|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
5-309 |
1.22e-148 |
|
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: 419.52 E-value: 1.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 5 KLQKAGLNISKLGLGTNAVGGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLILATK 83
Cdd:cd19083 3 KLGKSDIDVNPIGLGTNAVGGHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEyNRNEVVIATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 GGIQpLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLK 163
Cdd:cd19083 83 GAHK-FGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 164 EANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYKSNFK 243
Cdd:cd19083 162 EANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRNDKPLFKGERFSENLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446800691 244 KVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKrvmKEIQSIL 309
Cdd:cd19083 242 KVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTE---EEIAFID 304
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-305 |
4.05e-124 |
|
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: 356.84 E-value: 4.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGHNlYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGGIQPL 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTW-WGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 90 LNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHG 169
Cdd:cd19084 80 GGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 170 HIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYKSNFKKVEKLK 249
Cdd:cd19084 160 PIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPFFRGENFEKNLEIVDKLK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446800691 250 GIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19084 240 EIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-311 |
1.86e-123 |
|
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: 356.03 E-value: 1.86e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGhnLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLI 79
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGG--PWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGrPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 80 LATKGGIqPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNI 159
Cdd:COG0667 79 IATKVGR-RMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 160 EQLKEANQH----GHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDwRQNVNLFEE 235
Cdd:COG0667 158 EQLRRALAIaeglPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGD-RAATNFVQG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446800691 236 NTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSILED 311
Cdd:COG0667 237 YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAA 312
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-311 |
2.92e-108 |
|
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: 316.45 E-value: 2.92e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGGIQpllng 92
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVSPD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 93 etyiNNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGHID 172
Cdd:cd19085 76 ----NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 173 VVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQ-NVNLFEENTYKSNFKKVEKLKGI 251
Cdd:cd19085 152 SNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTrLFRHFEPGAEEETFEALEKLKEI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 252 AKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSILED 311
Cdd:cd19085 232 ADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-305 |
4.98e-96 |
|
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: 285.65 E-value: 4.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 2 KYTKLQKAGLNISKLGLGtnAVGGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILA 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLG--CMGMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 82 TKGGIQ-PLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIE 160
Cdd:cd19076 79 TKFGIVrDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 161 QLKEANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYKS 240
Cdd:cd19076 159 TIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNPRFQGENFDK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446800691 241 NFKKVEKLKGIAKENDIEVSHLALAWLLNKeGIDTV-IPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19076 239 NLKLVEKLEAIAAEKGCTPAQLALAWVLAQ-GDDIVpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-309 |
4.43e-90 |
|
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: 270.70 E-value: 4.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGG-HNLYA--DVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGGIQPL 89
Cdd:cd19102 1 LTTIGLGTWAIGGgGWGGGwgPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLLWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 90 LNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHG 169
Cdd:cd19102 81 EEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 170 HIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYRED--FKLNEVDWRQNVNLFEENTYKSNFKKVEK 247
Cdd:cd19102 161 PIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPErvASLPADDWRRRSPFFQEPNLARNLALVDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446800691 248 LKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSIL 309
Cdd:cd19102 241 LRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-310 |
2.34e-89 |
|
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: 269.14 E-value: 2.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 3 YTKLQKAGLNISKLGLGTNAVGGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILAT 82
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KGGIQPLLNGET----------YINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSI 152
Cdd:cd19149 81 KCGLRWDREGGSfffvrdgvtvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 153 GISNVNIEQLKEANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNL 232
Cdd:cd19149 161 GASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDARSGIPW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 233 FEentyKSNFKKV----EKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKrvmKEIQSI 308
Cdd:cd19149 241 FS----PENREKVlallEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSA---EDIATM 313
|
..
gi 446800691 309 LE 310
Cdd:cd19149 314 RS 315
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-292 |
9.47e-88 |
|
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: 262.41 E-value: 9.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 11 LNISKLGLGTNAVGGhNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGGIQPLL 90
Cdd:cd19086 1 LEVSEIGFGTWGLGG-DWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNRFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 91 NGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHftNPETSYIDS---IGELTRLKEEGKIRSIGISNVNIEQLKEANQ 167
Cdd:cd19086 80 GPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLH--NPPDEVLDNdelFEALEKLKQEGKIRAYGVSVGDPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 168 HGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKyredfklnevdwrqnvnlfeentyksnfkkvek 247
Cdd:cd19086 158 RGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK--------------------------------- 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446800691 248 lkgiakendieVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKV 292
Cdd:cd19086 205 -----------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-309 |
8.60e-86 |
|
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: 259.17 E-value: 8.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 16 LGLGTNAVGGHNLYadVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK---GKRHKLILATKGGIQPLLNG 92
Cdd:pfam00248 1 IGLGTWQLGGGWGP--ISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKdypVKRDKVVIATKVPDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 93 ETYinnEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGH-- 170
Cdd:pfam00248 79 SGG---SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKip 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 171 IDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNlfeeNTYKSNFKKVEKLKG 250
Cdd:pfam00248 156 IVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLK----KGTPLNLEALEALEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 251 IAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSIL 309
Cdd:pfam00248 232 IAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-308 |
1.47e-82 |
|
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: 251.72 E-value: 1.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGhnlyaDVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLIL 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGG-----RTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKGGiQPLLNGetyiNNEPS----YLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISN 156
Cdd:cd19087 76 ATKVF-GPMGDD----PNDRGlsrrHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 157 VNIEQLKEAN----QHG--HIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNV 230
Cdd:cd19087 151 FAAWQIAKAQgiaaRRGllRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 231 NLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19087 231 RYQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-309 |
1.83e-82 |
|
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: 251.07 E-value: 1.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGhNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK--GKRHKLILATKGGIQ 87
Cdd:cd19148 1 DLPVSRIALGTWAIGG-WMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKeyGKRDRVVIATKVGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 88 PLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQ 167
Cdd:cd19148 80 WDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 168 HGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYKSNFKKVEK 247
Cdd:cd19148 160 VAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDPKFQEPRFSQYLAAVEE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 248 LKGIAKEN-DIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSIL 309
Cdd:cd19148 240 LDKLAQERyGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAIL 302
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-291 |
6.24e-79 |
|
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: 239.73 E-value: 6.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGGhnlyaDVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK--GKRHKLILATKGGIqPLLN 91
Cdd:cd06660 1 SRLGLGTMTFGG-----DGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKgrGNRDDVVIATKGGH-PPGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 92 GETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN----Q 167
Cdd:cd06660 75 DPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALayakA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 168 HG--HIDVVQSPYNMLERT-AEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvnlfeentyksnfkk 244
Cdd:cd06660 155 HGlpGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARG----------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446800691 245 veklkgiakendieVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVK 291
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-309 |
7.45e-78 |
|
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: 239.44 E-value: 7.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGtnAVGGHNLYADV-NEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGG--I 86
Cdd:cd19078 1 GLEVSAIGLG--CMGMSHGYGPPpDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGfkI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 QPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN 166
Cdd:cd19078 79 DGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 QHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYKSNFKKVE 246
Cdd:cd19078 159 AVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEALEANQALVD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 247 KLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSIL 309
Cdd:cd19078 239 LLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDAL 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-297 |
7.14e-74 |
|
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: 229.81 E-value: 7.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGHNLY----ADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRH 76
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFfgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 77 KLILATKGGIqPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISN 156
Cdd:cd19091 81 DVLIATKVRG-RMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 157 VNIEQ----LKEANQHGHIDVV--QSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNE-----VD 225
Cdd:cd19091 160 FSAWQimkaLGISERRGLARFValQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEgsrlrRT 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446800691 226 WRQNVNLFEENTYKSnfkkVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19091 240 GFDFPPVDRERGYDV----VDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSL 307
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-297 |
3.88e-73 |
|
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: 225.94 E-value: 3.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGGHNLY-ADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGGIQPLLN 91
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWgPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGLVRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 92 GETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGHI 171
Cdd:cd19088 81 GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 172 DVVQSPYNMLERtAEEELLPYCIEAGISFIPYGPLAfgilGGKYREDfklnevdwrqnvnlfeentyksnfkkVEKLKGI 251
Cdd:cd19088 161 VSVQNRYNLANR-DDEGVLDYCEAAGIAFIPWFPLG----GGDLAQP--------------------------GGLLAEV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446800691 252 AKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19088 210 AARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRL 255
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-305 |
5.87e-71 |
|
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: 222.07 E-value: 5.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 2 KYTKLQKAGLNISKLGLGTNAVGGHNLYA-DVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK--GKRHKL 78
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWRPwVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKefAPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 79 ILATK--GGIQPLLNGE----TYINNEpsylrnaVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSI 152
Cdd:cd19079 81 VIATKvyFPMGDGPNGRglsrKHIMAE-------VDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 153 GISNVNIEQLKEAN----QHGHIDVV--QSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDw 226
Cdd:cd19079 154 GASSMYAWQFAKALhlaeKNGWTKFVsmQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRST- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 227 RQNVNLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19079 233 TDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
10-297 |
2.58e-70 |
|
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: 220.16 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGV-------GRSEELVGEVLK--GKRHKLIL 80
Cdd:cd19081 6 GLSVSPLCLGTMVFG-----WTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKsrGKRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKGGIQPLLNGETYinnEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIE 160
Cdd:cd19081 81 ATKVGFPMGPNGPGL---SRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 161 QLKEAN----QHGH--IDVVQSPYNMLERT-AEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLF 233
Cdd:cd19081 158 RLQEALelsrQHGLprYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEAAKR 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 234 EENTYksNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19081 238 YLNER--GLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRL 299
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-310 |
1.96e-69 |
|
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: 218.47 E-value: 1.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGtnAVGGHNLYADV-NEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLK---GKRH 76
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFG--AMGLSAFYGPPkPDEERFAVLDAAFELGCTFWDTADIYG--DSEELIGRWFKqnpGKRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 77 KLILATKGGIQ-PLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGIS 155
Cdd:cd19144 77 KIFLATKFGIEkNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 156 NVNIEQLKEANQHGHIDVVQ---SPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNL 232
Cdd:cd19144 157 ECSAETLRRAHAVHPIAAVQieySPFSLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRRMAPR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 233 FEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSILE 310
Cdd:cd19144 237 FQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAE 314
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-297 |
4.54e-69 |
|
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: 216.69 E-value: 4.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGHNlyadVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLILATKG--GI 86
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQ----VDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGwPRESYVISTKVfwPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 QPllngetyinnEPS-------YLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNI 159
Cdd:cd19074 77 GP----------GPNdrglsrkHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 160 EQLKEA----NQHGHIDVV--QSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYRE-------DFKLNEVDW 226
Cdd:cd19074 147 EQIAEAhdlaRQFGLIPPVveQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDgipppsrSRATDEDNR 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446800691 227 RQNVNLFEENtyksNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19074 227 DKKRRLLTDE----NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKL 293
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
5-305 |
4.60e-65 |
|
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: 206.90 E-value: 4.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 5 KLQKAGLNISKLGLGTNAVGGHnLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK-RHKLILATK 83
Cdd:cd19145 4 KLGSQGLEVSAQGLGCMGLSGD-YGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGpREKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 GGIQPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLK 163
Cdd:cd19145 83 FGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 164 EANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYKSNFK 243
Cdd:cd19145 163 RAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSHPRFQGENLEKNKV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 244 KVEKLKGIAKENDIEVSHLALAWLLNkEGIDTV-IPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19145 243 LYERVEALAKKKGCTPAQLALAWVLH-QGEDVVpIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-308 |
1.08e-64 |
|
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: 206.65 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGGHNlyadvNEEEGKQLVEEAIQQGITFFDTADSYGV-------GRSEELVGEVLK--GKRHKLILATK 83
Cdd:cd19094 1 VSEICLGTMTWGEQN-----TEAEAHEQLDYAFDEGVNFIDTAEMYPVppspetqGRTEEIIGSWLKkkGNRDKVVLATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 -----GGIQPLLNGETYINNEpsYLRNAVENSLRRLQTDYIDLYYLH-------------FTNPE-----TSYIDSIGEL 140
Cdd:cd19094 76 vagpgEGITWPRGGGTRLDRE--NIREAVEGSLKRLGTDYIDLYQLHwpdrytplfgggyYTEPSeeedsVSFEEQLEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 141 TRLKEEGKIRSIGISNVN----IEQLKEANQHG--HIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGK 214
Cdd:cd19094 154 GELVKAGKIRHIGLSNETpwgvMKFLELAEQLGlpRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 215 YREDFKLNEvDWRqnVNLFE--ENTYKSNFKK--VEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESV 290
Cdd:cd19094 234 YLDGAARPE-GGR--LNLFPgyMARYRSPQALeaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENI 310
|
330
....*....|....*...
gi 446800691 291 KVVDVSLNKRVMKEIQSI 308
Cdd:cd19094 311 DAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-308 |
1.68e-64 |
|
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: 204.00 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLILATKggiqp 88
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGfDREDLFITTK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 89 lLNGETYINNEpsyLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN-- 166
Cdd:cd19072 76 -VSPDHLKYDD---VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQsy 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 -QHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYRedfklnevdwrqnvnlfeentyksnfkkV 245
Cdd:cd19072 152 lKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG----------------------------S 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 246 EKLKGIAKENDIEVSHLALAWLLNKEGIdTVIPGGKRAEQIRESVKVVDVSLNKrvmKEIQSI 308
Cdd:cd19072 204 PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALGWELSE---EDLQRL 262
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-297 |
8.76e-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: 200.53 E-value: 8.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGGHNLYA--DVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK--GKRHKLILATKggiqp 88
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWGygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKelGDRDEVVIATK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 89 lLNGETYINNEPSYLRnAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGE-LTRLKEEGKIRSIGISNVNIEQLKEA-- 165
Cdd:cd19093 77 -FAPLPWRLTRRSVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQIEALMDgLADAVEEGLVRAVGVSNYSADQLRRAhk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 166 --NQHGhIDVV--QSPYNMLERTAEE-ELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNvnlfeentYKS 240
Cdd:cd19093 155 alKERG-VPLAsnQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLF--------GRK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446800691 241 NFKKV----EKLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19093 226 NLEKVqpllDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRL 284
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-293 |
1.53e-59 |
|
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: 190.87 E-value: 1.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGtnavGGHNLYADVNeeegkqLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLI 79
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG----GGGLPRESPE------LLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGlRRDKVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 80 LATKGGIQPLLNGetyinnePSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDS---IGELTRLKEEGKIRSIGIS- 155
Cdd:cd19105 71 LATKASPRLDKKD-------KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNeelLEALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 156 --NVNiEQLKEANQHGHIDVVQSPYNMLERTAE-EELLPYCIEAGIsfipyGPLAFGILGGKYREDFKLNEVdwrqnvnl 232
Cdd:cd19105 144 hdNMA-EVLQAAIESGWFDVIMVAYNFLNQPAElEEALAAAAEKGI-----GVVAMKTLAGGYLQPALLSVL-------- 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446800691 233 feentyksnfkkveklkgiaKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVV 293
Cdd:cd19105 210 --------------------KAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-305 |
1.45e-58 |
|
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: 190.12 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 6 LQKAGLNISKLGLGTNAVGGHNLYAdVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGG 85
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWGWG-ADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATKYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 86 IQPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLH---FTNPETSYIDSIGELTRlkeEGKIRSIGISNVNIEQL 162
Cdd:cd19080 82 MNRRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHawdFTTPVEEVMRALDDLVR---AGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 163 KEANQ----HGH--IDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKY-REDFKLNEVDWRQNVNLFEE 235
Cdd:cd19080 159 ARANTlaelRGWspFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYqRGEEGRAGEAKGVTVGFGKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 236 NtyKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19080 239 T--ERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-292 |
1.44e-56 |
|
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: 183.20 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGGHNLYADvnEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKGK-RHKLILATKGGiQPLLNG 92
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPS--EAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALAGLrRDDLFIATKVG-THGEGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 93 ETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNiEQLKEANQHGHID 172
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG-EELEAAIASGVFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 173 VVQSPYNMLERtAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDfklnevdwrqnvnlfeeNTYKSNFKKVEKLKGIA 252
Cdd:cd19095 155 VVQLPYNVLDR-EEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRR-----------------PLYADYARRPEFAAEIG 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446800691 253 KENDIEvshLALAWLLNKEGIDTVIPGGKRAEQIRESVKV 292
Cdd:cd19095 217 GATWAQ---AALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-291 |
1.26e-55 |
|
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: 181.60 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGGhnLYADVNEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKG-KRHKLILATKGGiqPLLNG 92
Cdd:cd19090 1 SALGLGTAGLGG--VFGGVDDDEAVATIRAALDLGINYIDTAPAYG--DSEERLGLALAElPREPLVLSTKVG--RLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 93 ETYINnePSYLRNAVENSLRRLQTDYIDLYYLHftNPETSYIDS-------IGELTRLKEEGKIRSIGISNVNIEQLKEA 165
Cdd:cd19090 75 TADYS--ADRVRRSVEESLERLGRDRIDLLMIH--DPERVPWVDilapggaLEALLELKEEGLIKHIGLGGGPPDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 166 NQHGHIDVVQS--PYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYrEDFKLNEVDWRQnvnlfeentyKSNFK 243
Cdd:cd19090 151 IETGDFDVVLTanRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRP-PERVRYTYRWLS----------PELLD 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446800691 244 KVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVK 291
Cdd:cd19090 220 RAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVA 267
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-308 |
2.72e-54 |
|
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: 179.38 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 2 KYTKLQKAGLNISKLGLGTNAVGGhnLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILA 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGG--LMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 82 TKGGIQPLLNGETYinnepSYLRNAVENSLRRLQTDYIDLYYLH-----------FTNPETSYIDSIGE----LTRLKEE 146
Cdd:cd19104 79 TKVRLDPDDLGDIG-----GQIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvGGTLSTTDVLGLGGvadaFERLRSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 147 GKIRSIGISNV-NIEQLKEANQHGHIDVVQSPYNMLERTAEE------------ELLPYCIEAGISFIPYGPLAFGILGG 213
Cdd:cd19104 154 GKIRFIGITGLgNPPAIRELLDSGKFDAVQVYYNLLNPSAAEarprgwsaqdygGIIDAAAEHGVGVMGIRVLAAGALTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 214 KyrEDFKLNEVDwrqnvnlFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVV 293
Cdd:cd19104 234 S--LDRGREAPP-------TSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAE 304
|
330
....*....|....*.
gi 446800691 294 DV-SLNKRVMKEIQSI 308
Cdd:cd19104 305 AAgPLPAENLARLEAL 320
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-308 |
3.77e-54 |
|
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: 178.94 E-value: 3.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGtNAVGGHNlyaDVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG---KRHK 77
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFG-SWVTFGN---QVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKElgwPRSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 LILATK---GGIQPLLNgETYINNEpsYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGI 154
Cdd:cd19143 77 YVVSTKifwGGGGPPPN-DRGLSRK--HIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIEQLKEANQ-----HGHIDVVQSP-YNMLERT-AEEELLPYCIEAGISFIPYGPLAFGILGGKYRED------FKL 221
Cdd:cd19143 154 SEWSAQQIEEAHEiadrlGLIPPVMEQPqYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGipegsrLAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 222 NEVDWRQNvNLFEENtyKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDV--SLNK 299
Cdd:cd19143 234 PGYEWLKD-RKEELG--QEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlpKLTP 310
|
....*....
gi 446800691 300 RVMKEIQSI 308
Cdd:cd19143 311 EVMEKIEAI 319
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-291 |
4.79e-54 |
|
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: 176.13 E-value: 4.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 3 YTKLQKAGLNISKLGLGTNAVGghnlyaDVNEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKGKRHKLILAT 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLG------RLSQEEAAAIIRRALDLGINYFDTAPSYG--DSEEKIGKALKGRRDKVFLAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KggiqpllngeTYinnEPSY--LRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGE------LTRLKEEGKIRSIGI 154
Cdd:cd19100 73 K----------TG---ARDYegAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGPggaleaLLEAKEEGKIRFIGI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIEQLKEANQHGHIDVVQSPYNMLERTA---EEELLPYCIEAGISFIPYGPLAFGILggkyredFKLNEVDWRQnvn 231
Cdd:cd19100 140 SGHSPEVLLRALETGEFDVVLFPINPAGDHIdsfREELLPLAREKGVGVIAMKVLAGGRL-------LSGDPLDPEQ--- 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 232 lfeentyksnfkkveklkgiakendievshlALAWLLNKEGIDTVIPGGKRAEQIRESVK 291
Cdd:cd19100 210 -------------------------------ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-294 |
1.16e-52 |
|
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: 174.75 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 3 YTKLQKAGLNISKLGLGTnavgGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYG--VGRSEELVGEVLK----GKRH 76
Cdd:cd19089 1 YRRCGRSGLHLPAISLGL----WHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGppPGSAEENFGRILKrdlrPYRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 77 KLILATKGGI--QPLLNGetyinNEPS--YLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSI 152
Cdd:cd19089 77 ELVISTKAGYgmWPGPYG-----DGGSrkYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 153 GISNVNIEQLKEA----NQHG-HIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWR 227
Cdd:cd19089 152 GISNYPGAKARRAiallRELGvPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 228 QNVNLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19089 232 ESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALK 298
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-297 |
6.09e-52 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 172.64 E-value: 6.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGHNLyadvNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK---GKRHK 77
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDL----SPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKlspSLREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 LILATKGGIQPL----LNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLH----FTNPEtsyidSIGE-LTRLKEEGK 148
Cdd:COG4989 77 IELQTKCGIRLPsearDNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHrpdpLMDPE-----EVAEaFDELKASGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 149 IRSIGISNVN---IEQLK-------EANQhghidvVQ-SPYN--MLertaEEELLPYCIEAGISFIPYGPLAFGILGGKY 215
Cdd:COG4989 152 VRHFGVSNFTpsqFELLQsaldqplVTNQ------IElSLLHtdAF----DDGTLDYCQLNGITPMAWSPLAGGRLFGGF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 216 REDFK-LNEVdwrqnvnlfeentyksnfkkvekLKGIAKENDIEVSHLALAWLLN-KEGIDTVIpGGKRAEQIRESVKVV 293
Cdd:COG4989 222 DEQFPrLRAA-----------------------LDELAEKYGVSPEAIALAWLLRhPAGIQPVI-GTTNPERIKAAAAAL 277
|
....
gi 446800691 294 DVSL 297
Cdd:COG4989 278 DIEL 281
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-297 |
5.40e-51 |
|
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: 170.04 E-value: 5.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGhnLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLI 79
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGG--VFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGiPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 80 LATKGGiQPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHftNPE-TSYID-----SIGELTRLKEEGKIRSIG 153
Cdd:cd19163 79 LATKVG-RYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVH--DIEfAPSLDqilneTLPALQKLKEEGKVRFIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 154 ISNVNIEQLKE--ANQHGHIDVVQS--PYNMLERTAeEELLPYCIEAGISFIPYGPLAFGILGgkyredfklnevdwrqN 229
Cdd:cd19163 156 ITGYPLDVLKEvlERSPVKIDTVLSycHYTLNDTSL-LELLPFFKEKGVGVINASPLSMGLLT----------------E 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 230 VNLFEENTYKSNFKKV-EKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19163 219 RGPPDWHPASPEIKEAcAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPL 287
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-311 |
1.19e-50 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 171.16 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGtnavGGHnlYADVNEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKGKRHKLIL 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFG----GMR--LPRKDEEEAEALIRRAIDNGINYIDTARGYG--DSEEFLGKALKGPRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKggiqplLNGETyinNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGE------LTRLKEEGKIRSIGI 154
Cdd:COG1453 73 ATK------LPPWV---RDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPggaleaLEKAKAEGKIRHIGF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SN-VNIEQLKEANQHGHIDVVQSPYNMLERT--AEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRqnvn 231
Cdd:COG1453 144 SThGSLEVIKEAIDTGDFDFVQLQYNYLDQDnqAGEEALEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLCPPLS---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 232 lfeentyksnfkkveklkgiakendieVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD--VSLN-------KRVM 302
Cdd:COG1453 220 ---------------------------PAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTeeelailERLA 272
|
....*....
gi 446800691 303 KEIQSILED 311
Cdd:COG1453 273 EELGELLKD 281
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-305 |
1.21e-46 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 158.12 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGHnLYADVN-EEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLILATKggIQ 87
Cdd:cd19137 1 GEKIPALGLGTWGIGGF-LTPDYSrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDfPREDLFIVTK--VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 88 PllngeTYINNEPsyLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQ 167
Cdd:cd19137 78 P-----TNLRYDD--LLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 168 HGHIDVV--QSPYNMLERTAEEE-LLPYCIEAGISFIPYGPLAFGILggkyredfklnevdwrqnvnlfeentyksnfKK 244
Cdd:cd19137 151 KSQTPIVcnQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLE-------------------------------KT 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446800691 245 VEKLKGIAKENDIEVSHLALAWLLNKEGIDTvIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19137 200 NRTLEEIAKNYGKTIAQIALAWLIQKPNVVA-IPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-305 |
1.63e-46 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 157.52 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGhnlyadvneEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKggi 86
Cdd:COG0656 2 GVEIPALGLGTWQLPG---------EEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAAsgvPREELFVTTK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 qpLLNGetyiNNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETsYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN 166
Cdd:COG0656 67 --VWND----NHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPGP-YVETWRALEELYEEGLIRAIGVSNFDPEHLEELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 QH--GHIDVVQ---SPYNmlertAEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvNLFEEntyksn 241
Cdd:COG0656 140 AEtgVKPAVNQvelHPYL-----QQRELLAFCREHGIVVEAYSPLGRG---------------------KLLDD------ 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 242 fkkvEKLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:COG0656 188 ----PVLAEIAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDAFDFELSDEDMAAI 245
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-294 |
3.36e-46 |
|
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: 157.71 E-value: 3.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGGhnlyaDVNEEEGKQLVEEAIQQGITFFDTADSYG----VGRSEELVGEVLK--GKRHKLILATKGGIq 87
Cdd:cd19082 1 SRIVLGTADFGT-----RIDEEEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKsrGNRDKVVIATKGGH- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 88 PLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSyIDSI-GELTRLKEEGKIRSIGISNVNIEQLKEAN 166
Cdd:cd19082 75 PDLEDMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVP-VGEIvDTLNELVRAGKIRAFGASNWSTERIAEAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 ----QHGH------------IDVVQSPYN--MLERTAEEELLPYCiEAGISFIPYGPLAFGILGGKYREdfklnevDWRQ 228
Cdd:cd19082 154 ayakAHGLpgfaasspqwslARPNEPPWPgpTLVAMDEEMRAWHE-ENQLPVFAYSSQARGFFSKRAAG-------GAED 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 229 NVNLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEgIDTV-IPGGKRAEQIRESVKVVD 294
Cdd:cd19082 226 DSELRRVYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQP-FPTVpIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-307 |
4.61e-46 |
|
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: 157.50 E-value: 4.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 11 LNISKLGLGTNA-----VGGHNLYAD-VNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-KRHKLILATK 83
Cdd:cd19103 2 KKLPKIALGTWSwgsggAGGDQVFGNhLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRyPREDYIISTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 ggIQPLLNGetyinNEPSYLRNAVENSLRRLQTDYIDLYYLHftNPeTSYIDSIGELTRLKEEGKIRSIGISNVNIEQLK 163
Cdd:cd19103 82 --FTPQIAG-----QSADPVADMLEGSLARLGTDYIDIYWIH--NP-ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 164 EAN----QHG-HIDVVQSPYNMLERTAEEE-LLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQnvnlfeeNT 237
Cdd:cd19103 152 RANeilaKAGvSLSAVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSGRA-------ET 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 238 YKSNFKKVEKL----KGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQS 307
Cdd:cd19103 225 YNPLLPQLEELtavmAEIGAKHGASIAQVAIAWAIAK-GT-TPIIGVTKPHHVEDAARAASITLTDDEIKELEQ 296
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-309 |
1.18e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 156.60 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 24 GGHNLYADvnEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKGKRHKLILATKggIQPLL-----NGETYINn 98
Cdd:cd19101 14 GGHGGIRD--EDAAVRAMAAYVDAGLTTFDCADIYG--PAEELIGEFRKRLRRERDAADD--VQIHTkwvpdPGELTMT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 99 ePSYLRNAVENSLRRLQTDYIDLYYLHFTNPE-TSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGhIDVV--Q 175
Cdd:cd19101 87 -RAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSdPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG-VPIVsnQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 176 SPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREdfkLNEVDWRQNvnlfeENTYKSNFKKV---------- 245
Cdd:cd19101 165 VQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLG---VPEPTGPAL-----ETRSLQKYKLMidewggwdlf 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 246 ----EKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSIL 309
Cdd:cd19101 237 qellRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAVL 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-291 |
1.22e-45 |
|
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: 156.56 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 18 LGTNAVGGHNLYADVneEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGKRhKLILATKggIQPLLNGetyiN 97
Cdd:cd19075 5 LGTMTFGSQGRFTTA--EAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGER-GFKIDTK--ANPGVGG----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 98 NEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKE----ANQHGHI-- 171
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEiveiCKENGWVlp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 172 DVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDfklnevDWRQNVNLFEENT---------Y--KS 240
Cdd:cd19075 156 TVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYS------EDKAGGGRFDPNNalgklyrdrYwkPS 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446800691 241 NFKKVEKLKGIAKENDIEVSHLALAWL-----LNKEGIDTVIPGGKRAEQIRESVK 291
Cdd:cd19075 230 YFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLA 285
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-294 |
1.95e-44 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 153.26 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGV-------GRSEELVGEVLK--GKRHKLILATKG 84
Cdd:cd19752 1 SELCLGTMYFG-----TRTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKdrGNRDDVVIATKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 85 GIQPLLNGETYINNE---PSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQ 161
Cdd:cd19752 76 GAGPRDPDGGPESPEglsAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 162 LKEANQHGH------IDVVQSPYNML----------ERTAEEELLPYCIEAG-ISFIPYGPLafgiLGGKY-REDFKLNE 223
Cdd:cd19752 156 LERARQIARqqgwaeFSAIQQRHSYLrprpgadfgvQRIVTDELLDYASSRPdLTLLAYSPL----LSGAYtRPDRPLPE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 224 vDWRQnvnlfeentyKSNFKKVEKLKGIAKENDIEVSHLALAWLLNkeGIDTVIP--GGKRAEQIRESVKVVD 294
Cdd:cd19752 232 -QYDG----------PDSDARLAVLEEVAGELGATPNQVVLAWLLH--RTPAIIPllGASTVEQLEENLAALD 291
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-299 |
6.92e-44 |
|
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: 151.55 E-value: 6.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 8 KAGLNISKLGLGTNAVGGHNLYAdvneEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK---GKRHKLILATKG 84
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESA----EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALAlnpGLREKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 85 GI----QPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLH----FTNPEtsyidSIGE-LTRLKEEGKIRSIGIS 155
Cdd:cd19092 77 GIrlgdDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHrpdpLMDPE-----EVAEaFDELVKSGKVRYFGVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 156 NVNIEQLKEANQHGHIDVV--QSPYNMLERTA-EEELLPYCIEAGISFIPYGPLAFGIL-GGKYREDFKLNEVdwrqnvn 231
Cdd:cd19092 152 NFTPSQIELLQSYLDQPLVtnQIELSLLHTEAiDDGTLDYCQLLDITPMAWSPLGGGRLfGGFDERFQRLRAA------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 232 lfeentyksnfkkvekLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNK 299
Cdd:cd19092 225 ----------------LEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTR 276
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-306 |
1.56e-43 |
|
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: 150.85 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 9 AGLNISKLGLGTNAVGGHnlYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGR---SEELVGEVLKG---KRHKLILAT 82
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDphaNLKLLARFFRKypeYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KGGiqplLNGETYI-NNEPSYLRNAVENSLRRL-QTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIE 160
Cdd:cd19077 79 KGG----LDPDTLRpDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 161 QLKEANQHGHIDVVQSPYNMLERTAEE-ELLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEVDWRQNVNLFEENTYK 239
Cdd:cd19077 155 TIRRAHAVHPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFNGENFE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 240 SNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTV-IPGGKRAEQIRESVKVVDVSLNKRVMKEIQ 306
Cdd:cd19077 235 KNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-305 |
3.34e-43 |
|
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: 148.78 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKggiqpL 89
Cdd:cd19071 1 MPLIGLGT---------YKLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIREsgvPREELFITTK-----L 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 90 LNgetyINNEPSYLRNAVENSLRRLQTDYIDLYYLHF------TNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLK 163
Cdd:cd19071 64 WP----TDHGYERVREALEESLKDLGLDYLDLYLIHWpvpgkeGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 164 EANQHGHI--DVVQ---SPYNmlertAEEELLPYCIEAGISFIPYGPLAfgilggkyredfklnevdwRQNVNLFEEnty 238
Cdd:cd19071 140 ELLAAARIkpAVNQielHPYL-----QQKELVEFCKEHGIVVQAYSPLG-------------------RGRRPLLDD--- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 239 ksnfkkvEKLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19071 193 -------PVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
10-305 |
1.28e-42 |
|
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: 147.78 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVG-GHNLYADvnEEEGKQLveeAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKggIQP 88
Cdd:cd19138 8 GTKVPALGQGTWYMGeDPAKRAQ--EIEALRA---GIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVSK--VLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 89 llngetyINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTN----PETsyidsIGELTRLKEEGKIRSIGISNVNIEQLKE 164
Cdd:cd19138 81 -------SNASRQGTVRACERSLRRLGTDYLDLYLLHWRGgvplAET-----VAAMEELKKEGKIRAWGVSNFDTDDMEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 165 ANQ---HGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvNLFEENTYKSn 241
Cdd:cd19138 149 LWAvpgGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQG---------------------GLLRRGLLEN- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 242 fkkvEKLKGIAKENDIEVSHLALAWLLNKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19138 207 ----PTLKEIAARHGATPAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-294 |
6.13e-42 |
|
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: 147.16 E-value: 6.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 2 KYTKLQKAGLNISKLGLGTnavgGHNlYADVNE-EEGKQLVEEAIQQGITFFDTADSYG--VGRSEELVGEVLK----GK 74
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGL----WHN-FGDVDRyENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKedlkPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 75 RHKLILATKGGiQPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGI 154
Cdd:cd19151 76 RDELIISTKAG-YTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIEQLKEA----NQHGHIDVVQSP-YNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYredfkLNEV--DWR 227
Cdd:cd19151 155 SNYPPEEAREAaailKDLGTPCLIHQPkYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRY-----LNGIpeDSR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 228 ---QNVNLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19151 230 aakGSSFLKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-305 |
2.81e-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: 143.57 E-value: 2.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKggIQPl 89
Cdd:cd19073 1 IPALGLGT---------WQLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAEsgvPREDLFITTK--VWR- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 90 lngetyINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHG 169
Cdd:cd19073 66 ------DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDIS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 170 H--IDVVQSPYNMLERtaEEELLPYCIEAGISFIPYGPLAFGilggkyrEDFklnevdwrqnvnlfeentyksnfkKVEK 247
Cdd:cd19073 140 PlpIAVNQVEFHPFLY--QAELLEYCRENDIVITAYSPLARG-------EVL------------------------RDPV 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 248 LKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19073 187 IQEIAEKYDKTPAQVALRWLVQK-GI-VVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-296 |
4.27e-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: 144.67 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGghNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK-RHKLILATKGG--IQPLL 90
Cdd:cd19152 1 PKLGFGTAPLG--NLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELgREDYVISTKVGrlLVPLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 91 NGET-----YINNEP-------SY--LRNAVENSLRRLQTDYIDLYYLHftNPETSYI-------------DSIGELTRL 143
Cdd:cd19152 79 EVEPtfepgFWNPLPfdavfdySYdgILRSIEDSLQRLGLSRIDLLSIH--DPDEDLAgaesdehfaqaikGAFRALEEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 144 KEEGKIRSIGISnVNIEQ-LKEANQHGHIDVVQSP--YNMLERTAEEELLPYCIEAGISFIPYGPLAFGIL-GGKYREDF 219
Cdd:cd19152 157 REEGVIKAIGLG-VNDWEvILRILEEADLDWVMLAgrYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLaGGDNFDYY 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 220 KLNEVDwrQNVnlfeentyksnFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVS 296
Cdd:cd19152 236 EYGPAP--PEL-----------IARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATE 299
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-290 |
5.86e-41 |
|
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: 144.39 E-value: 5.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGghNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK-RHKLILATKGG--IQP-- 88
Cdd:cd19161 1 SELGLGTAGLG--NLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKpRDEFVLSTKVGrlLKPar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 89 ---LLNGETYINNEP-------SY---LRnAVENSLRRLQTDYIDLYYLH----FTNPETSYIDSIGELTR--------L 143
Cdd:cd19161 79 egsVPDPNGFVDPLPfeivydySYdgiMR-SFEDSLQRLGLNRIDILYVHdigvYTHGDRKERHHFAQLMSggfkaleeL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 144 KEEGKIRSIGISNVNIEQLKEANQHGHID--VVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDFKL 221
Cdd:cd19161 158 KKAGVIKAFGLGVNEVQICLEALDEADLDcfLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSGAKF 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 222 NEVDWRQNVnlfeentyksnFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESV 290
Cdd:cd19161 238 NYGDAPAEI-----------ISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNV 295
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-291 |
8.93e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 144.38 E-value: 8.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 11 LNISKLGLGTnAVGGHNLYADvneEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG-------KRHKLILATK 83
Cdd:cd19099 1 LTLSSLGLGT-YRGDSDDETD---EEYREALKAALDSGINVIDTAINYRGGRSERLIGKALREliekggiKRDEVVIVTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 GG-IQP----LLNGETYINNE-------------------PSYLRNAVENSLRRLQTDYIDLYYLHftNPETS------- 132
Cdd:cd19099 77 AGyIPGdgdePLRPLKYLEEKlgrglidvadsaglrhcisPAYLEDQIERSLKRLGLDTIDLYLLH--NPEEQllelgee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 133 -YIDSIGE----LTRLKEEGKIRSIGIS-------------------NVNIEQLKEANQHgHIDVVQSPYNMLERTAEEE 188
Cdd:cd19099 155 eFYDRLEEafeaLEEAVAEGKIRYYGIStwdgfrappalpghlslekLVAAAEEVGGDNH-HFKVIQLPLNLLEPEALTE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 189 ----------LLPYCIEAGISFIPYGPLAFGILGGKYREDFKLNEvdwrqnvnlfeentyksnfkkveklkgiakENDIE 258
Cdd:cd19099 234 kntvkgealsLLEAAKELGLGVIASRPLNQGQLLGELRLADLLAL------------------------------PGGAT 283
|
330 340 350
....*....|....*....|....*....|...
gi 446800691 259 VSHLALAWLLNKEGIDTVIPGGKRAEQIRESVK 291
Cdd:cd19099 284 LAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
9-310 |
1.33e-40 |
|
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: 144.10 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 9 AGLNISKLGLGTNAVGG--HNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK--GKRHKLILATKG 84
Cdd:cd19146 7 AGVRVSPLCLGAMSFGEawKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMAsrGNRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 85 GIQPLLNGE-----TYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNI 159
Cdd:cd19146 87 TTGYRRGGPikiksNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 160 EQLKEANQ----HG--HIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAfgilGGKYR--EDFKLNEVDWRQNVN 231
Cdd:cd19146 167 WVVSKANAyaraHGltQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLG----QGQFRteEEFKRRGRSGRKGGP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 232 LFEENtyksnfKKV-EKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSILE 310
Cdd:cd19146 243 QTEKE------RKVsEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAYP 316
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-308 |
1.50e-39 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 141.91 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGHNLYADVNEEegkqlVEEAIQQGITFFDTADSYGV-------GRSEELVGEVLK- 72
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQ-----LDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 73 -GKRHKLILATK-GGiqPLLNGETYINNEPSY----LRNAVENSLRRLQTDYIDLYYLHF----TN-------------P 129
Cdd:PRK10625 76 rGSREKLIIASKvSG--PSRNNDKGIRPNQALdrknIREALHDSLKRLQTDYLDLYQVHWpqrpTNcfgklgyswtdsaP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 130 ETSYIDSIGELTRLKEEGKIRSIGISN------VNIEQLKEANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPY 203
Cdd:PRK10625 154 AVSLLETLDALAEQQRAGKIRYIGVSNetafgvMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 204 GPLAFGILGGKYREDFKlnEVDWRqnvnlfeeNTYKSNF---------KKVEKLKGIAKENDIEVSHLALAWLLNKEGID 274
Cdd:PRK10625 234 SCLAFGTLTGKYLNGAK--PAGAR--------NTLFSRFtrysgeqtqKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVA 303
|
330 340 350
....*....|....*....|....*....|....
gi 446800691 275 TVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:PRK10625 304 STLLGATTMEQLKTNIESLHLTLSEEVLAEIEAV 337
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-308 |
2.15e-38 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 136.23 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGhnlyadvneEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKGGI 86
Cdd:cd19140 5 GVRIPALGLGTYPLTG---------EECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAAsgvPRDELFLTTKVWP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 QpllngetyiNNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN 166
Cdd:cd19140 73 D---------NYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 QHGHIDVV--QSPYN-MLERTAeeeLLPYCIEAGISFIPYGPLAfgilGGKYREDFKLNEvdwrqnvnlfeentyksnfk 243
Cdd:cd19140 144 ELSEAPLFtnQVEYHpYLDQRK---LLDAAREHGIALTAYSPLA----RGEVLKDPVLQE-------------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446800691 244 kveklkgIAKENDIEVSHLALAWLLNKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19140 197 -------IGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-294 |
4.36e-37 |
|
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: 132.68 E-value: 4.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTnavggHNL----YADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK-GKRHKLILATKGGiqp 88
Cdd:cd19096 1 SVLGFGT-----MRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKeGPREKFYLATKLP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 89 llngeTYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYI-----DSIGELTRLKEEGKIRSIGIS-NVNIEQL 162
Cdd:cd19096 73 -----PWSVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEkarkgGLLEFLEKAKKEGLIRHIGFSfHDSPELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 163 KEANQHGHIDVVQSPYNML--ERTAEEELLPYCIEAGISFIPYGPLAFGILGgkyredfklnevdwrqnvnlfeentyks 240
Cdd:cd19096 148 KEILDSYDFDFVQLQYNYLdqENQAGRPGIEYAAKKGMGVIIMEPLKGGGLA---------------------------- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446800691 241 nfKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19096 200 --NNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-294 |
4.48e-37 |
|
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: 134.50 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 2 KYTKLQKAGLNISKLGLGTnavgGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYG--VGRSEELVGEVLK----GKR 75
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGL----WHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILRedfaGYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 76 HKLILATKGGIQpLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGIS 155
Cdd:cd19150 77 DELIISTKAGYD-MWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 156 NVNIEQLKEA----NQHGHIDVVQSP-YNMLERTAEE-ELLPYCIEAGISFIPYGPLAFGILGGKYredfkLNEV--DWR 227
Cdd:cd19150 156 SYSPERTREAaailRELGTPLLIHQPsYNMLNRWVEEsGLLDTLQELGVGCIAFTPLAQGLLTDKY-----LNGIpeGSR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 228 QNV--NLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19150 231 ASKerSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALD 299
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-290 |
1.13e-36 |
|
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: 132.87 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVGGHnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK-RHKLILATKGGIQPLLNG 92
Cdd:cd19162 1 PRLGLGAASLGNL---ARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHpRAEYVVSTKVGRLLEPGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 93 ETYINNEPSYL-------RNAVENSLRRLQTDYIDLYYLHftNPETSYIDSIGE----LTRLKEEGKIRSIGISNVNIEQ 161
Cdd:cd19162 78 AGRPAGADRRFdfsadgiRRSIEASLERLGLDRLDLVFLH--DPDRHLLQALTDafpaLEELRAEGVVGAIGVGVTDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 162 LKEANQHGHIDVV--QSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKYREDfklNEVDWRQnvnLFEENTyk 239
Cdd:cd19162 156 LLRAARRADVDVVmvAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAG---DRYDYRP---ATPEVL-- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446800691 240 snfKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESV 290
Cdd:cd19162 228 ---ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNL 275
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-294 |
4.70e-35 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 127.64 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGT----------NAVGGhnlyadVNEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKGKrHKLILATK 83
Cdd:cd19097 1 SKLALGTaqfgldygiaNKSGK------PSEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKRL-DKFKIITK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 ggIQPLLNGETYINNEpsyLRNAVENSLRRLQTDYIDLYYLHftNPETSYIDS---IGELTRLKEEGKIRSIGISNVNIE 160
Cdd:cd19097 72 --LPPLKEDKKEDEAA---IEASVEASLKRLKVDSLDGLLLH--NPDDLLKHGgklVEALLELKKEGLIRKIGVSVYSPE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 161 QLKEANQHGHIDVVQSPYNMLERTAEEE-LLPYCIEAGISFIpygplA---F--GILggkyredfklnevdwrqnvnLFE 234
Cdd:cd19097 145 ELEKALESFKIDIIQLPFNILDQRFLKSgLLAKLKKKGIEIH-----ArsvFlqGLL--------------------LME 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 235 ENTYKSNFKK----VEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19097 200 PDKLPAKFAPakplLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-309 |
9.70e-34 |
|
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: 125.97 E-value: 9.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGhnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK---RHK 77
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFG----GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrRSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 LILATK---GGiqpllNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGI 154
Cdd:cd19158 77 LVITTKifwGG-----KAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIEQLKEA----NQHGHIDVV--QSPYNMLERTAEEELLPYCI-EAGISFIPYGPLAFGILGGKYREDF------KL 221
Cdd:cd19158 152 SRWSSMEIMEAysvaRQFNLIPPIceQAEYHMFQREKVEVQLPELFhKIGVGAMTWSPLACGIVSGKYDSGIppysraSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 222 NEVDWRQNVNLFEENTYKSnfKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDV--SLNK 299
Cdd:cd19158 232 KGYQWLKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSS 309
|
330
....*....|
gi 446800691 300 RVMKEIQSIL 309
Cdd:cd19158 310 SIVHEIDSIL 319
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-309 |
1.94e-33 |
|
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: 125.10 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGhnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK---RHK 77
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFG----SQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKgwrRSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 LILATK---GGiqpllNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGI 154
Cdd:cd19160 79 YVVTTKiywGG-----QAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIEQLKE----ANQHGHIDVV--QSPYNMLERTAEEELLPYCI-EAGISFIPYGPLAFGILGGKYREDF------KL 221
Cdd:cd19160 154 SRWSAMEIMEaysvARQFNLIPPVceQAEYHLFQREKVEMQLPELYhKIGVGSVTWSPLACGLITGKYDGRVpdtcraAV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 222 NEVDWRQNVNLFEENtyKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDV--SLNK 299
Cdd:cd19160 234 KGYQWLKEKVQSEEG--KKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTP 311
|
330
....*....|
gi 446800691 300 RVMKEIQSIL 309
Cdd:cd19160 312 QTVMEIDALL 321
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-295 |
8.43e-33 |
|
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: 122.94 E-value: 8.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 2 KYTKLQKAGLNISKLGLGTNAVGGHNLYADVNEEegkqLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK---RHKL 78
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEE----LVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKgwrRSSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 79 ILATK---GGiqpllNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGIS 155
Cdd:cd19141 77 VITTKifwGG-----KAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 156 NVNIEQLKE----ANQHGHID--VVQSPYNMLERTAEEELLPYCIEA-GISFIPYGPLAFGILGGKYREDF------KLN 222
Cdd:cd19141 152 RWSAMEIMEaysvARQFNLIPpiVEQAEYHLFQREKVEMQLPELFHKiGVGAMTWSPLACGILSGKYDDGVpeysraSLK 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 223 EVDWRQNVNLFEENTYKSNfkKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDV 295
Cdd:cd19141 232 GYQWLKEKILSEEGRRQQA--KLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-309 |
3.84e-32 |
|
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: 121.69 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGHNLYADVNEeegkQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK---RHK 77
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAE----RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 LILATK---GGiqpllNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGI 154
Cdd:cd19159 77 LVITTKlywGG-----KAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIEQLKE----ANQHGHIDVV--QSPYNMLERTAEEELLPYCI-EAGISFIPYGPLAFGILGGKYREDF------KL 221
Cdd:cd19159 152 SRWSAMEIMEaysvARQFNMIPPVceQAEYHLFQREKVEVQLPELYhKIGVGAMTWSPLACGIISGKYGNGVpessraSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 222 NEVDWRQNVNLFEENTYKSNfkKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDV--SLNK 299
Cdd:cd19159 232 KCYQWLKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTS 309
|
330
....*....|
gi 446800691 300 RVMKEIQSIL 309
Cdd:cd19159 310 HVVNEIDNIL 319
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-310 |
3.48e-31 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 118.73 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 3 YTKLQKAGLNISKLGLGTNAVGghNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK---RHKLI 79
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLG--SVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgipREKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 80 LATKGGiqplLNGETYINNEPSYLRnAVENSLRRLQTDYIDLYYLH---FTNPETSYIDSIGELTRLKEEGKIRSIGISN 156
Cdd:PLN02587 79 VSTKCG----RYGEGFDFSAERVTK-SVDESLARLQLDYVDILHCHdieFGSLDQIVNETIPALQKLKESGKVRFIGITG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 157 VNIEQLK---EANQHGHIDVVQS-PYNMLERTAEEELLPYCIEAGISFIPYGPLAFGILGGKyredfklNEVDWRQNVNL 232
Cdd:PLN02587 154 LPLAIFTyvlDRVPPGTVDVILSyCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTEN-------GPPEWHPAPPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 233 FEENTYKSNFKKVEKLKGIAKendievshLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD----VSLNKRVMKEIQSI 308
Cdd:PLN02587 227 LKSACAAAATHCKEKGKNISK--------LALQYSLSNKDISTTLVGMNSVQQVEENVAAATeletSGIDEELLSEVEAI 298
|
..
gi 446800691 309 LE 310
Cdd:PLN02587 299 LA 300
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-311 |
5.51e-31 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 118.94 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGHNLYADVNeeegKQLVEEAIQQGITFFDTADSYG--VGRSEELVGEVLKGK---- 74
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQ----RAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfaay 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 75 RHKLILATKGGIQpLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGI 154
Cdd:PRK09912 89 RDELIISTKAGYD-MWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 155 SNVNIE---QLKEANQHGHIDVV--QSPYNMLERTAEEE-LLPYCIEAGISFIPYGPLAFGILGGKY----REDFKLNEv 224
Cdd:PRK09912 168 SSYSPErtqKMVELLREWKIPLLihQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYlngiPQDSRMHR- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 225 DWRQNVNLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVV-DVSLNKRVMK 303
Cdd:PRK09912 247 EGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALnNLTFSTEELA 326
|
....*...
gi 446800691 304 EIQSILED 311
Cdd:PRK09912 327 QIDQHIAD 334
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-311 |
6.40e-30 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 115.64 E-value: 6.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKAGLNISKLGLGTNAVGGHNLYADVNEEegkqLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKGK---RHK 77
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEE----IVTLAYENGINYFDTSDAFTSGQAETELGRILKKKgwkRSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 LILATKggiqpllngeTYINNEPS-------YLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIR 150
Cdd:cd19142 77 YIVSTK----------IYWSYGSEerglsrkHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 151 SIGI---SNVNI-EQLKEANQHGHIDVV--QSPYNMLERTAEEELLPYCI-EAGISFIPYGPLAFGILGGKYREDFKLne 223
Cdd:cd19142 147 YWGTsrwSPVEImEAFSIARQFNCPTPIceQSEYHMFCREKMELYMPELYnKVGVGLITWSPLSLGLDPGISEETRRL-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 224 VDWRQNVNLFEENTYKSNFK---------KVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19142 225 VTKLSFKSSKYKVGSDGNGIheetrrashKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQ 304
|
330
....*....|....*....
gi 446800691 295 V--SLNKRVMKEIQSILED 311
Cdd:cd19142 305 LlpKLNSAVMEELERILDN 323
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
5-294 |
7.35e-30 |
|
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: 114.94 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 5 KLQKAGLNISKLGLGTNAVGGhnLYAD-VNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLKG---KRHKLIL 80
Cdd:cd19153 4 TLEIALGNVSPVGLGTAALGG--VYGDgLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAAlqvPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKGGiqplLNGETYINNEPSYLRNAVENSLRRLQTDYIDLYYLH---FTNPETSYIDSIGELTRLKEEGKIRSIGISNV 157
Cdd:cd19153 82 ATKVG----RYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 158 NIEQLKEANQH---GHIDVVQSPYNM-LERTAEEELLPYCIEA-GISFIPYGPLAFGILGGKYREDFKLNEVDWRQnvnl 232
Cdd:cd19153 158 PLDTLTRATRRcspGSLDAVLSYCHLtLQDARLESDAPGLVRGaGPHVINASPLSMGLLTSQGPPPWHPASGELRH---- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 233 feentYKSNFKKVeklkgiAKENDIEVSHLALAWLL-NKEGIDTVIPGGKRAEQIRESVKVVD 294
Cdd:cd19153 234 -----YAAAADAV------CASVEASLPDLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-305 |
3.53e-28 |
|
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: 109.63 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgGHNLYADVNEEEGKQLVE---EAIQQGITFFDTADSYGvgrSEELVGEVLK---GKRHKLILATK 83
Cdd:cd19120 1 GSKIPAIAFGT----GTAWYKSGDDDIQRDLVDsvkLALKAGFRHIDTAEMYG---NEKEVGEALKesgVPREDLFITTK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 ggiqpllngetYINNEPSyLRNAVENSLRRLQTDYIDLYYLHF----TNPETSYIDSIGELTRLKEEGKIRSIGISNVNI 159
Cdd:cd19120 74 -----------VSPGIKD-PREALRKSLAKLGVDYVDLYLIHSpffaKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 160 EQLKEANQHGHI--DVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGIlggkYREDFKLNEVdwrqnvnlfeent 237
Cdd:cd19120 142 EDLEELLDTAKIkpAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLSPLT----RDAGGPLDPV------------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 238 yksnfkkvekLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19120 205 ----------LEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
9-306 |
5.96e-28 |
|
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: 110.30 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 9 AGLNISKLGLGTNAVGG--HNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGVGRSEELVGEVLK--GKRHKLILATKG 84
Cdd:cd19147 6 AGIRVSPLILGAMSIGDawSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKsrKNRDQIVIATKF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 85 GIQPLLNGE------TYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETSYIDSIGELTRLKEEGKIRSIGISNVN 158
Cdd:cd19147 86 TTDYKAYEVgkgkavNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 159 IEQLKEAN----QHGH--IDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAfgilGGKY-----REDFKLNEVDWR 227
Cdd:cd19147 166 AWVVSAANyyatAHGKtpFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLG----GGKFqskkaVEERKKNGEGLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 228 QNVNLFEENtyKSNFKKVEKLKGIAKENDIE-VSHLALAWLLNKEGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQ 306
Cdd:cd19147 242 SFVGGTEQT--PEEVKISEALEKVAEEHGTEsVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-308 |
2.10e-27 |
|
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: 107.33 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 16 LGLGTNAVGGhnlyadvnEEEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKG-------KRHKLILATKGGiqp 88
Cdd:cd19136 4 LGLGTFRLRG--------EEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDllpkyglSREDIFITSKLA--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 89 llngetyinnePSYL-----RNAVENSLRRLQTDYIDLYYLHF--------TNPETS--YIDSIGELTRLKEEGKIRSIG 153
Cdd:cd19136 70 -----------PKDQgyekaRAACLGSLERLGTDYLDLYLIHWpgvqglkpSDPRNAelRRESWRALEDLYKEGKLRAIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 154 ISNVNIEQLKEANQHGHID--VVQSPYN-MLERtaeEELLPYCIEAGISFIPYGPLAFGILggkyredfklnevdwrqnv 230
Cdd:cd19136 139 VSNYTVRHLEELLKYCEVPpaVNQVEFHpHLVQ---KELLKFCKDHGIHLQAYSSLGSGDL------------------- 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446800691 231 NLFEENTyksnfkkvekLKGIAKENDIEVSHLALAWLLnKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19136 197 RLLEDPT----------VLAIAKKYGRTPAQVLLRWAL-QQGI-GVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-308 |
3.20e-27 |
|
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: 107.02 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGHNLYAdvneeegkqlVEEAIQQ-GITFFDTADSYGVgrsEELVGEVLKG---KRHKLILATKgg 85
Cdd:cd19135 10 GVEMPILGLGTSHSGGYSHEA----------VVYALKEcGYRHIDTAKRYGC---EELLGKAIKEsgvPREDLFLTTK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 86 iqpLLNGETYINNepsyLRNAVENSLRRLQTDYIDLYYLHFTNPETSyIDSIGELTR--------LKEEGKIRSIGISNV 157
Cdd:cd19135 75 ---LWPSDYGYES----TKQAFEASLKRLGVDYLDLYLLHWPDCPSS-GKNVKETRAetwraleeLYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 158 NIEQLKEANQHGHI--DVVQSPYNMLERtaEEELLPYCIEAGISFIPYGPLAFGILggkyredfkLNEvdwrqnvnlfee 235
Cdd:cd19135 147 LIEHLEQLLEDCSVvpHVNQVEFHPFQN--PVELIEYCRDNNIVFEGYCPLAKGKA---------LEE------------ 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800691 236 ntyksnfKKVEKlkgIAKENDIEVSHLALAWLLnKEGIDTvIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19135 204 -------PTVTE---LAKKYQKTPAQILIRWSI-QNGVVT-IPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-305 |
3.27e-27 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 106.67 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGGhnlyadvneEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKGGIqpl 89
Cdd:cd19139 1 IPAFGLGTFRLKD---------DVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAEsgvPRDELFITTKIWI--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 90 lngetyINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNP--ETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQ 167
Cdd:cd19139 66 ------DNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 168 ---HGHIDVVQ---SPYnMLERTaeeeLLPYCIEAGISFIPYGPLAFGILGgkyredfklnevdwrqnvnlfeentyksn 241
Cdd:cd19139 140 vvgAGAIATNQielSPY-LQNRK----LVAHCKQHGIHVTSYMTLAYGKVL----------------------------- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 242 fkKVEKLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19139 186 --DDPVLAAIAERHGATPAQIALAWAMARGYA--VIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-308 |
2.03e-24 |
|
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: 99.37 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKggi 86
Cdd:cd19131 7 GNTIPQLGLGV---------WQVSNDEAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRAsgvPREELFITTK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 qpLLNGEtyiNNEPSYLRnAVENSLRRLQTDYIDLYYLHFTNP-ETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKE- 164
Cdd:cd19131 72 --LWNSD---QGYDSTLR-AFDESLRKLGLDYVDLYLIHWPVPaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 165 ANQHGHIDVVqspyNMLE---RTAEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvNLFEENTyksn 241
Cdd:cd19131 146 IDETGVVPVV----NQIElhpRFQQRELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPV---- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 242 fkkvekLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19131 197 ------IGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-308 |
2.29e-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: 96.49 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGhnlyadvnEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKGGI 86
Cdd:cd19133 6 GVEMPILGFGVFQIPD--------PEECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKsgiPREELFITTKLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 QpllngETYINNEPSylrnAVENSLRRLQTDYIDLYYLHftNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN 166
Cdd:cd19133 75 Q-----DAGYEKAKK----AFERSLKRLGLDYLDLYLIH--QPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 QHGHID--VVQ---SPYNMlertaEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqNVNLFEEntyksn 241
Cdd:cd19133 144 LHNEVKpaVNQietHPFNQ-----QIEAVEFLKKYGVQIEAWGPFAEG-------------------RNNLFEN------ 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 242 fkkvEKLKGIAKENDIEVSHLALAWLLnKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19133 194 ----PVLTEIAEKYGKSVAQVILRWLI-QRGI-VVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-308 |
2.30e-23 |
|
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: 97.48 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 8 KAGLNISKLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLK-------GKRHKLIL 80
Cdd:cd19154 7 SNGVKMPLIGLGT---------WQSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAelleegvVKREDLFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKggiqpLLNGETyinnEPSYLRNAVENSLRRLQTDYIDLYYLH----FTNPETSYIDSIG---------------ELT 141
Cdd:cd19154 75 TTK-----LWTHEH----APEDVEEALRESLKKLQLEYVDLYLIHapaaFKDDEGESGTMENgmsihdavdvedvwrGME 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 142 RLKEEGKIRSIGISNVNIEQLKEANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPlafgiLGGKYREDFKL 221
Cdd:cd19154 146 KVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYAT-----LGSPGRANFTK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 222 NEVDWRQNVNLFEENtyksnfkkvekLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRV 301
Cdd:cd19154 221 STGVSPAPNLLQDPI-----------VKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENFNIFDFSLSEED 287
|
....*..
gi 446800691 302 MKEIQSI 308
Cdd:cd19154 288 MATLEEI 294
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-308 |
4.88e-23 |
|
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: 96.20 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnlYADVNEEEGKQLVEEAIQQGITFFDTADSYGVgrsEELVGEVLKGK-------RHKLILAT 82
Cdd:cd19116 8 GNEIPAIALGT--------WKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREKiaegvvkREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KggiqpLLNgetyINNEPSYLRNAVENSLRRLQTDYIDLYYLHF----------------TNPETSYIDSIGELTRLKEE 146
Cdd:cd19116 77 K-----LWN----SYHEREQVEPALRESLKRLGLDYVDLYLIHWpvafkenndsesngdgSLSDIDYLETWRGMEDLVKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 147 GKIRSIGISNVNIEQLKE----------ANQhghIDVvqSPynmleRTAEEELLPYCIEAGISFIPYGPLafgilgGKYR 216
Cdd:cd19116 148 GLTRSIGVSNFNSEQINRllsncnikpaVNQ---IEV--HP-----TLTQEKLVAYCQSNGIVVMAYSPF------GRLV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 217 EDFKLNEVDWRQNvnlfeentyksnfkkvEKLKGIAKENDIEVSHLALAWLLNkEGIdTVIPGGKRAEQIRESVKVVDVS 296
Cdd:cd19116 212 PRGQTNPPPRLDD----------------PTLVAIAKKYGKTTAQIVLRYLID-RGV-VPIPKSSNKKRIKENIDIFDFQ 273
|
330
....*....|..
gi 446800691 297 LNKRVMKEIQSI 308
Cdd:cd19116 274 LTPEEVAALNSF 285
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
13-155 |
1.78e-22 |
|
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: 95.04 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTnAVGGHNLYADVNEEEGKQLVEEAIQQGITFFDTADSYGvgRSEELVGEVLKG-----KRHKLILATKGGiq 87
Cdd:cd19164 13 LPPLIFGA-ATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYG--PSEIILGRALKAlrdefPRDTYFIITKVG-- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446800691 88 pllngeTYINNE----PSYLRNAVENSLRRLQTDYIDLYYLH---FTNPEtSYIDSIGELTRLKEEGKIRSIGIS 155
Cdd:cd19164 88 ------RYGPDDfdysPEWIRASVERSLRRLHTDYLDLVYLHdveFVADE-EVLEALKELFKLKDEGKIRNVGIS 155
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-310 |
5.50e-22 |
|
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: 93.68 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnLYADVNEEegKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKG-------KRHKLILAT 82
Cdd:cd19129 3 SGAIPALGFGT-------LIPDPSAT--RNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEvfkagkiRREDLFVTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KggiqpLLNGetyiNNEPSYLRNAVENSLRRLQTDYIDLYYLH--FT-------NPE-----------TSYIDSIGELTR 142
Cdd:cd19129 71 K-----LWNT----NHRPERVKPAFEASLKRLQLDYLDLYLIHtpFAfqpgdeqDPRdangnviyddgVTLLDTWRAMER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 143 LKEEGKIRSIGISNVNIEQLKEANQHGHID--VVQ---SPYnmlerTAEEELLPYCIEAGISFIPYGPLAFGIlggkyre 217
Cdd:cd19129 142 LVDEGRCKAIGLSDVSLEKLREIFEAARIKpaVVQvesHPY-----LPEWELLDFCKNHGIVLQAFAPLGHGM------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 218 dfklnevdwrqNVNLFEENTYKSNFKKVEKLKgiakendievSHLALAWLLNKEGidTVIPGGKRAEQIRESvkvVDVS- 296
Cdd:cd19129 210 -----------EPKLLEDPVITAIARRVNKTP----------AQVLLAWAIQRGT--ALLTTSKTPSRIREN---FDISt 263
|
330
....*....|....
gi 446800691 297 LNKRVMKEIQSILE 310
Cdd:cd19129 264 LPEDAMREINEGIK 277
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
43-308 |
3.03e-21 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 91.18 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 43 EAIQQGITFFDTADSYGVGRSEELVGEVLKGKRHKLILATKGGIQPLLNGETYINNEPSYLRNAVENSLRRLQTDYIDLY 122
Cdd:PRK10376 48 EAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 123 YLH----FTNP-ETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGHIDVVQSPYNMLERtAEEELLPYCIEAG 197
Cdd:PRK10376 128 NLRlmgdGHGPaEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHR-ADDALIDALARDG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 198 ISFIPYGPlafgiLGGkyredfklnevdwrqnvnlfeentyksnFKKV--EKLKGIAKENDIEVSHLALAWLLNKEGIDT 275
Cdd:PRK10376 207 IAYVPFFP-----LGG----------------------------FTPLqsSTLSDVAASLGATPMQVALAWLLQRSPNIL 253
|
250 260 270
....*....|....*....|....*....|...
gi 446800691 276 VIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:PRK10376 254 LIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-311 |
3.16e-21 |
|
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: 90.91 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGghnlyadvNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKGK---RHKLILATKggi 86
Cdd:cd19157 7 GVKMPWLGLGVFKVE--------EGSEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKESgipREELFITSK--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 qpllngetYINNEPSYLRN--AVENSLRRLQTDYIDLYYLHFTNpETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKE 164
Cdd:cd19157 73 --------VWNADQGYDSTlkAFEASLERLGLDYLDLYLIHWPV-KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 165 ANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvNLFEENTyksnfkk 244
Cdd:cd19157 144 LLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQG---------------------QLLDNPV------- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 245 vekLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSILED 311
Cdd:cd19157 196 ---LKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENADVFDFELSQEDMDKIDALNEN 257
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-305 |
6.03e-20 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 86.94 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGHnlyadvneeEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATK--G 84
Cdd:cd19132 4 GTQIPAIGFGTYPLKGD---------EGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRsgvPREELFVTTKlpG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 85 GIQPllNGETyinnepsylRNAVENSLRRLQTDYIDLYYLHFTNPETS-YIDSIGELTRLKEEGKIRSIGISNVNIEQLK 163
Cdd:cd19132 72 RHHG--YEEA---------LRTIEESLYRLGLDYVDLYLIHWPNPSRDlYVEAWQALIEAREEGLVRSIGVSNFLPEHLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 164 EANQH-GHIDVVQ----SPYnmlerTAEEELLPYCIEAGISFIPYGPLAfgilggkyredfklnevdwrQNVNLFEEnty 238
Cdd:cd19132 141 RLIDEtGVTPAVNqielHPY-----FPQAEQRAYHREHGIVTQSWSPLG--------------------RGSGLLDE--- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 239 ksnfkkvEKLKGIAKENDIEVSHLALAWLLnKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19132 193 -------PVIKAIAEKHGKTPAQVVLRWHV-QLGV-VPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-230 |
1.02e-18 |
|
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: 84.12 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQkAGLNISKLGLGT-NAVGGhnlyadvneeEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG------ 73
Cdd:cd19121 1 MTSFKLN-TGASIPAVGLGTwQAKAG----------EVKAAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEaiaggv 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 74 KRHKLILATKggiqpLLNgetyinnepSYLRN---AVENSLRRLQTDYIDLYYLHF----------------------TN 128
Cdd:cd19121 67 KREDLFVTTK-----LWS---------TYHRRvelCLDRSLKSLGLDYVDLYLVHWpvllnpngnhdlfptlpdgsrdLD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 129 PETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGHI-----DVVQSPYnmlerTAEEELLPYCIEAGISFIPY 203
Cdd:cd19121 133 WDWNHVDTWKQMEKVLKTGKTKAIGVSNYSIPYLEELLKHATVvpavnQVENHPY-----LPQQELVDFCKEKGILIEAY 207
|
250 260
....*....|....*....|....*..
gi 446800691 204 GPLafGILGGKYREDFKLNEVDWRQNV 230
Cdd:cd19121 208 SPL--GSTGSPLISDEPVVEIAKKHNV 232
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-311 |
2.46e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 83.55 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 14 SKLGLGTNAVG-------GHNlyADVNEEEGKQLVEE--------AIQQGITFFDTADSYGvgRSEELVGEVLKGKRHK- 77
Cdd:cd19098 1 PRLGLGLAALGrpgyinlGHA--ADLGSGRSVEAMRAhthavldaAWAAGVRYFDAARSYG--RAEEFLGSWLRSRNIAp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 78 --LILATKGGIqpllngeTY-----INNEP--------SYLRNAVENSLRRLQtDYIDLYYLHFTNPETSYIDS---IGE 139
Cdd:cd19098 77 daVFVGSKWGY-------TYtadwqVDAAVhevkdhslARLLKQWEETRSLLG-KHLDLYQIHSATLESGVLEDadvLAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 140 LTRLKEEGkiRSIGIS------NVNIEQLKEANQHGH--IDVVQSPYNMLERTAEEELLPyCIEAGISFIPYGPLAFGIL 211
Cdd:cd19098 149 LAELKAEG--VKIGLSlsgpqqAETLRRALEIEIDGArlFDSVQATWNLLEQSAGEALEE-AHEAGMGVIVKEALANGRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 212 GGKyredfklnevdwrqnvnlfeeNTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEGIDTVIPGGKRAEQIRESVK 291
Cdd:cd19098 226 TDR---------------------NPSPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLR 284
|
330 340
....*....|....*....|...
gi 446800691 292 VVDVSLNKRV---MKEIQSILED 311
Cdd:cd19098 285 ALDVSLDLELlaaLADLAEPPED 307
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-308 |
6.36e-18 |
|
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: 81.33 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGtnavgghnLYADVNEEEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKGK---RHKLILATKggi 86
Cdd:cd19126 6 GTRMPWLGLG--------VFQTPDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESgvpREELFVTTK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 qpllngetYINNEPSYLR--NAVENSLRRLQTDYIDLYYLHFTNPEtSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKE 164
Cdd:cd19126 72 --------LWNDDQRARRteDAFQESLDRLGLDYVDLYLIHWPGKD-KFIDTWKALEKLYASGKVKAIGVSNFQEHHLEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 165 ANQHGhiDVVQSpYNMLE---RTAEEELLPYCIEAGISFIPYGPLAFGILggkyredfkLNEvdwrqnvnlfeentyksn 241
Cdd:cd19126 143 LLAHA--DVVPA-VNQVEfhpYLTQKELRGYCKSKGIVVEAWSPLGQGGL---------LSN------------------ 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 242 fkkvEKLKGIAKENDIEVSHLALAWLLnKEGIDTvIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19126 193 ----PVLAAIGEKYGKSAAQVVLRWDI-QHGVVT-IPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
33-308 |
7.24e-18 |
|
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: 82.15 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 33 NEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG-------KRHKLILATKggiqpllngetYINNEPSYLRN 105
Cdd:cd19112 22 EPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEafktglvKREDLFITTK-----------LWNSDHGHVIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 106 AVENSLRRLQTDYIDLYYLHFTNP-----------------------ETSYIDSIGELTRLKEEGKIRSIGISNVNIEQL 162
Cdd:cd19112 88 ACKDSLKKLQLDYLDLYLVHFPVAtkhtgvgttgsalgedgvldidvTISLETTWHAMEKLVSAGLVRSIGISNYDIFLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 163 KEANQHGHIdvvQSPYNMLERTA---EEELLPYCIEAGISFIPYGPlafgiLGGkyredfKLNEVDWRQNVNLFEENTyk 239
Cdd:cd19112 168 RDCLAYSKI---KPAVNQIETHPyfqRDSLVKFCQKHGISVTAHTP-----LGG------AAANAEWFGSVSPLDDPV-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 240 snfkkvekLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19112 232 --------LKDLAKKYGKSAAQIVLRWGIQRNTA--VIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-308 |
1.71e-17 |
|
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: 80.64 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 15 KLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG-------KRHKLILATKggIQ 87
Cdd:cd19128 3 RLGFGT---------YKITESESKEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEifkdggvKREDLFITSK--LW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 88 PllngetyINNEPSYLRNAVENSLRRLQTDYIDLYYLHF-----TNPETSYIDSIG--------------ELTRLKEEGK 148
Cdd:cd19128 69 P-------TMHQPENVKEQLLITLQDLQLEYLDLFLIHWplafdMDTDGDPRDDNQiqslskkpledtwrAMEQCVDEKL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 149 IRSIGISNVNIEQLKEANQHGHIdvvqSPY-NMLERTAE---EELLPYCIEAGISFIPYGPlafgiLGGKYREDfklnev 224
Cdd:cd19128 142 TKNIGVSNYSTKLLTDLLNYCKI----KPFmNQIECHPYfqnDKLIKFCIENNIHVTAYRP-----LGGSYGDG------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 225 dwrqnvnlfeentyKSNFKKVEKLKGIAKENDIEVSHLALAWLLNK-EGIDTVIPGGKRAEQIRESVKVVDVSLNKRVMK 303
Cdd:cd19128 207 --------------NLTFLNDSELKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTKEDMD 272
|
....*
gi 446800691 304 EIQSI 308
Cdd:cd19128 273 AINTL 277
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
11-305 |
2.28e-17 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 80.07 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 11 LNISKLGLGTNAVGGhnlyadvneeegkQLVEEAIQQGITF----FDTADSYGvgrSEELVGEVLKG---KRHKLILATK 83
Cdd:PRK11172 1 MSIPAFGLGTFRLKD-------------QVVIDSVKTALELgyraIDTAQIYD---NEAAVGQAIAEsgvPRDELFITTK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 ggiqpllngeTYINN-EPSYLRNAVENSLRRLQTDYIDLYYLHFTNP--ETSYIDSIGELTRLKEEGKIRSIGISNVNIE 160
Cdd:PRK11172 65 ----------IWIDNlAKDKLIPSLKESLQKLRTDYVDLTLIHWPSPndEVSVEEFMQALLEAKKQGLTREIGISNFTIA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 161 QLKEAnqhghIDVVqSPYNMleRTAEEELLPY---------CIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvn 231
Cdd:PRK11172 135 LMKQA-----IAAV-GAENI--ATNQIELSPYlqnrkvvafAKEHGIHVTSYMTLAYG---------------------- 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 232 lfeentyksnfkKVEK---LKGIAKENDIEVSHLALAWLLnKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:PRK11172 185 ------------KVLKdpvIARIAAKHNATPAQVILAWAM-QLGY-SVIPSSTKRENLASNLLAQDLQLDAEDMAAI 247
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
35-305 |
2.52e-17 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 80.14 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 35 EEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG---KRHKLILATKGGIQPLLNGETyinnepsylRNAVENSL 111
Cdd:cd19127 22 EETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRsgvDRSDIFVTTKLWISDYGYDKA---------LRGFDASL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 112 RRLQTDYIDLYYLHFTNPET--SYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHG----HIDVVQ-SPYnmlerT 184
Cdd:cd19127 90 RRLGLDYVDLYLLHWPVPNDfdRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATtvvpAVNQVElHPY-----F 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 185 AEEELLPYCIEAGISFIPYGPLAfGILggKYREDfklnevDWRQNVNLFEENTyksnfkkvekLKGIAKENDIEVSHLAL 264
Cdd:cd19127 165 SQKDLRAFHRRLGIVTQAWSPIG-GVM--RYGAS------GPTGPGDVLQDPT----------ITGLAEKYGKTPAQIVL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446800691 265 AWLLnKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19127 226 RWHL-QNGV-SAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
30-305 |
3.66e-17 |
|
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: 79.51 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 30 ADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKGK---RHKLILATKggiqpLLNGETYINNEpsylRNA 106
Cdd:cd19134 19 GELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASgipRGELFVTTK-----LATPDQGFTAS----QAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 107 VENSLRRLQTDYIDLYYLHFTNPETS-YIDSIGELTRLKEEGKIRSIGISNVNIEQLKE-ANQHGHIDVVqspyNMLE-- 182
Cdd:cd19134 87 CRASLERLGLDYVDLYLIHWPAGREGkYVDSWGGLMKLREEGLARSIGVSNFTAEHLENlIDLTFFTPAV----NQIElh 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 183 -RTAEEELLPYCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvNLFEENTYKSnfkkveklkgIAKENDIEVSH 261
Cdd:cd19134 163 pLLNQAELRKVNAQHGIVTQAYSPLGVG---------------------RLLDNPAVTA----------IAAAHGRTPAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446800691 262 LALAWLLNKEgiDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19134 212 VLLRWSLQLG--NVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-308 |
1.27e-16 |
|
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: 78.61 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 1 MKYTKLQKaGLNISKLGLGTnavgghnlyadVNEEEGK--QLVEEAIQQGITFFDTADSYGvgrSEELVGEVL------- 71
Cdd:cd19123 1 MKTLPLSN-GDLIPALGLGT-----------WKSKPGEvgQAVKQALEAGYRHIDCAAIYG---NEAEIGAALaevfkeg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 72 KGKRHKLILATKggiqpLLNGEtyinNEPSYLRNAVENSLRRLQTDYIDLYYLHF-----------TNPETSY------- 133
Cdd:cd19123 66 KVKREDLWITSK-----LWNNS----HAPEDVLPALEKTLADLQLDYLDLYLMHWpvalkkgvgfpESGEDLLslspipl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 134 IDSIGELTRLKEEGKIRSIGISNVNIEQLK----------EANQhghidVVQSPYnmlerTAEEELLPYCIEAGISFIPY 203
Cdd:cd19123 137 EDTWRAMEELVDKGLCRHIGVSNFSVKKLEdllatarikpAVNQ-----VELHPY-----LQQPELLAFCRDNGIHLTAY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 204 GPlafgiLGGKYREDfklnEVDWRQNVNLFEENTyksnfkkvekLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRA 283
Cdd:cd19123 207 SP-----LGSGDRPA----AMKAEGEPVLLEDPV----------INKIAEKHGASPAQVLIAWAIQRGTV--VIPKSVNP 265
|
330 340
....*....|....*....|....*
gi 446800691 284 EQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19123 266 ERIQQNLEAAEVELDASDMATIAAL 290
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
13-163 |
1.77e-16 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 13 ISKLGLGTNAVGghnlyadvnEEEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKGK---RHKLILATKggiqpl 89
Cdd:PRK11565 15 MPQLGLGVWQAS---------NEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEAsvaREELFITTK------ 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446800691 90 lngetYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPET-SYIDSIGELTRLKEEGKIRSIGISNVNIEQLK 163
Cdd:PRK11565 77 -----LWNDDHKRPREALEESLKKLQLDYVDLYLMHWPVPAIdHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQ 146
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-308 |
2.39e-16 |
|
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: 77.77 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 8 KAGLNISKLGLGTNAVGGhnlyadvneEEGKQLVEEAIQQGITFFDTADSYGVgrsEELVGEVLK-------GKRHKLIL 80
Cdd:cd19125 6 NTGAKIPAVGLGTWQADP---------GVVGNAVKTAIKEGYRHIDCAAIYGN---EKEIGKALKklfedgvVKREDLFI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKggiqpLLNGETyinnEPSYLRNAVENSLRRLQTDYIDLYYLHFTN--------------PETSYIDSIGELTRLKEE 146
Cdd:cd19125 74 TSK-----LWCTDH----APEDVPPALEKTLKDLQLDYLDLYLIHWPVrlkkgahmpepeevLPPDIPSTWKAMEKLVDS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 147 GKIRSIGISNVNIEQLKE----------ANQhghidVVQSPYNmlertAEEELLPYCIEAGISFIPYGPLAFGilggkyr 216
Cdd:cd19125 145 GKVRAIGVSNFSVKKLEDllavarvppaVNQ-----VECHPGW-----QQDKLHEFCKSKGIHLSAYSPLGSP------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 217 edfklnEVDWrQNVNLFEENTyksnfkkvekLKGIAKENDIEVSHLALAWLLNKEgiDTVIPGGKRAEQIRESVKVVDVS 296
Cdd:cd19125 208 ------GTTW-VKKNVLKDPI----------VTKVAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEERIKENIDVFDWS 268
|
330
....*....|..
gi 446800691 297 LNKRVMKEIQSI 308
Cdd:cd19125 269 IPEEDFAKFSSI 280
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
38-308 |
5.58e-16 |
|
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: 76.65 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 38 KQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKGK--------RHKLILATKggiqpLLNGEtyinNEPSYLRNAVEN 109
Cdd:cd19106 23 KAAVKYALDAGYRHIDCAAVYG---NEQEVGEALKEKvgpgkavpREDLFVTSK-----LWNTK----HHPEDVEPALRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 110 SLRRLQTDYIDLYYLHF------------TNP-------ETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGH 170
Cdd:cd19106 91 TLKDLQLDYLDLYLIHWpyafergdnpfpKNPdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 171 ID--VVQ---SPYnmlerTAEEELLPYCIEAGISFIPYGPlafgiLGGKYREdfklnevdWRQ--NVNLFEEntyksnfk 243
Cdd:cd19106 171 IKpaVLQvecHPY-----LAQNELIAHCKARGLVVTAYSP-----LGSPDRP--------WAKpdEPVLLEE-------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446800691 244 kvEKLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19106 225 --PKVKALAKKYNKSPAQILLRWQVQR-GV-VVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDAL 285
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-308 |
8.58e-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: 76.00 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGhnlyadvneEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG-------KRHKLILAT 82
Cdd:cd19111 1 GFPMPVIGLGTYQSPP---------EEVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWwlkngklKREEVFITT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KggIQPllngetyINNEPSYLRNAVENSLRRLQTDYIDLYYLH----FTN-------PETSY--IDSIGELTRLKEEGKI 149
Cdd:cd19111 69 K--LPP-------VYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgFVNkkdkgerELASSdvTSVWRAMEALVSEGKV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 150 RSIGISNVNIEQLKEANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLafGILGgkyredfKLNEVDWRQN 229
Cdd:cd19111 140 KSIGLSNFNPRQINKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPL--GSPG-------RANQSLWPDQ 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 230 VNLFEEntyksnfkkvEKLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19111 211 PDLLED----------PTVLAIAKELDKTPAQVLLRFVLQRGTG--VLPKSTNKERIEENFEVFDFELTEEHFKKLKTL 277
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
10-308 |
1.22e-14 |
|
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: 72.53 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKGK---RHKLILATKggi 86
Cdd:cd19117 11 GAEIPAVGLGT---------WQSKPNEVAKAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDSgvpREEIFITTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 qpllngetYINNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNP---------------------ETSYIDSIGELTRLKE 145
Cdd:cd19117 76 --------LWCTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPldpdgndflfkkddgtkdhepDWDFIKTWELMQKLPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 146 EGKIRSIGISN---VNIEQLKEANQHGHIDVVQS----PYNmlertAEEELLPYCIEAGISFIPYGPLAfgilggkyred 218
Cdd:cd19117 148 TGKVKAIGVSNfsiKNLEKLLASPSAKIVPAVNQielhPLL-----PQPKLVDFCKSKGIHATAYSPLG----------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 219 fklnevdwRQNVNLFEENTyksnfkkvekLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVvdVSLN 298
Cdd:cd19117 212 --------STNAPLLKEPV----------IIKIAKKHGKTPAQVIISWGLQR-GY-SVLPKSVTPSRIESNFKL--FTLS 269
|
330
....*....|
gi 446800691 299 KRVMKEIQSI 308
Cdd:cd19117 270 DEEFKEIDEL 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-296 |
1.76e-14 |
|
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: 72.06 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGT-NAVGGhnlyadvneeEGKQLVEEAIQQGITFFDTADSYG----VGRS-EELVGEVLKGKRHKLILATK 83
Cdd:cd19118 4 GNKIPAIGLGTwQAEPG----------EVGAAVKIALKAGYRHLDLAKVYQnqheVGQAlKELLKEEPGVKREDLFITSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 84 ggiqpLLNGetyiNNEPSYLRNAVENSLRRLQTDYIDLYYLH------FTNP------------------ETSYIDSIGE 139
Cdd:cd19118 74 -----LWNN----SHRPEYVEPALDDTLKELGLDYLDLYLIHwpvafkPTGDlnpltavptnggevdldlSVSLVDTWKA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 140 LTRLKEEGKIRSIGISNVNIEQLKEANQHGhiDVVQSpYNMLER---TAEEELLPYCIEAGISFIPYGPLAFGILGGKyr 216
Cdd:cd19118 145 MVELKKTGKVKSIGVSNFSIDHLQAIIEET--GVVPA-VNQIEAhplLLQDELVDYCKSKNIHITAYSPLGNNLAGLP-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 217 edfklnevdwrqnvnLFEENtyksnfkkvEKLKGIAKENDIEVSHLALAWLLnKEGIdTVIPGGKRAEQIRESVKVVDVS 296
Cdd:cd19118 220 ---------------LLVQH---------PEVKAIAAKLGKTPAQVLIAWGI-QRGH-SVIPKSVTPSRIRSNFEQVELS 273
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
41-305 |
1.10e-13 |
|
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: 70.17 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 41 VEEAIQQGITFFDTADSYGvgrSEELVGEVLKG-------KRHKLILATKggiqpLLNGetyiNNEPSYLRNAVENSLRR 113
Cdd:cd19113 30 IYQAIKAGYRLFDGAEDYG---NEKEVGEGVNRaideglvKREELFLTSK-----LWNN----FHDPKNVETALNKTLSD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 114 LQTDYIDLYYLHF-------------------------TNPETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQH 168
Cdd:cd19113 98 LKLDYVDLFLIHFpiafkfvpieekyppgfycgdgdnfVYEDVPILDTWKALEKLVDAGKIKSIGVSNFPGALILDLLRG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 169 GHI-----DVVQSPYnmlerTAEEELLPYCIEAGISFIPY---GPLAFgilggkyredFKLNEVDWRQNVNLFEENTYKS 240
Cdd:cd19113 178 ATIkpavlQIEHHPY-----LQQPKLIEYAQKAGITITAYssfGPQSF----------VELNQGRALNTPTLFEHDTIKS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446800691 241 nfkkveklkgIAKENDIEVSHLALAWlLNKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEI 305
Cdd:cd19113 243 ----------IAAKHNKTPAQVLLRW-ATQRGI-AVIPKSNLPERLLQNLSVNDFDLTKEDFEEI 295
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
35-308 |
1.70e-13 |
|
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: 69.86 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 35 EEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKG-------KRHKLILATKggIQPllngetyINNEPSYLRNAV 107
Cdd:cd19155 25 EEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKwidsgkvKREELFIVTK--LPP-------GGNRREKVEKFL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 108 ENSLRRLQTDYIDLYYLHF-------------TNPE--------TSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEAN 166
Cdd:cd19155 93 LKSLEKLQLDYVDLYLIHFpvgslskeddsgkLDPTgehkqdytTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 167 QHGHIdvvqSPYNM-LERTA---EEELLPYCIEAGISFIPYGPlafgiLGGKYREDFklnevdwrqNVNLFEENTYKSNF 242
Cdd:cd19155 173 KNARI----KPANLqVELHVylqQKDLVDFCSTHSITVTAYAP-----LGSPGAAHF---------SPGTGSPSGSSPDL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446800691 243 KKVEKLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19155 235 LQDPVVKAIAERHGKSPAQVLLRWLMQR-GV-VVIPKSTNAARIKENFQVFDFELTEADMAKLSSL 298
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
35-311 |
1.92e-13 |
|
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: 69.08 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 35 EEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKG---KRHKLILATKggiqpLLNGETYINNEPSylrnAVENSL 111
Cdd:cd19156 23 AEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIREsgvPREEVFVTTK-----LWNSDQGYESTLA----AFEESL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 112 RRLQTDYIDLYYLHFTNpETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEANQHGHIDVVQSPYNMLERTAEEELLP 191
Cdd:cd19156 91 EKLGLDYVDLYLIHWPV-KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 192 YCIEAGISFIPYGPLAFGilggkyredfklnevdwrqnvNLFEENTyksnfkkvekLKGIAKENDIEVSHLALAWLLNKE 271
Cdd:cd19156 170 FCKEKNIAVEAWSPLGQG---------------------KLLSNPV----------LKAIGKKYGKSAAQVIIRWDIQHG 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446800691 272 GIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSILED 311
Cdd:cd19156 219 II--TIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTD 256
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-308 |
3.91e-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: 68.01 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKGK---RHKLILATKggi 86
Cdd:cd19130 7 GNSIPQLGYGV---------FKVPPADTQRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASgipRDELFVTTK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 87 qpLLNGetyiNNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNPETS-YIDSIGELTRLKEEGKIRSIGISNVNIEQLKEA 165
Cdd:cd19130 72 --LWND----RHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGnYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 166 NQH-GHIDVVqspyNMLE---RTAEEELLPYCIEAGISFIPYGPLAFGILGGKyredfklnevdwrqnvnlfeentyksn 241
Cdd:cd19130 146 VAAtGVVPAV----NQIElhpAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGD--------------------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446800691 242 fkkvEKLKGIAKENDIEVSHLALAWLLNKEgiDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19130 195 ----PPVGAIAAAHGKTPAQIVLRWHLQKG--HVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-308 |
5.19e-13 |
|
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: 68.06 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 12 NISKLGLGT-NAVGGhnlyadvneeEGKQLVEEAIQQGITFFDTADSY------GVGRSEELVGEVLKgkRHKLILATKG 84
Cdd:cd19110 3 DIPAVGLGTwKASPG----------EVTEAVKVAIDAGYRHFDCAYLYhnesevGAGIREKIKEGVVR--REDLFIVSKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 85 GIQpllngetyiNNEPSYLRNAVENSLRRLQTDYIDLYYLH----FTNPE---------------TSYIDSIGELTRLKE 145
Cdd:cd19110 71 WCT---------CHKKSLVKTACTRSLKALKLNYLDLYLIHwpmgFKPGEpdlpldrsgmvipsdTDFLDTWEAMEDLVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 146 EGKIRSIGISNVNIEQLKE-ANQHGHidVVQSPYNMLE---RTAEEELLPYCIEAGISFIPYGPLAfGILGGkyredfkl 221
Cdd:cd19110 142 EGLVKNIGVSNFNHEQLERlLNKPGL--RVKPVTNQIEchpYLTQKKLISFCQSRNVSVTAYRPLG-GSCEG-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 222 nevdwrqnVNLFEENTyksnfkkvekLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRV 301
Cdd:cd19110 211 --------VDLIDDPV----------IQRIAKKHGKSPAQILIRFQIQRNVI--VIPKSVTPSRIKENIQVFDFELTEHD 270
|
....*..
gi 446800691 302 MKEIQSI 308
Cdd:cd19110 271 MDNLLSL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
30-308 |
2.92e-12 |
|
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: 66.04 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 30 ADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG-------KRHKLILATKggiqpLLNgeTYINNEpsY 102
Cdd:cd19114 12 AKIKANETEEVIYNAIKVGYRLIDGALLYG---NEAEVGRGIRKaiqeglvKREDLFIVTK-----LWN--NFHGKD--H 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 103 LRNAVENSLRRLQTDYIDLYYLHF------TNPETSYI-------------------DSIGELTRLKEEGKIRSIGISNV 157
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFpipaayVDPAENYPflwkdkelkkfpleqspmqECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 158 NIEQLKEANQHGHI--DVVQ---SPYnmLERtaeEELLPYCIEAGISFIPY---GPLAFgilggkyredfklnevdwrqn 229
Cdd:cd19114 160 NVQLILDLLTYAKIkpAVLQiehHPY--LQQ---KRLIDWAKKQGIQITAYssfGNAVY--------------------- 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 230 VNLFEENTYKSNFKKVEKLKGIAKENDIEVSHLALAWLLNKEgiDTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19114 214 TKVTKHLKHFTNLLEHPVVKKLADKHKRDTGQVLLRWAVQRN--ITVIPKSVNVERMKTNLDITSYKLDEEDMEALYEL 290
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-206 |
4.90e-11 |
|
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: 62.13 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAvgghnlyADVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLKG-------KRHKLILAT 82
Cdd:cd19119 9 GASIPALGLGTAS-------PHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRaiddgsiKREELFITT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 83 KggIQPLLNGEtyinnepsyLRNAVENSLRRLQTDYIDLYYLHF-----------------TNPETS--------YIDSI 137
Cdd:cd19119 79 K--VWPTFYDE---------VERSLDESLKALGLDYVDLLLVHWpvcfekdsddsgkpftpVNDDGKtryaasgdHITTY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446800691 138 GELTRLKEEGKIRSIGISNVNIEQLKEAnqhghIDVVQS--PYNMLE---RTAEEELLPYCIEAGISFIPYGPL 206
Cdd:cd19119 148 KQLEKIYLDGRAKAIGVSNYSIVYLERL-----IKECKVvpAVNQVElhpHLPQMDLRDFCFKHGILVTAYSPL 216
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
38-307 |
1.35e-10 |
|
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: 61.28 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 38 KQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKGK-------RHKLILATKggiqpLLNgeTYinNEPSYLRNAVENS 110
Cdd:cd19107 20 TEAVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEKikeqvvkREDLFIVSK-----LWC--TF--HEKGLVKGACQKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 111 LRRLQTDYIDLYYLHFTN-------------------PETSYIDSIGELTRLKEEGKIRSIGISNVNIEQLKEA-NQHG- 169
Cdd:cd19107 88 LSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIERIlNKPGl 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 170 -HIDVVQS----PYnmlerTAEEELLPYCIEAGISFIPYGPlafgiLGGKYREdfklnevdWRQ--NVNLFEEntyksnf 242
Cdd:cd19107 168 kYKPAVNQiechPY-----LTQEKLIQYCQSKGIVVTAYSP-----LGSPDRP--------WAKpeDPSLLED------- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446800691 243 kkvEKLKGIAKENDIEVSHLALAWLLNKEGIdtVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQS 307
Cdd:cd19107 223 ---PKIKEIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFKVFDFELSSEDMATILS 282
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-308 |
1.46e-10 |
|
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: 60.74 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 9 AGLNISKLGLGTNAVGghnlyadVNEEEGKQLVEEAIQQGITFFDTADSYGvgrSEELVGEVLK--------GKRHKLIL 80
Cdd:cd19124 1 SGQTMPVIGMGTASDP-------PSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAealrlglvKSRDELFV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKggiqpLLNGEtyinNEPSYLRNAVENSLRRLQTDYIDLYYLH---------FTNPET----------SYIDSIGELT 141
Cdd:cd19124 71 TSK-----LWCSD----AHPDLVLPALKKSLRNLQLEYVDLYLIHwpvslkpgkFSFPIEeedflpfdikGVWEAMEECQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 142 RLkeeGKIRSIGISNVNIEQLKEANQHGHIdvvqSP-YNMLERTA---EEELLPYCIEAGISFIPYGPLafGILGGKyre 217
Cdd:cd19124 142 RL---GLTKAIGVSNFSCKKLQELLSFATI----PPaVNQVEMNPawqQKKLREFCKANGIHVTAYSPL--GAPGTK--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 218 dfklnevdWRQNVNLfeENtyksnfkkvEKLKGIAKENDIEVSHLALAWLLnkEGIDTVIPGGKRAEQIRESVKVVDVSL 297
Cdd:cd19124 210 --------WGSNAVM--ES---------DVLKEIAAAKGKTVAQVSLRWVY--EQGVSLVVKSFNKERMKQNLDIFDWEL 268
|
330
....*....|.
gi 446800691 298 NKRVMKEIQSI 308
Cdd:cd19124 269 TEEDLEKISEI 279
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-308 |
3.36e-09 |
|
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: 57.12 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnlYADVN---EEEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVL-------KGKRHKLI 79
Cdd:cd19109 1 GNSIPIIGLGT--------YSEPKttpKGACAEAVKVAIDTGYRHIDGAYIY---QNEHEVGQAIrekiaegKVKREDIF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 80 LATKggiqpLLNgetyINNEPSYLRNAVENSLRRLQTDYIDLYYLH----FTNPETSY-IDSIG--------------EL 140
Cdd:cd19109 70 YCGK-----LWN----TCHPPELVRPTLERTLKVLQLDYVDLYIIEmpmaFKPGDEIYpRDENGkwlyhktnlcatweAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 141 TRLKEEGKIRSIGISNVNIEQL-----KEANQHGHI--DVVQSPYnmlerTAEEELLPYCIEAGISFIPYGPLafgilgG 213
Cdd:cd19109 141 EACKDAGLVKSIGVSNFNRRQLelilnKPGLKHKPVsnQVECHPY-----FTQPKLLEFCQQHDIVIVAYSPL------G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 214 KYREDFklnevdWrQNVN---LFEEntyksnfkkvEKLKGIAKENDIEVSHLALAWLLNKeGIdTVIPGGKRAEQIRESV 290
Cdd:cd19109 210 TCRDPI------W-VNVSsppLLED----------PLLNSIGKKYNKTAAQVVLRFNIQR-GV-VVIPKSFNPERIKENF 270
|
330
....*....|....*...
gi 446800691 291 KVVDVSLNKRVMKEIQSI 308
Cdd:cd19109 271 QIFDFSLTEEEMKDIEAL 288
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-224 |
1.69e-08 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 54.55 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTNAVGGhnlyadvNEEEGKQLVEEAIQQGITFFDTADSYgvgRSEELVGEVLKG--------KRHKLILA 81
Cdd:cd19122 6 GVKIPAVGFGTFANEG-------AKGETYAAVTKALDVGYRHLDCAWFY---LNEDEVGDAVRDflkenpsvKREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 82 TKggiqpLLNGEtyinNEPSYLRNAVENSLRRLQTDYIDLYYLHF-------------TNPETSYIdSIGELT------- 141
Cdd:cd19122 76 TK-----VWNHL----HEPEDVKWSIDNSLKNLKLDYIDLFLVHWpiaaekndqrspkLGPDGKYV-ILKDLTenpeptw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 142 ----RLKEEGKIRSIGISNVNIEQLKEANQHGHIDVVQSPYNMLERTAEEELLPYCIEAGISFIPYGPLA----FGILGG 213
Cdd:cd19122 146 rameEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGsqnqVPSTGE 225
|
250
....*....|.
gi 446800691 214 KYREDFKLNEV 224
Cdd:cd19122 226 RVSENPTLNEV 236
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
10-162 |
2.47e-08 |
|
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: 54.16 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 10 GLNISKLGLGTnavgghnlYA--DVNEEEGKQLVEEAIQQGITFFDTADSYGVgrsEELVGEVLKGK-------RHKLIL 80
Cdd:cd19108 8 GHFIPVLGFGT--------YApeEVPKSKALEATKLAIDAGFRHIDSAYLYQN---EEEVGQAIRSKiadgtvkREDIFY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 81 ATKGGIqpllngeTYinNEPSYLRNAVENSLRRLQTDYIDLYYLHFTNP-----ETSYIDSIGE--------------LT 141
Cdd:cd19108 77 TSKLWC-------TF--HRPELVRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeELFPKDENGKlifdtvdlcatweaME 147
|
170 180
....*....|....*....|.
gi 446800691 142 RLKEEGKIRSIGISNVNIEQL 162
Cdd:cd19108 148 KCKDAGLAKSIGVSNFNRRQL 168
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
32-308 |
1.12e-07 |
|
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: 52.42 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 32 VNEEEGKQLVEEAIQQGITFFDTADSY--------GVGR--SEELVgevlkgKRHKLILATKggiqpLLNGetyiNNEPS 101
Cdd:cd19115 23 VNNDTCADQVYNAIKAGYRLFDGACDYgneveagqGVARaiKEGIV------KREDLFIVSK-----LWNT----FHDGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 102 YLRNAVENSLRRLQTDYIDLYYLHF------TNPETSYI--------------DSIGE----LTRLKEEGKIRSIGISNV 157
Cdd:cd19115 88 RVEPICRKQLADWGIDYFDLFLIHFpialkyVDPAVRYPpgwfydgkkvefsnAPIQEtwtaMEKLVDKGLARSIGVSNF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800691 158 NIEQLKEANQHGHI--DVVQ---SPYnmlerTAEEELLPYCIEAGISFIPY---GPLAFGILGGKYREDFKLnevdwrqn 229
Cdd:cd19115 168 SAQLLMDLLRYARIrpATLQiehHPY-----LTQPRLVKYAQKEGIAVTAYssfGPQSFLELDLPGAKDTPP-------- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800691 230 vnLFEENTYKSnfkkveklkgIAKENDIEVSHLALAWlLNKEGIdTVIPGGKRAEQIRESVKVVDVSLNKRVMKEIQSI 308
Cdd:cd19115 235 --LFEHDVIKS----------IAEKHGKTPAQVLLRW-ATQRGI-AVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISAL 299
|
|
| |
