|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-300 |
0e+00 |
|
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: 529.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 1 MKTLPPVALGTWSWGTGFAGGDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILST 80
Cdd:cd19103 1 DKKLPKIALGTWSWGSGGAGGDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 81 KFTPQIADkQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILNA 160
Cdd:cd19103 81 KFTPQIAG-QSADPVADMLEGSLARLGTDYIDIYWIHNPADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 161 SGYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNAVLPQIERLTAAM 240
Cdd:cd19103 160 AGVSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSGRAETYNPLLPQLEELTAVM 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 241 KKMGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQLAA 300
Cdd:cd19103 240 AEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
4-296 |
3.52e-75 |
|
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: 232.50 E-value: 3.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGTGFAGGdtvfGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFP-RENIILSTKF 82
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWG----YGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGdRDEVVIATKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPqIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP----LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEIL 158
Cdd:cd19093 78 AP-LPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPgpwySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 159 NASGYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPmPAGSGRAESYNAVLPQIERLTA 238
Cdd:cd19093 157 KERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENP-PPGGRRRLFGRKNLEKVQPLLD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446777540 239 AMKKMGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19093 236 ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
3-301 |
5.97e-71 |
|
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: 222.36 E-value: 5.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTGFAGGDtvfgnhlsDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKF 82
Cdd:COG0667 12 KVSRLGLGTMTFGGPWGGVD--------EAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPQIADKQ-----SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRA 154
Cdd:COG0667 84 GRRMGPGPngrglSREHIRRAVEASLRRLGTDYIDLYQLHRPdpdTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 155 NEILnASGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNA--VLPQ 232
Cdd:COG0667 164 LAIA-EGLPPIVAVQNEYSLLDRSAEE-ELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAATNFVQgyLTER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 233 IERLTAAMKKMGAERNAS--------------VaqiaiawaiakgTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQL 298
Cdd:COG0667 242 NLALVDALRAIAAEHGVTpaqlalawllaqpgV------------TSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
...
gi 446777540 299 AAE 301
Cdd:COG0667 310 LAA 312
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
4-296 |
3.33e-56 |
|
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: 183.88 E-value: 3.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGTGFAGgdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFpRENIILSTKFT 83
Cdd:cd19084 4 VSRIGLGTWAIGGTWWG-------EVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR-RDDVVIATKCG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQS----AQPVSDM--LEASLGRLGVDAIDIYWIHNPlDVEkwTP------GLIPLLQSGKVKRVGVSNHNLAQI 151
Cdd:cd19084 76 LRWDGGKGvtkdLSPESIRkeVEQSLRRLQTDYIDLYQIHWP-DPN--TPieetaeALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 152 RRANEILNasgysLSAVQNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYN---A 228
Cdd:cd19084 153 EEARKYGP-----IVSLQPPYSMLEREIEEE-LLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPFfrgE 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 229 VLPQIERLTAAMKKMGAERNASVAQIAIAWAIAK--GTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19084 227 NFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
7-299 |
1.17e-54 |
|
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: 179.81 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWSWGTGFAGgdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALV--RQFPRENIILSTKFTP 84
Cdd:pfam00248 1 IGLGTWQLGGGWGP--------ISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALkdYPVKRDKVVIATKVPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 85 QIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRAneiL 158
Cdd:pfam00248 73 GDGPWPsggSKENIRKSLEESLKRLGTDYIDLYYLHWPdpdTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA---L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 159 NASGYSLSAVQNHYSLLYRAsEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRaESYNAVLPQIERLTA 238
Cdd:pfam00248 150 TKGKIPIVAVQVEYNLLRRR-QEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERR-RLLKKGTPLNLEALE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446777540 239 AMKKMGAERNASVAQIAI--AWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQLA 299
Cdd:pfam00248 228 ALEEIAKEHGVSPAQVALrwALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
5-205 |
6.65e-53 |
|
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: 173.09 E-value: 6.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTWSWGTgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFP-RENIILSTKFT 83
Cdd:cd06660 1 SRLGLGTMTFGG-----------DGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGnRDDVVIATKGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQSAQPVS-----DMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRAN 155
Cdd:cd06660 70 HPPGGDPSRSRLSpehirRDLEESLRRLGTDYIDLYYLHRDdpsTPVEETLEALNELVREGKIRYIGVSNWSAERLAEAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446777540 156 EILNASGYS-LSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGA 205
Cdd:cd06660 150 AYAKAHGLPgFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGP 200
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
4-301 |
6.71e-51 |
|
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: 170.07 E-value: 6.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGTGFAGGDTvfgnhlSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQfPRENIILSTKFT 83
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGDQ------DDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG-RRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PqiaDKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILNa 160
Cdd:cd19085 74 P---DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPssdVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 161 sgysLSAVQNHYSLLYRASEeAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNAVLPQIERLT--- 237
Cdd:cd19085 150 ----IDSNQLPYNLLWRAIE-YEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLFRHFEPGAEEETfea 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 238 -AAMKKMGAERNASVAQIAIAWAIAKGTL--PLVGATKVHHVLDAACASDIQLRDEEIILLEQLAAE 301
Cdd:cd19085 225 lEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
2-296 |
8.73e-50 |
|
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: 166.25 E-value: 8.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 2 KTLPPVALGTWswgtGFAGGDTvfgNHLSDTQMA-EVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILST 80
Cdd:cd19072 2 EEVPVLGLGTW----GIGGGMS---KDYSDDKKAiEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 81 KFTPQIADKQSAQPVsdmLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEI 157
Cdd:cd19072 75 KVSPDHLKYDDVIKA---AKESLKRLGTDYIDLYLIHWPnpsIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 158 LNasGYSLSAVQNHYSLLYRaSEEAGILDYCRQNNITFFAYMVLEQGALSGrydsnhpmpagsgraesynavlpqiERLT 237
Cdd:cd19072 152 LK--KGPIVANQVEYNLFDR-EEESGLLPYCQKNGIAIIAYSPLEKGKLSN-------------------------AKGS 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 238 AAMKKMGAERNASVAQIAIA-WAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19072 204 PLLDEIAKKYGKTPAQIALNwLISKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
5-292 |
6.77e-47 |
|
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: 160.13 E-value: 6.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTWSWGTGFAGGDTvfgnhlsDTQMA-EVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFpRENIILSTK-- 81
Cdd:cd19149 12 SVIGLGTWAIGGGPWWGGS-------DDNESiRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR-RDKVVLATKcg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 -----------FTP---QIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPlDVEkwTP------GLIPLLQSGKVKRV 141
Cdd:cd19149 84 lrwdreggsffFVRdgvTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQ-DVE--TPieetmeALEELKRQGKIRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 142 GVSNHNLAQIRRAneilnASGYSLSAVQNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSG 221
Cdd:cd19149 161 GASNVSVEQIKEY-----VKAGQLDIIQEKYSMLDRGIEKE-LLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 222 RA-------ESYNAVLPQIERltaaMKKMGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEEI 292
Cdd:cd19149 235 RSgipwfspENREKVLALLEK----WKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDI 310
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
15-298 |
7.07e-46 |
|
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: 157.58 E-value: 7.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 15 GTGFAGGDTVFGNhLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKFTPQIADKQSA-- 92
Cdd:cd19083 17 GTNAVGGHNLYPN-LDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVIATKGAHKFGGDGSVln 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 93 -QP--VSDMLEASLGRLGVDAIDIYWIHNPldvEKWTP------GLIPLLQSGKVKRVGVSNHNLAQIRRAneilNASGY 163
Cdd:cd19083 96 nSPefLRSAVEKSLKRLNTDYIDLYYIHFP---DGETPkaeavgALQELKDEGKIRAIGVSNFSLEQLKEA----NKDGY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 164 sLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGR-------AESYNAVLPQIERL 236
Cdd:cd19083 169 -VDVLQGEYNLLQREAEE-DILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRndkplfkGERFSENLDKVDKL 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 237 taamKKMGAERNASVAQIAIAWAIAKGTLPLV--GATKVHHVLDAACASDIQLRDEEIILLEQL 298
Cdd:cd19083 247 ----KSIADEKGVTVAHLALAWYLTRPAIDVVipGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
6-296 |
1.58e-44 |
|
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: 153.89 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTWSWGtgfaggDTVFGNHLSDTQMA-EVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQF-PRENIILSTKFT 83
Cdd:cd19079 14 RLCLGCMSFG------DPKWRPWVLDEEESrPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFaPRDEVVIATKVY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQSAQPVS-----DMLEASLGRLGVDAIDIYWIHNpLDVEkwTP------GLIPLLQSGKVKRVGVSNHNLAQIR 152
Cdd:cd19079 88 FPMGDGPNGRGLSrkhimAEVDASLKRLGTDYIDLYQIHR-WDYE--TPieetleALHDVVKSGKVRYIGASSMYAWQFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 153 RANEILNASGYS-LSAVQNHYSLLYRaSEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNH------PMPAGSGRAES 225
Cdd:cd19079 165 KALHLAEKNGWTkFVSMQNHYNLLYR-EEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTerrrstTDTAKLKYDYF 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 226 YNAVLPQIERLTAAMKKMGAERnASVAQIAIAWAIAkGTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19079 244 TEADKEIVDRVEEVAKERGVSM-AQVALAWLLSKPG-VTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
25-292 |
3.60e-39 |
|
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: 139.68 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 25 FGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFpRENIILSTKFTPQIADKQSAQPVSD------- 97
Cdd:cd19078 18 YGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF-RDQVVIATKFGFKIDGGKPGPLGLDsrpehir 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 98 -MLEASLGRLGVDAIDIYWIH------NPLDVEKWTPGLIpllQSGKVKRVGVSNHNLAQIRRANEILnasgySLSAVQN 170
Cdd:cd19078 97 kAVEGSLKRLQTDYIDLYYQHrvdpnvPIEEVAGTMKELI---KEGKIRHWGLSEAGVETIRRAHAVC-----PVTAVQS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 171 HYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRaesynAVLPQI--------ERLTAAMKK 242
Cdd:cd19078 169 EYSMMWREPEKE-VLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDR-----ASLPRFtpealeanQALVDLLKE 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446777540 243 MGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEEI 292
Cdd:cd19078 243 FAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEEL 294
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-299 |
3.81e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 137.03 E-value: 3.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGtgfaGGDTVFG-NHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFpRENIILSTKF 82
Cdd:cd19102 1 LTTIGLGTWAIG----GGGWGGGwGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL-RDRPIVATKC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TP------QIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLD----VEKWTpGLIPLLQSGKVKRVGVSNHNLAQIR 152
Cdd:cd19102 76 GLlwdeegRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPdepiEEAWG-ALAELKEEGKVRAIGVSNFSVDQMK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 153 RANEIlnasgYSLSAVQNHYSLLYRAsEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNAV--- 229
Cdd:cd19102 155 RCQAI-----HPIASLQPPYSLLRRG-IEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVASLPADDWRRRSPFfqe 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 230 --LPQIERLTAAMKKMGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEEIILLEQLA 299
Cdd:cd19102 229 pnLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPevTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
21-291 |
4.95e-38 |
|
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: 136.58 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 21 GDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQfPRENIILSTKFTPQIADKQ-------SAQ 93
Cdd:cd19076 21 GMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-RRDEVVIATKFGIVRDPGSgfrgvdgRPE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 94 PVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEIlnasgYSLSAVQN 170
Cdd:cd19076 100 YVRAACEASLKRLGTDVIDLYYQHRVdpnVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAV-----HPITAVQS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 171 HYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRA-------ESYNAVLPQIERLtaamKKM 243
Cdd:cd19076 175 EYSLWTRDIED-EVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRnnprfqgENFDKNLKLVEKL----EAI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446777540 244 GAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEE 291
Cdd:cd19076 250 AAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEE 299
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
15-304 |
1.23e-37 |
|
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: 136.42 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 15 GTGFAGGDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgSSETALGALVRQFP--RENIILSTKF-------TPQ 85
Cdd:cd19144 17 GFGAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYG--DSEELIGRWFKQNPgkREKIFLATKFgieknveTGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 86 IADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNpLD----VEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEIlnas 161
Cdd:cd19144 95 YSVDGSPEYVKKACETSLKRLGVDYIDLYYQHR-VDgktpIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAV---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 162 gYSLSAVQNHYS--LLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGR-------AESYNAVLPQ 232
Cdd:cd19144 170 -HPIAAVQIEYSpfSLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRrmaprfqAENFPKNLEL 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446777540 233 IERLTAAMKKMGAerNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQLAAETRV 304
Cdd:cd19144 249 VDKIKAIAKKKNV--TAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEV 318
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
7-290 |
9.57e-37 |
|
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: 133.10 E-value: 9.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWswgtgfaggdTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKF---- 82
Cdd:cd19074 7 LSLGTW----------LTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKVfwpt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPQIADKQ-SAQPVSDMLEASLGRLGVDAIDIYWIHNPlDVEkwTP------GLIPLLQSGKVKRVGVSNHNLAQIRRAN 155
Cdd:cd19074 77 GPGPNDRGlSRKHIFESIHASLKRLQLDYVDIYYCHRY-DPE--TPleetvrAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 156 EILNASG-YSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAES--------- 225
Cdd:cd19074 154 DLARQFGlIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEdnrdkkrrl 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446777540 226 -YNAVLPQIERLTAAMKKMG---AE-------RNASVaqiaiawaiakgTLPLVGATKVHHVLDAACASDIQLRDE 290
Cdd:cd19074 233 lTDENLEKVKKLKPIADELGltlAQlalawclRNPAV------------SSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
7-209 |
1.69e-36 |
|
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: 131.06 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWSWGTGFAGGdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQfPRENIILSTKF---- 82
Cdd:cd19086 6 IGFGTWGLGGDWWGD-------VDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG-RRDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 --TPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP----LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANE 156
Cdd:cd19086 78 dgGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpdevLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446777540 157 ilnasGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGR 209
Cdd:cd19086 158 -----RGGIDVVQVIYNLLDQRPEE-ELFPLAEEHGVGVIARVPLASGLLTGK 204
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-295 |
2.25e-35 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 130.03 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTWswgtgfaggdtVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYG-------MGSSETALGA-LVRQFPRENII 77
Cdd:cd19081 11 PLCLGTM-----------VFGWTADEETSFALLDAFVDAGGNFIDTADVYSawvpgnaGGESETIIGRwLKSRGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQI 151
Cdd:cd19081 80 IATKVGFPMGPNGpglSRKHIRRAVEASLRRLQTDYIDLYQAHWDdpaTPLEETLGALNDLIRQGKVRYIGASNYSAWRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 152 RRANEILNASGYS-LSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNAVL 230
Cdd:cd19081 160 QEALELSRQHGLPrYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEAAKRYL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446777540 231 -PQIERLTAAMKKMGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEEIILL 295
Cdd:cd19081 240 nERGLRILDALDEVAAEHGATPAQVALAWLLARPgvTAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
3-291 |
2.29e-34 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 126.80 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGtgfaggdtvfGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFP--RENIILST 80
Cdd:COG4989 12 SVSRIVLGCMRLG----------EWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPslREKIELQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 81 KFTPQIADKQSAQPV------------SdmLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSN 145
Cdd:COG4989 82 KCGIRLPSEARDNRVkhydtskehiiaS--VEGSLRRLGTDYLDLLLLHRPdplMDPEEVAEAFDELKASGKVRHFGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 146 HNLAQIrranEILN-ASGYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDsnhpmpagsgrae 224
Cdd:COG4989 160 FTPSQF----ELLQsALDQPLVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGGFD------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 225 synavlPQIERLTAAMKKMGAERNASvaqiaiawaiaKGT-------------LPLVGATKVHHVLDAACASDIQLRDEE 291
Cdd:COG4989 223 ------EQFPRLRAALDELAEKYGVS-----------PEAialawllrhpagiQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
7-222 |
6.42e-34 |
|
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: 125.88 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWSWGTGFAGGdtvfgnhlSDTQMA-EVFTAAMSKGLNLWDTAAVYGMGSSETALG-ALVRQFPRENIILSTKFTP 84
Cdd:cd19148 7 IALGTWAIGGWMWGG--------TDEKEAiETIHKALDLGINLIDTAPVYGFGLSEEIVGkALKEYGKRDRVVIATKVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 85 QIADKQ------SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRAN 155
Cdd:cd19148 79 EWDEGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPdplVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 156 eilnaSGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGR 222
Cdd:cd19148 159 -----KVAPLHTVQPPYNLFEREIEK-DVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLR 219
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
6-290 |
2.63e-33 |
|
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: 124.61 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTWSwgtgfaggdtvFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQfPRENIILSTKFTPQ 85
Cdd:cd19087 15 RLCLGTMN-----------FGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG-RRDDIVLATKVFGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 86 IADK-----QSAQPVSDMLEASLGRLGVDAIDIYWIHN-----PLDvEKWTpGLIPLLQSGKVKRVGVSNHNLAQIRRAN 155
Cdd:cd19087 83 MGDDpndrgLSRRHIRRAVEASLRRLQTDYIDLYQMHHfdrdtPLE-ETLR-ALDDLVRQGKIRYIGVSNFAAWQIAKAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 156 EILNASGYS-LSAVQNHYSLLYRASE-EagILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRA-ESYNAV--- 229
Cdd:cd19087 161 GIAARRGLLrFVSEQPMYNLLKRQAElE--ILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVErARYQARygl 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 230 ---LPQIERLTAAMKKMGAE----------RNASVaqiaiawaiakgTLPLVGATKVHHVLDAACASDIQLRDE 290
Cdd:cd19087 239 eeyRDIAERFEALAAEAGLTpaslalawvlSHPAV------------TSPIIGPRTLEQLEDSLAALEITLTPE 300
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
3-291 |
3.26e-32 |
|
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: 121.12 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGtgfaggdtvfGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFP--RENIILST 80
Cdd:cd19092 5 EVSRLVLGCMRLA----------DWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPglREKIEIQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 81 K---FTPQIADKQ-------SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHN 147
Cdd:cd19092 75 KcgiRLGDDPRPGrikhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPdplMDPEEVAEAFDELVKSGKVRYFGVSNFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 148 LAQIRRANEILNasgYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDsnhpmpagsgraesyn 227
Cdd:cd19092 155 PSQIELLQSYLD---QPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFD---------------- 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446777540 228 avlPQIERLTAAMKKMGAERNASVAQIAIA--WAIAKGTLPLVGATKVHHVLDAACASDIQLRDEE 291
Cdd:cd19092 216 ---ERFQRLRAALEELAEEYGVTIEAIALAwlLRHPARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
5-222 |
1.86e-31 |
|
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: 119.20 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGT--WSWGTGFAGGDTVfgnhlsdTQMAEVFTAAmskGLNLWDTAAVYGMGSSETALGALvrQFPRENIILSTKF 82
Cdd:cd19075 1 PKIILGTmtFGSQGRFTTAEAA-------AELLDAFLER---GHTEIDTARVYPDGTSEELLGEL--GLGERGFKIDTKA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILN 159
Cdd:cd19075 69 NPGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPdrsTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 160 ASGYSLSAV-QNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYdSNHPMPAGSGR 222
Cdd:cd19075 149 ENGWVLPTVyQGMYNAITRQVETE-LFPCLRKLGIRFYAYSPLAGGFLTGKY-KYSEDKAGGGR 210
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
23-291 |
2.16e-31 |
|
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: 119.27 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 23 TVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGAL---VRQFP--RENIILSTKFTPQIADKQ---SAQP 94
Cdd:cd19077 16 TWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLKLLarfFRKYPeyADKVVLSVKGGLDPDTLRpdgSPEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 95 VSDMLEASLGRLG-VDAIDIYwihNPLDVEKWTP------GLIPLLQSGKVKRVGVSNHNLAQIRRANEIlnasgYSLSA 167
Cdd:cd19077 96 VRKSIENILRALGgTKKIDIF---EPARVDPNVPieetikALKELVKEGKIRGIGLSEVSAETIRRAHAV-----HPIAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 168 VQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRA-------ESYNAVLPQIERLT--A 238
Cdd:cd19077 168 VEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRhldrfngENFEKNLKLVDALQelA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446777540 239 AMKKMGAernASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEE 291
Cdd:cd19077 248 EKKGCTP---AQLALAWILAQSGPKIIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-296 |
6.57e-31 |
|
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: 118.09 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGT------WSWGTGFAGGDTVFgnhlsdtqmaEVFTAAmskGLNLWDTAAVYGMGSSETALGALVRQFpRENIILS 79
Cdd:cd19080 12 PLALGTmtfgteWGWGADREEARAMF----------DAYVEA---GGNFIDTANNYTNGTSERLLGEFIAGN-RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 80 TKFT----PQIADKQSAQPVSDM--LEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQ 150
Cdd:cd19080 78 TKYTmnrrPGDPNAGGNHRKNLRrsVEASLRRLQTDYIDLLYVHAWdftTPVEEVMRALDDLVRAGKVLYVGISDTPAWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 151 IRRANEILNASGYS-LSAVQNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYDSNHpMPAGSGRAESYNAV 229
Cdd:cd19080 158 VARANTLAELRGWSpFVALQIEYSLLERTPERE-LLPMARALGLGVTPWSPLGGGLLTGKYQRGE-EGRAGEAKGVTVGF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446777540 230 LPQIER---LTAAMKKMGAERNASVAQIAIAWAIAK--GTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19080 236 GKLTERnwaIVDVVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
4-206 |
1.18e-29 |
|
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: 113.43 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGtGFAGGDtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKFT 83
Cdd:cd19137 4 IPALGLGTWGIG-GFLTPD-----YSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQSAQPVsdmLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILNA 160
Cdd:cd19137 78 PTNLRYDDLLRS---LQNSLRRLDTDYIDLYLIHWPnpnIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446777540 161 sgySLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGAL 206
Cdd:cd19137 155 ---PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE 197
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
3-304 |
4.36e-29 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 112.07 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILST 80
Cdd:COG0656 4 EIPALGLGTW---------------QLPGEEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAAsgVPREELFVTT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 81 KFTPQIADKQSAQPvsdMLEASLGRLGVDAIDIYWIHNPLD---VEKWtPGLIPLLQSGKVKRVGVSNHNLAQIRranEI 157
Cdd:COG0656 66 KVWNDNHGYDDTLA---AFEESLERLGLDYLDLYLIHWPGPgpyVETW-RALEELYEEGLIRAIGVSNFDPEHLE---EL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 158 LNASGYSLSAVQNHYSLLYRaseEAGILDYCRQNNITFFAYMVLEQGALSgrydsNHPmpagsgraesynavlpqierlt 237
Cdd:COG0656 139 LAETGVKPAVNQVELHPYLQ---QRELLAFCREHGIVVEAYSPLGRGKLL-----DDP---------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 238 aAMKKMGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQLAAETRV 304
Cdd:COG0656 189 -VLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
4-287 |
7.01e-29 |
|
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: 111.16 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGtgfagGDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPrENIILSTK-- 81
Cdd:cd19088 1 VSRLGYGAMRLT-----GPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP-DDVVIATKgg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 --------FTPQIADKQSAQPVsdmlEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQ 150
Cdd:cd19088 75 lvrtgpgwWGPDGSPEYLRQAV----EASLRRLGLDRIDLYQLHRIdpkVPFEEQLGALAELQDEGLIRHIGLSNVTVAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 151 IRRANEILnasgySLSAVQNHYSLLYRASEeaGILDYCRQNNITFFAYMVLEQGALSGrydsnhPMPAGSGRAESYNAVL 230
Cdd:cd19088 151 IEEARAIV-----RIVSVQNRYNLANRDDE--GVLDYCEAAGIAFIPWFPLGGGDLAQ------PGGLLAEVAARLGATP 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 231 PQIerltaamkKMGAERNASvaqiaiawaiaKGTLPLVGATKVHHVLDAACASDIQL 287
Cdd:cd19088 218 AQV--------ALAWLLARS-----------PVMLPIPGTSSVEHLEENLAAAGLRL 255
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-230 |
1.03e-27 |
|
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: 108.06 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 25 FGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKFTPQIaDKQSAQPVSDMLEASLG 104
Cdd:cd19105 18 FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVFLATKASPRL-DKKDKAELLKSVEESLK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 105 RLGVDAIDIYWIHNPLDVEKW--TPGLIP----LLQSGKVKRVGVSNHNLAQ--IRRAneilnASGYSLSAVQNHYSLLY 176
Cdd:cd19105 97 RLQTDYIDIYQLHGVDTPEERllNEELLEalekLKKEGKVRFIGFSTHDNMAevLQAA-----IESGWFDVIMVAYNFLN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446777540 177 RASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNAVL 230
Cdd:cd19105 172 QPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAKGFSLPQAALKWVL 225
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
3-296 |
1.24e-27 |
|
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: 108.10 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTGFAggdtvfgnhlSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQfPRENIILSTKF 82
Cdd:cd19138 10 KVPALGQGTWYMGEDPA----------KRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG-RRDKVFLVSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPQIADKQSaqpVSDMLEASLGRLGVDAIDIYWIHnpldvekWtPGLIP----------LLQSGKVKRVGVSNHNLAQIR 152
Cdd:cd19138 79 LPSNASRQG---TVRACERSLRRLGTDYLDLYLLH-------W-RGGVPlaetvaameeLKKEGKIRAWGVSNFDTDDME 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 153 RANEILNasGYSLSAVQNHYSLLYRASEeAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPmpagsgraesynavlpq 232
Cdd:cd19138 148 ELWAVPG--GGNCAANQVLYNLGSRGIE-YDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENP----------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446777540 233 ierltaAMKKMGAERNASVAQIAIA-WAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19138 208 ------TLKEIAARHGATPAQVALAwVLRDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
4-296 |
2.10e-27 |
|
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: 107.18 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF--PRENIILSTK 81
Cdd:cd19071 1 MPLIGLGTY---------------KLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESgvPREELFITTK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 FTPQIADKQSAQPvsdMLEASLGRLGVDAIDIYWIHNPLDVEKWTP---------GLIPLLQSGKVKRVGVSNHNLAQIR 152
Cdd:cd19071 63 LWPTDHGYERVRE---ALEESLKDLGLDYLDLYLIHWPVPGKEGGSkearletwrALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 153 ranEILNASGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAYMVLEQGALSGRYDsnhpmpagsgraesynavlpq 232
Cdd:cd19071 140 ---ELLAAARIKPAVNQIELHPYLQQKE---LVEFCKEHGIVVQAYSPLGRGRRPLLDD--------------------- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 233 ierltAAMKKMGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19071 193 -----PVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
5-251 |
2.98e-27 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 107.64 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTwswgtgfaggdTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYG----MGSSETALGALVRQFP-RENIILS 79
Cdd:cd19082 1 SRIVLGT-----------ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKSRGnRDKVVIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 80 TK--FTPQIADKQS---AQPVSDMLEASLGRLGVDAIDIYWIH--NP-LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQI 151
Cdd:cd19082 70 TKggHPDLEDMSRSrlsPEDIRADLEESLERLGTDYIDLYFLHrdDPsVPVGEIVDTLNELVRAGKIRAFGASNWSTERI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 152 RRANEILNASGY-SLSAVQNHYSL------------LYRASEEAgiLDYCRQNNITFFAYMVLEQGALSGRYDSNHPmPA 218
Cdd:cd19082 150 AEANAYAKAHGLpGFAASSPQWSLarpneppwpgptLVAMDEEM--RAWHEENQLPVFAYSSQARGFFSKRAAGGAE-DD 226
|
250 260 270
....*....|....*....|....*....|...
gi 446777540 219 GSGRAESYNAVlpQIERLTAAmKKMGAERNASV 251
Cdd:cd19082 227 SELRRVYYSEE--NFERLERA-KELAEEKGVSP 256
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-298 |
1.49e-26 |
|
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: 106.54 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 13 SWGTGFAGGDTVFGNHLSDTQMAE---VFTAAMSKGLNLWDTAAVYGMGSSETALG-ALVRQfpRENIILSTKFTPQIAD 88
Cdd:cd19091 17 ALGTMTFGGGGGFFGAWGGVDQEEadrLVDIALDAGINFFDTADVYSEGESEEILGkALKGR--RDDVLIATKVRGRMGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 89 K-----QSAQPVSDMLEASLGRLGVDAIDIYWIHnplDVEKWTP------GLIPLLQSGKVKRVGVSNHNLAQIRRANEI 157
Cdd:cd19091 95 GpndvgLSRHHIIRAVEASLKRLGTDYIDLYQLH---GFDALTPleetlrALDDLVRQGKVRYIGVSNFSAWQIMKALGI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 158 LNASGYS-LSAVQNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNAVLP----Q 232
Cdd:cd19091 172 SERRGLArFVALQAYYSLLGRDLEHE-LMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGSRLRRTGFDFPPvdreR 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446777540 233 IERLTAAMKKMGAERNASVAQIAIAWAIAKGTLP--LVGATKVHHVLDAACASDIQLRDEEIILLEQL 298
Cdd:cd19091 251 GYDVVDALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-292 |
1.66e-26 |
|
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: 106.19 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtGFaGGDTVFGNhlsdtqMAEVFTAAMSKGLNLWDTAAVYGM--GSSETALGALVRQF---PRENIIL 78
Cdd:cd19089 11 LPAISLGLWH---NF-GDYTSPEE------ARELLRTAFDLGITHFDLANNYGPppGSAEENFGRILKRDlrpYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 79 STK-----FTPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQ 150
Cdd:cd19089 81 STKagygmWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYdpdTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 151 IRRANEILNASGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYdSNHPMPAGSGRAESYN--- 227
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAED-GLLEVLEEAGIGFIAFSPLAQGLLTDKY-LNGIPPDSRRAAESKFlte 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446777540 228 -----AVLPQIERLTaamkKMGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASD-IQLRDEEI 292
Cdd:cd19089 239 ealtpEKLEQLRKLN----KIAAKRGQSLAQLALSWVLRDPrvTSVLIGASSPSQLEDNVAALKnLDFSEEEL 307
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
15-209 |
3.88e-26 |
|
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: 105.21 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 15 GTGFAGGDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKFTPQIAD------ 88
Cdd:cd19145 16 GLGCMGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLATKFGIHEIGgsgvev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 89 KQSAQPVSDMLEASLGRLGVDAIDIYWIHN-----PLDVekwTPG-LIPLLQSGKVKRVGVSNHNLAQIRRANEIlnasg 162
Cdd:cd19145 96 RGDPAYVRAACEASLKRLDVDYIDLYYQHRidttvPIEI---TMGeLKKLVEEGKIKYIGLSEASADTIRRAHAV----- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446777540 163 YSLSAVQNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGR 209
Cdd:cd19145 168 HPITAVQLEWSLWTRDIEEE-IIPTCRELGIGIVPYSPLGRGFFAGK 213
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
5-209 |
1.30e-25 |
|
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: 102.31 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTWSWGtgfaGGDTVFgnhlSDTQMAEVFTAAMSKGLNLWDTAAVYGMgsSETALGALVRQFPRENIILSTK--- 81
Cdd:cd19095 1 SVLGLGTSGIG----RVWGVP----SEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALAGLRRDDLFIATKvgt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 --FTPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDVEKwTPGLIPLLQ----SGKVKRVGVSNHN--LAQIRR 153
Cdd:cd19095 71 hgEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDEL-TGEVLETLEdlkaAGKVRYIGVSGDGeeLEAAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446777540 154 ANEIlnasgyslSAVQNHYSLLYRASEEagILDYCRQNNITFFAYMVLEQGALSGR 209
Cdd:cd19095 150 SGVF--------DVVQLPYNVLDREEEE--LLPLAAEAGLGVIVNRPLANGRLRRR 195
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
33-197 |
1.17e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 102.20 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 33 QMAEVFTAAMSKGLNLWDTAAVYGMgsSETALGALVRQfPRENIILSTKFTPQIADKQSAQpvsDMLEASLGRLGVDAID 112
Cdd:COG1453 30 EAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKG-PRDKVILATKLPPWVRDPEDMR---KDLEESLKRLQTDYID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 113 IYWIHNPLDVEKWTPGLIP---------LLQSGKVKRVGVSNHNLAQIrrANEILNAsgYSLSAVQNHYSLLYR---ASE 180
Cdd:COG1453 104 LYLIHGLNTEEDLEKVLKPggalealekAKAEGKIRHIGFSTHGSLEV--IKEAIDT--GDFDFVQLQYNYLDQdnqAGE 179
|
170
....*....|....*..
gi 446777540 181 EAgiLDYCRQNNITFFA 197
Cdd:COG1453 180 EA--LEAAAEKGIGVII 194
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
33-193 |
6.17e-23 |
|
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: 95.32 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 33 QMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTKFTPQiaDKQSAQPVSDMLEASLGRLGVDAID 112
Cdd:cd19096 22 KAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLPPW--SVKSAEDFRRILEESLKRLGVDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 113 IYWIHNPLDVEKWT--------PGLIPLLQSGKVKRVGVSNH-NLAQIRranEILNAsgYSLSAVQNHYSLL---YRASE 180
Cdd:cd19096 100 FYLLHGLNSPEWLEkarkggllEFLEKAKKEGLIRHIGFSFHdSPELLK---EILDS--YDFDFVQLQYNYLdqeNQAGR 174
|
170
....*....|...
gi 446777540 181 EAgiLDYCRQNNI 193
Cdd:cd19096 175 PG--IEYAAKKGM 185
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
4-204 |
3.34e-22 |
|
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: 93.10 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF--PRENIILSTK 81
Cdd:cd19073 1 IPALGLGTW---------------QLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESgvPREDLFITTK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 FTPqiaDKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIrraNEIL 158
Cdd:cd19073 63 VWR---DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPnptVPLEETLGALKELKEAGKVKSIGVSNFTIELL---EEAL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446777540 159 NASGYSLSAVQNHYS-LLYRAseeaGILDYCRQNNITFFAYMVLEQG 204
Cdd:cd19073 137 DISPLPIAVNQVEFHpFLYQA----ELLEYCRENDIVITAYSPLARG 179
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
5-212 |
9.80e-22 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 92.62 E-value: 9.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTWSWGTGFAGGDtvfgnhlsDTQMAEVFTAAMSKGLNLWDTAAVYGmgSSETALGALVRQFPRENIILSTKF-- 82
Cdd:cd19090 1 SALGLGTAGLGGVFGGVD--------DDEAVATIRAALDLGINYIDTAPAYG--DSEERLGLALAELPREPLVLSTKVgr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDVEKWTP----GLIPLLQS----GKVKRVGVSNHNLAQIRRA 154
Cdd:cd19090 71 LPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapgGALEALLElkeeGLIKHIGLGGGPPDLLRRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 155 NEilnaSG---YSLSAvqNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQGALSGRYDS 212
Cdd:cd19090 151 IE----TGdfdVVLTA--NRYTLLDQSAADE-LLPAAARHGVGVINASPLGMGLLAGRPPE 204
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-206 |
1.47e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 91.00 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgSSETALGALVRQfPRENIILSTKF 82
Cdd:cd19100 10 KVSRLGFGGGPLG------------RLSQEEAAAIIRRALDLGINYFDTAPSYG--DSEEKIGKALKG-RRDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 TPQiaDKQSAQPvsdMLEASLGRLGVDAIDIYWIHNPLDVEKWTP-----GLIPLLQS----GKVKRVGVSNHNLAQIRR 153
Cdd:cd19100 75 GAR--DYEGAKR---DLERSLKRLGTDYIDLYQLHAVDTEEDLDQvfgpgGALEALLEakeeGKIRFIGISGHSPEVLLR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446777540 154 AneilnASGYSLSAVQNHYSLLYR--ASEEAGILDYCRQNNITFFAYMVLEQGAL 206
Cdd:cd19100 150 A-----LETGEFDVVLFPINPAGDhiDSFREELLPLAREKGVGVIAMKVLAGGRL 199
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
6-220 |
2.33e-21 |
|
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: 92.24 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTWSWGTGfaggdtvfgNHLSDTQmaEVFTAAMSKGLNLWDTAAVYGM-------GSSETALGALVRQFP-RENII 77
Cdd:cd19094 3 EICLGTMTWGEQ---------NTEAEAH--EQLDYAFDEGVNFIDTAEMYPVppspetqGRTEEIIGSWLKKKGnRDKVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIAD---------KQSAQPVSDMLEASLGRLGVDAIDIYWIHNP------------LDVEKWtPGLIP----- 131
Cdd:cd19094 72 LATKVAGPGEGitwprgggtRLDRENIREAVEGSLKRLGTDYIDLYQLHWPdrytplfgggyyTEPSEE-EDSVSfeeql 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 132 -----LLQSGKVKRVGVSNHN---LAQIRRANEILNASGYsLSaVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQ 203
Cdd:cd19094 151 ealgeLVKAGKIRHIGLSNETpwgVMKFLELAEQLGLPRI-VS-IQNPYSLLNRNFEE-GLAEACHRENVGLLAYSPLAG 227
|
250
....*....|....*..
gi 446777540 204 GALSGRYDSNHPMPAGS 220
Cdd:cd19094 228 GVLTGKYLDGAARPEGG 244
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-206 |
2.86e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 91.05 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 8 ALGTWSWGTGFagGDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgSSETALGALVRQFPRENIIlsTKFTP-QI 86
Cdd:cd19097 4 ALGTAQFGLDY--GIANKSGKPSEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKRLDKFKII--TKLPPlKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 87 ADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDVEKWTPGLIPLLQS----GKVKRVGVSNHNLAQIRRANEIlnasg 162
Cdd:cd19097 78 DKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVEALLElkkeGLIRKIGVSVYSPEELEKALES----- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446777540 163 YSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGAL 206
Cdd:cd19097 153 FKIDIIQLPFNILDQRFLKSGLLAKLKKKGIEIHARSVFLQGLL 196
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
4-292 |
8.33e-21 |
|
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: 90.54 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtGFaGGDTVFGNhlsdtqMAEVFTAAMSKGLNLWDTAAVYG--MGSSETALGALVR---QFPRENIIL 78
Cdd:cd19151 12 LPAISLGLWH---NF-GDVDRYEN------SRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKedlKPYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 79 STK--FT----PqIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPlDVEkwTP------GLIPLLQSGKVKRVGVSNH 146
Cdd:cd19151 82 STKagYTmwpgP-YGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRP-DPE--TPleetmgALDQIVRQGKALYVGISNY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 147 NLAQIRRANEILNASGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRYdsNHPMPAGSgRAESY 226
Cdd:cd19151 158 PPEEAREAAAILKDLGTPCLIHQPKYSMFNRWVEE-GLLDVLEEEGIGCIAFSPLAQGLLTDRY--LNGIPEDS-RAAKG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446777540 227 NAVL--PQI--ERLTAAMK--KMGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDA-ACASDIQLRDEEI 292
Cdd:cd19151 234 SSFLkpEQIteEKLAKVRRlnEIAQARGQKLAQMALAWVLRNKrvTSVLIGASKPSQIEDAvGALDNREFSEEEL 308
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
3-153 |
1.31e-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: 88.87 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSwgtgfaggdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILST 80
Cdd:cd19132 6 QIPAIGFGTYP---------------LKGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRsgVPREELFVTT 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446777540 81 KFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIH--NP---LDVEKWTpGLIPLLQSGKVKRVGVSNHNLAQIRR 153
Cdd:cd19132 68 KLP---GRHHGYEEALRTIEESLYRLGLDYVDLYLIHwpNPsrdLYVEAWQ-ALIEAREEGLVRSIGVSNFLPEHLDR 141
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
3-193 |
4.30e-20 |
|
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: 88.38 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTgfaggdtVFGNhLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTK- 81
Cdd:cd19163 12 KVSKLGFGASPLGG-------VFGP-VDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSYYLATKv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 --FTPQIADKQ--SAQPVSDMLEASLGRLGVDAIDIYWIHnplDVEKwTPGL-------IPLLQ----SGKVKRVGVSNH 146
Cdd:cd19163 84 grYGLDPDKMFdfSAERITKSVEESLKRLGLDYIDIIQVH---DIEF-APSLdqilnetLPALQklkeEGKVRFIGITGY 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446777540 147 NLAQIRranEILNASGYSLSAVQ--NHYSLL-YRASEeagILDYCRQNNI 193
Cdd:cd19163 160 PLDVLK---EVLERSPVKIDTVLsyCHYTLNdTSLLE---LLPFFKEKGV 203
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-218 |
1.06e-19 |
|
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: 87.71 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 17 GFAGGDT--VFGNHLSDTQMAEVfTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPrENIILSTK--FTPQIADKQSA 92
Cdd:cd19104 16 TFGGGGIggLMGRTTREEQIAAV-RRALDLGINFFDTAPSYGDGKSEENLGRALKGLP-AGPYITTKvrLDPDDLGDIGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 93 QpVSDMLEASLGRLGVDAIDIYWIHN------------------PLDVEKWTPGLIPLLQSGKVKRVGVSnhNLAQIRRA 154
Cdd:cd19104 94 Q-IERSVEKSLKRLKRDSVDLLQLHNrigderdkpvggtlsttdVLGLGGVADAFERLRSEGKIRFIGIT--GLGNPPAI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446777540 155 NEILnASGySLSAVQNHYSLL-----------YRASEEAGILDYCRQNNITFFAYMVLEQGALSGryDSNHPMPA 218
Cdd:cd19104 171 RELL-DSG-KFDAVQVYYNLLnpsaaearprgWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTT--SLDRGREA 241
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
5-212 |
2.51e-19 |
|
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: 86.26 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTWSWGTGFAGGDTvfgnhlsdtQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTK--- 81
Cdd:cd19162 1 PRLGLGAASLGNLARAGED---------EAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKvgr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 -------FTPQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHNP-----LDVEKWTPGLIPLLQSGKVKRVGVSNH 146
Cdd:cd19162 72 llepgaaGRPAGADRRfdfSADGIRRSIEASLERLGLDRLDLVFLHDPdrhllQALTDAFPALEELRAEGVVGAIGVGVT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446777540 147 NLAQIRRAneiLNASGYSLSAVQNHYSLLYRASeEAGILDYCRQNNITFFAYMVLEQGAL------SGRYDS 212
Cdd:cd19162 152 DWAALLRA---ARRADVDVVMVAGRYTLLDRRA-ATELLPLCAAKGVAVVAAGVFNSGILatddpaGDRYDY 219
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-276 |
8.19e-19 |
|
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: 84.69 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 33 QMAEVFTAAmskGLNLWDTAAVYGM-------GSSETALGALVRQFP-RENIILSTK--FTPQIADK-------QSAQPV 95
Cdd:cd19752 21 AILDRYVAA---GGNFLDTANNYAFwteggvgGESERLIGRWLKDRGnRDDVVIATKvgAGPRDPDGgpespegLSAETI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 96 SDMLEASLGRLGVDAIDIYWIH-----NPLdvEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILNASGY-SLSAVQ 169
Cdd:cd19752 98 EQEIDKSLRRLGTDYIDLYYAHvddrdTPL--EETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWaEFSAIQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 170 NHYSLLYRAS--EEAG-------ILDYCRQN-NITFFAYMVLEQGALSgryDSNHPMPAGSGRAESyNAVLPQIERLTaa 239
Cdd:cd19752 176 QRHSYLRPRPgaDFGVqrivtdeLLDYASSRpDLTLLAYSPLLSGAYT---RPDRPLPEQYDGPDS-DARLAVLEEVA-- 249
|
250 260 270
....*....|....*....|....*....|....*..
gi 446777540 240 mKKMGAERNASVAQIAIAWAIakGTLPLVGATKVHHV 276
Cdd:cd19752 250 -GELGATPNQVVLAWLLHRTP--AIIPLLGASTVEQL 283
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
4-301 |
1.94e-18 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 84.27 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtgfaggdtVFG-NHLSDTQMAeVFTAAMSKGLNLWDTAAVYG--MGSSETALGALVRQ-FP--RENII 77
Cdd:PRK09912 25 LPALSLGLWH----------NFGhVNALESQRA-ILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdFAayRDELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTK-----FTPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNpldVEKWTP------GLIPLLQSGKVKRVGVSNH 146
Cdd:PRK09912 94 ISTKagydmWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHR---VDENTPmeetasALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 147 NLAQIRRANEILNASGYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNhpMPAGSGRAESY 226
Cdd:PRK09912 171 SPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG--IPQDSRMHREG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 227 NAVLPQIER-LTAA-------MKKMGAERNASVAQIAIA--WAIAKGTLPLVGATKVHHVLDAACA-SDIQLRDEEIILL 295
Cdd:PRK09912 249 NKVRGLTPKmLTEAnlnslrlLNEMAQQRGQSMAQMALSwlLKDERVTSVLIGASRAEQLEENVQAlNNLTFSTEELAQI 328
|
....*.
gi 446777540 296 EQLAAE 301
Cdd:PRK09912 329 DQHIAD 334
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-210 |
8.86e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 81.87 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSwgtgFAGGDtvfGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgSSETALGALVRQFPRE-----NII 77
Cdd:cd19101 1 TISRVINGMWQ----LSGGH---GGIRDEDAAVRAMAAYVDAGLTTFDCADIYG--PAEELIGEFRKRLRRErdaadDVQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIADKQ-SAQPVSDMLEASLGRLGVDAIDIYWIH-------NPLDVEKWtpgLIPLLQSGKVKRVGVSNHNLA 149
Cdd:cd19101 72 IHTKWVPDPGELTmTRAYVEAAIDRSLKRLGVDRLDLVQFHwwdysdpGYLDAAKH---LAELQEEGKIRHLGLTNFDTE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 150 QIRranEILNAsGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSGRY 210
Cdd:cd19101 149 RLR---EILDA-GVPIVSNQVQYSLLDRRPEN-GMAALCEDHGIKLLAYGTLAGGLLSEKY 204
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
3-201 |
1.13e-17 |
|
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: 81.12 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTwswGTG-FAGGDTVFGNHLSDTqmaevFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF--PRENIILS 79
Cdd:cd19120 3 KIPAIAFGT---GTAwYKSGDDDIQRDLVDS-----VKLALKAGFRHIDTAEMYG---NEKEVGEALKESgvPREDLFIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 80 TKFTPQIADKQSAqpvsdmLEASLGRLGVDAIDIYWIHNPLDVEKWTPGLI-------PLLQSGKVKRVGVSNHNLAQIR 152
Cdd:cd19120 72 TKVSPGIKDPREA------LRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLAeawaeleALKDAGLVRSIGVSNFRIEDLE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446777540 153 ranEILNASGYsLSAV-QNHYS-LLYRASEEagILDYCRQNNITFFAYMVL 201
Cdd:cd19120 146 ---ELLDTAKI-KPAVnQIEFHpYLYPQQPA--LLEYCREHGIVVSAYSPL 190
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
4-244 |
1.48e-17 |
|
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: 81.35 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtGFaGGDTVFgnhlsDTQMAEVFTAaMSKGLNLWDTAAVYG--MGSSETALGALVRQ-FP--RENIIL 78
Cdd:cd19150 12 LPALSLGLWH---NF-GDDTPL-----ETQRAILRTA-FDLGITHFDLANNYGppPGSAEENFGRILREdFAgyRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 79 STK-----FTPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIH-----NPLdvEKWTPGLIPLLQSGKVKRVGVSNHNL 148
Cdd:cd19150 82 STKagydmWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHrfdpdTPL--EETMGALDHAVRSGKALYVGISSYSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 149 AQIRRANEILNASGYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHPMPAGSGRAESYNA 228
Cdd:cd19150 160 ERTREAAAILRELGTPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERSLSP 239
|
250 260
....*....|....*....|..
gi 446777540 229 ------VLPQIERLTAAMKKMG 244
Cdd:cd19150 240 kmlteaNLNSIRALNEIAQKRG 261
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
4-300 |
1.51e-16 |
|
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: 77.39 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtGFAGGDTVfgnhlsdtqmaEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF--PRENIILSTK 81
Cdd:cd19139 1 IPAFGLGTF----RLKDDVVI-----------DSVRTALELGYRHIDTAQIYD---NEAAVGQAIAESgvPRDELFITTK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 FTPqiaDKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP-----LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANE 156
Cdd:cd19139 63 IWI---DNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPspndeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 157 ILNASGYSLSAVQNHYSLLYRAseeagILDYCRQNNITFFAYMVLEQGALsgrydsnhpmpagsGRAEsynavlpqierl 236
Cdd:cd19139 140 VVGAGAIATNQIELSPYLQNRK-----LVAHCKQHGIHVTSYMTLAYGKV--------------LDDP------------ 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 237 taAMKKMGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIillEQLAA 300
Cdd:cd19139 189 --VLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDM---AAIAA 247
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
3-207 |
8.66e-16 |
|
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: 75.37 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSwgtgfaggdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILST 80
Cdd:cd19140 7 RIPALGLGTYP---------------LTGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAAsgVPRDELFLTT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 81 KFTPqiaDKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP-LDVE-KWTPG-LIPLLQSGKVKRVGVSNHNLAQIRRANEI 157
Cdd:cd19140 69 KVWP---DNYSPDDFLASVEESLRKLRTDYVDLLLLHWPnKDVPlAETLGaLNEAQEAGLARHIGVSNFTVALLREAVEL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446777540 158 lnaSGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAYMVLEQGALS 207
Cdd:cd19140 146 ---SEAPLFTNQVEYHPYLDQRK---LLDAAREHGIALTAYSPLARGEVL 189
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
27-248 |
1.58e-15 |
|
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: 75.44 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 27 NHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTK----FTPQIADKQSA---------- 92
Cdd:cd19161 15 TAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKvgrlLKPAREGSVPDpngfvdplpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 93 QPVSD------M--LEASLGRLGVDAIDIYWIHnplDVEKWTPG------------------LIPLLQSGKVKRVGVSNh 146
Cdd:cd19161 95 EIVYDysydgiMrsFEDSLQRLGLNRIDILYVH---DIGVYTHGdrkerhhfaqlmsggfkaLEELKKAGVIKAFGLGV- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 147 NLAQIrrANEILNASGYSLSAVQNHYSLLYRASEEaGILDYCRQNNITFFAYMVLEQGALSgrydsnhpMPAGSGRAESY 226
Cdd:cd19161 171 NEVQI--CLEALDEADLDCFLLAGRYSLLDQSAEE-EFLPRCEQRGTSLVIGGVFNSGILA--------TGTKSGAKFNY 239
|
250 260
....*....|....*....|..
gi 446777540 227 NAVLPQIERLTAAMKKMGAERN 248
Cdd:cd19161 240 GDAPAEIISRVMEIEKICDAYN 261
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
30-206 |
1.75e-15 |
|
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: 74.78 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 30 SDTQMAEVFTAAMSKGLNLWDTAAVYgmgSSETALGALVRQ--FPRENIILSTKFTpqiADKQSAQPVSDMLEASLGRLG 107
Cdd:cd19126 21 DGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIREsgVPREELFVTTKLW---NDDQRARRTEDAFQESLDRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 108 VDAIDIYWIHNPLD---VEKWTpGLIPLLQSGKVKRVGVSN---HNLAQIRRANEILNAsgysLSAVQNHYSLLYRAsee 181
Cdd:cd19126 95 LDYVDLYLIHWPGKdkfIDTWK-ALEKLYASGKVKAIGVSNfqeHHLEELLAHADVVPA----VNQVEFHPYLTQKE--- 166
|
170 180
....*....|....*....|....*
gi 446777540 182 agILDYCRQNNITFFAYMVLEQGAL 206
Cdd:cd19126 167 --LRGYCKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
25-251 |
3.38e-15 |
|
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: 74.94 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 25 FGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQ--FPRENIILSTKF-----TPQIADKQ-SAQPVS 96
Cdd:cd19143 24 FGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKElgWPRSDYVVSTKIfwgggGPPPNDRGlSRKHIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 97 DMLEASLGRLGVDAIDIYWIHNPlDVEkwTP------GLIPLLQSGKVKRVGVSNHNLAQIRRANEIlnASGYSLSAV-- 168
Cdd:cd19143 104 EGTKASLKRLQLDYVDLVFCHRP-DPA--TPieetvrAMNDLIDQGKAFYWGTSEWSAQQIEEAHEI--ADRLGLIPPvm 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 169 -QNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYdsNHPMPAGSgRAEsynavLPQIERLTAAMKKMGAER 247
Cdd:cd19143 179 eQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKY--NNGIPEGS-RLA-----LPGYEWLKDRKEELGQEK 250
|
....
gi 446777540 248 NASV 251
Cdd:cd19143 251 IEKV 254
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
6-296 |
3.97e-15 |
|
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: 74.77 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTWSWGTGFAGGdtvFGNHLSDTQMAeVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFP-RENIILSTKFT- 83
Cdd:cd19146 13 PLCLGAMSFGEAWKSM---MGECDKETAFK-LLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGnRDEMVLATKYTt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 --------PQIADKQSAQPVSDML--EASLGRLGVDAIDIYWIH---NPLDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQ 150
Cdd:cd19146 89 gyrrggpiKIKSNYQGNHAKSLRLsvEASLKKLQTSYIDILYVHwwdYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 151 IRRANEILNASG-YSLSAVQNHYSLLYRaSEEAGILDYCRQNNITFFAYMVLEQGALsgRYDSNHPMPAGSGRAEsynav 229
Cdd:cd19146 169 VSKANAYARAHGlTQFVVYQGHWSAAFR-DFERDILPMCEAEGMALAPWGVLGQGQF--RTEEEFKRRGRSGRKG----- 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446777540 230 LPQIE---RLTAAMKKMGAERNASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19146 241 GPQTEkerKVSEKLEKVAEEKGTAITSVALAYVMHKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIE 312
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
21-239 |
5.38e-15 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 74.51 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 21 GDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGM-------GSSETALGA-LVRQFPRENIILSTKFT-PQIADKQS 91
Cdd:PRK10625 19 GTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNwLAKRGSREKLIIASKVSgPSRNNDKG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 92 AQP--------VSDMLEASLGRLGVDAIDIYWIHNP---------LDVEkWTPG--LIPLLQS----------GKVKRVG 142
Cdd:PRK10625 99 IRPnqaldrknIREALHDSLKRLQTDYLDLYQVHWPqrptncfgkLGYS-WTDSapAVSLLETldalaeqqraGKIRYIG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 143 VSNHNLAQIRRANEIlnASGYSLS---AVQNHYSLLYRaSEEAGILDYCRQNNITFFAYMVLEQGALSGRYdSNHPMPAG 219
Cdd:PRK10625 178 VSNETAFGVMRYLHL--AEKHDLPrivTIQNPYSLLNR-SFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY-LNGAKPAG 253
|
250 260
....*....|....*....|....*
gi 446777540 220 S-----GRAESYNAvlPQIERLTAA 239
Cdd:PRK10625 254 ArntlfSRFTRYSG--EQTQKAVAA 276
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-209 |
1.26e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 73.12 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSwgtgfagGDTVFGnhlSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVR------QFPRENI 76
Cdd:cd19099 2 TLSSLGLGTYR-------GDSDDE---TDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALReliekgGIKRDEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 77 ILSTK----------------------FTPQIADKQSAQPVSDM--------LEASLGRLGVDAIDIYWIHNP-----LD 121
Cdd:cd19099 72 VIVTKagyipgdgdeplrplkyleeklGRGLIDVADSAGLRHCIspayledqIERSLKRLGLDTIDLYLLHNPeeqllEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 122 VEKWTPGLIPLL--------QSGKVKRVGVS-------------NHNLAQIRRANEILNASGYSLSAVQ---NHYSL--L 175
Cdd:cd19099 152 GEEEFYDRLEEAfealeeavAEGKIRYYGIStwdgfrappalpgHLSLEKLVAAAEEVGGDNHHFKVIQlplNLLEPeaL 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 446777540 176 YRASEEAG----ILDYCRQNNITFFAYMVLEQGALSGR 209
Cdd:cd19099 232 TEKNTVKGealsLLEAAKELGLGVIASRPLNQGQLLGE 269
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
4-207 |
1.36e-14 |
|
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: 72.28 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGtgfaGGDTVFGnhlsdtqmaeVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF------PRENII 77
Cdd:cd19136 1 MPILGLGTFRLR----GEEEVRQ----------AVDAALKAGYRLIDTASVYR---NEADIGKALRDLlpkyglSREDIF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQiadKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPlDVEKWTPG--------------LIPLLQSGKVKRVGV 143
Cdd:cd19136 64 ITSKLAPK---DQGYEKARAACLGSLERLGTDYLDLYLIHWP-GVQGLKPSdprnaelrreswraLEDLYKEGKLRAIGV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 144 SNHNLAQIRranEILNASGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAYMVLEQGALS 207
Cdd:cd19136 140 SNYTVRHLE---ELLKYCEVPPAVNQVEFHPHLVQKE---LLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-298 |
1.73e-14 |
|
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: 71.97 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGtGFAGGDTVFgnhlsdtqmaevftAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILSTK 81
Cdd:cd19135 13 MPILGLGTSHSG-GYSHEAVVY--------------ALKECGYRHIDTAKRYG---CEELLGKAIKEsgVPREDLFLTTK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 FTPqiaDKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDV-----------EKWTpGLIPLLQSGKVKRVGVSNHnlaQ 150
Cdd:cd19135 75 LWP---SDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPssgknvketraETWR-ALEELYDEGLCRAIGVSNF---L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 151 IRRANEILNASGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAYMVLEQG-ALsgrydsNHPmpAGSGRAESYNAV 229
Cdd:cd19135 148 IEHLEQLLEDCSVVPHVNQVEFHPFQNPVE---LIEYCRDNNIVFEGYCPLAKGkAL------EEP--TVTELAKKYQKT 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446777540 230 LPQIerltaamkkmgaernasvaqiAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQL 298
Cdd:cd19135 217 PAQI---------------------LIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
31-206 |
3.77e-14 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 70.88 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 31 DTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILSTKFTpqiADKQSAQPVSDMLEASLGRLGV 108
Cdd:cd19157 23 GSEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKEsgIPREELFITSKVW---NADQGYDSTLKAFEASLERLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 109 DAIDIYWIHNP---LDVEKWTpGLIPLLQSGKVKRVGVSN---HNLAQIRRANEILNAsgysLSAVQNHYSLLYRAseea 182
Cdd:cd19157 97 DYLDLYLIHWPvkgKYKETWK-ALEKLYKDGRVRAIGVSNfqvHHLEDLLADAEIVPM----VNQVEFHPRLTQKE---- 167
|
170 180
....*....|....*....|....
gi 446777540 183 gILDYCRQNNITFFAYMVLEQGAL 206
Cdd:cd19157 168 -LRDYCKKQGIQLEAWSPLMQGQL 190
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-198 |
5.41e-14 |
|
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: 71.16 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSwgtgfaGGDtvfgnhlsDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF------PRENI 76
Cdd:cd19116 10 EIPAIALGTWK------LKD--------DEGVRQAVKHAIEAGYRHIDTAYLYG---NEAEVGEAIREKiaegvvKREDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 77 ILSTKFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLD--------------------VEKWTpGLIPLLQSG 136
Cdd:cd19116 73 FITTKLW---NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAfkenndsesngdgslsdidyLETWR-GMEDLVKLG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446777540 137 KVKRVGVSNHNLAQIRRaneILnASGYSLSAV---QNHYSLLYRAseeagILDYCRQNNITFFAY 198
Cdd:cd19116 149 LTRSIGVSNFNSEQINR---LL-SNCNIKPAVnqiEVHPTLTQEK-----LVAYCQSNGIVVMAY 204
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
2-145 |
1.49e-13 |
|
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: 69.50 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 2 KTLPPVALGTWSwgtgfaggdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILS 79
Cdd:cd19134 9 NTMPVIGLGVGE---------------LSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAAsgIPRGELFVT 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 80 TKFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLD-----VEKWTpGLIPLLQSGKVKRVGVSN 145
Cdd:cd19134 71 TKLA---TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAGregkyVDSWG-GLMKLREEGLARSIGVSN 137
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
41-145 |
2.76e-13 |
|
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: 68.37 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 41 AMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILSTKFTPQIADKQSAqpvSDMLEASLGRLGVDAIDIYWIHN 118
Cdd:cd19133 32 AIKAGYRLIDTAAAYG---NEEAVGRAIKKsgIPREELFITTKLWIQDAGYEKA---KKAFERSLKRLGLDYLDLYLIHQ 105
|
90 100
....*....|....*....|....*...
gi 446777540 119 PL-DVEKWTPGLIPLLQSGKVKRVGVSN 145
Cdd:cd19133 106 PFgDVYGAWRAMEELYKEGKIRAIGVSN 133
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-153 |
4.62e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 68.18 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILSTK 81
Cdd:PRK11565 15 MPQLGLGVW---------------QASNEEVITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEasVAREELFITTK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 82 FTPqiADKQSAQpvsDMLEASLGRLGVDAIDIYWIHNPLD-----VEKWTpGLIPLLQSGKVKRVGVSNHNLAQIRR 153
Cdd:PRK11565 77 LWN--DDHKRPR---EALEESLKKLQLDYVDLYLMHWPVPaidhyVEAWK-GMIELQKEGLIKSIGVCNFQIHHLQR 147
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
5-143 |
6.25e-13 |
|
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: 68.02 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 5 PPVALGTWSWGTGFAggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFPRENIILSTK--- 81
Cdd:cd19152 1 PKLGFGTAPLGNLYE--------AVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKvgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 -FTPQIADKQ------------------SAQPVSDMLEASLGRLGVDAIDIYWIHNPLDV---EKWT-----------PG 128
Cdd:cd19152 73 lLVPLQEVEPtfepgfwnplpfdavfdySYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDlagAESDehfaqaikgafRA 152
|
170
....*....|....*
gi 446777540 129 LIPLLQSGKVKRVGV 143
Cdd:cd19152 153 LEELREEGVIKAIGL 167
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-175 |
1.17e-12 |
|
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: 67.18 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTwswgtgfAGGDTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALG-ALVR-QFPRENIILSTKfT 83
Cdd:cd19153 14 PVGLGT-------AALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGkALAAlQVPRSSYTVATK-V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHN------PLDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRA 154
Cdd:cd19153 86 GRYRDSEfdySAERVRASVATSLERLHTTYLDVVYLHDiefvdyDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRA 165
|
170 180
....*....|....*....|...
gi 446777540 155 NEilNASGYSLSAVQN--HYSLL 175
Cdd:cd19153 166 TR--RCSPGSLDAVLSycHLTLQ 186
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
6-296 |
1.95e-12 |
|
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: 66.77 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 6 PVALGTWSWGTGFAGgdtvFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQFP-RENIILSTKFTP 84
Cdd:cd19147 12 PLILGAMSIGDAWSG----FMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKnRDQIVIATKFTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 85 QIADKQSAQPVSD------------MLEASLGRLGVDAIDIYWIHN---PLDVEKWTPGLIPLLQSGKVKRVGVSNHNLA 149
Cdd:cd19147 88 DYKAYEVGKGKAVnycgnhkrslhvSVRDSLRKLQTDWIDILYVHWwdyTTSIEEVMDSLHILVQQGKVLYLGVSDTPAW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 150 QIRRANEILNASGYS-LSAVQNHYSLLYRASEEAgILDYCRQNNITFFAYMVLEQG------ALSGRYDSNHPMPAGSGR 222
Cdd:cd19147 168 VVSAANYYATAHGKTpFSVYQGRWNVLNRDFERD-IIPMARHFGMALAPWDVLGGGkfqskkAVEERKKNGEGLRSFVGG 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 223 AESYnavlPQIERLTAAMKKMGAERN-ASVAQIAIAWAIAKG--TLPLVGATKVHHVLDAACASDIQLRDEEIILLE 296
Cdd:cd19147 247 TEQT----PEEVKISEALEKVAEEHGtESVTAIALAYVRSKApnVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
4-201 |
3.62e-12 |
|
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: 65.60 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGTgfaggdtvfgnhlsdtqmAEVFTA---AMSKGLNLWDTAAVYGmgsSETALGALVRQF------PRE 74
Cdd:cd19111 4 MPVIGLGTYQSPP------------------EEVRAAvdyALFVGYRHIDTALSYQ---NEKAIGEALKWWlkngklKRE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 75 NIILSTKFTPQiadKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDVE-KWTPGLIPLLQS---------------GKV 138
Cdd:cd19111 63 EVFITTKLPPV---YLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVnKKDKGERELASSdvtsvwramealvseGKV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446777540 139 KRVGVSNHNLAQIRRaneilnASGYSLSAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVL 201
Cdd:cd19111 140 KSIGLSNFNPRQINK------ILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPL 196
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
2-174 |
3.86e-12 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 65.76 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 2 KTLPPVALGTWSWGTGFAggdtvfgNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgSSETALG----ALVRQFPRENII 77
Cdd:cd19164 11 AGLPPLIFGAATFSYQYT-------TDPESIPPVDIVRRALELGIRAFDTSPYYG--PSEIILGralkALRDEFPRDTYF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKfTPQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHnplDVEKWTPG--------LIPLLQSGKVKRVGVSNH 146
Cdd:cd19164 82 IITK-VGRYGPDDfdySPEWIRASVERSLRRLHTDYLDLVYLH---DVEFVADEevlealkeLFKLKDEGKIRNVGISGY 157
|
170 180 190
....*....|....*....|....*....|.
gi 446777540 147 NLAQIRR-ANEILNASGYSLSAVQN--HYSL 174
Cdd:cd19164 158 PLPVLLRlAELARTTAGRPLDAVLSycHYTL 188
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
4-117 |
4.08e-12 |
|
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: 65.95 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtgfaggdtVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQ--FPRENIILSTK 81
Cdd:cd19142 13 VSNVGLGTWS----------TFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKkgWKRSSYIVSTK 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 446777540 82 F---TPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIH 117
Cdd:cd19142 83 IywsYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-201 |
4.44e-12 |
|
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: 65.51 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwGTGFAGgdtvfgnhlsdtqmAEVFTAAMSKGLNLWDTAAVYgmgSSETALGALVRQF------PRENII 77
Cdd:cd19154 12 MPLIGLGTWQ-SKGAEG--------------ITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegvvKREDLF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQiADKQSAqpVSDMLEASLGRLGVDAIDIYWIHNPL----------------------DVEKWTPGLIPLLQS 135
Cdd:cd19154 74 ITTKLWTH-EHAPED--VEEALRESLKKLQLEYVDLYLIHAPAafkddegesgtmengmsihdavDVEDVWRGMEKVYDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446777540 136 GKVKRVGVSNHNLAQIRRaneILNASGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAYMVL 201
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQR---ILDNARVKPHNNQVECHLYFPQKE---LVEFCKKHNISVTSYATL 210
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
7-215 |
1.01e-11 |
|
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: 64.39 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWswgtgfaggdTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVR--QFPRENIILSTK-FT 83
Cdd:cd19141 15 LGLGTW----------VTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKkkGWRRSSYVITTKiFW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEI 157
Cdd:cd19141 85 GGKAETErglSRKHIIEGLKASLERLQLEYVDIVFANRPdpnTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 158 lnASGYSL---SAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHP 215
Cdd:cd19141 165 --ARQFNLippIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVP 223
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
7-215 |
1.71e-11 |
|
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: 63.91 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWswgtgfaggdTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQ--FPRENIILSTKF-- 82
Cdd:cd19159 16 LGLGTW----------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLyw 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 83 --TPQIADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEI 157
Cdd:cd19159 86 ggKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPdsnTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 158 lnASGYSL---SAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHP 215
Cdd:cd19159 166 --ARQFNMippVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVP 224
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
2-255 |
2.55e-11 |
|
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: 62.77 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 2 KTLPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILS 79
Cdd:cd19131 8 NTIPQLGLGVW---------------QVSNDEAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRAsgVPREELFIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 80 TKFtpqiadKQSAQPVSDMLEA---SLGRLGVDAIDIYWIHNPLD-----VEKWTpGLIPLLQSGKVKRVGVSNHNLAQI 151
Cdd:cd19131 70 TKL------WNSDQGYDSTLRAfdeSLRKLGLDYVDLYLIHWPVPaqdkyVETWK-ALIELKKEGRVKSIGVSNFTIEHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 152 RRaneILNASGY--SLSAVQNHYSLLYRASEEagildYCRQNNITFFAYMvleqgalsgrydsnhpmPAGSGRAESyNAV 229
Cdd:cd19131 143 QR---LIDETGVvpVVNQIELHPRFQQRELRA-----FHAKHGIQTESWS-----------------PLGQGGLLS-DPV 196
|
250 260
....*....|....*....|....*.
gi 446777540 230 LPQIerltaamkkmGAERNASVAQIA 255
Cdd:cd19131 197 IGEI----------AEKHGKTPAQVV 212
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
7-215 |
2.83e-11 |
|
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: 63.18 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWswgtgfaggdTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQ--FPRENIILSTK-FT 83
Cdd:cd19158 16 LGLGTW----------VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKiFW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIHNP---LDVEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEI 157
Cdd:cd19158 86 GGKAETErglSRKHIIEGLKASLERLQLEYVDVVFANRPdpnTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 158 lnASGYSLS---AVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHP 215
Cdd:cd19158 166 --ARQFNLIppiCEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP 224
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
33-153 |
3.14e-11 |
|
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: 62.81 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 33 QMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILSTKFtpQIAD--KQSAQpvsDMLEASLGRLGV 108
Cdd:cd19127 23 ETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRsgVDRSDIFVTTKL--WISDygYDKAL---RGFDASLRRLGL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446777540 109 DAIDIYWIHNPL------DVEKWTpGLIPLLQSGKVKRVGVSNHNLAQIRR 153
Cdd:cd19127 95 DYVDLYLLHWPVpndfdrTIQAYK-ALEKLLAEGRVRAIGVSNFTPEHLER 144
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
41-206 |
4.58e-11 |
|
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: 62.15 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 41 AMSKGLNLWDTAAVYgmgSSETALGALVRQ--FPRENIILSTKFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIHN 118
Cdd:cd19156 32 AIEAGYRHIDTAAIY---KNEEGVGQGIREsgVPREEVFVTTKLW---NSDQGYESTLAAFEESLEKLGLDYVDLYLIHW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 119 PLD---VEKWTpGLIPLLQSGKVKRVGVSN---HNLAQIRRANEILNAsgysLSAVQNHYSLLYRASEEagildYCRQNN 192
Cdd:cd19156 106 PVKgkfKDTWK-AFEKLYKEKKVRAIGVSNfheHHLEELLKSCKVAPM----VNQIELHPLLTQEPLRK-----FCKEKN 175
|
170
....*....|....
gi 446777540 193 ITFFAYMVLEQGAL 206
Cdd:cd19156 176 IAVEAWSPLGQGKL 189
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
4-198 |
7.26e-11 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 61.78 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGTGfaggdtvfgnhlsdtQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ-----FPRENIIL 78
Cdd:cd19121 12 IPAVGLGTWQAKAG---------------EVKAAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEaiaggVKREDLFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 79 STKFTPQIADKqsaqpVSDMLEASLGRLGVDAIDIYWIHNPL--------------------------DVEKWTPgLIPL 132
Cdd:cd19121 74 TTKLWSTYHRR-----VELCLDRSLKSLGLDYVDLYLVHWPVllnpngnhdlfptlpdgsrdldwdwnHVDTWKQ-MEKV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446777540 133 LQSGKVKRVGVSNHNLAQIrranEILNASGYSLSA---VQNHYSLlyrasEEAGILDYCRQNNITFFAY 198
Cdd:cd19121 148 LKTGKTKAIGVSNYSIPYL----EELLKHATVVPAvnqVENHPYL-----PQQELVDFCKEKGILIEAY 207
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
17-144 |
1.17e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 61.33 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 17 GFAGG--DTVFGNHLSDTQMAEVFTAAmSKGLNLWDTAAVYGMGSSETALGALVR--QFPRENIILSTK---------Ft 83
Cdd:PLN02587 15 GFGASplGSVFGPVSEEDAIASVREAF-RLGINFFDTSPYYGGTLSEKVLGKALKalGIPREKYVVSTKcgrygegfdF- 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446777540 84 pqiadkqSAQPVSDMLEASLGRLGVDAIDIYWIHN----PLD--VEKWTPGLIPLLQSGKVKRVGVS 144
Cdd:PLN02587 93 -------SAERVTKSVDESLARLQLDYVDILHCHDiefgSLDqiVNETIPALQKLKESGKVRFIGIT 152
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
4-198 |
5.87e-10 |
|
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: 59.05 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ--FPRENIILSTK 81
Cdd:cd19117 14 IPAVGLGTW---------------QSKPNEVAKAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDsgVPREEIFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 82 ftpqIADKQSAQPvSDMLEASLGRLGVDAIDIYWIHNPL-------------------DVEKWTP----GLI-PLLQSGK 137
Cdd:cd19117 76 ----LWCTWHRRV-EEALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtkdHEPDWDFiktwELMqKLPATGK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446777540 138 VKRVGVSNHNLAQIRranEILNASGYSLSAVQNHYSLL-YRASEEagILDYCRQNNITFFAY 198
Cdd:cd19117 151 VKAIGVSNFSIKNLE---KLLASPSAKIVPAVNQIELHpLLPQPK--LVDFCKSKGIHATAY 207
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
7-215 |
1.74e-09 |
|
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: 58.07 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 7 VALGTWswgtgfaggdTVFGNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGMGSSETALGALVRQ--FPRENIILSTK-FT 83
Cdd:cd19160 18 LGLGTW----------VTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgWRRSSYVVTTKiYW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 84 PQIADKQ---SAQPVSDMLEASLGRLGVDAIDIYWIhNPLD----VEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANE 156
Cdd:cd19160 88 GGQAETErglSRKHIIEGLRGSLDRLQLEYVDIVFA-NRSDpnspMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446777540 157 IlnASGYSL---SAVQNHYSLLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRYDSNHP 215
Cdd:cd19160 167 V--ARQFNLippVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVP 226
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
21-298 |
2.79e-09 |
|
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: 56.84 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 21 GDTVFGNHLSDTQmaEVFTAAMSKGLNLWDTAAVYGmgsSETALGAL--VRQFPRENIILSTKFTpqiADKQSAQPVSDM 98
Cdd:cd19130 14 GYGVFKVPPADTQ--RAVATALEVGYRHIDTAAIYG---NEEGVGAAiaASGIPRDELFVTTKLW---NDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 99 LEASLGRLGVDAIDIYWIHNPLD-----VEKWTpGLIPLLQSGKVKRVGVSNHNLAQIRRaneILNASGYSLSAVQNHys 173
Cdd:cd19130 86 FAESLAKLGLDQVDLYLVHWPTPaagnyVHTWE-AMIELRAAGRTRSIGVSNFLPPHLER---IVAATGVVPAVNQIE-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 174 lLYRASEEAGILDYCRQNNITFFAYMVLEQGALSGRydsnhpmpagsgraesynavlPQIERLTAAMKKmgaernaSVAQ 253
Cdd:cd19130 160 -LHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGD---------------------PPVGAIAAAHGK-------TPAQ 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446777540 254 IAIAWAIAKGTLPLVGATKVHHVLDAACASDIQLRDEEIILLEQL 298
Cdd:cd19130 211 IVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
25-204 |
2.99e-09 |
|
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: 57.08 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 25 FGNHLSD-TQMAEVFTAAMSKGLNLWDTAAVYgmgSSETALGALVRQ------FPRENIILSTKFTPQIADKQSAQPVsd 97
Cdd:cd19129 11 FGTLIPDpSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEvfkagkIRREDLFVTTKLWNTNHRPERVKPA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 98 mLEASLGRLGVDAIDIYWIHNPLD------------------------VEKWTpGLIPLLQSGKVKRVGVSNHNLAQIRr 153
Cdd:cd19129 86 -FEASLKRLQLDYLDLYLIHTPFAfqpgdeqdprdangnviyddgvtlLDTWR-AMERLVDEGRCKAIGLSDVSLEKLR- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446777540 154 anEILNASGYSLSAVQ--NHYSLlyrasEEAGILDYCRQNNITFFAYMVLEQG 204
Cdd:cd19129 163 --EIFEAARIKPAVVQveSHPYL-----PEWELLDFCKNHGIVLQAFAPLGHG 208
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-244 |
7.34e-09 |
|
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: 55.97 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtgfaggdtvfgNHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ------FPRENII 77
Cdd:cd19119 12 IPALGLGTAS-------------PHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRaiddgsIKREELF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIADKqsaqpVSDMLEASLGRLGVDAIDIYWIHNPLDVEK------------WTPGLI--------------- 130
Cdd:cd19119 76 ITTKVWPTFYDE-----VERSLDESLKALGLDYVDLLLVHWPVCFEKdsddsgkpftpvNDDGKTryaasgdhittykql 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 131 -PLLQSGKVKRVGVSNHNLAQIRRaneILNASGY--SLSAVQNHYSLLYRAseeagILDYCRQNNITFFAYmvleqGALS 207
Cdd:cd19119 151 eKIYLDGRAKAIGVSNYSIVYLER---LIKECKVvpAVNQVELHPHLPQMD-----LRDFCFKHGILVTAY-----SPLG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446777540 208 GRYDSNHPMPAGSGRAESYN----------------AVLPQ---IERLTAAMKKMG 244
Cdd:cd19119 218 SHGAPNLKNPLVKKIAEKYNvstgdilisyhvrqgvIVLPKslkPVRIVSNGKIVS 273
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-198 |
7.36e-09 |
|
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: 55.99 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQF------PRENII 77
Cdd:cd19155 12 MPVVGLGTW---------------QSSPEEIETAVDTALEAGYRHIDTAYVYR---NEAAIGNVLKKWidsgkvKREELF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFtPQIADKqsAQPVSDMLEASLGRLGVDAIDIYWIHNPLD-------------------------VEKWTpGLIPL 132
Cdd:cd19155 74 IVTKL-PPGGNR--REKVEKFLLKSLEKLQLDYVDLYLIHFPVGslskeddsgkldptgehkqdyttdlLDIWK-AMEAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446777540 133 LQSGKVKRVGVSNHNLAQIRRaneILNASGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAY 198
Cdd:cd19155 150 VDQGLTRSIGLSNFNREQMAR---ILKNARIKPANLQVELHVYLQQKD---LVDFCSTHSITVTAY 209
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-160 |
9.42e-09 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 55.43 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTGFAGgDTVFgnhlsdtqmaevftAAMSKGLNLWDTAAVYGmgsSET----ALGALVRQ--FPRENI 76
Cdd:cd19125 10 KIPAVGLGTWQADPGVVG-NAVK--------------TAIKEGYRHIDCAAIYG---NEKeigkALKKLFEDgvVKREDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 77 ILSTKFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLDVEKWTPGLIP-----------------LLQSGKVK 139
Cdd:cd19125 72 FITSKLW---CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPeevlppdipstwkamekLVDSGKVR 148
|
170 180
....*....|....*....|.
gi 446777540 140 RVGVSNHNLAQIrraNEILNA 160
Cdd:cd19125 149 AIGVSNFSVKKL---EDLLAV 166
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
50-215 |
5.59e-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: 53.39 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 50 DTAAVYGmgsSETALGALVRQ------FPRENIILSTK-----FTPQIadkqsaqpVSDMLEASLGRLGVDAIDIYWIHN 118
Cdd:cd19108 45 DSAYLYQ---NEEEVGQAIRSkiadgtVKREDIFYTSKlwctfHRPEL--------VRPALEKSLKKLQLDYVDLYLIHF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 119 PLDVEkwtPG--LIPLLQSGK-----------------------VKRVGVSNHNLAQIRRaneILNASGYSLSAVQN--- 170
Cdd:cd19108 114 PVALK---PGeeLFPKDENGKlifdtvdlcatweamekckdaglAKSIGVSNFNRRQLEM---ILNKPGLKYKPVCNqve 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446777540 171 -HYSLlyrasEEAGILDYCRQNNITFFAYmvleqGAL-SGRY----DSNHP 215
Cdd:cd19108 188 cHPYL-----NQSKLLDFCKSKDIVLVAY-----SALgSQRDkewvDQNSP 228
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
1-201 |
8.75e-08 |
|
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: 52.65 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 1 MKTLPPVALGTWSWGTGfaggdtvfgnhlsdtQMAEVFTAAMSKGLNLWDTAAVY------GMGSSETALGALVRqfpRE 74
Cdd:cd19110 1 MEDIPAVGLGTWKASPG---------------EVTEAVKVAIDAGYRHFDCAYLYhnesevGAGIREKIKEGVVR---RE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 75 NIILSTKFTPQIADKQSaqpVSDMLEASLGRLGVDAIDIYWIHNPLDVEKWTPGLiPLLQSGK----------------- 137
Cdd:cd19110 63 DLFIVSKLWCTCHKKSL---VKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDL-PLDRSGMvipsdtdfldtweamed 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 138 ------VKRVGVSNHNLAQIRRaneILNASGYSLSAVQNHYSlLYRASEEAGILDYCRQNNITFFAYMVL 201
Cdd:cd19110 139 lvieglVKNIGVSNFNHEQLER---LLNKPGLRVKPVTNQIE-CHPYLTQKKLISFCQSRNVSVTAYRPL 204
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
3-201 |
1.19e-07 |
|
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: 52.03 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTGfaggdtvfgnhlsdtQMAEVFTAAMSKGLNLWDTAAVYG----MGSSETALGALVRQFPRENIIL 78
Cdd:cd19118 6 KIPAIGLGTWQAEPG---------------EVGAAVKIALKAGYRHLDLAKVYQnqheVGQALKELLKEEPGVKREDLFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 79 STKftpqiADKQSAQP--VSDMLEASLGRLGVDAIDIYWIHNP-----------------------LD-----VEKWTpG 128
Cdd:cd19118 71 TSK-----LWNNSHRPeyVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltavptnggevdLDlsvslVDTWK-A 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446777540 129 LIPLLQSGKVKRVGVSNHNlaqIRRANEILNASGY--SLSAVQNHYSLLYRAseeagILDYCRQNNITFFAYMVL 201
Cdd:cd19118 145 MVELKKTGKVKSIGVSNFS---IDHLQAIIEETGVvpAVNQIEAHPLLLQDE-----LVDYCKSKNIHITAYSPL 211
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
50-303 |
2.85e-07 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 50.79 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 50 DTAAVYGmgsSETALGALVRQ--FPRENIILSTKFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP-----LDV 122
Cdd:PRK11172 34 DTAQIYD---NEAAVGQAIAEsgVPRDELFITTKIW---IDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPspndeVSV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 123 EKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILNASGYSLSAVQNHYSLLYRAseeagILDYCRQNNITFFAYMVLe 202
Cdd:PRK11172 108 EEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYLQNRK-----VVAFAKEHGIHVTSYMTL- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 203 qgalsgrydsnhpmpagsgraeSYNAVL--PQIERLtaamkkmGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAA 280
Cdd:PRK11172 182 ----------------------AYGKVLkdPVIARI-------AAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNL 232
|
250 260
....*....|....*....|...
gi 446777540 281 CASDIQLRDEEiilLEQLAAETR 303
Cdd:PRK11172 233 LAQDLQLDAED---MAAIAALDR 252
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
4-198 |
3.52e-07 |
|
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: 50.88 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSWGTGfaggdtvfgnhlsdtQMAEVFTAAMSKGLNLWDTAAVYgmgSSETALGALVRQ------FPRENII 77
Cdd:cd19107 4 MPILGLGTWKSPPG---------------QVTEAVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEkikeqvVKREDLF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIADKQSaqpVSDMLEASLGRLGVDAIDIYWIH-----------NPLD------------VEKWTpGLIPLLQ 134
Cdd:cd19107 66 IVSKLWCTFHEKGL---VKGACQKTLSDLKLDYLDLYLIHwptgfkpgkelFPLDesgnvipsdttfLDTWE-AMEELVD 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446777540 135 SGKVKRVGVSNHNLAQIRRaneILNASGYSLSAVQNHYSLLYRASEEAGIlDYCRQNNITFFAY 198
Cdd:cd19107 142 EGLVKAIGVSNFNHLQIER---ILNKPGLKYKPAVNQIECHPYLTQEKLI-QYCQSKGIVVTAY 201
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
3-233 |
1.91e-06 |
|
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: 48.42 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTgfaggdtvfgnhlSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGA---------LVRQfpR 73
Cdd:cd19124 4 TMPVIGMGTASDPP-------------SPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEalaealrlgLVKS--R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 74 ENIILSTKFTPQIADKQSAQPVsdmLEASLGRLGVDAIDIYWIHNPLDVEK---WTP----GLIPL------------LQ 134
Cdd:cd19124 66 DELFVTSKLWCSDAHPDLVLPA---LKKSLRNLQLEYVDLYLIHWPVSLKPgkfSFPieeeDFLPFdikgvweameecQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 135 SGKVKRVGVSNHNLAQIrraNEILNASGYSLSAVQNHYSLLYRASEeagILDYCRQNNITFFAYMVLeqGALSGRYDSNH 214
Cdd:cd19124 143 LGLTKAIGVSNFSCKKL---QELLSFATIPPAVNQVEMNPAWQQKK---LREFCKANGIHVTAYSPL--GAPGTKWGSNA 214
|
250 260
....*....|....*....|.
gi 446777540 215 PMPAG--SGRAESYNAVLPQI 233
Cdd:cd19124 215 VMESDvlKEIAAAKGKTVAQV 235
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
2-198 |
2.61e-06 |
|
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: 48.15 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 2 KTLPPVALGTWSWGTGfaggdtvfgnhlsdtQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ-------FPRE 74
Cdd:cd19106 5 QKMPLIGLGTWKSKPG---------------QVKAAVKYALDAGYRHIDCAAVYG---NEQEVGEALKEkvgpgkaVPRE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 75 NIILSTKF--TpqiadKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPLD-----------------------VEKWTpGL 129
Cdd:cd19106 67 DLFVTSKLwnT-----KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAfergdnpfpknpdgtirydsthyKETWK-AM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446777540 130 IPLLQSGKVKRVGVSNHNLAQIrraNEILNASGY--SLSAVQNHyslLYRASEEagILDYCRQNNITFFAY 198
Cdd:cd19106 141 EKLVDKGLVKAIGLSNFNSRQI---DDILSVARIkpAVLQVECH---PYLAQNE--LIAHCKARGLVVTAY 203
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
25-198 |
8.79e-06 |
|
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: 46.46 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 25 FGNHLSDTQMAEVFTA---AMSKGLNLWDTAAVYgmgSSETALGALVRQF-------PRENIILSTKFTPQIadkQSAQP 94
Cdd:cd19122 14 FGTFANEGAKGETYAAvtkALDVGYRHLDCAWFY---LNEDEVGDAVRDFlkenpsvKREDLFICTKVWNHL---HEPED 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 95 VSDMLEASLGRLGVDAIDIYWIHNPLDVEK---WTPGLIP-----------------------LLQSGKVKRVGVSNHNL 148
Cdd:cd19122 88 VKWSIDNSLKNLKLDYIDLFLVHWPIAAEKndqRSPKLGPdgkyvilkdltenpeptwrameeIYESGKAKAIGVSNWTI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446777540 149 AQIRRAneilnasgYSLSAVQNHYSLL----YRASEEagILDYCRQNNITFFAY 198
Cdd:cd19122 168 PGLKKL--------LSFAKVKPHVNQIeihpFLPNEE--LVDYCFSNDILPEAY 211
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-198 |
2.69e-05 |
|
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: 45.13 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtgfaggdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ------FPRENII 77
Cdd:cd19113 11 MPSVGFGCWK---------------LDNATAADQIYQAIKAGYRLFDGAEDYG---NEKEVGEGVNRaideglVKREELF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIADKQSaqpVSDMLEASLGRLGVDAIDIYWIHNPLDV------EKWTPGL------------IPLL------ 133
Cdd:cd19113 73 LTSKLWNNFHDPKN---VETALNKTLSDLKLDYVDLFLIHFPIAFkfvpieEKYPPGFycgdgdnfvyedVPILdtwkal 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 134 ----QSGKVKRVGVSNHNLAQIRranEILNASGYSLSAVQ-NHYSLLyrasEEAGILDYCRQNNITFFAY 198
Cdd:cd19113 150 eklvDAGKIKSIGVSNFPGALIL---DLLRGATIKPAVLQiEHHPYL----QQPKLIEYAQKAGITITAY 212
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
3-312 |
1.26e-04 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 42.86 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSwgtgfAGGDTVFGNhlsdtqMAEVFTAAMSKGLNLWDTAAVYgmgSSETALGALVRQ------FPRENI 76
Cdd:cd19109 3 SIPIIGLGTYS-----EPKTTPKGA------CAEAVKVAIDTGYRHIDGAYIY---QNEHEVGQAIREkiaegkVKREDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 77 ILSTKFTPQIADKQSAQPVsdmLEASLGRLGVDAIDIYWIHNPLdveKWTPG--LIPLLQSGK----------------- 137
Cdd:cd19109 69 FYCGKLWNTCHPPELVRPT---LERTLKVLQLDYVDLYIIEMPM---AFKPGdeIYPRDENGKwlyhktnlcatwealea 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 138 ------VKRVGVSNHNlaqiRRANE-ILNASGYSLSAVQNHYSLlYRASEEAGILDYCRQNNITFFAYMVLeqgalsgry 210
Cdd:cd19109 143 ckdaglVKSIGVSNFN----RRQLElILNKPGLKHKPVSNQVEC-HPYFTQPKLLEFCQQHDIVIVAYSPL--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 211 dsnhpmpaGSGRAESY-NAVLPQI---ERLTAAMKKMgaerNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQ 286
Cdd:cd19109 209 --------GTCRDPIWvNVSSPPLledPLLNSIGKKY----NKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFS 276
|
330 340
....*....|....*....|....*.
gi 446777540 287 LRDEEIILLEQLAAETRVDTRGAWEK 312
Cdd:cd19109 277 LTEEEMKDIEALNKNVRYVELLMWRD 302
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
3-298 |
1.68e-04 |
|
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: 42.78 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 3 TLPPVALGTWSWGTGFAGgdtvfgnhlsdtqmaEVFTAAMSKGLNLWDTAAVYGmgsSETALGA---------LVRqfpR 73
Cdd:cd19123 11 LIPALGLGTWKSKPGEVG---------------QAVKQALEAGYRHIDCAAIYG---NEAEIGAalaevfkegKVK---R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 74 ENIILSTKFTpqiADKQSAQPVSDMLEASLGRLGVDAIDIYWIHNPL----------DVEKWTPGL-IPLLQS------- 135
Cdd:cd19123 70 EDLWITSKLW---NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPValkkgvgfpeSGEDLLSLSpIPLEDTwrameel 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 136 ---GKVKRVGVSN---HNLAQIRRANEILNAsgysLSAVQNHYSLlyrasEEAGILDYCRQNNITFFAYMVLeqgalsGR 209
Cdd:cd19123 147 vdkGLCRHIGVSNfsvKKLEDLLATARIKPA----VNQVELHPYL-----QQPELLAFCRDNGIHLTAYSPL------GS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 210 YDSNHPMpagsgRAESYNAVL--PQIerltaamKKMGAERNASVAQIAIAWAIAKGTLPLVGATKVHHVLDAACASDIQL 287
Cdd:cd19123 212 GDRPAAM-----KAEGEPVLLedPVI-------NKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVEL 279
|
330
....*....|.
gi 446777540 288 RDEEIILLEQL 298
Cdd:cd19123 280 DASDMATIAAL 290
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|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
37-181 |
5.76e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 40.72 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 37 VFTAAMSKGLNLWDTAAVYGMGSSEtalgALVRQ--FP-RENIILSTK--------------FTPQiadkQSAQPVSDML 99
Cdd:PRK10376 45 VLREAVALGVNHIDTSDFYGPHVTN----QLIREalHPyPDDLTIVTKvgarrgedgswlpaFSPA----ELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 100 EaslgRLGVDAIDI------YWIHNPLD--VEKWTPGLIPLLQSGKVKRVGVSNHNLAQIRRANEILnasgySLSAVQNH 171
Cdd:PRK10376 117 R----NLGLDVLDVvnlrlmGDGHGPAEgsIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA-----EIVCVQNH 187
|
170
....*....|
gi 446777540 172 YSLLYRASEE 181
Cdd:PRK10376 188 YNLAHRADDA 197
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
25-233 |
1.12e-03 |
|
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: 39.81 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 25 FGNHLSDTQMAE--VFTAAMSkGLNLWDTAAVYGmgsSETALG-ALVRQFP-----RENIILSTKFTPQIadkQSAQPVS 96
Cdd:cd19128 6 FGTYKITESESKeaVKNAIKA-GYRHIDCAYYYG---NEAFIGiAFSEIFKdggvkREDLFITSKLWPTM---HQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 97 DMLEASLGRLGVDAIDIYWIHNPLDVEKWTPGL------------IPLLQS----------GKVKRVGVSNHNLAQIRra 154
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDprddnqiqslskKPLEDTwrameqcvdeKLTKNIGVSNYSTKLLT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 155 nEILNASgySLSAVQNHYSL-LYRASEEagILDYCRQNNITFFAYmvleqGALSGRYDSNHPMPAGSGR----AESYNAV 229
Cdd:cd19128 157 -DLLNYC--KIKPFMNQIEChPYFQNDK--LIKFCIENNIHVTAY-----RPLGGSYGDGNLTFLNDSElkalATKYNTT 226
|
....
gi 446777540 230 LPQI 233
Cdd:cd19128 227 PPQV 230
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
4-151 |
1.62e-03 |
|
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: 39.46 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWSwgtgfaggdtvfgnhLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALGALVRQ------FPRENII 77
Cdd:cd19114 4 MPLVGFGTAK---------------IKANETEEVIYNAIKVGYRLIDGALLYG---NEAEVGRGIRKaiqeglVKREDLF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTPQIADKQSAQPVSDMleaSLGRLGVDAIDIYWIHNPLDV------EKWTPG----------------------L 129
Cdd:cd19114 66 IVTKLWNNFHGKDHVREAFDR---QLKDYGLDYIDLYLIHFPIPAayvdpaENYPFLwkdkelkkfpleqspmqecwreM 142
|
170 180
....*....|....*....|..
gi 446777540 130 IPLLQSGKVKRVGVSNHNLAQI 151
Cdd:cd19114 143 EKLVDAGLVRNIGIANFNVQLI 164
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-306 |
7.22e-03 |
|
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: 37.46 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 4 LPPVALGTWswgtgfaggdtvfgnHLSDTQMAEVFTAAMSKGLNLWDTAAVYGmgsSETALG-ALVRQF-----PRENII 77
Cdd:cd19112 11 MPVIGLGVW---------------RMEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGeALAEAFktglvKREDLF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 78 LSTKFTpqiadKQSAQPVSDMLEASLGRLGVDAIDIYWIHNP--------------------LDVEKWTP------GLIP 131
Cdd:cd19112 73 ITTKLW-----NSDHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvLDIDVTISlettwhAMEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 132 LLQSGKVKRVGVSNHNLAQIRranEILNASGY--SLSAVQNHySLLYRASeeagILDYCRQNNITFFAYMVLEQGALSG- 208
Cdd:cd19112 148 LVSAGLVRSIGISNYDIFLTR---DCLAYSKIkpAVNQIETH-PYFQRDS----LVKFCQKHGISVTAHTPLGGAAANAe 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446777540 209 RYDSNHPM--PAGSGRAESYNAVLPQIerltaaMKKMGAERNASVaqiaiawaiakgtLPlvGATKVHHVLDAACASDIQ 286
Cdd:cd19112 220 WFGSVSPLddPVLKDLAKKYGKSAAQI------VLRWGIQRNTAV-------------IP--KSSKPERLKENIDVFDFQ 278
|
330 340
....*....|....*....|
gi 446777540 287 LRDEEIILLEQLAAETRVDT 306
Cdd:cd19112 279 LSKEDMKLIKSLDRKYRTNQ 298
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