkdhiIASVEQSLRNFRTDYIDVLLIHRPDPfmNPEEVAEAF---CQLKADGKVRYFGVSNFKRSQ 160
Cdd:cd19134 75 T---PDQG---FTAS----QAACRASLERLGLDYVDLYLIHWPAG--REGKYVDSWgglMKLREEGLARSIGVSNFTAEH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 161 LSMLESYLPFPLVTNQIEV------SAYRLENLEDGTVDlclekrmppMVWSPLAGGAIfsADDDRAVRLRDtlEQVRge 234
Cdd:cd19134 143 LENLIDLTFFTPAVNQIELhpllnqAELRKVNAQHGIVT---------QAYSPLGVGRL--LDNPAVTAIAA--AHGR-- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 737525220 235 lgaeTIDEVLYAWLFAHPARMmpIVGSGKQERIERAVRALSFSLSREQWFAI 286
Cdd:cd19134 208 ----TPAQVLLRWSLQLGNVV--ISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
48-283 |
1.68e-09 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 57.36 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 48 DHADIYGNytcESRFGDALtlKPSLRSQIeiVTKCGIKLPSKygMKLYDTSKDHIIASVEQSLRNFRTDYIDVLLIHRP- 126
Cdd:cd19125 42 DCAAIYGN---EKEIGKAL--KKLFEDGV--VKREDLFITSK--LWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 127 -----DPFMNPEEVAE--------AFCQLKADGKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAYrleNLEDGTVD 193
Cdd:cd19125 113 rlkkgAHMPEPEEVLPpdipstwkAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARVPPAVNQVECHPG---WQQDKLHE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 194 LCLEKRMPPMVWSPLagGAIFSADDDRAVRLRDTLEQVRGELGaETIDEVLYAWLFAHPARMMPivGSGKQERIERAVRA 273
Cdd:cd19125 190 FCKSKGIHLSAYSPL--GSPGTTWVKKNVLKDPIVTKVAEKLG-KTPAQVALRWGLQRGTSVLP--KSTNEERIKENIDV 264
|
250
....*....|
gi 737525220 274 LSFSLSREQW 283
Cdd:cd19125 265 FDWSIPEEDF 274
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
22-287 |
8.74e-09 |
|
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: 55.35 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPS----LRSQIEIVTKcgiklpskygmkLYDT 97
Cdd:cd19110 9 LGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHN---ESEVGAGIREKIKegvvRREDLFIVSK------------LWCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 98 --SKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPE-------------------EVAEAFCQLKADGKVRYFGVSNF 156
Cdd:cd19110 74 chKKSLVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEpdlpldrsgmvipsdtdflDTWEAMEDLVIEGLVKNIGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 157 KRSQLSML--ESYLPFPLVTNQIEVSAYRLENledGTVDLCLEKRMPPMVWSPLAG-GAIFSADDDRAVRlrdTLEQVRG 233
Cdd:cd19110 154 NHEQLERLlnKPGLRVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPLGGsCEGVDLIDDPVIQ---RIAKKHG 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 737525220 234 ELGAETIDEvlyawlFAHPARMMPIVGSGKQERIERAVRALSFSLSREQWFAIL 287
Cdd:cd19110 228 KSPAQILIR------FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLL 275
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
105-182 |
5.33e-07 |
|
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: 49.92 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 105 SVEQSLRNFRTDYIDVLLIHRPDPfMNPEE--------------------VAEAFCQLKADGKVRYFGVSNFKRSQLSML 164
Cdd:cd19108 93 ALEKSLKKLQLDYVDLYLIHFPVA-LKPGEelfpkdengklifdtvdlcaTWEAMEKCKDAGLAKSIGVSNFNRRQLEMI 171
|
90 100
....*....|....*....|...
gi 737525220 165 ES-----YLPfplVTNQIEVSAY 182
Cdd:cd19108 172 LNkpglkYKP---VCNQVECHPY 191
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
22-208 |
8.34e-07 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 49.69 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALT-----LKPSLRSQIEIVTKcgiklpskygmkLYD 96
Cdd:cd19106 12 LGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGN---EQEVGEALKekvgpGKAVPREDLFVTSK------------LWN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 97 TsKDH---IIASVEQSLRNFRTDYIDVLLIHRP-------DPF------------MNPEEVAEAFCQLKADGKVRYFGVS 154
Cdd:cd19106 77 T-KHHpedVEPALRKTLKDLQLDYLDLYLIHWPyafergdNPFpknpdgtirydsTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 737525220 155 NFKRSQLSMLESYLPFPLVTNQIEVSAYRLENledGTVDLCLEKRMPPMVWSPL 208
Cdd:cd19106 156 NFNSRQIDDILSVARIKPAVLQVECHPYLAQN---ELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
31-211 |
1.61e-06 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 48.65 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 31 QLLSLIEFCLERGITTFDHADIYGnytCESRFGDALTlkpslrsqiEIVTKCGIKLPSKY-GMKLYDTSKDHIIASVEQS 109
Cdd:cd19119 28 EVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIK---------RAIDDGSIKREELFiTTKVWPTFYDEVERSLDES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 110 LRNFRTDYIDVLLIHRPDPFM-NPEEVAEAFCQLKADGKVRY------------------------FGVSNFKRSQL-SM 163
Cdd:cd19119 96 LKALGLDYVDLLLVHWPVCFEkDSDDSGKPFTPVNDDGKTRYaasgdhittykqlekiyldgrakaIGVSNYSIVYLeRL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 737525220 164 LESYLPFPLVtNQIEVSAYrLENLEdgTVDLCLEKRMPPMVWSPLAGG 211
Cdd:cd19119 176 IKECKVVPAV-NQVELHPH-LPQMD--LRDFCFKHGILVTAYSPLGSH 219
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
90-182 |
1.96e-06 |
|
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: 48.26 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 90 YGMKLYDTSKD-HII-ASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVA-------------------EAFCQLKADGKV 148
Cdd:cd19109 70 YCGKLWNTCHPpELVrPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYprdengkwlyhktnlcatwEALEACKDAGLV 149
|
90 100 110
....*....|....*....|....*....|....*.
gi 737525220 149 RYFGVSNFKRSQLSML--ESYLPFPLVTNQIEVSAY 182
Cdd:cd19109 150 KSIGVSNFNRRQLELIlnKPGLKHKPVSNQVECHPY 185
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
22-208 |
3.65e-06 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 47.41 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDALTLKPS----LRSQIEIVTKcgiklpskygmkLYDT 97
Cdd:cd19107 9 LGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQN---ENEVGEAIQEKIKeqvvKREDLFIVSK------------LWCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 98 --SKDHIIASVEQSLRNFRTDYIDVLLIHRPDPFMNPEEVA-------------------EAFCQLKADGKVRYFGVSNF 156
Cdd:cd19107 74 fhEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFpldesgnvipsdttfldtwEAMEELVDEGLVKAIGVSNF 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 737525220 157 KRSQLSML--ESYLPFPLVTNQIEVSAY-RLENLedgtVDLCLEKRMPPMVWSPL 208
Cdd:cd19107 154 NHLQIERIlnKPGLKYKPAVNQIECHPYlTQEKL----IQYCQSKGIVVTAYSPL 204
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
18-248 |
2.04e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 45.35 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 18 GCWRLAD-----WGYSARQL---------------LSLIEFCLERGITTFDHADIYGNYTCESRFGDALtlKPsLRSQIE 77
Cdd:PRK10376 8 GTFTLGGrsvnrLGYGAMQLagpgvfgppkdrdaaIAVLREAVALGVNHIDTSDFYGPHVTNQLIREAL--HP-YPDDLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 78 IVTKCGIKLPSKyGMKLYDTSKDHIIASVEQSLRNFRTDYIDVL------LIHRPDPfMNPEEVAEAFCQLKADGKVRYF 151
Cdd:PRK10376 85 IVTKVGARRGED-GSWLPAFSPAELRRAVHDNLRNLGLDVLDVVnlrlmgDGHGPAE-GSIEEPLTVLAELQRQGLVRHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 152 GVSNFKRSQLSMLESYLPFPLVTNQievsaYRLENL-EDGTVDLCLEKRMPPMVWSPLAGgaiFSAdddravrLR-DTLE 229
Cdd:PRK10376 163 GLSNVTPTQVAEARKIAEIVCVQNH-----YNLAHRaDDALIDALARDGIAYVPFFPLGG---FTP-------LQsSTLS 227
|
250
....*....|....*....
gi 737525220 230 QVRGELGAeTIDEVLYAWL 248
Cdd:PRK10376 228 DVAASLGA-TPMQVALAWL 245
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
22-182 |
2.88e-05 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 44.82 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 22 LADWGYSARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDAL-------TLKpslRSQIEIVTKcgikLPsKYGMKL 94
Cdd:cd19155 17 LGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRN---EAAIGNVLkkwidsgKVK---REELFIVTK----LP-PGGNRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 95 YDTSKdhiiaSVEQSLRNFRTDYIDVLLIHRP---------DPFMNPE-EVAEAFCQLKAD-----------GKVRYFGV 153
Cdd:cd19155 86 EKVEK-----FLLKSLEKLQLDYVDLYLIHFPvgslskeddSGKLDPTgEHKQDYTTDLLDiwkameaqvdqGLTRSIGL 160
|
170 180
....*....|....*....|....*....
gi 737525220 154 SNFKRSQLSMLESYLPFPLVTNQIEVSAY 182
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVY 189
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-156 |
2.51e-04 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 42.05 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 4 VQLADNLSFSRVIYGCWRLaDWGYSARQLLSLIEFclerGITTFDHADIYGNytcESRFGDAL--TLKPSLRSQIEIVtk 81
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKL-DNATAADQIYQAIKA----GYRLFDGAEDYGN---EKEVGEGVnrAIDEGLVKREELF-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 82 cgikLPSKYGMKLYDtsKDHIIASVEQSLRNFRTDYIDVLLIHRPDPF--------------------MNPEEVA----- 136
Cdd:cd19113 73 ----LTSKLWNNFHD--PKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfvpieekyppgfycgdgdnFVYEDVPildtw 146
|
170 180
....*....|....*....|
gi 737525220 137 EAFCQLKADGKVRYFGVSNF 156
Cdd:cd19113 147 KALEKLVDAGKIKSIGVSNF 166
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
17-182 |
3.91e-04 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 41.39 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 17 YGCWRLadwgySARQLLSLIEFCLERGITTFDHADIYGNytcESRFGDAL--TLKPSL--RSQIEIVTKcgiklpskygm 92
Cdd:cd19114 9 FGTAKI-----KANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIrkAIQEGLvkREDLFIVTK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737525220 93 kLYDT--SKDHIIASVEQSLRNFRTDYIDVLLIHRPDP--FMNPEE--------------------VAEAFCQLKA---D 145
Cdd:cd19114 70 -LWNNfhGKDHVREAFDRQLKDYGLDYIDLYLIHFPIPaaYVDPAEnypflwkdkelkkfpleqspMQECWREMEKlvdA 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 737525220 146 GKVRYFGVSNFKRSQLSMLESYLPFPLVTNQIEVSAY 182
Cdd:cd19114 149 GLVRNIGIANFNVQLILDLLTYAKIKPAVLQIEHHPY 185
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
99-155 |
1.23e-03 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 39.84 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737525220 99 KDHIIASVEQSLRNFRTDYIDVLLIHRPD-----------------PFMNPEEVAEAFCQLKADGKVRYFGVSN 155
Cdd:PRK10625 107 RKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| |
