|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-319 |
0e+00 |
|
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: 522.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 3 KIPLGTTDITLSRMGLGTWAIGGGPaWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVV 82
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGP-WWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR-RDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 83 ETKCGIVWERKGSLFNKVGD-RQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKAEG 161
Cdd:cd19149 79 ATKCGLRWDREGGSFFFVRDgVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVE---TPIEETMEALEELKRQG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 162 KIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTIT--RDYVPGGAR 239
Cdd:cd19149 156 KIRAIGASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITpdREFDAGDAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 240 ANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADATLMRE 319
Cdd:cd19149 236 SGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-313 |
9.28e-137 |
|
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: 389.58 E-value: 9.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 10 DITLSRMGLGTWAIGGGpaWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVVETKCGIV 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGGT--WWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR-RDDVVIATKCGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WERKGSLFnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:cd19084 78 WDGGKGVT---------KDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPN---TPIEETAEALEKLKKEGKIRYIGVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV--PGGARANKVWFQR 247
Cdd:cd19084 146 NFSVEQLEEARKYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTfpPDDRRSRFPFFRG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446646352 248 ENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19084 226 ENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEE 291
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-326 |
9.11e-119 |
|
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: 344.85 E-value: 9.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGgpaWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGG---PWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGIVWerkgslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAE 160
Cdd:COG0667 78 VIATKVGRRM----------GPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHR---PDPDTPIEETLGALDELVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVDADHIREYLQYGE----LDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRD-YVP 235
Cdd:COG0667 145 GKIRYIGVSNYSAEQLRRALAIAEglppIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGaTFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 236 GGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADat 315
Cdd:COG0667 225 EGDRAATNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAED-- 302
|
330
....*....|.
gi 446646352 316 lMREMAEALER 326
Cdd:COG0667 303 -LAALDAALAA 312
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-326 |
5.68e-99 |
|
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: 293.34 E-value: 5.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWAIGGGPAWnGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKCGivwer 92
Cdd:cd19085 1 VSRLGLGCWQFGGGYWW-GDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG-RRDDVVIATKVS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnkvgdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd19085 74 -------------PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHW---PSSDVPLEETMEALEKLKEEGKIRAIGVSNFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 173 ADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTG--TITRDYVPGGARANKVW-FQREN 249
Cdd:cd19085 138 PAQLEEALDAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGkfSSAEDFPPGDARTRLFRhFEPGA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446646352 250 MLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADatlMREMAEALER 326
Cdd:cd19085 218 EEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSV---LERLDEISDP 291
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-324 |
4.48e-94 |
|
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: 281.48 E-value: 4.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWAIGGG--PAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVVETKCGIVW 90
Cdd:cd19102 1 LTTIGLGTWAIGGGgwGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL-RDRPIVATKCGLLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 ERKGSLFNkvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAAN 170
Cdd:cd19102 80 DEEGRIRR---------SLKPASIRAECEASLRRLGVDVIDLYQIHW---PDPDEPIEEAWGALAELKEEGKVRAIGVSN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 171 VDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV----PGGARANKVWFQ 246
Cdd:cd19102 148 FSVDQMKRCQAIHPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVaslpADDWRRRSPFFQ 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 247 RENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADatlMREMAEAL 324
Cdd:cd19102 228 EPNLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEE---LAEIEALL 302
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-320 |
6.03e-85 |
|
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: 258.01 E-value: 6.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 10 DITLSRMGLGTWAIGGgpAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL-PREQVVVETKCGI 88
Cdd:cd19148 1 DLPVSRIALGTWAIGG--WMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgKRDRVVIATKVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 89 VWERKGSLFnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGA 168
Cdd:cd19148 79 EWDEGGEVV---------RNSSPARIRKEVEDSLRRLQTDYIDLYQVHW---PDPLVPIEETAEALKELLDEGKIRAIGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 169 ANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV-PGG-ARANKVWFQ 246
Cdd:cd19148 147 SNFSPEQMETFRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKfEGDdLRRTDPKFQ 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446646352 247 RENMLKVIDMLEQWQPLC-ARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADatlMREM 320
Cdd:cd19148 227 EPRFSQYLAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDED---MKEI 298
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-313 |
1.43e-78 |
|
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: 241.94 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 3 KIPLGTTDITLSRMGLGTWAIGGGPAWNgDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVV 82
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGGHNLYP-NLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 83 ETKCGIVWERKGSLFNKvgdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGK 162
Cdd:cd19083 80 ATKGAHKFGGDGSVLNN----------SPEFLRSAVEKSLKRLNTDYIDLYYIHF---PDGETPKAEAVGALQELKDEGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 163 IRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV--PGGARA 240
Cdd:cd19083 147 IRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKfpDNDLRN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446646352 241 NKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19083 227 DKPLFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-313 |
1.47e-76 |
|
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: 236.73 E-value: 1.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 2 KKIPLGTTDITLSRMGLG----TWAIGGgpawngdLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPR 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSAFYGP-------ADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 78 EQVVVETKCGIVWeRKGSLFNKVgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNEL 157
Cdd:cd19076 73 DEVVIATKFGIVR-DPGSGFRGV-------DGRPEYVRAACEASLKRLGTDVIDLYYQH--RVDPN-VPIEETVGAMAEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 158 KAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITR--DYVP 235
Cdd:cd19076 142 VEEGKVRYIGLSEASADTIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSpeDLPE 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 236 GGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19076 222 DDFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEE 299
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-304 |
3.45e-76 |
|
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: 233.52 E-value: 3.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 11 ITLSRMGLGTWAIGGGpaWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKCGIVW 90
Cdd:cd19086 1 LEVSEIGFGTWGLGGD--WWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG-RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 ErkgslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHwqsVPPF-FTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:cd19086 78 D---------GGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLH---NPPDeVLDNDELFEALEKLKQEGKIRAYGVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGtitrdyvpggarankvwfqren 249
Cdd:cd19086 146 VGDPEEALAALRRGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTG---------------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446646352 250 mlkvidmleqwqplcaryqcTIPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19086 204 --------------------KLAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-313 |
4.61e-75 |
|
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: 232.59 E-value: 4.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGGPAWNGDLDQQICIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLP--REQVVVETKCGivwerK 93
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEALEALRAALEA---GINFIDTAEVYGDGKSEELLGEALKDYPvkRDKVVIATKVP-----D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 94 GSLFNKVGdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVDA 173
Cdd:pfam00248 73 GDGPWPSG-------GSKENIRKSLEESLKRLGTDYIDLYYLHW---PDPDTPIEETWDALEELKKEGKIRAIGVSNFDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 174 DHIREYLQYGELDI--IQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGgaRANKVWFQRENML 251
Cdd:pfam00248 143 EQIEKALTKGKIPIvaVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKG--PGERRRLLKKGTP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446646352 252 KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:pfam00248 221 LNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEE 282
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-313 |
6.27e-71 |
|
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: 220.95 E-value: 6.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 10 DITLSRMGLGTWAIGGGPAWNGDLDQQIcIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKcgiV 89
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDKKA-IEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTK---V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WERkgslfnkvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:cd19072 77 SPD---------------HLKYDDVIKAAKESLKRLGTDYIDLYLIHW---PNPSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIRE---YLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRdyvpggarankvwfq 246
Cdd:cd19072 139 NFSLEELEEaqsYLKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS--------------- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446646352 247 reNMLKVIdmleqwqplCARYQCTIPTLALAWILKQSDLISIlSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19072 204 --PLLDEI---------AKKYGKTPAQIALNWLISKPNVIAI-PKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-303 |
2.48e-70 |
|
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: 218.16 E-value: 2.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGgpawngDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP-REQVVVETKCGIVWer 92
Cdd:cd06660 1 SRLGLGTMTFGG------DGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGnRDDVVIATKGGHPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd06660 73 --------GGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHR---DDPSTPVEETLEALNELVREGKIRYIGVSNWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 173 ADHIREYLQYG------ELDIIQAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLltgtitrdyvpggarankvwf 245
Cdd:cd06660 142 AERLAEALAYAkahglpGFAAVQPQYSLLDRsPMEEELLDWAEENGLPLLAYSPLARGP--------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 246 qrenmlkvidmleqwqplcaryqctiPTLALAWILKQSDLISILSGATAPEQVRENVA 303
Cdd:cd06660 201 --------------------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-311 |
6.21e-68 |
|
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: 214.38 E-value: 6.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWA-IGGGpawngdLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCgivwe 91
Cdd:cd19074 4 VSELSLGTWLtFGGQ------VDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 92 rkgslFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKAEGKIRAIGAANV 171
Cdd:cd19074 73 -----FWPTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPE---TPLEETVRAMDDLIRQGKILYWGTSEW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 172 DADHIREYL----QYGELDII--QAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPG-GARA---- 240
Cdd:cd19074 145 SAEQIAEAHdlarQFGLIPPVveQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPsRSRAtded 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 241 NKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19074 225 NRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-313 |
1.21e-67 |
|
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: 214.40 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGGPAWN---GDLDQQIC---IDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKK 74
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFgawGGVDQEEAdrlVDIALDA---GINFFDTADVYSEGESEEILGKALKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 75 LpREQVVVETKcgiVWERKGSLFNKVGdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTH-WQSVppffTPIAETVAV 153
Cdd:cd19091 78 R-RDDVLIATK---VRGRMGEGPNDVG-------LSRHHIIRAVEASLKRLGTDYIDLYQLHgFDAL----TPLEETLRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 154 LNELKAEGKIRAIGAANVDADH------IREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTG 227
Cdd:cd19091 143 LDDLVRQGKVRYIGVSNFSAWQimkalgISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 228 TITRDY-VPGGARANKVWFQ-----RENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVREN 301
Cdd:cd19091 223 KYRRGQpAPEGSRLRRTGFDfppvdRERGYDVVDALRE---IAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDN 299
|
330
....*....|..
gi 446646352 302 VAALNINLSDAD 313
Cdd:cd19091 300 LGAAGLSLTPEE 311
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-313 |
3.10e-65 |
|
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: 207.84 E-value: 3.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 5 PLGTTDITLSRMGLGTWAIGggpaWNGDLDQQICI-DTILEAhrcGINLIDTA-------PGYNFGNSEVIVGQALKK-L 75
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFG----WTADEETSFALlDAFVDA---GGNFIDTAdvysawvPGNAGGESETIIGRWLKSrG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 76 PREQVVVETKCGivWERKGslfNKVGdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLN 155
Cdd:cd19081 74 KRDRVVIATKVG--FPMGP---NGPG-------LSRKHIRRAVEASLRRLQTDYIDLYQAHW---DDPATPLEETLGALN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 156 ELKAEGKIRAIGAANVDADHIREYLQ------YGELDIIQAKYSILDRAM-ESELLPLCRDNGIVVQVYSPLEQGLLTGT 228
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALElsrqhgLPRYVSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGFLTGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 229 ITRDY-VPGGARANKVWFQREN--MLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL 305
Cdd:cd19081 219 YRSEAdLPGSTRRGEAAKRYLNerGLRILDALDE---VAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAA 295
|
....*...
gi 446646352 306 NINLSDAD 313
Cdd:cd19081 296 GLRLTDEE 303
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-313 |
8.79e-65 |
|
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: 206.67 E-value: 8.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 2 KKIPLGTTDITLSRMGLGTWAIGGGPAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL-PREQV 80
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFaPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCgivwerkgslFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvppFF--TPIAETVAVLNELK 158
Cdd:cd19079 81 VIATKV----------YFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHR-----WDyeTPIEETLEALHDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAANVDADHIREYLQYGELD------IIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLtgtiTRD 232
Cdd:cd19079 146 KSGKVRYIGASSMYAWQFAKALHLAEKNgwtkfvSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRL----ARP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 233 YVPGGARAN--------KVWFQRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19079 222 WGDTTERRRsttdtaklKYDYFTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAA 298
|
....*....
gi 446646352 305 LNINLSDAD 313
Cdd:cd19079 299 LDIKLSEEE 307
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-313 |
5.93e-63 |
|
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: 201.69 E-value: 5.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWAIGGGPAWNG-DLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP-REQVVVETKCGIVW 90
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWGYgEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGdRDEVVIATKFAPLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 ERkgslfnkvgdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTHWqsVPPFFTPIAETVAVLNELKAEGKIRAIGAAN 170
Cdd:cd19093 82 WR----------------LTRRSVVKALKASLERLGLDSIDLYQLHW--PGPWYSQIEALMDGLADAVEEGLVRAVGVSN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 171 VDADHIREYLQY-GELDI----IQAKYSILDRAME-SELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANKvw 244
Cdd:cd19093 144 YSADQLRRAHKAlKERGVplasNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRL-- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446646352 245 FQRENMLKV---IDMLEQwqpLCARYQCTIPTLALAWILKQSDLisILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19093 222 FGRKNLEKVqplLDALEE---IAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEE 288
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-312 |
6.44e-61 |
|
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: 195.85 E-value: 6.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGGPawnGDLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKLPREQVVVETKCGivwerk 93
Cdd:cd19090 1 SALGLGTAGLGGVF---GGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPREPLVLSTKVG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 94 gslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFFTPIAE--TVAVLNELKAEGKIRAIGAANV 171
Cdd:cd19090 70 -------RLPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggALEALLELKEEGLIKHIGLGGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 172 DADHIREYLQYGELDII--QAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGtitRDyvPGGARANKVWFQREN 249
Cdd:cd19090 143 PPDLLRRAIETGDFDVVltANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAG---RP--PERVRYTYRWLSPEL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446646352 250 MLKVIDMLEqwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19090 218 LDRAKRLYE----LCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-324 |
1.89e-60 |
|
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: 195.14 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 10 DITLSRMGLGTWAI--GGGPAwngdLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKCG 87
Cdd:cd19078 1 GLEVSAIGLGCMGMshGYGPP----PDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP-FRDQVVIATKFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 88 IVwerkgslFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELKAEGKIRAIG 167
Cdd:cd19078 76 FK-------IDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQH--RVDPN-VPIEEVAGTMKELIKEGKIRHWG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 168 AANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRD--YVPGGARANKVWF 245
Cdd:cd19078 146 LSEAGVETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENtkFDEGDDRASLPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 246 QRENM---LKVIDMLEQWqplCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADatlMREMAE 322
Cdd:cd19078 226 TPEALeanQALVDLLKEF---AEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEE---LREIED 299
|
..
gi 446646352 323 AL 324
Cdd:cd19078 300 AL 301
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-313 |
5.00e-59 |
|
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: 192.02 E-value: 5.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGgpawNGDLDQQICI-DTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLpREQ 79
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGG----RTDEETSFAImDRALDA---GINFFDTADVYGGGRSEEIIGRWIAGR-RDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 80 VVVETKCgivwerkgslFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIY-MTHWQSvppfFTPIAETVAVLNELK 158
Cdd:cd19087 73 IVLATKV----------FGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYqMHHFDR----DTPLEETLRALDDLV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAAN------VDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRD 232
Cdd:cd19087 139 RQGKIRYIGVSNfaawqiAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 233 YVP--GGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLS 310
Cdd:cd19087 219 KRPesGRLVERARYQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLT 298
|
...
gi 446646352 311 DAD 313
Cdd:cd19087 299 PEL 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-326 |
6.12e-56 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 182.18 E-value: 6.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 11 ITLSRMGLGTWAIGGgpawngdldqQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgi 88
Cdd:COG0656 3 VEIPALGLGTWQLPG----------EEAAAAVRTALEAGYRHIDTAAMY--GN-EEGVGEAIAAsgVPREELFVTTK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 89 VWERkgslfnkvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKAEGKIRAIGA 168
Cdd:COG0656 67 VWND---------------NHGYDDTLAAFEESLERLGLDYLDLYLIHW----PGPGPYVETWRALEELYEEGLIRAIGV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 169 ANVDADHIREYLQYGE--LDIIQAKYSILDRamESELLPLCRDNGIVVQVYSPLEQG-LLTG-TITRdyvpggarankvw 244
Cdd:COG0656 128 SNFDPEHLEELLAETGvkPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGkLLDDpVLAE------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 245 fqrenmlkvidmleqwqpLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDADatlMREMAeAL 324
Cdd:COG0656 193 ------------------IAEKHGKTPAQVVLRWHL-QRGVVVI-PKSVTPERIRENLDAFDFELSDED---MAAID-AL 248
|
..
gi 446646352 325 ER 326
Cdd:COG0656 249 DR 250
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-305 |
1.02e-55 |
|
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: 182.75 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGGPawnGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVF---GPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGivweRKGSLFNKVGDrqlyknLSPESIREEVEASLQRLGIDYIDIYMTHwqsvPPFFTP-----IAETVAVLN 155
Cdd:cd19163 78 YLATKVG----RYGLDPDKMFD------FSAERITKSVEESLKRLGLDYIDIIQVH----DIEFAPsldqiLNETLPALQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 156 ELKAEGKIRAIGAANVDADHIREYLQ--YGELDIIQ--AKYSILDRAMeSELLPLCRDNGIVVQVYSPLEQGLLTGTITR 231
Cdd:cd19163 144 KLKEEGKVRFIGITGYPLDVLKEVLErsPVKIDTVLsyCHYTLNDTSL-LELLPFFKEKGVGVINASPLSMGLLTERGPP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446646352 232 DYVPGGARankvwfQRENMLKVIDmleqwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL 305
Cdd:cd19163 223 DWHPASPE------IKEACAKAAA-------YCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-304 |
3.11e-55 |
|
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: 180.51 E-value: 3.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGGPawnGDLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKLPREQVVVETKCGIVWErk 93
Cdd:cd19095 1 SVLGLGTSGIGRVW---GVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLFIATKVGTHGE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 94 gslfnkvgDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKAEGKIRAIGaANVDA 173
Cdd:cd19095 74 --------GGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDD---ELTGEVLETLEDLKAAGKVRYIG-VSGDG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 174 DHIREYLQYGELDIIQAKYSILDRAMEsELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANKVWFQRenmlkv 253
Cdd:cd19095 142 EELEAAIASGVFDVVQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAE------ 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446646352 254 idmLEQWQPlcaryqctiPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19095 215 ---IGGATW---------AQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-325 |
2.85e-54 |
|
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: 179.95 E-value: 2.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 6 LGTTDITLSRMGLGTWAI--GGGPAwNGDLDQQICIDTILEAhrcGINLIDTAPGYnfGNSEVIVGQALKKLP--REQVV 81
Cdd:cd19144 6 LGRNGPSVPALGFGAMGLsaFYGPP-KPDEERFAVLDAAFEL---GCTFWDTADIY--GDSEELIGRWFKQNPgkREKIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 82 VETKCGIVWERKGSLFNKVGdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELKAEG 161
Cdd:cd19144 80 LATKFGIEKNVETGEYSVDG--------SPEYVKKACETSLKRLGVDYIDLYYQH--RVDGK-TPIEKTVAAMAELVQEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 162 KIRAIGAANVDADHIREYLQYGELDIIQAKYS--ILD-RAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITR--DYVPG 236
Cdd:cd19144 149 KIKHIGLSECSAETLRRAHAVHPIAAVQIEYSpfSLDiERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSpdDFEEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 237 GARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADATL 316
Cdd:cd19144 229 DFRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKE 308
|
....*....
gi 446646352 317 MREMAEALE 325
Cdd:cd19144 309 IREIAEEAE 317
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-313 |
5.35e-53 |
|
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: 175.13 E-value: 5.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 9 TDITLSRMGLGTWAIGGGPAwngdlDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKcgi 88
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPA-----KRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG-RRDKVFLVSK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 89 VWERkgslfnkvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVppffTPIAETVAVLNELKAEGKIRAIGA 168
Cdd:cd19138 78 VLPS---------------NASRQGTVRACERSLRRLGTDYLDLYLLHWRGG----VPLAETVAAMEELKKEGKIRAWGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 169 ANVDADHIREYLQY---GELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTitrdyvpgGARANKVwf 245
Cdd:cd19138 139 SNFDTDDMEELWAVpggGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRR--------GLLENPT-- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 246 qrenmLKVIdmleqwqplCARYQCTIPTLALAWILKQSDLISIlSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19138 209 -----LKEI---------AARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADLELTEED 261
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-310 |
1.55e-52 |
|
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: 173.56 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWAIGGGPAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPrEQVVVETKCGIVwer 92
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP-DDVVIATKGGLV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd19088 77 ------RTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHR---IDPKVPFEEQLGALAELQDEGLIRHIGLSNVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 173 ADHIREYLQYGELDIIQAKYSILDRAMEsELLPLCRDNGIVVQVYSPLEQGLLTGtitrdyvPGGARANkvwfqrenmlk 252
Cdd:cd19088 148 VAQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQ-------PGGLLAE----------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 253 vidmleqwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLS 310
Cdd:cd19088 209 ----------VAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-313 |
4.84e-52 |
|
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: 173.77 E-value: 4.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 3 KIPLGTTDITLSRMGLGTWAIGGGpaWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVV 82
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGD--YGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 83 ETKCGIVwERKGSLFNKVGDrqlyknlsPESIREEVEASLQRLGIDYIDIYMTHW--QSVppfftPIAETVAVLNELKAE 160
Cdd:cd19145 80 ATKFGIH-EIGGSGVEVRGD--------PAYVRAACEASLKRLDVDYIDLYYQHRidTTV-----PIEITMGELKKLVEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTG--TITRDYVPGGA 238
Cdd:cd19145 146 GKIKYIGLSEASADTIRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGkaKLEELLENSDV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446646352 239 RANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19145 226 RKSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKED 300
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
6-307 |
3.20e-51 |
|
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: 172.01 E-value: 3.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 6 LGTTDITLSRMGLGTWAigggpAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL--PREQVVVE 83
Cdd:cd19143 6 LGRSGLKVSALSFGSWV-----TFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELgwPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 84 TKcgIVWERKGSLFNKVGdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELKAEGKI 163
Cdd:cd19143 81 TK--IFWGGGGPPPNDRG-------LSRKHIVEGTKASLKRLQLDYVDLVFCH---RPDPATPIEETVRAMNDLIDQGKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIREYLQYGE-LDII-----QAKYSILDRA-MESELLPLCRDNGIVVQVYSPLEQGLLTGTITrDYVPG 236
Cdd:cd19143 149 FYWGTSEWSAQQIEEAHEIADrLGLIppvmeQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYN-NGIPE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446646352 237 GARA---NKVW---FQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19143 228 GSRLalpGYEWlkdRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEV 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-312 |
4.08e-51 |
|
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: 171.00 E-value: 4.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGgPAWNGDLDQQICIDTileAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCGIVWERK 93
Cdd:cd19162 1 PRLGLGAASLGN-LARAGEDEAAATLDA---AWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVGRLLEPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 94 GSLFNKVGDRQLykNLSPESIREEVEASLQRLGIDYIDIYMTHwQSVPPFFTPIAETVAVLNELKAEGKIRAIGAANVDA 173
Cdd:cd19162 77 AAGRPAGADRRF--DFSADGIRRSIEASLERLGLDRLDLVFLH-DPDRHLLQALTDAFPALEELRAEGVVGAIGVGVTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 174 DHIREYLQYGELD--IIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTgtitrdyvpGGARANKVWFQRENML 251
Cdd:cd19162 154 AALLRAARRADVDvvMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILA---------TDDPAGDRYDYRPATP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 252 KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19162 225 EVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-305 |
9.75e-51 |
|
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: 170.43 E-value: 9.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGGPAWNGDLDQqiCIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLPReqVVVETKCGIVWErkgs 95
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAE--LLDAFLER---GHTEIDTARVYPDGTSEELLGELGLGERG--FKIDTKANPGVG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 96 lfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELKAEGKIRAIGAANVDADH 175
Cdd:cd19075 74 -----------GGLSPENVRKQLETSLKRLKVDKVDVFYLH---APDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 176 IREYLQYGELD------IIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITR-DYVPGGAR--------- 239
Cdd:cd19075 140 VAEIVEICKENgwvlptVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYsEDKAGGGRfdpnnalgk 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 240 ANKVWFQRENMLkviDMLEQWQPLCARYQCTIPTLALAWILKQSDLIS-----ILSGATAPEQVRENVAAL 305
Cdd:cd19075 220 LYRDRYWKPSYF---EALEKVEEAAEKEGISLAEAALRWLYHHSALDGekgdgVILGASSLEQLEENLAAL 287
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-312 |
2.02e-50 |
|
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: 169.71 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 6 LGTTDITLSRMGLGTWAIGGGPAWNGDLDQQICI-DTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVVET 84
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWGWGADREEARAMfDAYVEA---GGNFIDTANNYTNGTSERLLGEFIAGN-RDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 85 KCGivWERKGSLFNKVGDRQlyKNLspesiREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIR 164
Cdd:cd19080 79 KYT--MNRRPGDPNAGGNHR--KNL-----RRSVEASLRRLQTDYIDLLYVHA---WDFTTPVEEVMRALDDLVRAGKVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 165 AIGAANVDA------DHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGA 238
Cdd:cd19080 147 YVGISDTPAwvvaraNTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAG 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 239 RANKVWF----QRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19080 227 EAKGVTVgfgkLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPE 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-310 |
1.81e-49 |
|
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: 166.58 E-value: 1.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 8 TTDITLSRMGLGTWAIGGgpaWNGDLDQqiCIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP--REQVVVETK 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAD---WGESAEE--LLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPglREKIEIQTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 86 CGIVWErkgslFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHwqsVP-PFFTPiAETVAVLNELKAEGKIR 164
Cdd:cd19092 76 CGIRLG-----DDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLH---RPdPLMDP-EEVAEAFDELVKSGKVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 165 AIGAANVDADHIrEYLQ-YGELDII--QAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVpggaRA 240
Cdd:cd19092 147 YFGVSNFTPSQI-ELLQsYLDQPLVtnQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQ----RL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 241 NKVwfqrenmlkvidmLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLS 310
Cdd:cd19092 222 RAA-------------LEE---LAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
14-322 |
1.27e-48 |
|
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: 165.43 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGggpawngdldQQIcidTILEAHRC-------GINLIDTAPGYNF-------GNSEVIVGQALKKLP-RE 78
Cdd:cd19094 2 SEICLGTMTWG----------EQN---TEAEAHEQldyafdeGVNFIDTAEMYPVppspetqGRTEEIIGSWLKKKGnRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 79 QVVVETK-CG----IVWERKGSLfnkvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHW--QSVPPF-------- 143
Cdd:cd19094 69 KVVLATKvAGpgegITWPRGGGT-----------RLDRENIREAVEGSLKRLGTDYIDLYQLHWpdRYTPLFgggyytep 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 144 -----FTPIAETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDI------IQAKYSILDRAMESELLPLCRDNGI 212
Cdd:cd19094 138 seeedSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGlprivsIQNPYSLLNRNFEEGLAEACHRENV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 213 VVQVYSPLEQGLLTGTIT-RDYVPGGARANKV--WFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISIL 289
Cdd:cd19094 218 GLLAYSPLAGGVLTGKYLdGAARPEGGRLNLFpgYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTI 297
|
330 340 350
....*....|....*....|....*....|...
gi 446646352 290 SGATAPEQVRENVAALNINLSDAdatLMREMAE 322
Cdd:cd19094 298 IGATTLEQLKENIDAFDVPLSDE---LLAEIDA 327
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-305 |
7.74e-47 |
|
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: 158.52 E-value: 7.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGtwaiGGGpawngdlDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG----GGG-------LPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKcgIVWERKGSlfnkvgdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKAE 160
Cdd:cd19105 70 FLATK--ASPRLDKK--------------DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALEKLKKE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVDADH--IREYLQYGELDIIQAKYSIL-DRAMESELLPLCRDNGIvvqvyspleqglltGTITRDYVPGG 237
Cdd:cd19105 134 GKVRFIGFSTHDNMAevLQAAIESGWFDVIMVAYNFLnQPAELEEALAAAAEKGI--------------GVVAMKTLAGG 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 238 ARANkvWFQRENMLKVIdmleqwqplcaryqcTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL 305
Cdd:cd19105 200 YLQP--ALLSVLKAKGF---------------SLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-317 |
3.88e-46 |
|
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: 156.96 E-value: 3.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWAIGGGPAWNGDLDQQIcIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKcgiVWer 92
Cdd:cd19137 4 IPALGLGTWGIGGFLTPDYSRDEEM-VELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTK---VW-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnkvgdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd19137 78 -------------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHW---PNPNIPLEETLSAMAEGVRQGLIRYIGVSNFN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 173 ADHIREYLQYGELDII--QAKYSILDRA-MESELLPLCRDNGIVVQVYSPLEQGLltgtitrdyvpggarankvwfqren 249
Cdd:cd19137 142 RRLLEEAISKSQTPIVcnQVKYNLEDRDpERDGLLEYCQKNGITVVAYSPLRRGL------------------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 250 mLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISIlSGATAPEQVRENVAALNINLSDADATLM 317
Cdd:cd19137 197 -EKTNRTLEE---IAKNYGKTIAQIALAWLIQKPNVVAI-PKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-313 |
4.70e-46 |
|
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: 158.17 E-value: 4.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 11 ITLSRMGLG----TWaigggpaWNGDLDQQICIDTILEAHRCGINLIDTA----PGYNFGNSEVIvGQALKKLP--REQV 80
Cdd:cd19077 3 KLVGPIGLGlmglTW-------RPNPTPDEEAFETMKAALDAGSNLWNGGefygPPDPHANLKLL-ARFFRKYPeyADKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGIvwerKGSLFNKVGdrqlyknlSPESIREEVEASLQRLG-IDYIDIYMThwQSVPPFfTPIAETVAVLNELKA 159
Cdd:cd19077 75 VLSVKGGL----DPDTLRPDG--------SPEAVRKSIENILRALGgTKKIDIFEP--ARVDPN-VPIEETIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 160 EGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMES-ELLPLCRDNGIVVQVYSPLEQGLLTGTI-TRDYVPGG 237
Cdd:cd19077 140 EGKIRGIGLSEVSAETIRRAHAVHPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIkSLADIPEG 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 238 A-RANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQS-DLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19077 220 DfRRHLDRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSgPKIIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-308 |
2.50e-44 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 152.68 E-value: 2.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIG---GGPAWNGDLDQQIcIDTILE-AHRCGINLIDTAPGYnfGNSEVIVGQALKKLPREQVVveTKCGIV 89
Cdd:cd19097 1 SKLALGTAQFGldyGIANKSGKPSEKE-AKKILEyALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFKII--TKLPPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WERKGSLfnkvgdrqlyknlsPESIREEVEASLQRLGIDYIDIYMTHWQSVppFFTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:cd19097 76 KEDKKED--------------EAAIEASVEASLKRLKVDSLDGLLLHNPDD--LLKHGGKLVEALLELKKEGLIRKIGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIREYLQYGELDIIQAKYSILDRAMESE-LLPLCRDNGIVVQVYSPLEQGLLtgTITRDYVPggarankvwfqrE 248
Cdd:cd19097 140 VYSPEELEKALESFKIDIIQLPFNILDQRFLKSgLLAKLKKKGIEIHARSVFLQGLL--LMEPDKLP------------A 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 249 NMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNIN 308
Cdd:cd19097 206 KFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKP 265
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-326 |
7.34e-44 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 153.82 E-value: 7.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGgpawngdLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKlPREQV 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPR-------KDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG-PRDKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGiVWERkgslfnkvgdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFF-TPIAET--VAVLNEL 157
Cdd:COG1453 71 ILATKLP-PWVR-----------------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLeKVLKPGgaLEALEKA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 158 KAEGKIRAIGAAN-VDADHIREYLQYGELDIIQAKYSILDRAMES--ELLPLCRDNGIVVQVYSPLEQGLLTgtitrdyv 234
Cdd:COG1453 133 KAEGKIRHIGFSThGSLEVIKEAIDTGDFDFVQLQYNYLDQDNQAgeEALEAAAEKGIGVIIMKPLKGGRLA-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 235 pggarankvwfqreNMLKVIDMLeqwqpLCARYqcTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN--INLSDA 312
Cdd:COG1453 205 --------------NPPEKLVEL-----LCPPL--SPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEE 263
|
330
....*....|....
gi 446646352 313 DATLMREMAEALER 326
Cdd:COG1453 264 ELAILERLAEELGE 277
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
29-306 |
1.78e-43 |
|
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: 150.02 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 29 WNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCGiVWERKgslfnkvgdrqlykn 108
Cdd:cd19096 14 DDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLP-PWSVK--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 109 lSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFFTPIAE--TVAVLNELKAEGKIRAIG-AANVDADHIREYLQYGEL 185
Cdd:cd19096 78 -SAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKARKggLLEFLEKAKKEGLIRHIGfSFHDSPELLKEILDSYDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 186 DIIQAKYSILDRAMES--ELLPLCRDNGIVVQVYSPLEQGLLTgtitrdYVPGGARAnkvwfqrenmlkvidmleqwqpL 263
Cdd:cd19096 157 DFVQLQYNYLDQENQAgrPGIEYAAKKGMGVIIMEPLKGGGLA------NNPPEALA----------------------I 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446646352 264 CARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19096 209 LCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-303 |
3.22e-43 |
|
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: 148.78 E-value: 3.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 3 KIPLGTTDITLSRMGLGTWAIGggpawngDLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKlPREQVVV 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLG-------RLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG-RRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 83 ETKcgiVWERkgslfnkvgdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHWQSVPP-FFTPIAE--TVAVLNELKA 159
Cdd:cd19100 71 ATK---TGAR-----------------DYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEdLDQVFGPggALEALLEAKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 160 EGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMES---ELLPLCRDNGIVVQVYSPLEQGLLTGTITRDyvpg 236
Cdd:cd19100 131 EGKIRFIGISGHSPEVLLRALETGEFDVVLFPINPAGDHIDSfreELLPLAREKGVGVIAMKVLAGGRLLSGDPLD---- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446646352 237 garankvwfqrenmlkvidmleqwqplcaryqctiPTLALAWILKQSDLISILSGATAPEQVRENVA 303
Cdd:cd19100 207 -----------------------------------PEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
17-313 |
4.70e-42 |
|
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: 145.88 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWaigggpawngDLDQQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWerkg 94
Cdd:cd19073 5 GLGTW----------QLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAEsgVPREDLFITTK---VW---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 95 slfnkvgdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVDAD 174
Cdd:cd19073 65 -----------RDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHW---PNPTVPLEETLGALKELKEAGKVKSIGVSNFTIE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 175 HIREYLQYGELDII--QAKYSILDRamESELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfqrenmlK 252
Cdd:cd19073 131 LLEEALDISPLPIAvnQVEFHPFLY--QAELLEYCRENDIVITAYSPLARG----------------------------E 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 253 VIDmLEQWQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19073 181 VLR-DPVIQEIAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-312 |
7.68e-42 |
|
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: 147.37 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGGpaWNGDLDQQIcIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCG--IVWE 91
Cdd:cd19152 1 PKLGFGTAPLGNL--YEAVSDEEA-KATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVGrlLVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 92 RKGSlfnkVGDRQLYKNLSP---------ESIREEVEASLQRLGIDYIDIYMTH--------WQSVPPFFTPIAETVAVL 154
Cdd:cd19152 78 QEVE----PTFEPGFWNPLPfdavfdysyDGILRSIEDSLQRLGLSRIDLLSIHdpdedlagAESDEHFAQAIKGAFRAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 155 NELKAEGKIRAIGAANVDADHIREYLQYGELDIIQA--KYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRD 232
Cdd:cd19152 154 EELREEGVIKAIGLGVNDWEVILRILEEADLDWVMLagRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 233 YVPGGARANKVWFQRenmlkvidmlEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19152 234 YYEYGPAPPELIARR----------DRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
5-313 |
1.10e-40 |
|
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: 144.32 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 5 PLGTTDITLSRMGLGTWAiggGPAWNGDLDQQICIdtILEAHRCGINLIDTAPGYN--FGNSEVIVGQALK---KLPREQ 79
Cdd:cd19089 3 RCGRSGLHLPAISLGLWH---NFGDYTSPEEAREL--LRTAFDLGITHFDLANNYGppPGSAEENFGRILKrdlRPYRDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 80 VVVETKCGI-VWerkGSLFNKVGDRQlyknlspeSIREEVEASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELK 158
Cdd:cd19089 78 LVISTKAGYgMW---PGPYGDGGSRK--------YLLASLDQSLKRMGLDYVDIFYHH--RYDPD-TPLEETMTALADAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAANVDADHIREYLQY-GELD----IIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDY 233
Cdd:cd19089 144 RSGKALYVGISNYPGAKARRAIALlRELGvpliIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 234 VPGGARANKVWFQRENML--KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL-NINLS 310
Cdd:cd19089 224 PPDSRRAAESKFLTEEALtpEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkNLDFS 303
|
...
gi 446646352 311 DAD 313
Cdd:cd19089 304 EEE 306
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-321 |
1.32e-40 |
|
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: 142.24 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 15 RMGLGTWAIGGGPawngdldqqiCIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiVWer 92
Cdd:cd19071 3 LIGLGTYKLKPEE----------TAEAVLAALEAGYRHIDTAAAY--GN-EAEVGEAIREsgVPREELFITTK---LW-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnkvgdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHW---QSVPPFFTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:cd19071 65 -------------PTDHGYERVREALEESLKDLGLDYLDLYLIHWpvpGKEGGSKEARLETWRALEELVDEGLVRSIGVS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIREYLQYGEL--DIIQAKYSILDRamESELLPLCRDNGIVVQVYSPLeqglltgtitrdyvpggARANKVWFQR 247
Cdd:cd19071 132 NFNVEHLEELLAAARIkpAVNQIELHPYLQ--QKELVEFCKEHGIVVQAYSPL-----------------GRGRRPLLDD 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446646352 248 ENMLKvidmleqwqpLCARYQCTIPTLALAWILkQSDlISILSGATAPEQVRENVAALNINLSDADatlMREMA 321
Cdd:cd19071 193 PVLKE----------IAKKYGKTPAQVLLRWAL-QRG-VVVIPKSSNPERIKENLDVFDFELSEED---MAAID 251
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
5-325 |
1.63e-40 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 143.77 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 5 PLGTTDITLSRMGLGtwaigGGPAWN--GDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL--PREQV 80
Cdd:PLN02587 3 ELGSTGLKVSSVGFG-----ASPLGSvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgiPREKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGivweRKGSLFNkvgdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKAE 160
Cdd:PLN02587 78 VVSTKCG----RYGEGFD----------FSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIPALQKLKES 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVDADHIREYLQY---GELDII--QAKYSILDRAMEsELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVP 235
Cdd:PLN02587 144 GKVRFIGITGLPLAIFTYVLDRvppGTVDVIlsYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTENGPPEWHP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 236 GGARankvwfqrenmLKVIdmLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENV-AALNINLSDADA 314
Cdd:PLN02587 223 APPE-----------LKSA--CAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVaAATELETSGIDE 289
|
330
....*....|.
gi 446646352 315 TLMREMAEALE 325
Cdd:PLN02587 290 ELLSEVEAILA 300
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-306 |
4.03e-40 |
|
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: 142.31 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGgpawngDLDQQ---ICIDTILEAhrcGINLIDTAPGY----NFGNSEVIVGQALKKLP-REQVVVETK 85
Cdd:cd19082 1 SRIVLGTADFGT------RIDEEeafALLDAFVEL---GGNFIDTARVYgdwvERGASERVIGEWLKSRGnRDKVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 86 CGIvwerkgslfnKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHW--QSVppfftPIAETVAVLNELKAEGKI 163
Cdd:cd19082 72 GGH----------PDLEDMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRddPSV-----PVGEIVDTLNELVRAGKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIREYLQYGE------LDIIQAKYSILDR-----------AMESELLPLCRDNGIVVQVYSPLEQGLLT 226
Cdd:cd19082 137 RAFGASNWSTERIAEANAYAKahglpgFAASSPQWSLARPneppwpgptlvAMDEEMRAWHEENQLPVFAYSSQARGFFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 227 GTITRDYVPGGARAnKVWFQRENmLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19082 217 KRAAGGAEDDSELR-RVYYSEEN-FERLERAKE---LAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-306 |
1.61e-39 |
|
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: 140.54 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGgpawNGDLDQ--QIcIDTILEAhrcGINLIDTAPGYNF-------GNSEVIVGQALK-KLPREQVVVE 83
Cdd:cd19752 1 SELCLGTMYFGT----RTDEETsfAI-LDRYVAA---GGNFLDTANNYAFwteggvgGESERLIGRWLKdRGNRDDVVIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 84 TKCGivwerkGSLFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELKAEGKI 163
Cdd:cd19752 73 TKVG------AGPRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAH---VDDRDTPLEETLEAFNELVKAGKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIREYLQ------YGELDIIQAKYSIL----------DRAMESELLPLCRDNGIVVQV-YSPleqgLLT 226
Cdd:cd19752 144 RAIGASNFAAWRLERARQiarqqgWAEFSAIQQRHSYLrprpgadfgvQRIVTDELLDYASSRPDLTLLaYSP----LLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 227 GTITRDyvpggARANKVWFQRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19752 220 GAYTRP-----DRPLPEQYDGPDSDARLAVLEE---VAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-313 |
2.19e-38 |
|
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: 136.62 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 15 RMGLGTWAIGGGPawngdldqqiCIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWEr 92
Cdd:cd19140 10 ALGLGTYPLTGEE----------CTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAAsgVPRDELFLTTK---VWP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd19140 73 --------------DNYSPDDFLASVEESLRKLRTDYVDLLLLHW---PNKDVPLAETLGALNEAQEAGLARHIGVSNFT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 173 ADHIREYLQYGELDI--IQAKYSI-LDramESELLPLCRDNGIVVQVYSPLEQglltGTITRDYVpggarankvwFQRen 249
Cdd:cd19140 136 VALLREAVELSEAPLftNQVEYHPyLD---QRKLLDAAREHGIALTAYSPLAR----GEVLKDPV----------LQE-- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446646352 250 mlkvidmleqwqpLCARYQCTIPTLALAWILKQSDLISIlSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19140 197 -------------IGRKHGKTPAQVALRWLLQQEGVAAI-PKATNPERLEENLDIFDFTLSDEE 246
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-307 |
3.99e-38 |
|
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: 137.46 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGGgpaWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCG--IVWE 91
Cdd:cd19161 1 SELGLGTAGLGN---LYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVGrlLKPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 92 RKGSLFNKVGdrqLYKNL--------SPESIREEVEASLQRLGIDYIDIYMTH-----WQSVPPFFTPIAETVA----VL 154
Cdd:cd19161 78 REGSVPDPNG---FVDPLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGDRKERHHFAQLMSggfkAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 155 NELKAEGKIRAIGAANVDADHIREYLQYGELDI--IQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLL-TGTITR 231
Cdd:cd19161 155 EELKKAGVIKAFGLGVNEVQICLEALDEADLDCflLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILaTGTKSG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446646352 232 ---DYVPGGArankvwfqrenmlKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19161 235 akfNYGDAPA-------------EIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQT 300
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-304 |
1.49e-37 |
|
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: 136.24 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 2 KKIPLGTTDITLSRMGLGTWAIGGgpAWnGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPrEQVV 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGG--LM-GRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLP-AGPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 82 VETKCGIVWERKGSLfnkvgdrqlyknlsPESIREEVEASLQRLGIDYIDIYMTHWQ-----SVPPFFTPIAETVAVLN- 155
Cdd:cd19104 77 ITTKVRLDPDDLGDI--------------GGQIERSVEKSLKRLKRDSVDLLQLHNRigderDKPVGGTLSTTDVLGLGg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 156 ------ELKAEGKIRAIGAANVD-ADHIREYLQYGELDIIQAKYSILD--------RAMES----ELLPLCRDNGIVVQV 216
Cdd:cd19104 143 vadafeRLRSEGKIRFIGITGLGnPPAIRELLDSGKFDAVQVYYNLLNpsaaearpRGWSAqdygGIIDAAAEHGVGVMG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 217 YSPLEQGLLTGTITRDYVPGGARANKVWFQRENMLKVIDMLEQWQPlcaryqcTIPTLALAWILKQSDLISILSGATAPE 296
Cdd:cd19104 223 IRVLAAGALTTSLDRGREAPPTSDSDVAIDFRRAAAFRALAREWGE-------TLAQLAHRFALSNPGVSTVLVGVKNRE 295
|
....*...
gi 446646352 297 QVRENVAA 304
Cdd:cd19104 296 ELEEAVAA 303
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-303 |
1.47e-35 |
|
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: 130.90 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 12 TLSRMGLGTWAigGGPAWNGDLDQQiciDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL------PREQVVVETK 85
Cdd:cd19099 2 TLSSLGLGTYR--GDSDDETDEEYR---EALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekggiKRDEVVIVTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 86 CGIV---------------WERKGSLFNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTH-------WQSVPPF 143
Cdd:cd19099 77 AGYIpgdgdeplrplkyleEKLGRGLIDVADSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllELGEEEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 144 FTPIAETVAVLNELKAEGKIRAIG-------AANVDADHIREYLQYGE-----------LDIIQAKYSILDRAMESE--- 202
Cdd:cd19099 157 YDRLEEAFEALEEAVAEGKIRYYGistwdgfRAPPALPGHLSLEKLVAaaeevggdnhhFKVIQLPLNLLEPEALTEknt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 203 -------LLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANkvwfqrenmlkvidmleqwqplcaryqcTIPTLA 275
Cdd:cd19099 237 vkgealsLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGA----------------------------TLAQRA 288
|
330 340
....*....|....*....|....*...
gi 446646352 276 LAWILKQSDLISILSGATAPEQVRENVA 303
Cdd:cd19099 289 LQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-307 |
3.10e-35 |
|
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: 129.58 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 6 LGTTDITLSRMGLGTWAIGGgpAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL--PREQVVVE 83
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGG--VYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALqvPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 84 TKCGivwerkgslfnKVGDRQLykNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKAEGKI 163
Cdd:cd19153 83 TKVG-----------RYRDSEF--DYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPALRTLKDEGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIREYLQY---GELDIIQA--KYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGG- 237
Cdd:cd19153 150 KRIGIAGYPLDTLTRATRRcspGSLDAVLSycHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQGPPPWHPASg 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446646352 238 -----ARANKVWfqrenmlkvidmleqwqplCARYQCTIPTLALAWIL-KQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19153 230 elrhyAAAADAV-------------------CASVEASLPDLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-322 |
1.10e-34 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 128.22 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 10 DITLSRMGLGTWAIG-GGPAWNGDLDQQICIDTIL----EAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVET 84
Cdd:cd19103 1 DKKLPKIALGTWSWGsGGAGGDQVFGNHLDEDTLKavfdKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 85 KcgivwerkgslFNKVGDRQlyknlSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPFFTPiaetvaVLNELKAEGKIR 164
Cdd:cd19103 81 K-----------FTPQIAGQ-----SADPVADMLEGSLARLGTDYIDIYWIHNPADVERWTP------ELIPLLKSGKVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 165 AIGAANVDADHIR---EYLQYGELDI--IQAKYSILDRAME-SELLPLCRDNGIVVQVYSPLEQGLLTGTITRD--YVPG 236
Cdd:cd19103 139 HVGVSNHNLAEIKranEILAKAGVSLsaVQNHYSLLYRSSEeAGILDYCKENGITFFAYMVLEQGALSGKYDTKhpLPEG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 237 GARA---NKVWFQRENMLKVIdmleqwQPLCARYQCTIPTLALAWILKQSDLISIlsGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19103 219 SGRAetyNPLLPQLEELTAVM------AEIGAKHGASIAQVAIAWAIAKGTTPII--GVTKPHHVEDAARAASITLTDDE 290
|
....*....
gi 446646352 314 ATLMREMAE 322
Cdd:cd19103 291 IKELEQLAD 299
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-313 |
1.41e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 125.40 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 12 TLSRMGLGTWAIGGGpaWNGDLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKLPRE-----QVVVETKc 86
Cdd:cd19101 1 TISRVINGMWQLSGG--HGGIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRErdaadDVQIHTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 87 givWerkgslfnkVGDRQLyKNLSPESIREEVEASLQRLGIDYIDIYMTHWQ--SVPPFFtpiaETVAVLNELKAEGKIR 164
Cdd:cd19101 76 ---W---------VPDPGE-LTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWdySDPGYL----DAAKHLAELQEEGKIR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 165 AIGAANVDADHIREYLQYGeLDII--QAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTgtitRDYV----PGGA 238
Cdd:cd19101 139 HLGLTNFDTERLREILDAG-VPIVsnQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLS----EKYLgvpePTGP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 239 RANKV----------------WFQrenmlkviDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENV 302
Cdd:cd19101 214 ALETRslqkyklmidewggwdLFQ--------ELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNV 285
|
330
....*....|.
gi 446646352 303 AALNINLSDAD 313
Cdd:cd19101 286 RAFSFRLDDED 296
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
3-311 |
2.27e-33 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 125.74 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 3 KIPLGTTDItlSRMGLGTWAIGggpAWNGDLDQQICIDTILEAhrcGINLIDTAPGYNF-------GNSEVIVGQALKKL 75
Cdd:PRK10625 5 RIPHSSLEV--STLGLGTMTFG---EQNSEADAHAQLDYAVAQ---GINLIDVAEMYPVpprpetqGLTETYIGNWLAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 76 -PREQVVVETK-CGIVWERKGSLF-NKVGDRqlyKNlspesIREEVEASLQRLGIDYIDIYMTHWQSVPP-FF------- 144
Cdd:PRK10625 77 gSREKLIIASKvSGPSRNNDKGIRpNQALDR---KN-----IREALHDSLKRLQTDYLDLYQVHWPQRPTnCFgklgysw 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 145 ---TPIA---ETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGE------LDIIQAKYSILDRAMESELLPLCRDNGI 212
Cdd:PRK10625 149 tdsAPAVsllETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEkhdlprIVTIQNPYSLLNRSFEVGLAEVSQYEGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 213 VVQVYSPLEQGLLTGTITRDYVPGGARaNKVW--FQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILS 290
Cdd:PRK10625 229 ELLAYSCLAFGTLTGKYLNGAKPAGAR-NTLFsrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLL 307
|
330 340
....*....|....*....|.
gi 446646352 291 GATAPEQVRENVAALNINLSD 311
Cdd:PRK10625 308 GATTMEQLKTNIESLHLTLSE 328
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-320 |
2.53e-33 |
|
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: 123.51 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWAIGGgpawngdldQQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK------LPREQVVVETKcgivw 90
Cdd:cd19136 5 GLGTFRLRG---------EEEVRQAVDAALKAGYRLIDTASVY--RN-EADIGKALRDllpkygLSREDIFITSK----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 erkgslfnkVGDrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHW---QSVPPfFTPI-----AETVAVLNELKAEGK 162
Cdd:cd19136 68 ---------LAP----KDQGYEKARAACLGSLERLGTDYLDLYLIHWpgvQGLKP-SDPRnaelrRESWRALEDLYKEGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 163 IRAIGAANVDADHIREYLQYGELD--IIQAKYSilDRAMESELLPLCRDNGIVVQVYSPLEQGLLTgTITRDYVPGGAra 240
Cdd:cd19136 134 LRAIGVSNYTVRHLEELLKYCEVPpaVNQVEFH--PHLVQKELLKFCKDHGIHLQAYSSLGSGDLR-LLEDPTVLAIA-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 241 nkvwfqrenmlkvidmleqwqplcARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADATLMREM 320
Cdd:cd19136 209 ------------------------KKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-307 |
3.34e-33 |
|
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: 124.77 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGGPAWNGDLDQQICIdtileAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPRE 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTI-----AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 79 QVVVETKcgIVWErkgslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYmthWQSVPPFFTPIAETVAVLNELK 158
Cdd:cd19159 76 SLVITTK--LYWG---------GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV---FANRPDSNTPMEEIVRAMTHVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLLTGTItR 231
Cdd:cd19159 142 NQGMAMYWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY-G 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 232 DYVPGGARANKVWFQ-------RENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19159 221 NGVPESSRASLKCYQwlkerivSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 300
|
...
gi 446646352 305 LNI 307
Cdd:cd19159 301 IQV 303
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-323 |
7.09e-31 |
|
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: 117.33 E-value: 7.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 22 AIGGGPAWNG---DLDQQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgivwerkgsL 96
Cdd:cd19120 8 AFGTGTAWYKsgdDDIQRDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKEsgVPREDLFITTK----------V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 97 FNKVGDrqlyknlspesIREEVEASLQRLGIDYIDIYMTHWqsvpPFFTP-----IAETVAVLNELKAEGKIRAIGAANV 171
Cdd:cd19120 75 SPGIKD-----------PREALRKSLAKLGVDYVDLYLIHS----PFFAKeggptLAEAWAELEALKDAGLVRSIGVSNF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 172 DADHIREYLQYGEL--DIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLeqglltGTITRDyvPGGArankvwfqren 249
Cdd:cd19120 140 RIEDLEELLDTAKIkpAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPL------SPLTRD--AGGP----------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446646352 250 mlkVIDMLEQwqpLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADatlMREMAEA 323
Cdd:cd19120 201 ---LDPVLEK---IAEKYGVTPAQVLLRWALQKG--IVVVTTSSKEERMKEYLEAFDFELTEEE---VEEIDKA 263
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
16-320 |
1.04e-30 |
|
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: 116.65 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGgpawngdldqqICIDTILEAHR-CGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiVWer 92
Cdd:cd19135 16 LGLGTSHSGG-----------YSHEAVVYALKeCGYRHIDTAKRY--GC-EELLGKAIKEsgVPREDLFLTTK---LW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 kgslfnkvgdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHW----QSVPPFFTPIAETVAVLNELKAEGKIRAIGA 168
Cdd:cd19135 77 -------------PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWpdcpSSGKNVKETRAETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 169 ANVDADHIREYLQYGEL--DIIQAKYSILDRAMesELLPLCRDNGIVVQVYSPLEQGLLtgtitrdyvpggarankvwFQ 246
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVvpHVNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA-------------------LE 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446646352 247 RENMLKvidmleqwqpLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDADATLMREM 320
Cdd:cd19135 203 EPTVTE----------LAKKYQKTPAQILIRWSI-QNGVVTI-PKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
8-325 |
1.45e-30 |
|
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: 117.91 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 8 TTDITLSRMGLGTWAIGGgpAWN---GDLDQQIC---IDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLP-REQV 80
Cdd:cd19146 6 TAGVRVSPLCLGAMSFGE--AWKsmmGECDKETAfklLDAFYEQ---GGNFIDTANNYQGEESERWVGEWMASRGnRDEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGIVWERKGSLFNKVGdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSvppFFTPIAETVAVLNELKAE 160
Cdd:cd19146 81 VLATKYTTGYRRGGPIKIKSN----YQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWD---YTTSIPELMQSLNHLVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVDA-------DHIREYLQYgELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLtgTITRDY 233
Cdd:cd19146 154 GKVLYLGVSDTPAwvvskanAYARAHGLT-QFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQF--RTEEEF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 234 VPGGARANKVWFQRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19146 231 KRRGRSGRKGGPQTEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEE 307
|
330
....*....|..
gi 446646352 314 atlMREMAEALE 325
Cdd:cd19146 308 ---IQEIEDAYP 316
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-325 |
2.15e-30 |
|
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: 117.18 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWaigggPAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPRE 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTW-----STFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKkgWKRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 79 QVVVETKcgIVWERKGSlfnkvgDRqlykNLSPESIREEVEASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELK 158
Cdd:cd19142 76 SYIVSTK--IYWSYGSE------ER----GLSRKHIIESVRASLRRLQLDYIDIVIIH--KADPM-CPMEEVVRAMSYLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLLTGT--I 229
Cdd:cd19142 141 DNGLIMYWGTSRWSPVEIMEaFSIARQFNCPtpiceQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSLGLDPGIseE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 230 TRDYVPGGARANKVWFQRENMLKVID-------MLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENV 302
Cdd:cd19142 221 TRRLVTKLSFKSSKYKVGSDGNGIHEetrrashKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQL 300
|
330 340
....*....|....*....|...
gi 446646352 303 AALNInLSDADATLMREMAEALE 325
Cdd:cd19142 301 NSLQL-LPKLNSAVMEELERILD 322
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-306 |
3.16e-30 |
|
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: 116.35 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 7 GTTDITLSRMGLGTWAigggpawN-GDLDQ-QICIDTILEAHRCGINLIDTAPGYN--FGNSEVIVGQALK---KLPREQ 79
Cdd:cd19151 6 GRSGLKLPAISLGLWH-------NfGDVDRyENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKedlKPYRDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 80 VVVETKCG-IVWErkgslfNKVGDRQLYKNLSpesirEEVEASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELK 158
Cdd:cd19151 79 LIISTKAGyTMWP------GPYGDWGSKKYLI-----ASLDQSLKRMGLDYVDIFYHH---RPDPETPLEETMGALDQIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAANVDADHIREYL----QYGELDII-QAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDy 233
Cdd:cd19151 145 RQGKALYVGISNYPPEEAREAAailkDLGTPCLIhQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNG- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446646352 234 VPGGARANKVW-FQRENML--KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19151 224 IPEDSRAAKGSsFLKPEQIteEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-307 |
7.00e-30 |
|
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: 115.62 E-value: 7.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 6 LGTTDITLSRMGLGTWAIGGGpawngDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPREQVVVE 83
Cdd:cd19141 5 LGKSGLRVSCLGLGTWVTFGS-----QISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKkgWRRSSYVIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 84 TKcgIVWERKGslfnkvgdrQLYKNLSPESIREEVEASLQRLGIDYIDIYMThwqSVPPFFTPIAETVAVLNELKAEGKI 163
Cdd:cd19141 80 TK--IFWGGKA---------ETERGLSRKHIIEGLKASLERLQLEYVDIVFA---NRPDPNTPMEEIVRAFTHVINQGMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLLTGTITrDYVPG 236
Cdd:cd19141 146 MYWGTSRWSAMEIMEaYSVARQFNLIppiveQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYD-DGVPE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 237 GARA---NKVWF----QRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19141 225 YSRAslkGYQWLkekiLSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-307 |
2.29e-28 |
|
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: 111.72 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 6 LGTTDITLSRMGLGTWAIGGGPAWNGDLDQQICIdtileAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPREQVVVE 83
Cdd:cd19158 6 LGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTL-----AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 84 TKcgIVWErkgslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYmthWQSVPPFFTPIAETVAVLNELKAEGKI 163
Cdd:cd19158 81 TK--IFWG---------GKAETERGLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNTPMEETVRAMTHVINQGMA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDyVPG 236
Cdd:cd19158 147 MYWGTSRWSSMEIMEaYSVARQFNLIppiceQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG-IPP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 237 GARANKVWFQ-------RENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19158 226 YSRASLKGYQwlkdkilSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-307 |
2.33e-28 |
|
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: 112.00 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDITLSRMGLGTWAIGGGpawngDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPRE 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGS-----QISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgWRRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 79 QVVVETKcgIVWErkgslfnkvGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHwQSVPPffTPIAETVAVLNELK 158
Cdd:cd19160 78 SYVVTTK--IYWG---------GQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFAN-RSDPN--SPMEEIVRAMTYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 159 AEGKIRAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMESELLPLCRDNGIVVQVYSPLEQGLLTGTITr 231
Cdd:cd19160 144 NQGMAMYWGTSRWSAMEIMEaYSVARQFNLIppvceQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYD- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 232 DYVPGGARANKVWFQ-----------RENMLKVIDMLeqwqPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRE 300
Cdd:cd19160 223 GRVPDTCRAAVKGYQwlkekvqseegKKQQAKVKELH----PIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIE 298
|
....*..
gi 446646352 301 NVAALNI 307
Cdd:cd19160 299 NLGSIQV 305
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
7-313 |
9.37e-28 |
|
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: 109.85 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 7 GTTDITLSRMGLGTWAIGGGpawngDLDQQICIDTILEAHRCGINLIDTAPGYN--FGNSEVIVGQALKK---LPREQVV 81
Cdd:cd19150 6 GKSGLKLPALSLGLWHNFGD-----DTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdfaGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 82 VETKCGivWERKGSLFNKVGDRqlyKNLspesiREEVEASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELKAEG 161
Cdd:cd19150 81 ISTKAG--YDMWPGPYGEWGSR---KYL-----LASLDQSLKRMGLDYVDIFYSH--RFDPD-TPLEETMGALDHAVRSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 162 KIRAIGAANVDADHIREYL----QYG-ELDIIQAKYSILDRAME-SELLPLCRDNGIVVQVYSPLEQGLLTGTITrDYVP 235
Cdd:cd19150 148 KALYVGISSYSPERTREAAailrELGtPLLIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-NGIP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 236 GGARANKVWFQRENML--KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL-NINLSDA 312
Cdd:cd19150 227 EGSRASKERSLSPKMLteANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALdNLTFSAD 306
|
.
gi 446646352 313 D 313
Cdd:cd19150 307 E 307
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-313 |
5.00e-27 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 106.28 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 13 LSRMGLGTWAIGGgpawngdldqQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVW 90
Cdd:cd19139 1 IPAFGLGTFRLKD----------DVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAEsgVPRDELFITTK---IW 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 ErkgslfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSvPPFFTPIAETVAVLNELKAEGKIRAIGAAN 170
Cdd:cd19139 65 I---------------DNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPS-PNDEVPVEEYIGALAEAKEQGLTRHIGVSN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 171 VDADHIREYLQ-YGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfqren 249
Cdd:cd19139 129 FTIALLDEAIAvVGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYG-------------------------- 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446646352 250 mlKVIDMlEQWQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19139 183 --KVLDD-PVLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
12-320 |
7.91e-27 |
|
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: 105.92 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 12 TLSRMGLGTWAIgggpawngdlDQQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiv 89
Cdd:cd19131 9 TIPQLGLGVWQV----------SNDEAASAVREALEVGYRSIDTAAIY--GN-EEGVGKAIRAsgVPREELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 werkgsLFNkvgDRQLYknlspESIREEVEASLQRLGIDYIDIYMTHWQSvpPFFTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:cd19131 72 ------LWN---SDQGY-----DSTLRAFDESLRKLGLDYVDLYLIHWPV--PAQDKYVETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIREYLqyGELDIIQAKYSI--LDRAMESELLPLCRDNGIVVQVYSPLEQglltgtitrdyvpGGARANKVwfqr 247
Cdd:cd19131 136 NFTIEHLQRLI--DETGVVPVVNQIelHPRFQQRELRAFHAKHGIQTESWSPLGQ-------------GGLLSDPV---- 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446646352 248 enmlkvidmLEQwqpLCARYQCTIPTLALAWILkQSDLISILSGATaPEQVRENVAALNINLSDADATLMREM 320
Cdd:cd19131 197 ---------IGE---IAEKHGKTPAQVVIRWHL-QNGLVVIPKSVT-PSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
23-304 |
8.31e-27 |
|
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: 106.98 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 23 IGGGP---AWNGDLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKL----PREQVVVETKCGivweRKG- 94
Cdd:cd19164 18 FGAATfsyQYTTDPESIPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALrdefPRDTYFIITKVG----RYGp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 95 SLFNkvgdrqlYknlSPESIREEVEASLQRLGIDYIDIYMTHwqSVpPFFTP--IAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd19164 92 DDFD-------Y---SPEWIRASVERSLRRLHTDYLDLVYLH--DV-EFVADeeVLEALKELFKLKDEGKIRNVGISGYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 173 ADHIREYLQY------GELDIIQ--AKYSILDRAMeSELLPLCRDNGIVVQVY--SPLEQGLLTGTITRDYVPGGArank 242
Cdd:cd19164 159 LPVLLRLAELarttagRPLDAVLsyCHYTLQNTTL-LAYIPKFLAAAGVKVVLnaSPLSMGLLRSQGPPEWHPASP---- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446646352 243 vwFQRENMLKVIDMLEQWQPlcaryqcTIPTLALAWILKQSDLI-SILSGATAPEQVRENVAA 304
Cdd:cd19164 234 --ELRAAAAKAAEYCQAKGT-------DLADVALRYALREWGGEgPTVVGCSNVDELEEAVEA 287
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
7-310 |
3.19e-26 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 106.61 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 7 GTTDITLSRMGLGTWAIGGgpaWNGDLDQQICIdtILEAHRCGINLIDTAPGYN--FGNSEVIVGQALK---KLPREQVV 81
Cdd:PRK09912 19 GKSGLRLPALSLGLWHNFG---HVNALESQRAI--LRKAFDLGITHFDLANNYGppPGSAEENFGRLLRedfAAYRDELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 82 VETKCGI-VWErkgSLFNKVGDRQLyknlspesIREEVEASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKAE 160
Cdd:PRK09912 94 ISTKAGYdMWP---GPYGSGGSRKY--------LLASLDQSLKRMGLEYVDIFYSHRVDEN---TPMEETASALAHAVQS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVD-------ADHIREYLQygELDIIQAKYSILDRAME-SELLPLCRDNGIVVQVYSPLEQGLLTGTITRD 232
Cdd:PRK09912 160 GKALYVGISSYSpertqkmVELLREWKI--PLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 233 yVPGGAR----ANKVWFQRENMLKVIDM--LEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:PRK09912 238 -IPQDSRmhreGNKVRGLTPKMLTEANLnsLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALN 316
|
....
gi 446646352 307 iNLS 310
Cdd:PRK09912 317 -NLT 319
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
11-313 |
7.14e-26 |
|
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: 103.62 E-value: 7.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 11 ITLSRMGLGTWAIGGGpawngdldqQICIDTILEAHRCGINLIDTAPGYnfGNSEvIVGQALKK--LPREQVVVETKcgi 88
Cdd:cd19157 8 VKMPWLGLGVFKVEEG---------SEVVNAVKTALKNGYRSIDTAAIY--GNEE-GVGKGIKEsgIPREELFITSK--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 89 VWErkgslfnkvgDRQLYknlspESIREEVEASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKAEGKIRAIGA 168
Cdd:cd19157 73 VWN----------ADQGY-----DSTLKAFEASLERLGLDYLDLYLIHW----PVKGKYKETWKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 169 ANVDADHIREYLQYGELD--IIQAKYSilDRAMESELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfq 246
Cdd:cd19157 134 SNFQVHHLEDLLADAEIVpmVNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQG----------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446646352 247 renmlKVIDMlEQWQPLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19157 189 -----QLLDN-PVLKEIAEKYNKSVAQVILRWDL-QNGVVTI-PKSIKEHRIIENADVFDFELSQED 247
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
17-321 |
3.58e-24 |
|
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: 98.80 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWAIGggpawngdlDQQICIDTILEAHRCGINLIDTAPGYnfGNSEViVGQALKK--LPREQVVVETKCGIvwerkg 94
Cdd:cd19133 13 GFGVFQIP---------DPEECERAVLEAIKAGYRLIDTAAAY--GNEEA-VGRAIKKsgIPREELFITTKLWI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 95 slfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHWQsvppfFTPIAETVAVLNELKAEGKIRAIGAANVDAD 174
Cdd:cd19133 75 ------------QDAGYEKAKKAFERSLKRLGLDYLDLYLIHQP-----FGDVYGAWRAMEELYKEGKIRAIGVSNFYPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 175 HIREYLQYGELD--IIQAKYSILDRamESELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfqRENMLK 252
Cdd:cd19133 138 RLVDLILHNEVKpaVNQIETHPFNQ--QIEAVEFLKKYGVQIEAWGPFAEG-----------------------RNNLFE 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 253 --VIdmleqwQPLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDADatlMREMA 321
Cdd:cd19133 193 npVL------TEIAEKYGKSVAQVILRWLI-QRGIVVI-PKSVRPERIAENFDIFDFELSDED---MEAIA 252
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
16-315 |
5.51e-24 |
|
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: 98.28 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGggpawNGDLDQQICidtiLEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWErk 93
Cdd:cd19126 12 LGLGVFQTP-----DGDETERAV----QTALENGYRSIDTAAIYK---NEEGVGEAIREsgVPREELFVTTK---LWN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 94 gslfnkvgDRQLYknlspESIREEVEASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKAEGKIRAIGAANVDA 173
Cdd:cd19126 75 --------DDQRA-----RRTEDAFQESLDRLGLDYVDLYLIHW----PGKDKFIDTWKALEKLYASGKVKAIGVSNFQE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 174 DHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTgtitrdyvpggarANKVWFQrenmlkv 253
Cdd:cd19126 138 HHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLL-------------SNPVLAA------- 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446646352 254 idmleqwqpLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDADAT 315
Cdd:cd19126 198 ---------IGEKYGKSAAQVVLRWDI-QHGVVTI-PKSVHASRIKENADIFDFELSEDDMT 248
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-326 |
8.92e-24 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 97.73 E-value: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 11 ITLSRMGLGTWAIGGGPAwngdldqqicIDTILEAHRCGINLIDTApgYNFGNsEVIVGQALK--KLPREQVVVETKCGi 88
Cdd:cd19132 5 TQIPAIGFGTYPLKGDEG----------VEAVVAALQAGYRLLDTA--FNYEN-EGAVGEAVRrsGVPREELFVTTKLP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 89 vwerkgslfnkvGDRQLYknlspESIREEVEASLQRLGIDYIDIYMTHWqsvP-PFFTPIAETVAVLNELKAEGKIRAIG 167
Cdd:cd19132 71 ------------GRHHGY-----EEALRTIEESLYRLGLDYVDLYLIHW---PnPSRDLYVEAWQALIEAREEGLVRSIG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 168 AANVDADHIreylqygelDIIQAKYSILDRAMESELLPL---------CRDNGIVVQVYSPLEQGLltgtitrdyvpgga 238
Cdd:cd19132 131 VSNFLPEHL---------DRLIDETGVTPAVNQIELHPYfpqaeqrayHREHGIVTQSWSPLGRGS-------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 239 rankvwfqrenmlkviDMLEQ--WQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADatl 316
Cdd:cd19132 188 ----------------GLLDEpvIKAIAEKHGKTPAQVVLRWHVQLG--VVPIPKSANPERQRENLAIFDFELSDED--- 246
|
330
....*....|
gi 446646352 317 MREMAeALER 326
Cdd:cd19132 247 MAAIA-ALDR 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
38-313 |
3.50e-23 |
|
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: 96.71 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 38 CIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWerkgslFNKVGDrqlyknlspESIR 115
Cdd:cd19127 24 TADAVATALADGYRLIDTAAAYG---NEREVGEGIRRsgVDRSDIFVTTK---LW------ISDYGY---------DKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 116 EEVEASLQRLGIDYIDIYMTHWqSVPPFFTPIAETVAVLNELKAEGKIRAIGAANVDADHireylqygeLDIIQAKYSIL 195
Cdd:cd19127 83 RGFDASLRRLGLDYVDLYLLHW-PVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEH---------LERLIDATTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 196 DRAMESELLPLC---------RDNGIVVQVYSPLeqglltGTITRdYVPGGARANKVWFQRENMLKvidmleqwqpLCAR 266
Cdd:cd19127 153 PAVNQVELHPYFsqkdlrafhRRLGIVTQAWSPI------GGVMR-YGASGPTGPGDVLQDPTITG----------LAEK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446646352 267 YQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19127 216 YGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFDFALSAED 260
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
8-310 |
1.72e-20 |
|
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: 89.88 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 8 TTDITLSRMGLGTWAIGGgpAWNGDL-----DQQI-CIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQ--ALKKLpREQ 79
Cdd:cd19147 5 TAGIRVSPLILGAMSIGD--AWSGFMgsmdkEQAFeLLDAFYEA---GGNFIDTANNYQDEQSETWIGEwmKSRKN-RDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 80 VVVETKCGIVWERKGslfNKVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSvppFFTPIAETVAVLNELKA 159
Cdd:cd19147 79 IVIATKFTTDYKAYE---VGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWD---YTTSIEEVMDSLHILVQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 160 EGKIRAIGAANVDA---DHIREYLQ-YGE--LDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPL-----------EQ 222
Cdd:cd19147 153 QGKVLYLGVSDTPAwvvSAANYYATaHGKtpFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLgggkfqskkavEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 223 GLLTGTITRDYVPGGArankvwfQRENMLKVIDMLEQwqplCARYQCT--IPTLALAWILKQSDLISILSGATAPEQVRE 300
Cdd:cd19147 233 RKKNGEGLRSFVGGTE-------QTPEEVKISEALEK----VAEEHGTesVTAIALAYVRSKAPNVFPLVGGRKIEHLKD 301
|
330
....*....|
gi 446646352 301 NVAALNINLS 310
Cdd:cd19147 302 NIEALSIKLT 311
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
15-225 |
2.61e-20 |
|
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: 88.73 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 15 RMGLGTWAIGGGpawngdldqQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWER 92
Cdd:cd19156 11 RLGLGVWRVQDG---------AEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIREsgVPREEVFVTTK---LWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 93 KgslfnkvgdrQLYknlspESIREEVEASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKAEGKIRAIGAANVD 172
Cdd:cd19156 76 D----------QGY-----ESTLAAFEESLEKLGLDYVDLYLIHW----PVKGKFKDTWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446646352 173 ADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLL 225
Cdd:cd19156 137 EHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL 189
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-326 |
7.01e-20 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 87.39 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 12 TLSRMGLGTWAIGGgpawngdldqQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiV 89
Cdd:PRK11172 2 SIPAFGLGTFRLKD----------QVVIDSVKTALELGYRAIDTAQIY--DN-EAAVGQAIAEsgVPRDELFITTK---I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WerkgslfnkvgdrqlYKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSvPPFFTPIAETVAVLNELKAEGKIRAIGAA 169
Cdd:PRK11172 66 W---------------IDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPS-PNDEVSVEEFMQALLEAKKQGLTREIGIS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 170 NVDADHIREylqygELDIIQAKySILDRAME-------SELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggaranK 242
Cdd:PRK11172 130 NFTIALMKQ-----AIAAVGAE-NIATNQIElspylqnRKVVAFAKEHGIHVTSYMTLAYG------------------K 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 243 VwfqrenmLK--VIdmleqwQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADatlMREM 320
Cdd:PRK11172 186 V-------LKdpVI------ARIAAKHNATPAQVILAWAMQLG--YSVIPSSTKRENLASNLLAQDLQLDAED---MAAI 247
|
....*.
gi 446646352 321 AeALER 326
Cdd:PRK11172 248 A-ALDR 252
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
17-313 |
4.64e-19 |
|
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: 85.48 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWAIGGGpawngdldqqICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVvetkcgivwERKgSL 96
Cdd:cd19125 15 GLGTWQADPG----------VVGNAVKTAIKEGYRHIDCAAIY--GN-EKEIGKALKKLFEDGVV---------KRE-DL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 97 FnkVGDRQLYKNLSPESIREEVEASLQRLGIDYIDIYMTHW-------------QSVPPFftPIAETVAVLNELKAEGKI 163
Cdd:cd19125 72 F--ITSKLWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWpvrlkkgahmpepEEVLPP--DIPSTWKAMEKLVDSGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 164 RAIGAANVDADHIREYLQYGEldIIQAKYSildraME-------SELLPLCRDNGIVVQVYSPLeqglltgtitrdyvpg 236
Cdd:cd19125 148 RAIGVSNFSVKKLEDLLAVAR--VPPAVNQ-----VEchpgwqqDKLHEFCKSKGIHLSAYSPL---------------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446646352 237 gARANKVWFQReNMLK--VIDMLEQwqplcaRYQCTIPTLALAWILKQSDliSILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19125 205 -GSPGTTWVKK-NVLKdpIVTKVAE------KLGKTPAQVALRWGLQRGT--SVLPKSTNEERIKENIDVFDWSIPEED 273
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-325 |
1.82e-18 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 84.05 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 22 AIGGGPAWNGDLDQQICIDTILEAhrcGINLIDTAPGYNfgnSEVIVGQALK------KLPREQVVVETKcgivwerkgs 95
Cdd:cd19129 8 ALGFGTLIPDPSATRNAVKAALEA---GFRHFDCAERYR---NEAEVGEAMQevfkagKIRREDLFVTTK---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 96 LFNKvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHwqsvPPF-FTP--------------------IAETVAVL 154
Cdd:cd19129 72 LWNT--------NHRPERVKPAFEASLKRLQLDYLDLYLIH----TPFaFQPgdeqdprdangnviyddgvtLLDTWRAM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 155 NELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV 234
Cdd:cd19129 140 ERLVDEGRCKAIGLSDVSLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPKLLEDPVI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 235 PGGARankvwfqrenmlkvidmleqwqplcaRYQCTIPTLALAWILKQSdlISILSGATAPEQVRENvaaLNINLSDADA 314
Cdd:cd19129 220 TAIAR--------------------------RVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIREN---FDISTLPEDA 268
|
330
....*....|.
gi 446646352 315 tlMREMAEALE 325
Cdd:cd19129 269 --MREINEGIK 277
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-322 |
3.94e-18 |
|
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: 83.23 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTTDiTLSRMGLGTWAIGGGPAWngdldqqiciDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALK------K 74
Cdd:cd19123 1 MKTLPLSNGD-LIPALGLGTWKSKPGEVG----------QAVKQALEAGYRHIDCAAIY--GN-EAEIGAALAevfkegK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 75 LPREQVVVETKcgivwerkgsLFNKVGDrqlyknlsPESIREEVEASLQRLGIDYIDIYMTHW----QSVPPFFT----- 145
Cdd:cd19123 67 VKREDLWITSK----------LWNNSHA--------PEDVLPALEKTLADLQLDYLDLYLMHWpvalKKGVGFPEsgedl 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 146 ------PIAETVAVLNELKAEGKIRAIGAANVDADHIREYLQygeldiiQAKYSILDRAME-------SELLPLCRDNGI 212
Cdd:cd19123 129 lslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLA-------TARIKPAVNQVElhpylqqPELLAFCRDNGI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 213 VVQVYSPLeqglltGTitrdyvPGGARANKVwfQRENML---KVIdmleqwQPLCARYQCTIPTLALAWILKQSdlISIL 289
Cdd:cd19123 202 HLTAYSPL------GS------GDRPAAMKA--EGEPVLledPVI------NKIAEKHGASPAQVLIAWAIQRG--TVVI 259
|
330 340 350
....*....|....*....|....*....|...
gi 446646352 290 SGATAPEQVRENVAALNINLSDADatlMREMAE 322
Cdd:cd19123 260 PKSVNPERIQQNLEAAEVELDASD---MATIAA 289
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
17-319 |
4.20e-18 |
|
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: 82.72 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWAIGGGPAwngdldqqiCIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK------LPREQVVVETKcgiVW 90
Cdd:cd19116 15 ALGTWKLKDDEG---------VRQAVKHAIEAGYRHIDTAYLY--GN-EAEVGEAIREkiaegvVKREDLFITTK---LW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 erkGSLFnkvgdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLN--------------- 155
Cdd:cd19116 80 ---NSYH------------EREQVEPALRESLKRLGLDYVDLYLIHW---PVAFKENNDSESNGDgslsdidyletwrgm 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 156 -ELKAEGKIRAIGAANVDADHIREYLQYGelDIIQAKYSI-----LDRAmesELLPLCRDNGIVVQVYSPLEQglltgti 229
Cdd:cd19116 142 eDLVKLGLTRSIGVSNFNSEQINRLLSNC--NIKPAVNQIevhptLTQE---KLVAYCQSNGIVVMAYSPFGR------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 230 trdYVPGGARANKVWFQRENMLKvidmleqwqpLCARYQCTIPTLALAWILkQSDLISILSgATAPEQVRENVAALNINL 309
Cdd:cd19116 210 ---LVPRGQTNPPPRLDDPTLVA----------IAKKYGKTTAQIVLRYLI-DRGVVPIPK-SSNKKRIKENIDIFDFQL 274
|
330
....*....|
gi 446646352 310 SDADATLMRE 319
Cdd:cd19116 275 TPEEVAALNS 284
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
16-220 |
4.37e-17 |
|
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: 79.88 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGGPAwngdldqqicIDTILEAHRCGINLIDTApgYNFGNsEVIVGQALKK-----LPREQVVVETKCGIVW 90
Cdd:cd19121 15 VGLGTWQAKAGEV----------KAAVAHALKIGYRHIDGA--LCYQN-EDEVGEGIKEaiaggVKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 91 ERKgslfnkvgdrqlyknlspesIREEVEASLQRLGIDYIDIYMTHW------QSVPPFFTPI-------------AETV 151
Cdd:cd19121 82 HRR--------------------VELCLDRSLKSLGLDYVDLYLVHWpvllnpNGNHDLFPTLpdgsrdldwdwnhVDTW 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 152 AVLNELKAEGKIRAIGAANVDADHIREYLQYGEldIIQAKYSILDRAM--ESELLPLCRDNGIVVQVYSPL 220
Cdd:cd19121 142 KQMEKVLKTGKTKAIGVSNYSIPYLEELLKHAT--VVPAVNQVENHPYlpQQELVDFCKEKGILIEAYSPL 210
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-324 |
8.40e-17 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 79.38 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 8 TTDITLS---RM---GLGTWAIgggpawNGDlDQQICIDTILEAhrcGINLIDTApgYNFGNSEVIvGQALK------KL 75
Cdd:cd19154 1 SASITLSngvKMpliGLGTWQS------KGA-EGITAVRTALKA---GYRLIDTA--FLYQNEEAI-GEALAelleegVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 76 PREQVVVETKcgivwerkgsLFNKVgdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTH--W---QSVPPFFT----- 145
Cdd:cd19154 68 KREDLFITTK----------LWTHE--------HAPEDVEEALRESLKKLQLEYVDLYLIHapAafkDDEGESGTmengm 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 146 ------PIAETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSP 219
Cdd:cd19154 130 sihdavDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYAT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 220 LeqglltGTITRDYVPGgarANKVWFQRENMLKVIdMLEqwqpLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVR 299
Cdd:cd19154 210 L------GSPGRANFTK---STGVSPAPNLLQDPI-VKA----IAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIK 273
|
330 340
....*....|....*....|....*
gi 446646352 300 ENVAALNINLSDADATLMREMAEAL 324
Cdd:cd19154 274 ENFNIFDFSLSEEDMATLEEIEKSL 298
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-220 |
1.29e-16 |
|
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: 78.69 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 9 TDITLSRMGLGTWAIGGGPAWNgdldqqicidTILEAHRCGINLIDTApgYNFGNSEViVGQALKK--LPREQVVVETKC 86
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNEVAK----------AVEAALKAGYRHIDTA--AIYGNEEE-VGQGIKDsgVPREEIFITTKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 87 GIVWERKgslfnkvgdrqlyknlsPEsirEEVEASLQRLGIDYIDIYMTHWQS-------------------VPPFFTPI 147
Cdd:cd19117 77 WCTWHRR-----------------VE---EALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtkdHEPDWDFI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446646352 148 aETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAM--ESELLPLCRDNGIVVQVYSPL 220
Cdd:cd19117 137 -KTWELMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLlpQPKLVDFCKSKGIHATAYSPL 210
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-225 |
2.50e-16 |
|
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: 77.59 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 10 DITLSRMGLGTWAIGggpawngDLDQQICIDTILEAhrcGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcg 87
Cdd:cd19134 8 DNTMPVIGLGVGELS-------DDEAERSVSAALEA---GYRLIDTAAAY--GN-EAAVGRAIAAsgIPRGELFVTTK-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 88 iVWErkgslfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHWQSVPPffTPIAETVAVLNELKAEGKIRAIG 167
Cdd:cd19134 73 -LAT---------------PDQGFTASQAACRASLERLGLDYVDLYLIHWPAGRE--GKYVDSWGGLMKLREEGLARSIG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446646352 168 AANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLL 225
Cdd:cd19134 135 VSNFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRL 192
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-316 |
3.43e-16 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 77.32 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLGTT----DITLSRMGLGTWAIGGGPAWNGDLDQQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP 76
Cdd:PRK10376 1 MSTIMSSGTftlgGRSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 77 REQVVVeTKCGIVWERKGSLFnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIY-MTHWQSV-PPFFTPIAETVAVL 154
Cdd:PRK10376 81 DDLTIV-TKVGARRGEDGSWL---------PAFSPAELRRAVHDNLRNLGLDVLDVVnLRLMGDGhGPAEGSIEEPLTVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 155 NELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDnGIVVQVYSPLeqglltgtitrdyv 234
Cdd:PRK10376 151 AELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARD-GIAYVPFFPL-------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 235 pGGARAnkvwFQRENMLKVIDMLEQwQPLCaryqctiptLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD- 313
Cdd:PRK10376 216 -GGFTP----LQSSTLSDVAASLGA-TPMQ---------VALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVl 280
|
...
gi 446646352 314 ATL 316
Cdd:PRK10376 281 AEL 283
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
16-223 |
8.69e-16 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 75.88 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGggpawngdlDQQIcIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgivwerk 93
Cdd:PRK11565 18 LGLGVWQAS---------NEEV-ITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEasVAREELFITTK-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 94 gsLFNkvgDRQLyknlspeSIREEVEASLQRLGIDYIDIYMTHWqSVPPFFTPIaETVAVLNELKAEGKIRAIGAANVDA 173
Cdd:PRK11565 77 --LWN---DDHK-------RPREALEESLKKLQLDYVDLYLMHW-PVPAIDHYV-EAWKGMIELQKEGLIKSIGVCNFQI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446646352 174 DHIREYLQygELDIIQAKYSIldramesELLPLCRD---------NGIVVQVYSPLEQG 223
Cdd:PRK11565 143 HHLQRLID--ETGVTPVINQI-------ELHPLMQQrqlhawnatHKIQTESWSPLAQG 192
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-313 |
1.58e-15 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 75.61 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGGpawngdlDQQICIDTILEAhrcGINLIDTAPGYnfGNSEVIvGQALK------KLPREQVVVETKCGIV 89
Cdd:cd19111 7 IGLGTYQSPPE-------EVRAAVDYALFV---GYRHIDTALSY--QNEKAI-GEALKwwlkngKLKREEVFITTKLPPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WerkgslfnkvgdrqlyknLSPESIREEVEASLQRLGIDYIDIYMTH--WQSV--------PPFFTPIAETVAVLNELKA 159
Cdd:cd19111 74 Y------------------LEFKDTEKSLEKSLENLKLPYVDLYLIHhpCGFVnkkdkgerELASSDVTSVWRAMEALVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 160 EGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLeqglltGTITR--DYVPGG 237
Cdd:cd19111 136 EGKVKSIGLSNFNPRQINKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPL------GSPGRanQSLWPD 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446646352 238 AranKVWFQRENMLKVIDMLEQwqplcaryqcTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19111 210 Q---PDLLEDPTVLAIAKELDK----------TPAQVLLRFVLQRG--TGVLPKSTNKERIEENFEVFDFELTEEH 270
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
2-220 |
6.19e-15 |
|
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: 73.96 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 2 KKIPLgttditlsrMGLGTWAIGGGPAWNGdldqqicidtILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK------- 74
Cdd:cd19106 5 QKMPL---------IGLGTWKSKPGQVKAA----------VKYALDAGYRHIDCAAVY--GN-EQEVGEALKEkvgpgka 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 75 LPREQVVVETKcgiVWERKGSlfnkvgdrqlyknlsPESIREEVEASLQRLGIDYIDIYMTHWqsvPPFF---------- 144
Cdd:cd19106 63 VPREDLFVTSK---LWNTKHH---------------PEDVEPALRKTLKDLQLDYLDLYLIHW---PYAFergdnpfpkn 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 145 ---------TPIAETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQ 215
Cdd:cd19106 122 pdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVT 201
|
....*
gi 446646352 216 VYSPL 220
Cdd:cd19106 202 AYSPL 206
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-326 |
8.44e-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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 73.92 E-value: 8.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 14 SRMGLGTWAIGG------------GPAWNGDLDQQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALK--KLPREQ 79
Cdd:cd19098 1 PRLGLGLAALGRpgyinlghaadlGSGRSVEAMRAHTHAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRsrNIAPDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 80 VVVETKCGIV----WerkgslfNKVGDRQLYKNLSPESIREEVEASLQRLGiDYIDIYMTHwqSVPpFFTPIAETVAVLN 155
Cdd:cd19098 79 VFVGSKWGYTytadW-------QVDAAVHEVKDHSLARLLKQWEETRSLLG-KHLDLYQIH--SAT-LESGVLEDADVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 156 EL---KAEGkiRAIG---AANVDADHIREYLQY---GE--LDIIQAKYSILDRAMeSELLPLCRDNGIVVQVYSPLEQGL 224
Cdd:cd19098 148 ALaelKAEG--VKIGlslSGPQQAETLRRALEIeidGArlFDSVQATWNLLEQSA-GEALEEAHEAGMGVIVKEALANGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 225 LTGTITRDYVPGGARANKvwfqrenmlkvidmleqwqPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19098 225 LTDRNPSPELAPLMAVLK-------------------AVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRA 285
|
330 340
....*....|....*....|..
gi 446646352 305 LNINLSDADATLMREMAEALER 326
Cdd:cd19098 286 LDVSLDLELLAALADLAEPPED 307
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-313 |
9.65e-14 |
|
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: 70.24 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 15 RMGLGTWAIgggpawNGDLDQQicidTILEAHRCGINLIDTApgYNFGNSEVIvGQALKKL------PREQVVVETKcgi 88
Cdd:cd19128 3 RLGFGTYKI------TESESKE----AVKNAIKAGYRHIDCA--YYYGNEAFI-GIAFSEIfkdggvKREDLFITSK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 89 VWErkgslfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHW-------QSVPPFF---------TPIAETVA 152
Cdd:cd19128 67 LWP---------------TMHQPENVKEQLLITLQDLQLEYLDLFLIHWplafdmdTDGDPRDdnqiqslskKPLEDTWR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 153 VLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLeqglltgtitrd 232
Cdd:cd19128 132 AMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPL------------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 233 yvpGGARANKvwfqrENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQ-SDLISILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19128 200 ---GGSYGDG-----NLTFLNDSELKA---LATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTK 268
|
..
gi 446646352 312 AD 313
Cdd:cd19128 269 ED 270
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
16-220 |
1.45e-13 |
|
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: 69.75 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGGPAWNGdldqqicidtILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVEtkcgivwerKGS 95
Cdd:cd19118 10 IGLGTWQAEPGEVGAA----------VKIALKAGYRHLDLAKVY--QN-QHEVGQALKELLKEEPGVK---------RED 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 96 LFNKvgdRQLYKNL-SPESIREEVEASLQRLGIDYIDIYMTHW-------QSVPPFFTP--------------IAETVAV 153
Cdd:cd19118 68 LFIT---SKLWNNShRPEYVEPALDDTLKELGLDYLDLYLIHWpvafkptGDLNPLTAVptnggevdldlsvsLVDTWKA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446646352 154 LNELKAEGKIRAIGAANVDADHIREYLQ-YGELDII-QAKYSILdrAMESELLPLCRDNGIVVQVYSPL 220
Cdd:cd19118 145 MVELKKTGKVKSIGVSNFSIDHLQAIIEeTGVVPAVnQIEAHPL--LLQDELVDYCKSKNIHITAYSPL 211
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
3-311 |
2.80e-13 |
|
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: 68.78 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 3 KIPLGTtDITLSRMGLGTWAIGggpawngDLDQQICIDTILEAhrcGINLIDTAPGYnfGNsEVIVGQAL--KKLPREQV 80
Cdd:cd19130 1 SIVLND-GNSIPQLGYGVFKVP-------PADTQRAVATALEV---GYRHIDTAAIY--GN-EEGVGAAIaaSGIPRDEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 81 VVETKCGivwerkgslfnkvGDRQlyknlSPESIREEVEASLQRLGIDYIDIYMTHWQSvpPFFTPIAETVAVLNELKAE 160
Cdd:cd19130 67 FVTTKLW-------------NDRH-----DGDEPAAAFAESLAKLGLDQVDLYLVHWPT--PAAGNYVHTWEAMIELRAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 161 GKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTitrdyVPGGARA 240
Cdd:cd19130 127 GRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGD-----PPVGAIA 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446646352 241 nkvwfqrenmlkvidmleqwqplcARYQCTIPTLALAWILKQSDliSILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19130 202 ------------------------AAHGKTPAQIVLRWHLQKGH--VVFPKSVRRERMEDNLDVFDFDLTD 246
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
16-220 |
4.94e-13 |
|
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: 68.29 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWaigggpawNGDLDQQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALK------KLPREQVVVETKcgiV 89
Cdd:cd19119 15 LGLGTA--------SPHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKraiddgSIKREELFITTK---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WErkgSLFNKVgdrqlyknlspesiREEVEASLQRLGIDYIDIYMTHW--------QSVPPFFTPI-------------- 147
Cdd:cd19119 81 WP---TFYDEV--------------ERSLDESLKALGLDYVDLLLVHWpvcfekdsDDSGKPFTPVnddgktryaasgdh 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446646352 148 AETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPL 220
Cdd:cd19119 144 ITTYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPL 216
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-313 |
1.00e-12 |
|
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: 67.29 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 11 ITLSRMGLGTWAIGGGPawngdldqQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK-------LPREQVVVE 83
Cdd:cd19124 3 QTMPVIGMGTASDPPSP--------EDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlglvKSRDELFVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 84 TKcgiVWerkgslfnkVGDrqLYKNLSPESIREeveaSLQRLGIDYIDIYMTHW--QSVP-PFFTPIAE----------T 150
Cdd:cd19124 72 SK---LW---------CSD--AHPDLVLPALKK----SLRNLQLEYVDLYLIHWpvSLKPgKFSFPIEEedflpfdikgV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 151 VAVLNELKAEGKIRAIGAANVDADHIREYLQYG---------ELDII-QAKysildramesELLPLCRDNGIVVQVYSPL 220
Cdd:cd19124 134 WEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAtippavnqvEMNPAwQQK----------KLREFCKANGIHVTAYSPL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 221 eqglltgtitrdyvpgGARANKvWFQRENMLKviDMLEQwqpLCARYQCTIPTLALAWILKQSDliSILSGATAPEQVRE 300
Cdd:cd19124 204 ----------------GAPGTK-WGSNAVMES--DVLKE---IAAAKGKTVAQVSLRWVYEQGV--SLVVKSFNKERMKQ 259
|
330
....*....|...
gi 446646352 301 NVAALNINLSDAD 313
Cdd:cd19124 260 NLDIFDWELTEED 272
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
16-320 |
4.50e-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: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAigggpawngdLDQQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK------LPREQVVVETKcgiV 89
Cdd:cd19112 14 IGLGVWR----------MEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEafktglVKREDLFITTK---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 WerkgslfnkvgdrqlykNLSPESIREEVEASLQRLGIDYIDIYMTHWqSVPPFFTPIAETVAVLNE------------- 156
Cdd:cd19112 78 W-----------------NSDHGHVIEACKDSLKKLQLDYLDLYLVHF-PVATKHTGVGTTGSALGEdgvldidvtisle 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 157 --------LKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLeqglltgt 228
Cdd:cd19112 140 ttwhamekLVSAGLVRSIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPL-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 229 itrdyvpGGARANKVWFQRENMLKVIDMLEqwqpLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNIN 308
Cdd:cd19112 212 -------GGAAANAEWFGSVSPLDDPVLKD----LAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENIDVFDFQ 278
|
330
....*....|..
gi 446646352 309 LSDADATLMREM 320
Cdd:cd19112 279 LSKEDMKLIKSL 290
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
16-320 |
5.86e-11 |
|
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: 62.54 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAigggpawNGDLDQQICIDTILEAhrcGINLIDTApgYNFGNsEVIVGQALK------KLPREQVVVETKcgiv 89
Cdd:cd19155 15 VGLGTWQ-------SSPEEIETAVDTALEA---GYRHIDTA--YVYRN-EAAIGNVLKkwidsgKVKREELFIVTK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 90 werkgslFNKVGDRqlyknlsPESIREEVEASLQRLGIDYIDIYMTHW------------------QSVPPFFTPIAETV 151
Cdd:cd19155 78 -------LPPGGNR-------REKVEKFLLKSLEKLQLDYVDLYLIHFpvgslskeddsgkldptgEHKQDYTTDLLDIW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 152 AVLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYSPLEQGLLTGTITR 231
Cdd:cd19155 144 KAMEAQVDQGLTRSIGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 232 DYVPGGARANkvwFQRENMLKVIdmleqwqplCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19155 224 TGSPSGSSPD---LLQDPVVKAI---------AERHGKSPAQVLLRWLMQRG--VVVIPKSTNAARIKENFQVFDFELTE 289
|
....*....
gi 446646352 312 ADATLMREM 320
Cdd:cd19155 290 ADMAKLSSL 298
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-322 |
1.43e-10 |
|
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: 61.10 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 8 TTDITLSRMGLGTWAIGG--GPAWNGdldqqicidtILEAHRCGINLIDTAPGYNfgnSEVIVGQA----LKKLP---RE 78
Cdd:cd19122 4 NNGVKIPAVGFGTFANEGakGETYAA----------VTKALDVGYRHLDCAWFYL---NEDEVGDAvrdfLKENPsvkRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 79 QVVVETKcgiVWErkgslfnkvgdrQLYKnlsPESIREEVEASLQRLGIDYIDIYMTHW--------QSVPPF------- 143
Cdd:cd19122 71 DLFICTK---VWN------------HLHE---PEDVKWSIDNSLKNLKLDYIDLFLVHWpiaaekndQRSPKLgpdgkyv 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 144 ----FTPIAE-TVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMESELLPLCRDNGIVVQVYS 218
Cdd:cd19122 133 ilkdLTENPEpTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 219 PLEqglltgtiTRDYVPggARANKVwfqRENmlKVIDMLEQwqplcaRYQCTIPTLALAWILKQSDLisILSGATAPEQV 298
Cdd:cd19122 213 PLG--------SQNQVP--STGERV---SEN--PTLNEVAE------KGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRI 269
|
330 340
....*....|....*....|....
gi 446646352 299 RENVAAlnINLSDADATLMREMAE 322
Cdd:cd19122 270 ESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
17-218 |
2.19e-10 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 60.51 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWAIgggpawngdlDQQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVETKCGIVwerkGSL 96
Cdd:cd19115 17 GFGLWKV----------NNDTCADQVYNAIKAGYRLFDGACDY--GN-EVEAGQGVARAIKEGIVKREDLFIV----SKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 97 FNKVGDRqlyknlspesirEEVEASLQR----LGIDYIDIYMTH-----------------WQS----VPPFFTPIAETV 151
Cdd:cd19115 80 WNTFHDG------------ERVEPICRKqladWGIDYFDLFLIHfpialkyvdpavryppgWFYdgkkVEFSNAPIQETW 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446646352 152 AVLNELKAEGKIRAIGAANVDADHIREYLQYGE-----LDIIQAKYsildrAMESELLPLCRDNGIVVQVYS 218
Cdd:cd19115 148 TAMEKLVDKGLARSIGVSNFSAQLLMDLLRYARirpatLQIEHHPY-----LTQPRLVKYAQKEGIAVTAYS 214
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
16-218 |
2.35e-10 |
|
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: 60.54 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWaigggpawngDLDQQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVETKCGIVwerkGS 95
Cdd:cd19113 14 VGFGCW----------KLDNATAADQIYQAIKAGYRLFDGAEDY--GN-EKEVGEGVNRAIDEGLVKREELFLT----SK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 96 LFNKVGDrqlyknlsPESIREEVEASLQRLGIDYIDIYMTHW----------QSVPPFF------------TPIAETVAV 153
Cdd:cd19113 77 LWNNFHD--------PKNVETALNKTLSDLKLDYVDLFLIHFpiafkfvpieEKYPPGFycgdgdnfvyedVPILDTWKA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 154 LNELKAEGKIRAIGAANVDADHIREYLQYGE-----LDIIQAKYsildrAMESELLPLCRDNGIVVQVYS 218
Cdd:cd19113 149 LEKLVDAGKIKSIGVSNFPGALILDLLRGATikpavLQIEHHPY-----LQQPKLIEYAQKAGITITAYS 213
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-220 |
1.84e-09 |
|
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: 57.81 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIGGGpawngdldqqicidTILEAHRCGINL----IDTAPGYNfgnSEVIVGQALKKLPREQVVVETKCGIVwe 91
Cdd:cd19107 7 LGLGTWKSPPG--------------QVTEAVKVAIDAgyrhIDCAYVYQ---NENEVGEAIQEKIKEQVVKREDLFIV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 92 rkGSLFNKVGDRQLyknlspesIREEVEASLQRLGIDYIDIYMTHW----QSVPPFF------------TPIAETVAVLN 155
Cdd:cd19107 68 --SKLWCTFHEKGL--------VKGACQKTLSDLKLDYLDLYLIHWptgfKPGKELFpldesgnvipsdTTFLDTWEAME 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446646352 156 ELKAEGKIRAIGAANVDADHIREYLQYGELdiiqaKYSILDRAMES-------ELLPLCRDNGIVVQVYSPL 220
Cdd:cd19107 138 ELVDEGLVKAIGVSNFNHLQIERILNKPGL-----KYKPAVNQIEChpyltqeKLIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
17-189 |
4.07e-09 |
|
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: 56.80 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 17 GLGTWAIgggpawngdlDQQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVETKCGIVwerkGSL 96
Cdd:cd19114 8 GFGTAKI----------KANETEEVIYNAIKVGYRLIDGALLY--GN-EAEVGRGIRKAIQEGLVKREDLFIV----TKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 97 FNKVGdrqlyknlSPESIREEVEASLQRLGIDYIDIYMTHW----------QSVPPFF------------TPIAETVAVL 154
Cdd:cd19114 71 WNNFH--------GKDHVREAFDRQLKDYGLDYIDLYLIHFpipaayvdpaENYPFLWkdkelkkfpleqSPMQECWREM 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 446646352 155 NELKAEGKIRAIGAANVDADHIREYLQYGEL--DIIQ 189
Cdd:cd19114 143 EKLVDAGLVRNIGIANFNVQLILDLLTYAKIkpAVLQ 179
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
16-326 |
3.90e-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: 47.87 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 16 MGLGTWAIgggpawngdlDQQICIDTILEAHRCGINL----IDTApgYNFGNsEVIVGQALK------KLPREQVVVetk 85
Cdd:cd19109 7 IGLGTYSE----------PKTTPKGACAEAVKVAIDTgyrhIDGA--YIYQN-EHEVGQAIRekiaegKVKREDIFY--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 86 CGIVWErkgslfnkvgdrqlyKNLSPESIREEVEASLQRLGIDYIDIYMTHwqsVPPFFTPIAE---------------- 149
Cdd:cd19109 71 CGKLWN---------------TCHPPELVRPTLERTLKVLQLDYVDLYIIE---MPMAFKPGDEiyprdengkwlyhktn 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 150 ---TVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELdiiqaKYSILDRAME-------SELLPLCRDNGIVVQVYSP 219
Cdd:cd19109 133 lcaTWEALEACKDAGLVKSIGVSNFNRRQLELILNKPGL-----KHKPVSNQVEchpyftqPKLLEFCQQHDIVIVAYSP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 220 LeqglltgtitrdyvpgGARANKVWFQrenmLKVIDMLEqwQPLCA----RYQCTIPTLALAWILKQSdlISILSGATAP 295
Cdd:cd19109 208 L----------------GTCRDPIWVN----VSSPPLLE--DPLLNsigkKYNKTAAQVVLRFNIQRG--VVVIPKSFNP 263
|
330 340 350
....*....|....*....|....*....|.
gi 446646352 296 EQVRENVAALNINLSDADatlMREMaEALER 326
Cdd:cd19109 264 ERIKENFQIFDFSLTEEE---MKDI-EALNK 290
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
1-315 |
6.34e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 44.18 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 1 MKKIPLgttditlsrMGLGTWAIGGGPAwngdldqqicIDTILEAHRCGINLIDTAPGYNfGNSEVIVGQALK----KLP 76
Cdd:cd19110 1 MEDIPA---------VGLGTWKASPGEV----------TEAVKVAIDAGYRHFDCAYLYH-NESEVGAGIREKikegVVR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 77 REQVVVETKCGIVWERKgSLfnkvgdrqlyknlspesIREEVEASLQRLGIDYIDIYMTHW----------------QSV 140
Cdd:cd19110 61 REDLFIVSKLWCTCHKK-SL-----------------VKTACTRSLKALKLNYLDLYLIHWpmgfkpgepdlpldrsGMV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 141 PPFFTPIAETVAVLNELKAEGKIRAIGAANVDADHIREYLQYGELDI--IQAKYSILDRAMESELLPLCRDNGIVVQVYS 218
Cdd:cd19110 123 IPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLRVkpVTNQIECHPYLTQKKLISFCQSRNVSVTAYR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 219 PLeqglltgtitrdyvpgGARANKVWFQRENMLKVIdmleqwqplcARYQCTIPTLALAWILKQSDLIsILSGATAPEQV 298
Cdd:cd19110 203 PL----------------GGSCEGVDLIDDPVIQRI----------AKKHGKSPAQILIRFQIQRNVI-VIPKSVTPSRI 255
|
330
....*....|....*..
gi 446646352 299 RENVAALNINLSDADAT 315
Cdd:cd19110 256 KENIQVFDFELTEHDMD 272
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
53-137 |
1.78e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 42.60 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446646352 53 IDTAPGYNfgnSEVIVGQALKK------LPREQVVVETKcgiVWerkgSLFnkvgdrqlyknLSPESIREEVEASLQRLG 126
Cdd:cd19108 44 IDSAYLYQ---NEEEVGQAIRSkiadgtVKREDIFYTSK---LW----CTF-----------HRPELVRPALEKSLKKLQ 102
|
90
....*....|.
gi 446646352 127 IDYIDIYMTHW 137
Cdd:cd19108 103 LDYVDLYLIHF 113
|
|
| |
