|
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: 520.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 3 KIPLGTTDITLSRMGLGTWAIGGGPaWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVV 82
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGP-WWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR-RDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 83 ETKCGIVWERKGSLFNKVGD-RQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKSEG 161
Cdd:cd19149 79 ATKCGLRWDREGGSFFFVRDgVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVE---TPIEETMEALEELKRQG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 162 KIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTIT--RDYVPGGAR 239
Cdd:cd19149 156 KIRAIGASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITpdREFDAGDAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 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 |
9.12e-136 |
|
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: 386.88 E-value: 9.12e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 10 DITLSRMGLGTWAIGGGpaWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVVETKCGIV 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGGT--WWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR-RDDVVIATKCGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WERKGSLFnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:cd19084 78 WDGGKGVT---------KDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPN---TPIEETAEALEKLKKEGKIRYIGVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV--PGGARANKVWFQR 247
Cdd:cd19084 146 NFSVEQLEEARKYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTfpPDDRRSRFPFFRG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3123121 248 ENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19084 226 ENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEE 291
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-326 |
1.81e-117 |
|
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: 341.39 E-value: 1.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGgpaWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGG---PWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGIVWerkgslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSE 160
Cdd:COG0667 78 VIATKVGRRM----------GPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHR---PDPDTPIEETLGALDELVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDADHIREYLQYGE----LDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRD-YVP 235
Cdd:COG0667 145 GKIRYIGVSNYSAEQLRRALAIAEglppIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGaTFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 236 GGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADat 315
Cdd:COG0667 225 EGDRAATNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAED-- 302
|
330
....*....|.
gi 3123121 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 |
1.37e-98 |
|
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: 292.57 E-value: 1.37e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 13 LSRMGLGTWAIGGGPAWnGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKCGivwer 92
Cdd:cd19085 1 VSRLGLGCWQFGGGYWW-GDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG-RRDDVVIATKVS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnkvgdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd19085 74 -------------PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHW---PSSDVPLEETMEALEKLKEEGKIRAIGVSNFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 173 ADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTG--TITRDYVPGGARANKVW-FQREN 249
Cdd:cd19085 138 PAQLEEALDAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGkfSSAEDFPPGDARTRLFRhFEPGA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3123121 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 |
1.26e-92 |
|
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: 277.63 E-value: 1.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 13 LSRMGLGTWAIGGG--PAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVVETKCGIVW 90
Cdd:cd19102 1 LTTIGLGTWAIGGGgwGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL-RDRPIVATKCGLLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 ERKGSLFNkvgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAAN 170
Cdd:cd19102 80 DEEGRIRR---------SLKPASIRAECEASLRRLGVDVIDLYQIHW---PDPDEPIEEAWGALAELKEEGKVRAIGVSN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 171 VDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV----PGGARANKVWFQ 246
Cdd:cd19102 148 FSVDQMKRCQAIHPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVaslpADDWRRRSPFFQ 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 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 |
5.22e-83 |
|
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: 253.38 E-value: 5.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 10 DITLSRMGLGTWAIGGgpAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL-PREQVVVETKCGI 88
Cdd:cd19148 1 DLPVSRIALGTWAIGG--WMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgKRDRVVIATKVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 89 VWERKGSLFnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGA 168
Cdd:cd19148 79 EWDEGGEVV---------RNSSPARIRKEVEDSLRRLQTDYIDLYQVHW---PDPLVPIEETAEALKELLDEGKIRAIGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 169 ANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV-PGG-ARANKVWFQ 246
Cdd:cd19148 147 SNFSPEQMETFRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKfEGDdLRRTDPKFQ 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3123121 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 |
2.95e-77 |
|
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: 238.86 E-value: 2.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 3 KIPLGTTDITLSRMGLGTWAIGGGPAWNgDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVV 82
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGGHNLYP-NLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 83 ETKCGIVWERKGSLFNKvgdrqlyknlSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGK 162
Cdd:cd19083 80 ATKGAHKFGGDGSVLNN----------SPEFLRSAVEKSLKRLNTDYIDLYYIHF---PDGETPKAEAVGALQELKDEGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 163 IRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV--PGGARA 240
Cdd:cd19083 147 IRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKfpDNDLRN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3123121 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 |
2.77e-75 |
|
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: 233.65 E-value: 2.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 2 KKIPLGTTDITLSRMGLG----TWAIGGgpawngdLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPR 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSAFYGP-------ADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 78 EQVVVETKCGIVWeRKGSLFNKVgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNEL 157
Cdd:cd19076 73 DEVVIATKFGIVR-DPGSGFRGV-------DGRPEYVRAACEASLKRLGTDVIDLYYQH--RVDPN-VPIEETVGAMAEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 158 KSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITR--DYVP 235
Cdd:cd19076 142 VEEGKVRYIGLSEASADTIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSpeDLPE 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 236 GGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19076 222 DDFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEE 299
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-304 |
4.82e-75 |
|
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: 230.44 E-value: 4.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 11 ITLSRMGLGTWAIGGGpaWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKCGIVW 90
Cdd:cd19086 1 LEVSEIGFGTWGLGGD--WWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG-RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 ErkgslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHwqsVPPF-FTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:cd19086 78 D---------GGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLH---NPPDeVLDNDELFEALEKLKQEGKIRAYGVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGtitrdyvpggarankvwfqren 249
Cdd:cd19086 146 VGDPEEALAALRRGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTG---------------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 3123121 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 |
2.37e-74 |
|
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: 230.66 E-value: 2.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGGpawNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP--REQVVVETKCGivwerK 93
Cdd:pfam00248 1 IGLGTWQLGGG---WGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPvkRDKVVIATKVP-----D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 94 GSLFNKVGdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVDA 173
Cdd:pfam00248 73 GDGPWPSG-------GSKENIRKSLEESLKRLGTDYIDLYYLHW---PDPDTPIEETWDALEELKKEGKIRAIGVSNFDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 174 DHIREYLQYGELDI--IQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGgaRANKVWFQRENML 251
Cdd:pfam00248 143 EQIEKALTKGKIPIvaVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKG--PGERRRLLKKGTP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3123121 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 |
3.37e-69 |
|
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: 216.33 E-value: 3.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 10 DITLSRMGLGTWAIGGGPAWNGDLDRQIcIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKcgiV 89
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDKKA-IEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTK---V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WERkgslfnkvgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:cd19072 77 SPD---------------HLKYDDVIKAAKESLKRLGTDYIDLYLIHW---PNPSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIRE---YLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRdyvpggarankvwfq 246
Cdd:cd19072 139 NFSLEELEEaqsYLKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS--------------- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3123121 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 |
8.49e-69 |
|
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: 214.30 E-value: 8.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGgpawngDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP-REQVVVETKCGIVWer 92
Cdd:cd06660 1 SRLGLGTMTFGG------DGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGnRDDVVIATKGGHPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd06660 73 --------GGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHR---DDPSTPVEETLEALNELVREGKIRYIGVSNWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 173 ADHIREYLQYG------ELDIIQAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLltgtitrdyvpggarankvwf 245
Cdd:cd06660 142 AERLAEALAYAkahglpGFAAVQPQYSLLDRsPMEEELLDWAEENGLPLLAYSPLARGP--------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 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 |
1.90e-66 |
|
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: 210.53 E-value: 1.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 13 LSRMGLGTWA-IGGGpawNGDLDRQICIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCgivwe 91
Cdd:cd19074 4 VSELSLGTWLtFGGQ---VDDEDAKACVRKAYDL---GINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 92 rkgslFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKSEGKIRAIGAANV 171
Cdd:cd19074 73 -----FWPTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPE---TPLEETVRAMDDLIRQGKILYWGTSEW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 172 DADHIREYL----QYGELDII--QAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPG-GARA---- 240
Cdd:cd19074 145 SAEQIAEAHdlarQFGLIPPVveQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPsRSRAtded 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 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 |
3.78e-66 |
|
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: 210.55 E-value: 3.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGGPAWNG--------DLDRQIciDTILEAhrcGINLIDTAPGYNFGNSEVIVGQAL 72
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFGawggvdqeEADRLV--DIALDA---GINFFDTADVYSEGESEEILGKAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 73 KKLpREQVVVETKcgiVWERKGSLFNKVGdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTH-WQSVppffTPIAETV 151
Cdd:cd19091 76 KGR-RDDVLIATK---VRGRMGEGPNDVG-------LSRHHIIRAVEASLKRLGTDYIDLYQLHgFDAL----TPLEETL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 152 AVLNELKSEGKIRAIGAANVDADH------IREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLL 225
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQimkalgISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 226 TGTITRDY-VPGGARANKVWFQ-----RENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVR 299
Cdd:cd19091 221 SGKYRRGQpAPEGSRLRRTGFDfppvdRERGYDVVDALRE---IAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLE 297
|
330
....*....|....
gi 3123121 300 ENVAALNINLSDAD 313
Cdd:cd19091 298 DNLGAAGLSLTPEE 311
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-313 |
2.81e-64 |
|
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: 205.51 E-value: 2.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 2 KKIPLGTTDITLSRMGLGTWAIG--GGPAWNGDLD--RQIcIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKL-P 76
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGdpKWRPWVLDEEesRPI-IKRALDL---GINFFDTANVYSGGASEEILGRALKEFaP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 77 REQVVVETKCgivwerkgslFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvppFF--TPIAETVAVL 154
Cdd:cd19079 77 RDEVVIATKV----------YFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHR-----WDyeTPIEETLEAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 155 NELKSEGKIRAIGAANVDADHIREYLQYGELD------IIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLtgt 228
Cdd:cd19079 142 HDVVKSGKVRYIGASSMYAWQFAKALHLAEKNgwtkfvSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRL--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 229 iTRDYVPGGARAN--------KVWFQRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRE 300
Cdd:cd19079 219 -ARPWGDTTERRRsttdtaklKYDYFTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLED 294
|
330
....*....|...
gi 3123121 301 NVAALNINLSDAD 313
Cdd:cd19079 295 AVAALDIKLSEEE 307
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-313 |
4.17e-63 |
|
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: 202.44 E-value: 4.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 5 PLGTTDITLSRMGLGTWAIGggpaWNGDLDRQICI-DTILEAhrcGINLIDTA-------PGYNFGNSEVIVGQALKK-L 75
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFG----WTADEETSFALlDAFVDA---GGNFIDTAdvysawvPGNAGGESETIIGRWLKSrG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 76 PREQVVVETKCGivWERKGslfNKVGdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLN 155
Cdd:cd19081 74 KRDRVVIATKVG--FPMGP---NGPG-------LSRKHIRRAVEASLRRLQTDYIDLYQAHW---DDPATPLEETLGALN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 156 ELKSEGKIRAIGAANVDADHIREYLQ------YGELDIIQAKYSILDRAM-ENELLPLCRDNGIVVQVYSPLEQGLLTGT 228
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALElsrqhgLPRYVSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGFLTGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 229 ITRDY-VPGGARANKVWFQREN--MLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL 305
Cdd:cd19081 219 YRSEAdLPGSTRRGEAAKRYLNerGLRILDALDE---VAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAA 295
|
....*...
gi 3123121 306 NINLSDAD 313
Cdd:cd19081 296 GLRLTDEE 303
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-313 |
5.87e-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: 5.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 13 LSRMGLGTWAIGGGPAWNG-DLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP-REQVVVETKCGIVW 90
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWGYgEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGdRDEVVIATKFAPLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 ERkgslfnkvgdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTHWqsVPPFFTPIAETVAVLNELKSEGKIRAIGAAN 170
Cdd:cd19093 82 WR----------------LTRRSVVKALKASLERLGLDSIDLYQLHW--PGPWYSQIEALMDGLADAVEEGLVRAVGVSN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 171 VDADHIREYLQY-GELDI----IQAKYSILDRAME-NELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANKvw 244
Cdd:cd19093 144 YSADQLRRAHKAlKERGVplasNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRL-- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3123121 245 FQRENMLKV---IDMLEQwqpLCARYQCTIPTLALAWILKQSDLisILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19093 222 FGRKNLEKVqplLDALEE---IAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEE 288
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-324 |
1.32e-59 |
|
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: 193.22 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 10 DITLSRMGLGTWAI--GGGPAwngdLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKCG 87
Cdd:cd19078 1 GLEVSAIGLGCMGMshGYGPP----PDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP-FRDQVVIATKFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 88 IVwerkgslFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELKSEGKIRAIG 167
Cdd:cd19078 76 FK-------IDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQH--RVDPN-VPIEEVAGTMKELIKEGKIRHWG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 168 AANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRD--YVPGGARANKVWF 245
Cdd:cd19078 146 LSEAGVETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENtkFDEGDDRASLPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 246 QRENM---LKVIDMLEQWqplCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADatlMREMAE 322
Cdd:cd19078 226 TPEALeanQALVDLLKEF---AEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEE---LREIED 299
|
..
gi 3123121 323 AL 324
Cdd:cd19078 300 AL 301
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-312 |
3.25e-59 |
|
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: 191.23 E-value: 3.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGGPawnGDLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKLPREQVVVETKCGivwerk 93
Cdd:cd19090 1 SALGLGTAGLGGVF---GGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPREPLVLSTKVG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 94 gslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPIAE--TVAVLNELKSEGKIRAIGAANV 171
Cdd:cd19090 70 -------RLPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggALEALLELKEEGLIKHIGLGGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 172 DADHIREYLQYGELDII--QAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGtitRDyvPGGARANKVWFQREN 249
Cdd:cd19090 143 PPDLLRRAIETGDFDVVltANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAG---RP--PERVRYTYRWLSPEL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3123121 250 MLKVIDMLEqwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19090 218 LDRAKRLYE----LCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-313 |
1.21e-57 |
|
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: 188.16 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGgpawNGDLD--RQIcIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLpRE 78
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGG----RTDEEtsFAI-MDRALDA---GINFFDTADVYGGGRSEEIIGRWIAGR-RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 79 QVVVETKCgivwerkgslFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIY-MTHWQSvppfFTPIAETVAVLNEL 157
Cdd:cd19087 72 DIVLATKV----------FGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYqMHHFDR----DTPLEETLRALDDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 158 KSEGKIRAIGAAN------VDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITR 231
Cdd:cd19087 138 VRQGKIRYIGVSNfaawqiAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 232 DYVP--GGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINL 309
Cdd:cd19087 218 GKRPesGRLVERARYQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITL 297
|
....
gi 3123121 310 SDAD 313
Cdd:cd19087 298 TPEL 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-326 |
1.54e-54 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 178.71 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 11 ITLSRMGLGTWAIGGgpawngdldrQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgi 88
Cdd:COG0656 3 VEIPALGLGTWQLPG----------EEAAAAVRTALEAGYRHIDTAAMY--GN-EEGVGEAIAAsgVPREELFVTTK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 89 VWERkgslfnkvgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKSEGKIRAIGA 168
Cdd:COG0656 67 VWND---------------NHGYDDTLAAFEESLERLGLDYLDLYLIHW----PGPGPYVETWRALEELYEEGLIRAIGV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 169 ANVDADHIREYLQYGE--LDIIQAKYSILDRamENELLPLCRDNGIVVQVYSPLEQG-LLTG-TITRdyvpggarankvw 244
Cdd:COG0656 128 SNFDPEHLEELLAETGvkPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGkLLDDpVLAE------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 245 fqrenmlkvidmleqwqpLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDADatlMREMAeAL 324
Cdd:COG0656 193 ------------------IAEKHGKTPAQVVLRWHL-QRGVVVI-PKSVTPERIRENLDAFDFELSDED---MAAID-AL 248
|
..
gi 3123121 325 ER 326
Cdd:COG0656 249 DR 250
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-325 |
2.01e-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: 180.33 E-value: 2.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 6 LGTTDITLSRMGLGTWAI--GGGPAwNGDLDRQICIDTILEAhrcGINLIDTAPGYnfGNSEVIVGQALKKLP--REQVV 81
Cdd:cd19144 6 LGRNGPSVPALGFGAMGLsaFYGPP-KPDEERFAVLDAAFEL---GCTFWDTADIY--GDSEELIGRWFKQNPgkREKIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 82 VETKCGIVWERKGSLFNKVGdrqlyknlSPESIREEVAASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELKSEG 161
Cdd:cd19144 80 LATKFGIEKNVETGEYSVDG--------SPEYVKKACETSLKRLGVDYIDLYYQH--RVDGK-TPIEKTVAAMAELVQEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 162 KIRAIGAANVDADHIREYLQYGELDIIQAKYS--ILD-RAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITR--DYVPG 236
Cdd:cd19144 149 KIKHIGLSECSAETLRRAHAVHPIAAVQIEYSpfSLDiERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSpdDFEEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 237 GARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADATL 316
Cdd:cd19144 229 DFRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKE 308
|
....*....
gi 3123121 317 MREMAEALE 325
Cdd:cd19144 309 IREIAEEAE 317
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-305 |
3.68e-54 |
|
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: 178.90 E-value: 3.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGGPawnGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVF---GPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGivweRKGSLFNKVGDrqlyknLSPESIREEVAASLQRLGIDYIDIYMTHwqsvPPFFTP-----IAETVAVLN 155
Cdd:cd19163 78 YLATKVG----RYGLDPDKMFD------FSAERITKSVEESLKRLGLDYIDIIQVH----DIEFAPsldqiLNETLPALQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 156 ELKSEGKIRAIGAANVDADHIREYLQ--YGELDIIQ--AKYSILDRAMEnELLPLCRDNGIVVQVYSPLEQGLLTGTITR 231
Cdd:cd19163 144 KLKEEGKVRFIGITGYPLDVLKEVLErsPVKIDTVLsyCHYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLTERGPP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3123121 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 |
5.15e-54 |
|
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: 177.04 E-value: 5.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGGPawnGDLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKLPREQVVVETKCGIVWErk 93
Cdd:cd19095 1 SVLGLGTSGIGRVW---GVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLFIATKVGTHGE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 94 gslfnkvgDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKSEGKIRAIGaANVDA 173
Cdd:cd19095 74 --------GGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDD---ELTGEVLETLEDLKAAGKVRYIG-VSGDG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 174 DHIREYLQYGELDIIQAKYSILDRAMEnELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANKVWFQRenmlkv 253
Cdd:cd19095 142 EELEAAIASGVFDVVQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAE------ 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 3123121 254 idmLEQWQPlcaryqctiPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19095 215 ---IGGATW---------AQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-313 |
6.29e-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: 174.74 E-value: 6.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 9 TDITLSRMGLGTWAIGGGPAwngdlDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKlPREQVVVETKcgi 88
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPA-----KRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG-RRDKVFLVSK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 89 VWERkgslfnkvgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVppffTPIAETVAVLNELKSEGKIRAIGA 168
Cdd:cd19138 78 VLPS---------------NASRQGTVRACERSLRRLGTDYLDLYLLHWRGG----VPLAETVAAMEELKKEGKIRAWGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 169 ANVDADHIREYLQY---GELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTitrdyvpgGARANKVwf 245
Cdd:cd19138 139 SNFDTDDMEELWAVpggGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRR--------GLLENPT-- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 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 3123121 13 LSRMGLGTWAIGGGPAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPrEQVVVETKCGIVwer 92
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP-DDVVIATKGGLV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd19088 77 ------RTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHR---IDPKVPFEEQLGALAELQDEGLIRHIGLSNVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 173 ADHIREYLQYGELDIIQAKYSILDRAMEnELLPLCRDNGIVVQVYSPLEQGLLTGtitrdyvPGGARANkvwfqrenmlk 252
Cdd:cd19088 148 VAQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQ-------PGGLLAE----------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 253 vidmleqwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLS 310
Cdd:cd19088 209 ----------VAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
6-307 |
1.23e-50 |
|
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: 170.47 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 6 LGTTDITLSRMGLGTWAigggpAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL--PREQVVVE 83
Cdd:cd19143 6 LGRSGLKVSALSFGSWV-----TFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELgwPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 84 TKcgIVWERKGSLFNKVGdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELKSEGKI 163
Cdd:cd19143 81 TK--IFWGGGGPPPNDRG-------LSRKHIVEGTKASLKRLQLDYVDLVFCH---RPDPATPIEETVRAMNDLIDQGKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDADHIREYLQYGE-LDII-----QAKYSILDRA-MENELLPLCRDNGIVVQVYSPLEQGLLTGTITrDYVPG 236
Cdd:cd19143 149 FYWGTSEWSAQQIEEAHEIADrLGLIppvmeQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYN-NGIPE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3123121 237 GARA---NKVW---FQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19143 228 GSRLalpGYEWlkdRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEV 304
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-313 |
1.70e-50 |
|
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: 169.54 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 3 KIPLGTTDITLSRMGLGTWAIGGGpaWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVV 82
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGD--YGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 83 ETKCGIVwERKGSLFNKVGDrqlyknlsPESIREEVAASLQRLGIDYIDIYMTHW--QSVppfftPIAETVAVLNELKSE 160
Cdd:cd19145 80 ATKFGIH-EIGGSGVEVRGD--------PAYVRAACEASLKRLDVDYIDLYYQHRidTTV-----PIEITMGELKKLVEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTG--TITRDYVPGGA 238
Cdd:cd19145 146 GKIKYIGLSEASADTIRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGkaKLEELLENSDV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3123121 239 RANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19145 226 RKSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKED 300
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-312 |
2.85e-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: 169.32 E-value: 2.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 6 LGTTDITLSRMGLGTWAIGGGPAWNGDLD--RQIcIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLpREQVVVE 83
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWGWGADREeaRAM-FDAYVEA---GGNFIDTANNYTNGTSERLLGEFIAGN-RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 84 TKCGivWERKGSLFNKVGDRQlyKNLspesiREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKI 163
Cdd:cd19080 78 TKYT--MNRRPGDPNAGGNHR--KNL-----RRSVEASLRRLQTDYIDLLYVHA---WDFTTPVEEVMRALDDLVRAGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDA------DHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGG 237
Cdd:cd19080 146 LYVGISDTPAwvvaraNTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3123121 238 ARANKVWF----QRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19080 226 GEAKGVTVgfgkLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPE 301
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-312 |
1.70e-49 |
|
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: 166.77 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGgPAWNGDLDRQICIDTileAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCGIVWERK 93
Cdd:cd19162 1 PRLGLGAASLGN-LARAGEDEAAATLDA---AWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVGRLLEPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 94 GSLFNKVGDRQLykNLSPESIREEVAASLQRLGIDYIDIYMTHwQSVPPFFTPIAETVAVLNELKSEGKIRAIGAANVDA 173
Cdd:cd19162 77 AAGRPAGADRRF--DFSADGIRRSIEASLERLGLDRLDLVFLH-DPDRHLLQALTDAFPALEELRAEGVVGAIGVGVTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 174 DHIREYLQYGELD--IIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTgtitrdyvpGGARANKVWFQRENML 251
Cdd:cd19162 154 AALLRAARRADVDvvMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILA---------TDDPAGDRYDYRPATP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 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 |
1.74e-48 |
|
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: 164.27 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGGPAWNGDLDRqiCIDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLPReqVVVETKCGIVWErkgs 95
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAE--LLDAFLER---GHTEIDTARVYPDGTSEELLGELGLGERG--FKIDTKANPGVG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 96 lfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELKSEGKIRAIGAANVDADH 175
Cdd:cd19075 74 -----------GGLSPENVRKQLETSLKRLKVDKVDVFYLH---APDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 176 IREYLQYGELD------IIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITR-DYVPGGAR--------- 239
Cdd:cd19075 140 VAEIVEICKENgwvlptVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYsEDKAGGGRfdpnnalgk 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 240 ANKVWFQRENMLkviDMLEQWQPLCARYQCTIPTLALAWILKQSDLIS-----ILSGATAPEQVRENVAAL 305
Cdd:cd19075 220 LYRDRYWKPSYF---EALEKVEEAAEKEGISLAEAALRWLYHHSALDGekgdgVILGASSLEQLEENLAAL 287
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-310 |
1.87e-48 |
|
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: 163.88 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 8 TTDITLSRMGLGTWAIGGgpaWNGDLDRqiCIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP--REQVVVETK 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAD---WGESAEE--LLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPglREKIEIQTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 86 CGIVWErkgslFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHwqsVP-PFFTPiAETVAVLNELKSEGKIR 164
Cdd:cd19092 76 CGIRLG-----DDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLH---RPdPLMDP-EEVAEAFDELVKSGKVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 165 AIGAANVDADHIrEYLQ-YGELDII--QAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVpggaRA 240
Cdd:cd19092 147 YFGVSNFTPSQI-ELLQsYLDQPLVtnQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQ----RL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 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 ... |
49-322 |
3.11e-47 |
|
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: 161.96 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 49 GINLIDTAPGYNF-------GNSEVIVGQALKKLP-REQVVVETK-CG----IVWERKGSLfnkvgdrqlykNLSPESIR 115
Cdd:cd19094 31 GVNFIDTAEMYPVppspetqGRTEEIIGSWLKKKGnRDKVVLATKvAGpgegITWPRGGGT-----------RLDRENIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 116 EEVAASLQRLGIDYIDIYMTHW--QSVPPF-------------FTPIAETVAVLNELKSEGKIRAIGAANVDADHIREYL 180
Cdd:cd19094 100 EAVEGSLKRLGTDYIDLYQLHWpdRYTPLFgggyytepseeedSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 181 QYGELDI------IQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTIT-RDYVPGGARANKV--WFQRENML 251
Cdd:cd19094 180 ELAEQLGlprivsIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLdGAARPEGGRLNLFpgYMARYRSP 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 252 KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAdatLMREMAE 322
Cdd:cd19094 260 QALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVPLSDE---LLAEIDA 327
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-313 |
2.56e-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: 158.94 E-value: 2.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 11 ITLSRMGLG----TWaigggpaWNGDLDRQICIDTILEAHRCGINLIDTA----PGYNFGNSEVIvGQALKKLP--REQV 80
Cdd:cd19077 3 KLVGPIGLGlmglTW-------RPNPTPDEEAFETMKAALDAGSNLWNGGefygPPDPHANLKLL-ARFFRKYPeyADKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGIvwerKGSLFNKVGdrqlyknlSPESIREEVAASLQRLG-IDYIDIYMThwQSVPPFfTPIAETVAVLNELKS 159
Cdd:cd19077 75 VLSVKGGL----DPDTLRPDG--------SPEAVRKSIENILRALGgTKKIDIFEP--ARVDPN-VPIEETIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 160 EGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAME-NELLPLCRDNGIVVQVYSPLEQGLLTGTI-TRDYVPGG 237
Cdd:cd19077 140 EGKIRGIGLSEVSAETIRRAHAVHPIAAVEVEYSLFSREIEeNGVLETCAELGIPIIAYSPLGRGLLTGRIkSLADIPEG 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 238 A-RANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQS-DLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19077 220 DfRRHLDRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSgPKIIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-305 |
1.70e-45 |
|
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: 155.05 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTwaiGGGPAWNgdldrqicIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG---GGLPRES--------PELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKcgIVWERKGSlfnkvgdrqlyknlSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKSE 160
Cdd:cd19105 70 FLATK--ASPRLDKK--------------DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALEKLKKE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDADH--IREYLQYGELDIIQAKYSIL-DRAMENELLPLCRDNGIvvqvyspleqglltGTITRDYVPGG 237
Cdd:cd19105 134 GKVRFIGFSTHDNMAevLQAAIESGWFDVIMVAYNFLnQPAELEEALAAAAEKGI--------------GVVAMKTLAGG 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 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 |
1.78e-45 |
|
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: 155.42 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 13 LSRMGLGTWAIGGGPAWNGDLDRQIcIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKcgiVWer 92
Cdd:cd19137 4 IPALGLGTWGIGGFLTPDYSRDEEM-VELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTK---VW-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnkvgdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd19137 78 -------------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHW---PNPNIPLEETLSAMAEGVRQGLIRYIGVSNFN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 173 ADHIREYLQYGELDII--QAKYSILDRA-MENELLPLCRDNGIVVQVYSPLEQGLltgtitrdyvpggarankvwfqren 249
Cdd:cd19137 142 RRLLEEAISKSQTPIVcnQVKYNLEDRDpERDGLLEYCQKNGITVVAYSPLRRGL------------------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 250 mLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISIlSGATAPEQVRENVAALNINLSDADATLM 317
Cdd:cd19137 197 -EKTNRTLEE---IAKNYGKTIAQIALAWLIQKPNVVAI-PKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-308 |
3.57e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 149.60 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIG---GGPAWNGDLDRQIcIDTILE-AHRCGINLIDTAPGYnfGNSEVIVGQALKKLPREQVVveTKCGIV 89
Cdd:cd19097 1 SKLALGTAQFGldyGIANKSGKPSEKE-AKKILEyALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFKII--TKLPPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WERKGSLfnkvgdrqlyknlsPESIREEVAASLQRLGIDYIDIYMTHWQSVppFFTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:cd19097 76 KEDKKED--------------EAAIEASVEASLKRLKVDSLDGLLLHNPDD--LLKHGGKLVEALLELKKEGLIRKIGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIREYLQYGELDIIQAKYSILDRAME-NELLPLCRDNGIVVQVYSPLEQGLLtgTITRDYVPggarankvwfqrE 248
Cdd:cd19097 140 VYSPEELEKALESFKIDIIQLPFNILDQRFLkSGLLAKLKKKGIEIHARSVFLQGLL--LMEPDKLP------------A 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 249 NMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNIN 308
Cdd:cd19097 206 KFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKP 265
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-326 |
4.67e-42 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 149.20 E-value: 4.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGgpawngdLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKlPREQV 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPR-------KDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG-PRDKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGiVWERkgslfnkvgdrqlyknlSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFF-TPIAET--VAVLNEL 157
Cdd:COG1453 71 ILATKLP-PWVR-----------------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLeKVLKPGgaLEALEKA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 158 KSEGKIRAIGAAN-VDADHIREYLQYGELDIIQAKYSILDR--AMENELLPLCRDNGIVVQVYSPLEQGLLTgtitrdyv 234
Cdd:COG1453 133 KAEGKIRHIGFSThGSLEVIKEAIDTGDFDFVQLQYNYLDQdnQAGEEALEAAAEKGIGVIIMKPLKGGRLA-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 235 pggarankvwfqreNMLKVIDMLeqwqpLCARYqcTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN--INLSDA 312
Cdd:COG1453 205 --------------NPPEKLVEL-----LCPPL--SPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEE 263
|
330
....*....|....
gi 3123121 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 |
3.60e-41 |
|
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: 143.86 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 29 WNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCGiVWERKgslfnkvgdrqlykn 108
Cdd:cd19096 14 DDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLP-PWSVK--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 109 lSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPIAE--TVAVLNELKSEGKIRAIG-AANVDADHIREYLQYGEL 185
Cdd:cd19096 78 -SAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKARKggLLEFLEKAKKEGLIRHIGfSFHDSPELLKEILDSYDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 186 DIIQAKYSILDRAMEN--ELLPLCRDNGIVVQVYSPLEQGLLTgtitrdYVPGGARAnkvwfqrenmlkvidmleqwqpL 263
Cdd:cd19096 157 DFVQLQYNYLDQENQAgrPGIEYAAKKGMGVIIMEPLKGGGLA------NNPPEALA----------------------I 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 3123121 264 CARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19096 209 LCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-312 |
5.60e-41 |
|
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: 145.06 E-value: 5.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGGpaWNGDLDRQIcIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCG--IVWE 91
Cdd:cd19152 1 PKLGFGTAPLGNL--YEAVSDEEA-KATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVGrlLVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 92 RKGSlfnkVGDRQLYKNLSP---------ESIREEVAASLQRLGIDYIDIYMTH--------WQSVPPFFTPIAETVAVL 154
Cdd:cd19152 78 QEVE----PTFEPGFWNPLPfdavfdysyDGILRSIEDSLQRLGLSRIDLLSIHdpdedlagAESDEHFAQAIKGAFRAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 155 NELKSEGKIRAIGAANVDADHIREYLQYGELDIIQA--KYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRD 232
Cdd:cd19152 154 EELREEGVIKAIGLGVNDWEVILRILEEADLDWVMLagRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 233 YVPGGARANKVWFQRenmlkvidmlEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDA 312
Cdd:cd19152 234 YYEYGPAPPELIARR----------DRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-303 |
6.69e-41 |
|
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: 142.62 E-value: 6.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 3 KIPLGTTDITLSRMGLGTWAIGggpawngDLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKlPREQVVV 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLG-------RLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG-RRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 83 ETKcgiVWERkgslfnkvgdrqlyknlSPESIREEVAASLQRLGIDYIDIYMTHWQSVPP-FFTPIAE--TVAVLNELKS 159
Cdd:cd19100 71 ATK---TGAR-----------------DYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEdLDQVFGPggALEALLEAKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 160 EGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAM---ENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDyvpg 236
Cdd:cd19100 131 EGKIRFIGISGHSPEVLLRALETGEFDVVLFPINPAGDHIdsfREELLPLAREKGVGVIAMKVLAGGRLLSGDPLD---- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3123121 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 |
6.85e-41 |
|
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: 142.80 E-value: 6.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWaigggpawngDLDRQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWerkg 94
Cdd:cd19073 5 GLGTW----------QLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAEsgVPREDLFITTK---VW---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 95 slfnkvgdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVDAD 174
Cdd:cd19073 65 -----------RDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHW---PNPTVPLEETLGALKELKEAGKVKSIGVSNFTIE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 175 HIREYLQYGELDII--QAKYSI-LDRAmenELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfqrenml 251
Cdd:cd19073 131 LLEEALDISPLPIAvnQVEFHPfLYQA---ELLEYCRENDIVITAYSPLARG---------------------------- 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3123121 252 KVIDmLEQWQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19073 180 EVLR-DPVIQEIAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
5-325 |
3.33e-40 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 142.99 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 5 PLGTTDITLSRMGLGtwaigGGPAWN--GDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL--PREQV 80
Cdd:PLN02587 3 ELGSTGLKVSSVGFG-----ASPLGSvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgiPREKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGivweRKGSLFNkvgdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKSE 160
Cdd:PLN02587 78 VVSTKCG----RYGEGFD----------FSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIPALQKLKES 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDADHIREYLQY---GELDII--QAKYSILDRAMEnELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVP 235
Cdd:PLN02587 144 GKVRFIGITGLPLAIFTYVLDRvppGTVDVIlsYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTENGPPEWHP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 236 GGARankvwfqrenmLKVIdmLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENV-AALNINLSDADA 314
Cdd:PLN02587 223 APPE-----------LKSA--CAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVaAATELETSGIDE 289
|
330
....*....|.
gi 3123121 315 TLMREMAEALE 325
Cdd:PLN02587 290 ELLSEVEAILA 300
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
5-313 |
4.10e-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: 142.78 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 5 PLGTTDITLSRMGLGTWAiggGPAWNGDLDRQICIdtILEAHRCGINLIDTAPGYN--FGNSEVIVGQALK---KLPREQ 79
Cdd:cd19089 3 RCGRSGLHLPAISLGLWH---NFGDYTSPEEAREL--LRTAFDLGITHFDLANNYGppPGSAEENFGRILKrdlRPYRDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 80 VVVETKCGI-VWerkGSLFNKVGDRQlyknlspeSIREEVAASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELK 158
Cdd:cd19089 78 LVISTKAGYgMW---PGPYGDGGSRK--------YLLASLDQSLKRMGLDYVDIFYHH--RYDPD-TPLEETMTALADAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 159 SEGKIRAIGAANVDADHIREYLQY-GELD----IIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDY 233
Cdd:cd19089 144 RSGKALYVGISNYPGAKARRAIALlRELGvpliIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 234 VPGGARANKVWFQRENML--KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL-NINLS 310
Cdd:cd19089 224 PPDSRRAAESKFLTEEALtpEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkNLDFS 303
|
...
gi 3123121 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 |
1.16e-39 |
|
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: 139.92 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 15 RMGLGTWAIGGGPawngdldrqiCIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiVWer 92
Cdd:cd19071 3 LIGLGTYKLKPEE----------TAEAVLAALEAGYRHIDTAAAY--GN-EAEVGEAIREsgVPREELFITTK---LW-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnkvgdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHW---QSVPPFFTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:cd19071 65 -------------PTDHGYERVREALEESLKDLGLDYLDLYLIHWpvpGKEGGSKEARLETWRALEELVDEGLVRSIGVS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIREYLQYGEL--DIIQAKYSILDRamENELLPLCRDNGIVVQVYSPLeqglltgtitrdyvpggARANKVWFQR 247
Cdd:cd19071 132 NFNVEHLEELLAAARIkpAVNQIELHPYLQ--QKELVEFCKEHGIVVQAYSPL-----------------GRGRRPLLDD 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3123121 248 ENMLKvidmleqwqpLCARYQCTIPTLALAWILkQSDlISILSGATAPEQVRENVAALNINLSDADatlMREMA 321
Cdd:cd19071 193 PVLKE----------IAKKYGKTPAQVLLRWAL-QRG-VVVIPKSSNPERIKENLDVFDFELSEED---MAAID 251
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-306 |
2.38e-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: 140.16 E-value: 2.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGGPawNGDLDRQIcIDTILEAhrcGINLIDTAPGYNF-------GNSEVIVGQALK-KLPREQVVVETK 85
Cdd:cd19752 1 SELCLGTMYFGTRT--DEETSFAI-LDRYVAA---GGNFLDTANNYAFwteggvgGESERLIGRWLKdRGNRDDVVIATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 86 CGivwerkGSLFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLNELKSEGKIRA 165
Cdd:cd19752 75 VG------AGPRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAH---VDDRDTPLEETLEAFNELVKAGKVRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 166 IGAANVDADHIREYLQ------YGELDIIQAKYSIL----------DRAMENELLPLCRDNGIVVQV-YSPleqgLLTGT 228
Cdd:cd19752 146 IGASNFAAWRLERARQiarqqgWAEFSAIQQRHSYLrprpgadfgvQRIVTDELLDYASSRPDLTLLaYSP----LLSGA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 229 ITRDyvpggARANKVWFQRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19752 222 YTRP-----DRPLPEQYDGPDSDARLAVLEE---VAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-306 |
1.76e-38 |
|
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: 138.07 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGgpawngDLDRQ---ICIDTILEAhrcGINLIDTAPGY----NFGNSEVIVGQALKKLP-REQVVVETK 85
Cdd:cd19082 1 SRIVLGTADFGT------RIDEEeafALLDAFVEL---GGNFIDTARVYgdwvERGASERVIGEWLKSRGnRDKVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 86 CGIvwerkgslfnKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHW--QSVppfftPIAETVAVLNELKSEGKI 163
Cdd:cd19082 72 GGH----------PDLEDMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRddPSV-----PVGEIVDTLNELVRAGKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDADHIREYLQYGE------LDIIQAKYSILDRAMENELLPLC-----------RDNGIVVQVYSPLEQGLLT 226
Cdd:cd19082 137 RAFGASNWSTERIAEANAYAKahglpgFAASSPQWSLARPNEPPWPGPTLvamdeemrawhEENQLPVFAYSSQARGFFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 227 GTITRDYVPGGARAnKVWFQRENmLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19082 217 KRAAGGAEDDSELR-RVYYSEEN-FERLERAKE---LAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-304 |
4.79e-38 |
|
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: 137.40 E-value: 4.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 2 KKIPLGTTDITLSRMGLGTWAIGGgpAWnGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPrEQVV 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGG--LM-GRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLP-AGPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 82 VETKCGIVWERKGSLfnkvgdrqlyknlsPESIREEVAASLQRLGIDYIDIYMTHWQ-----SVPPFFTPIAETVAVLN- 155
Cdd:cd19104 77 ITTKVRLDPDDLGDI--------------GGQIERSVEKSLKRLKRDSVDLLQLHNRigderDKPVGGTLSTTDVLGLGg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 156 ------ELKSEGKIRAIGAANVD-ADHIREYLQYGELDIIQAKYSILD--------RAME----NELLPLCRDNGIVVQV 216
Cdd:cd19104 143 vadafeRLRSEGKIRFIGITGLGnPPAIRELLDSGKFDAVQVYYNLLNpsaaearpRGWSaqdyGGIIDAAAEHGVGVMG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 217 YSPLEQGLLTGTITRDYVPGGARANKVWFQRENMLKVIDMLEQWQPlcaryqcTIPTLALAWILKQSDLISILSGATAPE 296
Cdd:cd19104 223 IRVLAAGALTTSLDRGREAPPTSDSDVAIDFRRAAAFRALAREWGE-------TLAQLAHRFALSNPGVSTVLVGVKNRE 295
|
....*...
gi 3123121 297 QVRENVAA 304
Cdd:cd19104 296 ELEEAVAA 303
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-307 |
2.12e-37 |
|
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: 135.53 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGGgpaWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCG--IVWE 91
Cdd:cd19161 1 SELGLGTAGLGN---LYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVGrlLKPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 92 RKGSLFNKVGdrqLYKNL--------SPESIREEVAASLQRLGIDYIDIYMTH-----WQSVPPFFTPIAETVA----VL 154
Cdd:cd19161 78 REGSVPDPNG---FVDPLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGDRKERHHFAQLMSggfkAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 155 NELKSEGKIRAIGAANVDADHIREYLQYGELDI--IQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLL-TGTITR 231
Cdd:cd19161 155 EELKKAGVIKAFGLGVNEVQICLEALDEADLDCflLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILaTGTKSG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3123121 232 ---DYVPGGArankvwfqrenmlKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19161 235 akfNYGDAPA-------------EIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQT 300
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-313 |
4.45e-37 |
|
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: 133.15 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 15 RMGLGTWAIGGGPawngdldrqiCIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWEr 92
Cdd:cd19140 10 ALGLGTYPLTGEE----------CTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAAsgVPRDELFLTTK---VWP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd19140 73 --------------DNYSPDDFLASVEESLRKLRTDYVDLLLLHW---PNKDVPLAETLGALNEAQEAGLARHIGVSNFT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 173 ADHIREYLQYGELDI--IQAKYSI-LDramENELLPLCRDNGIVVQVYSPLEQglltGTITRDYVpggarankvwFQRen 249
Cdd:cd19140 136 VALLREAVELSEAPLftNQVEYHPyLD---QRKLLDAAREHGIALTAYSPLAR----GEVLKDPV----------LQE-- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3123121 250 mlkvidmleqwqpLCARYQCTIPTLALAWILKQSDLISIlSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19140 197 -------------IGRKHGKTPAQVALRWLLQQEGVAAI-PKATNPERLEENLDIFDFTLSDEE 246
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-303 |
2.31e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 127.82 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 12 TLSRMGLGTWAIGggpawNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL------PREQVVVETK 85
Cdd:cd19099 2 TLSSLGLGTYRGD-----SDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekggiKRDEVVIVTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 86 CGIV---------------WERKGSLFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTH-------WQSVPPF 143
Cdd:cd19099 77 AGYIpgdgdeplrplkyleEKLGRGLIDVADSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllELGEEEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 144 FTPIAETVAVLNELKSEGKIRAIG-------AANVDADHIREYLQYGE-----------LDIIQAKYSILDRAMENE--- 202
Cdd:cd19099 157 YDRLEEAFEALEEAVAEGKIRYYGistwdgfRAPPALPGHLSLEKLVAaaeevggdnhhFKVIQLPLNLLEPEALTEknt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 203 -------LLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANkvwfqrenmlkvidmleqwqplcaryqcTIPTLA 275
Cdd:cd19099 237 vkgealsLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGA----------------------------TLAQRA 288
|
330 340
....*....|....*....|....*...
gi 3123121 276 LAWILKQSDLISILSGATAPEQVRENVA 303
Cdd:cd19099 289 LQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-322 |
3.89e-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: 126.68 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 10 DITLSRMGLGTWAIGGGPAwNGD------LDR---QICIDtilEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQV 80
Cdd:cd19103 1 DKKLPKIALGTWSWGSGGA-GGDqvfgnhLDEdtlKAVFD---KAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKcgivwerkgslFNKVGDRQlyknlSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPiaetvaVLNELKSE 160
Cdd:cd19103 77 IISTK-----------FTPQIAGQ-----SADPVADMLEGSLARLGTDYIDIYWIHNPADVERWTP------ELIPLLKS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDADHIR---EYLQYGELDI--IQAKYSILDRAME-NELLPLCRDNGIVVQVYSPLEQGLLTGTITRD-- 232
Cdd:cd19103 135 GKVKHVGVSNHNLAEIKranEILAKAGVSLsaVQNHYSLLYRSSEeAGILDYCKENGITFFAYMVLEQGALSGKYDTKhp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 233 YVPGGARA---NKVWFQRENMLKVIdmleqwQPLCARYQCTIPTLALAWILKQSDLISIlsGATAPEQVRENVAALNINL 309
Cdd:cd19103 215 LPEGSGRAetyNPLLPQLEELTAVM------AEIGAKHGASIAQVAIAWAIAKGTTPII--GVTKPHHVEDAARAASITL 286
|
330
....*....|...
gi 3123121 310 SDADATLMREMAE 322
Cdd:cd19103 287 TDDEIKELEQLAD 299
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-307 |
4.55e-34 |
|
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: 126.50 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 6 LGTTDITLSRMGLGTWAIGGgpAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKL--PREQVVVE 83
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGG--VYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALqvPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 84 TKCGivwerkgslfnKVGDRQLykNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKSEGKI 163
Cdd:cd19153 83 TKVG-----------RYRDSEF--DYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPALRTLKDEGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDADHIREYLQY---GELDIIQA--KYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGG- 237
Cdd:cd19153 150 KRIGIAGYPLDTLTRATRRcspGSLDAVLSycHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQGPPPWHPASg 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3123121 238 -----ARANKVWfqrenmlkvidmleqwqplCARYQCTIPTLALAWIL-KQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19153 230 elrhyAAAADAV-------------------CASVEASLPDLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-313 |
7.32e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 126.17 E-value: 7.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 12 TLSRMGLGTWAIGGGpaWNGDLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKLPRE-----QVVVETKc 86
Cdd:cd19101 1 TISRVINGMWQLSGG--HGGIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRErdaadDVQIHTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 87 givWerkgslfnkVGDRQLyKNLSPESIREEVAASLQRLGIDYIDIYMTHWQ--SVPPFFtpiaETVAVLNELKSEGKIR 164
Cdd:cd19101 76 ---W---------VPDPGE-LTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWdySDPGYL----DAAKHLAELQEEGKIR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 165 AIGAANVDADHIREYLQYGeLDII--QAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTgtitRDYV----PGGA 238
Cdd:cd19101 139 HLGLTNFDTERLREILDAG-VPIVsnQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLS----EKYLgvpePTGP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 239 RANKV----------------WFQrenmlkviDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENV 302
Cdd:cd19101 214 ALETRslqkyklmidewggwdLFQ--------ELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNV 285
|
330
....*....|.
gi 3123121 303 AALNINLSDAD 313
Cdd:cd19101 286 RAFSFRLDDED 296
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-320 |
5.50e-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: 122.74 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWAIGGgpawngdldRQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK------LPREQVVVETKcgivw 90
Cdd:cd19136 5 GLGTFRLRG---------EEEVRQAVDAALKAGYRLIDTASVY--RN-EADIGKALRDllpkygLSREDIFITSK----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 erkgslfnkVGDrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHW---QSVPPfFTPI-----AETVAVLNELKSEGK 162
Cdd:cd19136 68 ---------LAP----KDQGYEKARAACLGSLERLGTDYLDLYLIHWpgvQGLKP-SDPRnaelrRESWRALEDLYKEGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 163 IRAIGAANVDADHIREYLQYGELD--IIQAKYSilDRAMENELLPLCRDNGIVVQVYSPLEQGLLTgTITRDYVPGGAra 240
Cdd:cd19136 134 LRAIGVSNYTVRHLEELLKYCEVPpaVNQVEFH--PHLVQKELLKFCKDHGIHLQAYSSLGSGDLR-LLEDPTVLAIA-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 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 |
9.04e-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: 123.61 E-value: 9.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGGPAWNGDLDRQICIdtileAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPRE 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTI-----AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 79 QVVVETKcgIVWErkgslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYmthWQSVPPFFTPIAETVAVLNELK 158
Cdd:cd19159 76 SLVITTK--LYWG---------GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV---FANRPDSNTPMEEIVRAMTHVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 159 SEGKIRAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLLTGTItR 231
Cdd:cd19159 142 NQGMAMYWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY-G 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 232 DYVPGGARANKVWFQ-------RENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19159 221 NGVPESSRASLKCYQwlkerivSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 300
|
...
gi 3123121 305 LNI 307
Cdd:cd19159 301 IQV 303
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
3-311 |
1.74e-32 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 123.43 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 3 KIPLGTTDItlSRMGLGTWAIGggpAWNGDLDRQICIDTILEAhrcGINLIDTAPGYNF-------GNSEVIVGQALKKL 75
Cdd:PRK10625 5 RIPHSSLEV--STLGLGTMTFG---EQNSEADAHAQLDYAVAQ---GINLIDVAEMYPVpprpetqGLTETYIGNWLAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 76 -PREQVVVETK-CGIVWERKGSLF-NKVGDRqlyKNlspesIREEVAASLQRLGIDYIDIYMTHWQSVPP-FF------- 144
Cdd:PRK10625 77 gSREKLIIASKvSGPSRNNDKGIRpNQALDR---KN-----IREALHDSLKRLQTDYLDLYQVHWPQRPTnCFgklgysw 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 145 ---TPIA---ETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGE------LDIIQAKYSILDRAMENELLPLCRDNGI 212
Cdd:PRK10625 149 tdsAPAVsllETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEkhdlprIVTIQNPYSLLNRSFEVGLAEVSQYEGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 213 VVQVYSPLEQGLLTGTITRDYVPGGARaNKVW--FQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILS 290
Cdd:PRK10625 229 ELLAYSCLAFGTLTGKYLNGAKPAGAR-NTLFsrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLL 307
|
330 340
....*....|....*....|.
gi 3123121 291 GATAPEQVRENVAALNINLSD 311
Cdd:PRK10625 308 GATTMEQLKTNIESLHLTLSE 328
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-306 |
3.33e-31 |
|
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: 119.04 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 7 GTTDITLSRMGLGTWAigggpawN-GDLDR-QICIDTILEAHRCGINLIDTAPGYN--FGNSEVIVGQALK---KLPREQ 79
Cdd:cd19151 6 GRSGLKLPAISLGLWH-------NfGDVDRyENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKedlKPYRDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 80 VVVETKCG-IVWErkgslfNKVGDRQLYKNLspesireeVAA---SLQRLGIDYIDIYMTHwqsVPPFFTPIAETVAVLN 155
Cdd:cd19151 79 LIISTKAGyTMWP------GPYGDWGSKKYL--------IASldqSLKRMGLDYVDIFYHH---RPDPETPLEETMGALD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 156 ELKSEGKIRAIGAANVDADHIREYL----QYGELDII-QAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTIT 230
Cdd:cd19151 142 QIVRQGKALYVGISNYPPEEAREAAailkDLGTPCLIhQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3123121 231 RDyVPGGARANKVW-FQRENML--KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALN 306
Cdd:cd19151 222 NG-IPEDSRAAKGSsFLKPEQIteEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
16-320 |
2.35e-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: 115.88 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGgpawngdldrqICIDTILEAHR-CGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiVWer 92
Cdd:cd19135 16 LGLGTSHSGG-----------YSHEAVVYALKeCGYRHIDTAKRY--GC-EELLGKAIKEsgVPREDLFLTTK---LW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 kgslfnkvgdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHW----QSVPPFFTPIAETVAVLNELKSEGKIRAIGA 168
Cdd:cd19135 77 -------------PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWpdcpSSGKNVKETRAETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 169 ANVDADHIREYLQYGEL--DIIQAKYSILDRAMenELLPLCRDNGIVVQVYSPLEQGLLtgtitrdyvpggarankvwFQ 246
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVvpHVNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA-------------------LE 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3123121 247 RENMLKvidmleqwqpLCARYQCTIPTLALAWILkQSDLISIlSGATAPEQVRENVAALNINLSDADATLMREM 320
Cdd:cd19135 203 EPTVTE----------LAKKYQKTPAQILIRWSI-QNGVVTI-PKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-325 |
1.61e-29 |
|
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: 114.87 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWaigggPAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPRE 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTW-----STFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKkgWKRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 79 QVVVETKcgIVWERKGSlfnkvgDRqlykNLSPESIREEVAASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELK 158
Cdd:cd19142 76 SYIVSTK--IYWSYGSE------ER----GLSRKHIIESVRASLRRLQLDYIDIVIIH--KADPM-CPMEEVVRAMSYLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 159 SEGKIRAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLLTGT--I 229
Cdd:cd19142 141 DNGLIMYWGTSRWSPVEIMEaFSIARQFNCPtpiceQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSLGLDPGIseE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 230 TRDYVPGGARANKVWFQRENMLKVID-------MLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENV 302
Cdd:cd19142 221 TRRLVTKLSFKSSKYKVGSDGNGIHEetrrashKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQL 300
|
330 340
....*....|....*....|...
gi 3123121 303 AALNInLSDADATLMREMAEALE 325
Cdd:cd19142 301 NSLQL-LPKLNSAVMEELERILD 322
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-307 |
1.86e-29 |
|
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: 114.47 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 6 LGTTDITLSRMGLGTWAIGGGpawngDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPREQVVVE 83
Cdd:cd19141 5 LGKSGLRVSCLGLGTWVTFGS-----QISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKkgWRRSSYVIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 84 TKcgIVWERKGslfnkvgdrQLYKNLSPESIREEVAASLQRLGIDYIDIYMThwqSVPPFFTPIAETVAVLNELKSEGKI 163
Cdd:cd19141 80 TK--IFWGGKA---------ETERGLSRKHIIEGLKASLERLQLEYVDIVFA---NRPDPNTPMEEIVRAFTHVINQGMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLLTGTITrDYVPG 236
Cdd:cd19141 146 MYWGTSRWSAMEIMEaYSVARQFNLIppiveQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYD-DGVPE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 237 GARA---NKVWF----QRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNI 307
Cdd:cd19141 225 YSRAslkGYQWLkekiLSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-323 |
2.61e-29 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 113.10 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 22 AIGGGPAWN----GDLDRQiCIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgivwerkgs 95
Cdd:cd19120 8 AFGTGTAWYksgdDDIQRD-LVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKEsgVPREDLFITTK---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 96 LFNKVGDrqlyknlspesIREEVAASLQRLGIDYIDIYMTHWqsvpPFFTP-----IAETVAVLNELKSEGKIRAIGAAN 170
Cdd:cd19120 74 VSPGIKD-----------PREALRKSLAKLGVDYVDLYLIHS----PFFAKeggptLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 171 VDADHIREYLQYGEL--DIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLeqglltGTITRDyvPGGArankvwfqre 248
Cdd:cd19120 139 FRIEDLEELLDTAKIkpAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPL------SPLTRD--AGGP---------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3123121 249 nmlkVIDMLEQwqpLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADatlMREMAEA 323
Cdd:cd19120 201 ----LDPVLEK---IAEKYGVTPAQVLLRWALQKG--IVVVTTSSKEERMKEYLEAFDFELTEEE---VEEIDKA 263
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
8-325 |
3.68e-29 |
|
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: 114.06 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 8 TTDITLSRMGLGTWAIGGgpAWN---GDLDRQIC---IDTILEAhrcGINLIDTAPGYNFGNSEVIVGQALKKLP-REQV 80
Cdd:cd19146 6 TAGVRVSPLCLGAMSFGE--AWKsmmGECDKETAfklLDAFYEQ---GGNFIDTANNYQGEESERWVGEWMASRGnRDEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGIVWERKGSLFNKVGdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSvppFFTPIAETVAVLNELKSE 160
Cdd:cd19146 81 VLATKYTTGYRRGGPIKIKSN----YQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWD---YTTSIPELMQSLNHLVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDA-------DHIREYLQYgELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLtgTITRDY 233
Cdd:cd19146 154 GKVLYLGVSDTPAwvvskanAYARAHGLT-QFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQF--RTEEEF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 234 VPGGARANKVWFQRENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19146 231 KRRGRSGRKGGPQTEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEE 307
|
330
....*....|..
gi 3123121 314 atlMREMAEALE 325
Cdd:cd19146 308 ---IQEIEDAYP 316
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-307 |
4.69e-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: 110.95 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 6 LGTTDITLSRMGLGTWAIGGGpawngDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPREQVVVE 83
Cdd:cd19158 6 LGKSGLRVSCLGLGTWVTFGG-----QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 84 TKcgIVWErkgslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYmthWQSVPPFFTPIAETVAVLNELKSEGKI 163
Cdd:cd19158 81 TK--IFWG---------GKAETERGLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNTPMEETVRAMTHVINQGMA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDyVPG 236
Cdd:cd19158 147 MYWGTSRWSSMEIMEaYSVARQFNLIppiceQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG-IPP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 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 |
5.16e-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: 110.85 E-value: 5.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDITLSRMGLGTWAIGGGpawngDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKK--LPRE 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGS-----QISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgWRRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 79 QVVVETKcgIVWErkgslfnkvGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHwQSVPPffTPIAETVAVLNELK 158
Cdd:cd19160 78 SYVVTTK--IYWG---------GQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFAN-RSDPN--SPMEEIVRAMTYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 159 SEGKIRAIGAANVDADHIRE-YLQYGELDII-----QAKYSILDR-AMENELLPLCRDNGIVVQVYSPLEQGLLTGTITr 231
Cdd:cd19160 144 NQGMAMYWGTSRWSAMEIMEaYSVARQFNLIppvceQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYD- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 232 DYVPGGARANKVWFQ-----------RENMLKVIDMLeqwqPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRE 300
Cdd:cd19160 223 GRVPDTCRAAVKGYQwlkekvqseegKKQQAKVKELH----PIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIE 298
|
....*..
gi 3123121 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 |
5.01e-27 |
|
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: 107.93 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 7 GTTDITLSRMGLGTWAIGGGpawngDLDRQICIDTILEAHRCGINLIDTAPGYN--FGNSEVIVGQALKK---LPREQVV 81
Cdd:cd19150 6 GKSGLKLPALSLGLWHNFGD-----DTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdfaGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 82 VETKCGivWERKGSLFNKVGDRqlyKNLspesiREEVAASLQRLGIDYIDIYMTHwqSVPPFfTPIAETVAVLNELKSEG 161
Cdd:cd19150 81 ISTKAG--YDMWPGPYGEWGSR---KYL-----LASLDQSLKRMGLDYVDIFYSH--RFDPD-TPLEETMGALDHAVRSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 162 KIRAIGAANVDADHIREYL----QYG-ELDIIQAKYSILDRAME-NELLPLCRDNGIVVQVYSPLEQGLLTGTITrDYVP 235
Cdd:cd19150 148 KALYVGISSYSPERTREAAailrELGtPLLIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-NGIP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 236 GGARANKVWFQRENML--KVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL-NINLSDA 312
Cdd:cd19150 227 EGSRASKERSLSPKMLteANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALdNLTFSAD 306
|
.
gi 3123121 313 D 313
Cdd:cd19150 307 E 307
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
23-304 |
3.30e-26 |
|
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: 105.44 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 23 IGGGP---AWNGDLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALKKL----PREQVVVETKCGivweRKG- 94
Cdd:cd19164 18 FGAATfsyQYTTDPESIPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALrdefPRDTYFIITKVG----RYGp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 95 SLFNkvgdrqlYknlSPESIREEVAASLQRLGIDYIDIYMTHwqSVpPFFTP--IAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd19164 92 DDFD-------Y---SPEWIRASVERSLRRLHTDYLDLVYLH--DV-EFVADeeVLEALKELFKLKDEGKIRNVGISGYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 173 ADHIREYLQY------GELDIIQ--AKYSILDRAMENeLLPLCRDNGIVVQVY--SPLEQGLLTGTITRDYVPGGArank 242
Cdd:cd19164 159 LPVLLRLAELarttagRPLDAVLsyCHYTLQNTTLLA-YIPKFLAAAGVKVVLnaSPLSMGLLRSQGPPEWHPASP---- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3123121 243 vwFQRENMLKVIDMLEQWQPlcaryqcTIPTLALAWILKQSDLI-SILSGATAPEQVRENVAA 304
Cdd:cd19164 234 --ELRAAAAKAAEYCQAKGT-------DLADVALRYALREWGGEgPTVVGCSNVDELEEAVEA 287
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
12-320 |
7.62e-26 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 103.61 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 12 TLSRMGLGTWAIGGGPAwngdldrqicIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiv 89
Cdd:cd19131 9 TIPQLGLGVWQVSNDEA----------ASAVREALEVGYRSIDTAAIY--GN-EEGVGKAIRAsgVPREELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 werkgsLFNkvgDRQLYknlspESIREEVAASLQRLGIDYIDIYMTHWQSvpPFFTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:cd19131 72 ------LWN---SDQGY-----DSTLRAFDESLRKLGLDYVDLYLIHWPV--PAQDKYVETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIREYLqyGELDIIQAKYSI--LDRAMENELLPLCRDNGIVVQVYSPLEQglltgtitrdyvpGGARANKVwfqr 247
Cdd:cd19131 136 NFTIEHLQRLI--DETGVVPVVNQIelHPRFQQRELRAFHAKHGIQTESWSPLGQ-------------GGLLSDPV---- 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3123121 248 enmlkvidmLEQwqpLCARYQCTIPTLALAWILkQSDLISILSGATaPEQVRENVAALNINLSDADATLMREM 320
Cdd:cd19131 197 ---------IGE---IAEKHGKTPAQVVIRWHL-QNGLVVIPKSVT-PSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-313 |
1.07e-25 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 102.82 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 13 LSRMGLGTWAIGGgpawngdldrQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVW 90
Cdd:cd19139 1 IPAFGLGTFRLKD----------DVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAEsgVPRDELFITTK---IW 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 ErkgslfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSvPPFFTPIAETVAVLNELKSEGKIRAIGAAN 170
Cdd:cd19139 65 I---------------DNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPS-PNDEVPVEEYIGALAEAKEQGLTRHIGVSN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 171 VDADHIREYLQ-YGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfqren 249
Cdd:cd19139 129 FTIALLDEAIAvVGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYG-------------------------- 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3123121 250 mlKVIDMlEQWQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19139 183 --KVLDD-PVLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNLLALDLTLDADD 241
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
7-310 |
2.79e-25 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 103.92 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 7 GTTDITLSRMGLGTWAIGGgpaWNGDLDRQICIdtILEAHRCGINLIDTAPGYN--FGNSEVIVGQALK---KLPREQVV 81
Cdd:PRK09912 19 GKSGLRLPALSLGLWHNFG---HVNALESQRAI--LRKAFDLGITHFDLANNYGppPGSAEENFGRLLRedfAAYRDELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 82 VETKCGI-VWErkgSLFNKVGDRQ-LYKNLSpesireevaASLQRLGIDYIDIYMTHWQSVPpffTPIAETVAVLNELKS 159
Cdd:PRK09912 94 ISTKAGYdMWP---GPYGSGGSRKyLLASLD---------QSLKRMGLEYVDIFYSHRVDEN---TPMEETASALAHAVQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 160 EGKIRAIGAANVD-------ADHIREYLQygELDIIQAKYSILDRAMENE-LLPLCRDNGIVVQVYSPLEQGLLTGTITR 231
Cdd:PRK09912 159 SGKALYVGISSYSpertqkmVELLREWKI--PLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 232 DyVPGGAR----ANKVWFQRENMLKVIDM--LEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAAL 305
Cdd:PRK09912 237 G-IPQDSRmhreGNKVRGLTPKMLTEANLnsLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAL 315
|
....*
gi 3123121 306 NiNLS 310
Cdd:PRK09912 316 N-NLT 319
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
11-313 |
9.53e-25 |
|
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: 100.54 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 11 ITLSRMGLGTWAIGGGpawngdldrQICIDTILEAHRCGINLIDTAPGYnfGNSEvIVGQALKK--LPREQVVVETKcgi 88
Cdd:cd19157 8 VKMPWLGLGVFKVEEG---------SEVVNAVKTALKNGYRSIDTAAIY--GNEE-GVGKGIKEsgIPREELFITSK--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 89 VWErkgslfnkvgDRQLYknlspESIREEVAASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKSEGKIRAIGA 168
Cdd:cd19157 73 VWN----------ADQGY-----DSTLKAFEASLERLGLDYLDLYLIHW----PVKGKYKETWKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 169 ANVDADHIREYLQYGELD--IIQAKYSilDRAMENELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfq 246
Cdd:cd19157 134 SNFQVHHLEDLLADAEIVpmVNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQG----------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3123121 247 renmlKVIDMlEQWQPLCARYQCTIPTLALAWILkQSDLISILSgATAPEQVRENVAALNINLSDAD 313
Cdd:cd19157 189 -----QLLDN-PVLKEIAEKYNKSVAQVILRWDL-QNGVVTIPK-SIKEHRIIENADVFDFELSQED 247
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
17-321 |
1.51e-23 |
|
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: 97.26 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWAIGggpawngdlDRQICIDTILEAHRCGINLIDTAPGYnfGNSEViVGQALKK--LPREQVVVETKCGIvwerkg 94
Cdd:cd19133 13 GFGVFQIP---------DPEECERAVLEAIKAGYRLIDTAAAY--GNEEA-VGRAIKKsgIPREELFITTKLWI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 95 slfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHWQsvppfFTPIAETVAVLNELKSEGKIRAIGAANVDAD 174
Cdd:cd19133 75 ------------QDAGYEKAKKAFERSLKRLGLDYLDLYLIHQP-----FGDVYGAWRAMEELYKEGKIRAIGVSNFYPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 175 HIREYLQYGELD--IIQAKYSILDRamENELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggarankvwfqRENMLK 252
Cdd:cd19133 138 RLVDLILHNEVKpaVNQIETHPFNQ--QIEAVEFLKKYGVQIEAWGPFAEG-----------------------RNNLFE 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 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 |
1.58e-23 |
|
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: 97.12 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGggpawNGDLDRQICidtiLEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWErk 93
Cdd:cd19126 12 LGLGVFQTP-----DGDETERAV----QTALENGYRSIDTAAIYK---NEEGVGEAIREsgVPREELFVTTK---LWN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 94 gslfnkvgDRQLYKnlSPESIREEvaaSLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKSEGKIRAIGAANVDA 173
Cdd:cd19126 75 --------DDQRAR--RTEDAFQE---SLDRLGLDYVDLYLIHW----PGKDKFIDTWKALEKLYASGKVKAIGVSNFQE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 174 DHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTgtitrdyvpggarANKVWFQrenmlkv 253
Cdd:cd19126 138 HHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLL-------------SNPVLAA------- 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3123121 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 |
1.88e-23 |
|
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: 96.96 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 11 ITLSRMGLGTWAIGGGPAwngdldrqicIDTILEAHRCGINLIDTApgYNFGNsEVIVGQALK--KLPREQVVVETKCGi 88
Cdd:cd19132 5 TQIPAIGFGTYPLKGDEG----------VEAVVAALQAGYRLLDTA--FNYEN-EGAVGEAVRrsGVPREELFVTTKLP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 89 vwerkgslfnkvGDRQLYknlspESIREEVAASLQRLGIDYIDIYMTHWqsvP-PFFTPIAETVAVLNELKSEGKIRAIG 167
Cdd:cd19132 71 ------------GRHHGY-----EEALRTIEESLYRLGLDYVDLYLIHW---PnPSRDLYVEAWQALIEAREEGLVRSIG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 168 AANVDADHIreylqygelDIIQAKYSILDRAMENELLPL---------CRDNGIVVQVYSPLEQGLltgtitrdyvpgga 238
Cdd:cd19132 131 VSNFLPEHL---------DRLIDETGVTPAVNQIELHPYfpqaeqrayHREHGIVTQSWSPLGRGS-------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 239 rankvwfqrenmlkviDMLEQ--WQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADatl 316
Cdd:cd19132 188 ----------------GLLDEpvIKAIAEKHGKTPAQVVLRWHVQLG--VVPIPKSANPERQRENLAIFDFELSDED--- 246
|
330
....*....|
gi 3123121 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 |
2.30e-21 |
|
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: 91.70 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 38 CIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWerkgslFNKVGDrqlyknlspESIR 115
Cdd:cd19127 24 TADAVATALADGYRLIDTAAAYG---NEREVGEGIRRsgVDRSDIFVTTK---LW------ISDYGY---------DKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 116 EEVAASLQRLGIDYIDIYMTHWqSVPPFFTPIAETVAVLNELKSEGKIRAIGAANVDADHireylqygeLDIIQAKYSIL 195
Cdd:cd19127 83 RGFDASLRRLGLDYVDLYLLHW-PVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEH---------LERLIDATTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 196 DRAMENELLPLC---------RDNGIVVQVYSPLeqglltGTITRdYVPGGARANKVWFQRENMLKvidmleqwqpLCAR 266
Cdd:cd19127 153 PAVNQVELHPYFsqkdlrafhRRLGIVTQAWSPI------GGVMR-YGASGPTGPGDVLQDPTITG----------LAEK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 3123121 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 |
8.87e-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: 87.96 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 8 TTDITLSRMGLGTWAIGGgpAWNGDL---DRQIC---IDTILEAhrcGINLIDTAPGYNFGNSEVIVGQ--ALKKLpREQ 79
Cdd:cd19147 5 TAGIRVSPLILGAMSIGD--AWSGFMgsmDKEQAfelLDAFYEA---GGNFIDTANNYQDEQSETWIGEwmKSRKN-RDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 80 VVVETKCGIVWERKGslfNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSvppFFTPIAETVAVLNELKS 159
Cdd:cd19147 79 IVIATKFTTDYKAYE---VGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWD---YTTSIEEVMDSLHILVQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 160 EGKIRAIGAANVDA---DHIREYLQ-YGE--LDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPL-----------EQ 222
Cdd:cd19147 153 QGKVLYLGVSDTPAwvvSAANYYATaHGKtpFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLgggkfqskkavEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 223 GLLTGTITRDYVPGGArankvwfQRENMLKVIDMLEQwqplCARYQCT--IPTLALAWILKQSDLISILSGATAPEQVRE 300
Cdd:cd19147 233 RKKNGEGLRSFVGGTE-------QTPEEVKISEALEK----VAEEHGTesVTAIALAYVRSKAPNVFPLVGGRKIEHLKD 301
|
330
....*....|
gi 3123121 301 NVAALNINLS 310
Cdd:cd19147 302 NIEALSIKLT 311
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-326 |
1.90e-19 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 86.23 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 12 TLSRMGLGTWAIGGgpawngdldrQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcgiV 89
Cdd:PRK11172 2 SIPAFGLGTFRLKD----------QVVIDSVKTALELGYRAIDTAQIY--DN-EAAVGQAIAEsgVPRDELFITTK---I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WerkgslfnkvgdrqlYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSvPPFFTPIAETVAVLNELKSEGKIRAIGAA 169
Cdd:PRK11172 66 W---------------IDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPS-PNDEVSVEEFMQALLEAKKQGLTREIGIS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 170 NVDADHIREYLQYGELDIIQAKYSILDRAMEN-ELLPLCRDNGIVVQVYSPLEQGlltgtitrdyvpggaranKVwfqre 248
Cdd:PRK11172 130 NFTIALMKQAIAAVGAENIATNQIELSPYLQNrKVVAFAKEHGIHVTSYMTLAYG------------------KV----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 249 nmLK--VIdmleqwQPLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDADatlMREMAeALER 326
Cdd:PRK11172 187 --LKdpVI------ARIAAKHNATPAQVILAWAMQLG--YSVIPSSTKRENLASNLLAQDLQLDAED---MAAIA-ALDR 252
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
17-313 |
3.96e-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: 85.86 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWAIGGGpawngdldrqICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVvetkcgivwERKgSL 96
Cdd:cd19125 15 GLGTWQADPG----------VVGNAVKTAIKEGYRHIDCAAIY--GN-EKEIGKALKKLFEDGVV---------KRE-DL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 97 FnkVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHW-------------QSVPPFftPIAETVAVLNELKSEGKI 163
Cdd:cd19125 72 F--ITSKLWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWpvrlkkgahmpepEEVLPP--DIPSTWKAMEKLVDSGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 164 RAIGAANVDADHIREYLQYGEldIIQAKYSildraME-------NELLPLCRDNGIVVQVYSPLeqglltgtitrdyvpg 236
Cdd:cd19125 148 RAIGVSNFSVKKLEDLLAVAR--VPPAVNQ-----VEchpgwqqDKLHEFCKSKGIHLSAYSPL---------------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3123121 237 gARANKVWFQReNMLK--VIDMLEQwqplcaRYQCTIPTLALAWILKQSDliSILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19125 205 -GSPGTTWVKK-NVLKdpIVTKVAE------KLGKTPAQVALRWGLQRGT--SVLPKSTNEERIKENIDVFDWSIPEED 273
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
15-225 |
4.77e-19 |
|
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: 85.26 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 15 RMGLGTWAIGGGpawngdldrQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgiVWER 92
Cdd:cd19156 11 RLGLGVWRVQDG---------AEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIREsgVPREEVFVTTK---LWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 93 KgslfnkvgdrQLYknlspESIREEVAASLQRLGIDYIDIYMTHWqsvpPFFTPIAETVAVLNELKSEGKIRAIGAANVD 172
Cdd:cd19156 76 D----------QGY-----ESTLAAFEESLEKLGLDYVDLYLIHW----PVKGKFKDTWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3123121 173 ADHIREYLQYGELdiiqakysildRAMEN--ELLPL---------CRDNGIVVQVYSPLEQGLL 225
Cdd:cd19156 137 EHHLEELLKSCKV-----------APMVNqiELHPLltqeplrkfCKEKNIAVEAWSPLGQGKL 189
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
17-319 |
1.94e-17 |
|
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: 81.17 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWAIGGGPAwngdldrqiCIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK------LPREQVVVETKcgivw 90
Cdd:cd19116 15 ALGTWKLKDDEG---------VRQAVKHAIEAGYRHIDTAYLY--GN-EAEVGEAIREkiaegvVKREDLFITTK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 erkgsLFNKVGDRQLYKnlspESIREevaaSLQRLGIDYIDIYMTHWqsvPPFFTPIAETVAVLN--------------- 155
Cdd:cd19116 78 -----LWNSYHEREQVE----PALRE----SLKRLGLDYVDLYLIHW---PVAFKENNDSESNGDgslsdidyletwrgm 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 156 -ELKSEGKIRAIGAANVDADHIREYLQYGelDIIQAKYSI-----LDRAmenELLPLCRDNGIVVQVYSPLEQglltgti 229
Cdd:cd19116 142 eDLVKLGLTRSIGVSNFNSEQINRLLSNC--NIKPAVNQIevhptLTQE---KLVAYCQSNGIVVMAYSPFGR------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 230 trdYVPGGARANKVWFQRENMLKvidmleqwqpLCARYQCTIPTLALAWILkQSDLISILSgATAPEQVRENVAALNINL 309
Cdd:cd19116 210 ---LVPRGQTNPPPRLDDPTLVA----------IAKKYGKTTAQIVLRYLI-DRGVVPIPK-SSNKKRIKENIDIFDFQL 274
|
330
....*....|
gi 3123121 310 SDADATLMRE 319
Cdd:cd19116 275 TPEEVAALNS 284
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-322 |
2.02e-17 |
|
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: 80.92 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTTDiTLSRMGLGTWAIGGGPAWngdldrqiciDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALK------K 74
Cdd:cd19123 1 MKTLPLSNGD-LIPALGLGTWKSKPGEVG----------QAVKQALEAGYRHIDCAAIY--GN-EAEIGAALAevfkegK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 75 LPREQVVVETKcgivwerkgsLFNKVGDrqlyknlsPESIREEVAASLQRLGIDYIDIYMTHW----QSVPPFFT----- 145
Cdd:cd19123 67 VKREDLWITSK----------LWNNSHA--------PEDVLPALEKTLADLQLDYLDLYLMHWpvalKKGVGFPEsgedl 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 146 ------PIAETVAVLNELKSEGKIRAIGAANVDADHIREYLQygeldiiQAKYSILDRAME-------NELLPLCRDNGI 212
Cdd:cd19123 129 lslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLA-------TARIKPAVNQVElhpylqqPELLAFCRDNGI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 213 VVQVYSPLeqglltGTitrdyvPGGARANKVwfQRENML---KVIdmleqwQPLCARYQCTIPTLALAWILKQSdlISIL 289
Cdd:cd19123 202 HLTAYSPL------GS------GDRPAAMKA--EGEPVLledPVI------NKIAEKHGASPAQVLIAWAIQRG--TVVI 259
|
330 340 350
....*....|....*....|....*....|...
gi 3123121 290 SGATAPEQVRENVAALNINLSDADatlMREMAE 322
Cdd:cd19123 260 PKSVNPERIQQNLEAAEVELDASD---MATIAA 289
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-325 |
3.67e-17 |
|
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: 80.19 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 22 AIGGGPAWNGDLDRQICIDTILEAhrcGINLIDTAPGYNfgnSEVIVGQALK------KLPREQVVVETKcgivwerkgs 95
Cdd:cd19129 8 ALGFGTLIPDPSATRNAVKAALEA---GFRHFDCAERYR---NEAEVGEAMQevfkagKIRREDLFVTTK---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 96 LFNKvgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHwqsvPPF-FTP--------------------IAETVAVL 154
Cdd:cd19129 72 LWNT--------NHRPERVKPAFEASLKRLQLDYLDLYLIH----TPFaFQPgdeqdprdangnviyddgvtLLDTWRAM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 155 NELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYV 234
Cdd:cd19129 140 ERLVDEGRCKAIGLSDVSLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPKLLEDPVI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 235 PGGARankvwfqrenmlkvidmleqwqplcaRYQCTIPTLALAWILKQSdlISILSGATAPEQVRENvaaLNINLSDADA 314
Cdd:cd19129 220 TAIAR--------------------------RVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIREN---FDISTLPEDA 268
|
330
....*....|.
gi 3123121 315 tlMREMAEALE 325
Cdd:cd19129 269 --MREINEGIK 277
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-220 |
9.65e-17 |
|
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: 79.08 E-value: 9.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 9 TDITLSRMGLGTWAIGGGPAWNgdldrqicidTILEAHRCGINLIDTApgYNFGNSEViVGQALKK--LPREQVVVETKC 86
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNEVAK----------AVEAALKAGYRHIDTA--AIYGNEEE-VGQGIKDsgVPREEIFITTKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 87 GIVWERKgslfnkvgdrqlyknlsPEsirEEVAASLQRLGIDYIDIYMTHWQS-------------------VPPFFTPI 147
Cdd:cd19117 77 WCTWHRR-----------------VE---EALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtkdHEPDWDFI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3123121 148 aETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAM--ENELLPLCRDNGIVVQVYSPL 220
Cdd:cd19117 137 -KTWELMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLlpQPKLVDFCKSKGIHATAYSPL 210
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-324 |
1.11e-16 |
|
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: 78.99 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 8 TTDITLS---RM---GLGTWAIgggpawNGDlDRQICIDTILEAhrcGINLIDTApgYNFGNSEVIvGQALK------KL 75
Cdd:cd19154 1 SASITLSngvKMpliGLGTWQS------KGA-EGITAVRTALKA---GYRLIDTA--FLYQNEEAI-GEALAelleegVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 76 PREQVVVETKcgivwerkgsLFNKVgdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTH--W---QSVPPFFT----- 145
Cdd:cd19154 68 KREDLFITTK----------LWTHE--------HAPEDVEEALRESLKKLQLEYVDLYLIHapAafkDDEGESGTmengm 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 146 ------PIAETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSP 219
Cdd:cd19154 130 sihdavDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYAT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 220 LeqglltGTITRDYVPGgarANKVWFQRENMLKVIdMLEqwqpLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVR 299
Cdd:cd19154 210 L------GSPGRANFTK---STGVSPAPNLLQDPI-VKA----IAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIK 273
|
330 340
....*....|....*....|....*
gi 3123121 300 ENVAALNINLSDADATLMREMAEAL 324
Cdd:cd19154 274 ENFNIFDFSLSEEDMATLEEIEKSL 298
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-316 |
1.66e-16 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 78.47 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLGTT----DITLSRMGLGTWAIGGGPAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLP 76
Cdd:PRK10376 1 MSTIMSSGTftlgGRSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 77 REQVVVeTKCGIVWERKGSLFnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIY-MTHWQSV-PPFFTPIAETVAVL 154
Cdd:PRK10376 81 DDLTIV-TKVGARRGEDGSWL---------PAFSPAELRRAVHDNLRNLGLDVLDVVnLRLMGDGhGPAEGSIEEPLTVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 155 NELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDnGIVVQVYSPLeqglltgtitrdyv 234
Cdd:PRK10376 151 AELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARD-GIAYVPFFPL-------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 235 pGGARAnkvwFQRENMLKVIDMLEQwQPLCaryqctiptLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDAD- 313
Cdd:PRK10376 216 -GGFTP----LQSSTLSDVAASLGA-TPMQ---------VALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVl 280
|
...
gi 3123121 314 ATL 316
Cdd:PRK10376 281 AEL 283
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
16-220 |
5.06e-16 |
|
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: 76.80 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGGPAwngdldRQicidTILEAHRCGINLIDTApgYNFGNsEVIVGQALKK-----LPREQVVVETKCGIVW 90
Cdd:cd19121 15 VGLGTWQAKAGEV------KA----AVAHALKIGYRHIDGA--LCYQN-EDEVGEGIKEaiaggVKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 91 ERKgslfnkvgdrqlyknlsPESIREEvaaSLQRLGIDYIDIYMTHW------QSVPPFFTPI-------------AETV 151
Cdd:cd19121 82 HRR-----------------VELCLDR---SLKSLGLDYVDLYLVHWpvllnpNGNHDLFPTLpdgsrdldwdwnhVDTW 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 152 AVLNELKSEGKIRAIGAANVDADHIREYLQYGEldIIQAKYSILDRAM--ENELLPLCRDNGIVVQVYSPL 220
Cdd:cd19121 142 KQMEKVLKTGKTKAIGVSNYSIPYLEELLKHAT--VVPAVNQVENHPYlpQQELVDFCKEKGILIEAYSPL 210
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-313 |
6.22e-16 |
|
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: 76.77 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGGpawngdlDRQICIDTILEAhrcGINLIDTAPGYnfGNSEVIvGQALK------KLPREQVVVETKCGIV 89
Cdd:cd19111 7 IGLGTYQSPPE-------EVRAAVDYALFV---GYRHIDTALSY--QNEKAI-GEALKwwlkngKLKREEVFITTKLPPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WerkgslfnkvgdrqlyknLSPESIREEVAASLQRLGIDYIDIYMTH--WQSV--------PPFFTPIAETVAVLNELKS 159
Cdd:cd19111 74 Y------------------LEFKDTEKSLEKSLENLKLPYVDLYLIHhpCGFVnkkdkgerELASSDVTSVWRAMEALVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 160 EGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLeqglltGTITR--DYVPGG 237
Cdd:cd19111 136 EGKVKSIGLSNFNPRQINKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPL------GSPGRanQSLWPD 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3123121 238 AranKVWFQRENMLKVIDMLEQwqplcaryqcTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSDAD 313
Cdd:cd19111 210 Q---PDLLEDPTVLAIAKELDK----------TPAQVLLRFVLQRG--TGVLPKSTNKERIEENFEVFDFELTEEH 270
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-225 |
1.16e-15 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 75.66 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 10 DITLSRMGLGTWAIGggpawngDLDRQICIDTILEAhrcGINLIDTAPGYnfGNsEVIVGQALKK--LPREQVVVETKcg 87
Cdd:cd19134 8 DNTMPVIGLGVGELS-------DDEAERSVSAALEA---GYRLIDTAAAY--GN-EAAVGRAIAAsgIPRGELFVTTK-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 88 iVWErkgslfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPffTPIAETVAVLNELKSEGKIRAIG 167
Cdd:cd19134 73 -LAT---------------PDQGFTASQAACRASLERLGLDYVDLYLIHWPAGRE--GKYVDSWGGLMKLREEGLARSIG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 168 AANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLL 225
Cdd:cd19134 135 VSNFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRL 192
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
2-220 |
7.72e-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: 73.57 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 2 KKIPLgttditlsrMGLGTWAIGGGPAWNGdldrqicidtILEAHRCGINLIDTAPGYnfGNsEVIVGQALKK------- 74
Cdd:cd19106 5 QKMPL---------IGLGTWKSKPGQVKAA----------VKYALDAGYRHIDCAAVY--GN-EQEVGEALKEkvgpgka 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 75 LPREQVVVETKcgiVWERKGSlfnkvgdrqlyknlsPESIREEVAASLQRLGIDYIDIYMTHWqsvPPFF---------- 144
Cdd:cd19106 63 VPREDLFVTSK---LWNTKHH---------------PEDVEPALRKTLKDLQLDYLDLYLIHW---PYAFergdnpfpkn 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 145 ---------TPIAETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQ 215
Cdd:cd19106 122 pdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVT 201
|
....*
gi 3123121 216 VYSPL 220
Cdd:cd19106 202 AYSPL 206
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
16-223 |
1.43e-14 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 72.41 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGggpawngdlDRQIcIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK--LPREQVVVETKcgivwerk 93
Cdd:PRK11565 18 LGLGVWQAS---------NEEV-ITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEasVAREELFITTK-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 94 gsLFNkvgDRQLyknlspeSIREEVAASLQRLGIDYIDIYMTHWqSVPPFFTPIaETVAVLNELKSEGKIRAIGAANVDA 173
Cdd:PRK11565 77 --LWN---DDHK-------RPREALEESLKKLQLDYVDLYLMHW-PVPAIDHYV-EAWKGMIELQKEGLIKSIGVCNFQI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3123121 174 DHIREYLQygELDIIQAKYSIldramenELLPLCRD---------NGIVVQVYSPLEQG 223
Cdd:PRK11565 143 HHLQRLID--ETGVTPVINQI-------ELHPLMQQrqlhawnatHKIQTESWSPLAQG 192
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-326 |
5.03e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 71.61 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 14 SRMGLGTWAIGG------------GPAWNGDLDRQICIDTILEAHRCGINLIDTAPGYnfGNSEVIVGQALK--KLPREQ 79
Cdd:cd19098 1 PRLGLGLAALGRpgyinlghaadlGSGRSVEAMRAHTHAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRsrNIAPDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 80 VVVETKCGIV----WerkgslfNKVGDRQLYKNLSPESIREEVAASLQRLGiDYIDIYMTHwqSVPpFFTPIAETVAVLN 155
Cdd:cd19098 79 VFVGSKWGYTytadW-------QVDAAVHEVKDHSLARLLKQWEETRSLLG-KHLDLYQIH--SAT-LESGVLEDADVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 156 EL---KSEGkiRAIG---AANVDADHIREYLQY---GE--LDIIQAKYSILDRAMeNELLPLCRDNGIVVQVYSPLEQGL 224
Cdd:cd19098 148 ALaelKAEG--VKIGlslSGPQQAETLRRALEIeidGArlFDSVQATWNLLEQSA-GEALEEAHEAGMGVIVKEALANGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 225 LTGTITRDYVPGGARANKvwfqrenmlkvidmleqwqPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAA 304
Cdd:cd19098 225 LTDRNPSPELAPLMAVLK-------------------AVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRA 285
|
330 340
....*....|....*....|..
gi 3123121 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 |
5.70e-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: 71.01 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 15 RMGLGTWAIgggpawNGDLDRQicidTILEAHRCGINLIDTApgYNFGNSEVIvGQALKKL------PREQVVVETKcgi 88
Cdd:cd19128 3 RLGFGTYKI------TESESKE----AVKNAIKAGYRHIDCA--YYYGNEAFI-GIAFSEIfkdggvKREDLFITSK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 89 VWErkgslfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHW-------QSVPPFF---------TPIAETVA 152
Cdd:cd19128 67 LWP---------------TMHQPENVKEQLLITLQDLQLEYLDLFLIHWplafdmdTDGDPRDdnqiqslskKPLEDTWR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 153 VLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLeqglltgtitrd 232
Cdd:cd19128 132 AMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPL------------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 233 yvpGGARANKvwfqrENMLKVIDMLEQwqpLCARYQCTIPTLALAWILKQ-SDLISILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19128 200 ---GGSYGDG-----NLTFLNDSELKA---LATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTK 268
|
..
gi 3123121 312 AD 313
Cdd:cd19128 269 ED 270
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
16-220 |
9.03e-14 |
|
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: 70.60 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWaigggpawNGDLDRQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALK------KLPREQVVVETKcgiV 89
Cdd:cd19119 15 LGLGTA--------SPHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKraiddgSIKREELFITTK---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WErkgSLFNKVgDRQLYKnlspesireevaaSLQRLGIDYIDIYMTHW--------QSVPPFFTPI-------------- 147
Cdd:cd19119 81 WP---TFYDEV-ERSLDE-------------SLKALGLDYVDLLLVHWpvcfekdsDDSGKPFTPVnddgktryaasgdh 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3123121 148 AETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPL 220
Cdd:cd19119 144 ITTYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPL 216
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
16-220 |
1.00e-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: 70.13 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGGPAWNGdldrqicidtILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVEtkcgivwerKGS 95
Cdd:cd19118 10 IGLGTWQAEPGEVGAA----------VKIALKAGYRHLDLAKVY--QN-QHEVGQALKELLKEEPGVK---------RED 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 96 LFNKvgdRQLYKNL-SPESIREEVAASLQRLGIDYIDIYMTHW-------QSVPPFFTP--------------IAETVAV 153
Cdd:cd19118 68 LFIT---SKLWNNShRPEYVEPALDDTLKELGLDYLDLYLIHWpvafkptGDLNPLTAVptnggevdldlsvsLVDTWKA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3123121 154 LNELKSEGKIRAIGAANVDADHIREYLQ-YGELDII-QAKYSILdrAMENELLPLCRDNGIVVQVYSPL 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 |
2.93e-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: 68.40 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 3 KIPLGTtDITLSRMGLGTWAIGggpawngDLDRQICIDTILEAhrcGINLIDTAPGYnfGNsEVIVGQAL--KKLPREQV 80
Cdd:cd19130 1 SIVLND-GNSIPQLGYGVFKVP-------PADTQRAVATALEV---GYRHIDTAAIY--GN-EEGVGAAIaaSGIPRDEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 81 VVETKCGivwerkgslfnkvGDRQlyknlSPESIREEVAASLQRLGIDYIDIYMTHWQSvpPFFTPIAETVAVLNELKSE 160
Cdd:cd19130 67 FVTTKLW-------------NDRH-----DGDEPAAAFAESLAKLGLDQVDLYLVHWPT--PAAGNYVHTWEAMIELRAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 161 GKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTitrdyVPGGARA 240
Cdd:cd19130 127 GRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGD-----PPVGAIA 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3123121 241 nkvwfqrenmlkvidmleqwqplcARYQCTIPTLALAWILKQSDliSILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19130 202 ------------------------AAHGKTPAQIVLRWHLQKGH--VVFPKSVRRERMEDNLDVFDFDLTD 246
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-313 |
6.37e-13 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 67.68 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 11 ITLSRMGLGTWAIGGGPawngdldrQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK-------LPREQVVVE 83
Cdd:cd19124 3 QTMPVIGMGTASDPPSP--------EDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlglvKSRDELFVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 84 TKcgiVWerkgslfnkVGDrqLYKNLSPESIREevaaSLQRLGIDYIDIYMTHW--QSVP-PFFTPIAE----------T 150
Cdd:cd19124 72 SK---LW---------CSD--AHPDLVLPALKK----SLRNLQLEYVDLYLIHWpvSLKPgKFSFPIEEedflpfdikgV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 151 VAVLNELKSEGKIRAIGAANVDADHIREYLQYG---------ELDII-QAKysildramenELLPLCRDNGIVVQVYSPL 220
Cdd:cd19124 134 WEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAtippavnqvEMNPAwQQK----------KLREFCKANGIHVTAYSPL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 221 eqglltgtitrdyvpgGARANKvWFQRENMLKviDMLEQwqpLCARYQCTIPTLALAWILKQSDliSILSGATAPEQVRE 300
Cdd:cd19124 204 ----------------GAPGTK-WGSNAVMES--DVLKE---IAAAKGKTVAQVSLRWVYEQGV--SLVVKSFNKERMKQ 259
|
330
....*....|...
gi 3123121 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 |
3.77e-12 |
|
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: 65.97 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAigggpawngdLDRQICIDTILEAHRCGINLIDTAPGYNfgnSEVIVGQALKK------LPREQVVVETKcgiV 89
Cdd:cd19112 14 IGLGVWR----------MEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEafktglVKREDLFITTK---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 WerkgslfnkvgdrqlykNLSPESIREEVAASLQRLGIDYIDIYMTHWqSVPPFFTPIAETVAVLNE------------- 156
Cdd:cd19112 78 W-----------------NSDHGHVIEACKDSLKKLQLDYLDLYLVHF-PVATKHTGVGTTGSALGEdgvldidvtisle 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 157 --------LKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLeqglltgt 228
Cdd:cd19112 140 ttwhamekLVSAGLVRSIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPL-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 229 itrdyvpGGARANKVWFQRENMLKVIDMLEqwqpLCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNIN 308
Cdd:cd19112 212 -------GGAAANAEWFGSVSPLDDPVLKD----LAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENIDVFDFQ 278
|
330
....*....|..
gi 3123121 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 |
4.19e-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: 62.93 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAigggpawNGDLDRQICIDTILEAhrcGINLIDTApgYNFGNsEVIVGQALK------KLPREQVVVETKcgiv 89
Cdd:cd19155 15 VGLGTWQ-------SSPEEIETAVDTALEA---GYRHIDTA--YVYRN-EAAIGNVLKkwidsgKVKREELFIVTK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 90 werkgslFNKVGDRqlyknlsPESIREEVAASLQRLGIDYIDIYMTHW------------------QSVPPFFTPIAETV 151
Cdd:cd19155 78 -------LPPGGNR-------REKVEKFLLKSLEKLQLDYVDLYLIHFpvgslskeddsgkldptgEHKQDYTTDLLDIW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 152 AVLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITR 231
Cdd:cd19155 144 KAMEAQVDQGLTRSIGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 232 DYVPGGARANkvwFQRENMLKVIdmleqwqplCARYQCTIPTLALAWILKQSdlISILSGATAPEQVRENVAALNINLSD 311
Cdd:cd19155 224 TGSPSGSSPD---LLQDPVVKAI---------AERHGKSPAQVLLRWLMQRG--VVVIPKSTNAARIKENFQVFDFELTE 289
|
....*....
gi 3123121 312 ADATLMREM 320
Cdd:cd19155 290 ADMAKLSSL 298
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
16-218 |
3.22e-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: 60.15 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWaigggpawngDLDRQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVETKCGIVwerkGS 95
Cdd:cd19113 14 VGFGCW----------KLDNATAADQIYQAIKAGYRLFDGAEDY--GN-EKEVGEGVNRAIDEGLVKREELFLT----SK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 96 LFNKVGDrqlyknlsPESIREEVAASLQRLGIDYIDIYMTHW----------QSVPPFF------------TPIAETVAV 153
Cdd:cd19113 77 LWNNFHD--------PKNVETALNKTLSDLKLDYVDLFLIHFpiafkfvpieEKYPPGFycgdgdnfvyedVPILDTWKA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 154 LNELKSEGKIRAIGAANVDADHIREYLQYGE-----LDIIQAKYsildrAMENELLPLCRDNGIVVQVYS 218
Cdd:cd19113 149 LEKLVDAGKIKSIGVSNFPGALILDLLRGATikpavLQIEHHPY-----LQQPKLIEYAQKAGITITAYS 213
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
17-218 |
3.58e-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: 60.13 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWAIgggpawngdlDRQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVETKCGIVwerkGSL 96
Cdd:cd19115 17 GFGLWKV----------NNDTCADQVYNAIKAGYRLFDGACDY--GN-EVEAGQGVARAIKEGIVKREDLFIV----SKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 97 FNKVGDRqlyknlspESIREEVAASLQRLGIDYIDIYMTH-----------------WQS----VPPFFTPIAETVAVLN 155
Cdd:cd19115 80 WNTFHDG--------ERVEPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppgWFYdgkkVEFSNAPIQETWTAME 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3123121 156 ELKSEGKIRAIGAANVDADHIREYLQYGE-----LDIIQAKYsildrAMENELLPLCRDNGIVVQVYS 218
Cdd:cd19115 152 KLVDKGLARSIGVSNFSAQLLMDLLRYARirpatLQIEHHPY-----LTQPRLVKYAQKEGIAVTAYS 214
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
17-218 |
3.30e-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: 57.18 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 17 GLGTWAIgggpawngdlDRQICIDTILEAHRCGINLIDTAPGYnfGNsEVIVGQALKKLPREQVVVETKCGIVwerkGSL 96
Cdd:cd19114 8 GFGTAKI----------KANETEEVIYNAIKVGYRLIDGALLY--GN-EAEVGRGIRKAIQEGLVKREDLFIV----TKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 97 FNKVGdrqlyknlSPESIREEVAASLQRLGIDYIDIYMTHW----------QSVPPFF------------TPIAETVAVL 154
Cdd:cd19114 71 WNNFH--------GKDHVREAFDRQLKDYGLDYIDLYLIHFpipaayvdpaENYPFLWkdkelkkfpleqSPMQECWREM 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3123121 155 NELKSEGKIRAIGAANVDADHIREYLQYGEL--DIIQAK-YSILDRameNELLPLCRDNGIVVQVYS 218
Cdd:cd19114 143 EKLVDAGLVRNIGIANFNVQLILDLLTYAKIkpAVLQIEhHPYLQQ---KRLIDWAKKQGIQITAYS 206
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-220 |
4.74e-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: 56.66 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIGGGpawngdldrqicidTILEAHRCGINL----IDTAPGYNfgnSEVIVGQALKKLPREQVVVETKCGIVwe 91
Cdd:cd19107 7 LGLGTWKSPPG--------------QVTEAVKVAIDAgyrhIDCAYVYQ---NENEVGEAIQEKIKEQVVKREDLFIV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 92 rkGSLFNKVGDRQLyknlspesIREEVAASLQRLGIDYIDIYMTHW----QSVPPFF------------TPIAETVAVLN 155
Cdd:cd19107 68 --SKLWCTFHEKGL--------VKGACQKTLSDLKLDYLDLYLIHWptgfKPGKELFpldesgnvipsdTTFLDTWEAME 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3123121 156 ELKSEGKIRAIGAANVDADHIREYLQYGELdiiqaKYSILDRAME-------NELLPLCRDNGIVVQVYSPL 220
Cdd:cd19107 138 ELVDEGLVKAIGVSNFNHLQIERILNKPGL-----KYKPAVNQIEchpyltqEKLIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
16-326 |
1.78e-05 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 45.56 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 16 MGLGTWAIgggpawngdlDRQICIDTILEAHRCGINL----IDTApgYNFGNsEVIVGQALK------KLPREQVVVetk 85
Cdd:cd19109 7 IGLGTYSE----------PKTTPKGACAEAVKVAIDTgyrhIDGA--YIYQN-EHEVGQAIRekiaegKVKREDIFY--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 86 CGIVWErkgslfnkvgdrqlyKNLSPESIREEVAASLQRLGIDYIDIYMTHwqsVPPFFTPIAE---------------- 149
Cdd:cd19109 71 CGKLWN---------------TCHPPELVRPTLERTLKVLQLDYVDLYIIE---MPMAFKPGDEiyprdengkwlyhktn 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 150 ---TVAVLNELKSEGKIRAIGAANVDADhireylqygELDIIQAKYSILDRAMENE-----------LLPLCRDNGIVVQ 215
Cdd:cd19109 133 lcaTWEALEACKDAGLVKSIGVSNFNRR---------QLELILNKPGLKHKPVSNQvechpyftqpkLLEFCQQHDIVIV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 216 VYSPLeqglltgtitrdyvpgGARANKVWFQrenmLKVIDMLEqwQPLCA----RYQCTIPTLALAWILKQSdlISILSG 291
Cdd:cd19109 204 AYSPL----------------GTCRDPIWVN----VSSPPLLE--DPLLNsigkKYNKTAAQVVLRFNIQRG--VVVIPK 259
|
330 340 350
....*....|....*....|....*....|....*
gi 3123121 292 ATAPEQVRENVAALNINLSDADatlMREMaEALER 326
Cdd:cd19109 260 SFNPERIKENFQIFDFSLTEEE---MKDI-EALNK 290
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
1-315 |
7.65e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 43.79 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 1 MKKIPLgttditlsrMGLGTWAIGGGPAwngdldrqicIDTILEAHRCGINLIDTAPGYNfGNSEVIVGQALK----KLP 76
Cdd:cd19110 1 MEDIPA---------VGLGTWKASPGEV----------TEAVKVAIDAGYRHFDCAYLYH-NESEVGAGIREKikegVVR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 77 REQVVVETKCGIVWERKgSLfnkvgdrqlyknlspesIREEVAASLQRLGIDYIDIYMTHW----------------QSV 140
Cdd:cd19110 61 REDLFIVSKLWCTCHKK-SL-----------------VKTACTRSLKALKLNYLDLYLIHWpmgfkpgepdlpldrsGMV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 141 PPFFTPIAETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGELDI--IQAKYSILDRAMENELLPLCRDNGIVVQVYS 218
Cdd:cd19110 123 IPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLRVkpVTNQIECHPYLTQKKLISFCQSRNVSVTAYR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 219 PLeqglltgtitrdyvpgGARANKVWFQRENMLKVIdmleqwqplcARYQCTIPTLALAWILKQSDLIsILSGATAPEQV 298
Cdd:cd19110 203 PL----------------GGSCEGVDLIDDPVIQRI----------AKKHGKSPAQILIRFQIQRNVI-VIPKSVTPSRI 255
|
330
....*....|....*..
gi 3123121 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 |
2.72e-03 |
|
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: 39.14 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3123121 53 IDTAPGYNfgnSEVIVGQALKK------LPREQVVVETKcgiVWerkgSLFnkvgdrqlyknLSPESIREEVAASLQRLG 126
Cdd:cd19108 44 IDSAYLYQ---NEEEVGQAIRSkiadgtVKREDIFYTSK---LW----CTF-----------HRPELVRPALEKSLKKLQ 102
|
90
....*....|.
gi 3123121 127 IDYIDIYMTHW 137
Cdd:cd19108 103 LDYVDLYLIHF 113
|
|
| |
