|
Name |
Accession |
Description |
Interval |
E-value |
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-294 |
3.75e-145 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 409.93 E-value: 3.75e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYGFWRWEkESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVL 80
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLG-EWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 81 FSKCGVNIPDSSKpEIRVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVS 160
Cdd:COG4989 80 QTKCGIRLPSEAR-DNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 161 NFSVYQHQLLESFLSIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGGRIEHGTDELALKVRKKLVEMAEK 240
Cdd:COG4989 159 NFTPSQFELLQSALDQPLVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRAALDELAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391131612 241 YESNIESIAVAWIVKL--GALPLIGTLEEKRIRNIVNSFSVKLDHQDWYELYHTTR 294
Cdd:COG4989 239 YGVSPEAIALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREEWYELYEAAR 294
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
10-290 |
7.76e-112 |
|
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: 324.89 E-value: 7.76e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 10 GPKVSPAIYGFWRWEkESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKCGVnIP 89
Cdd:cd19092 3 GLEVSRLVLGCMRLA-DWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGI-RL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 90 DSSKPEIRVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQL 169
Cdd:cd19092 81 GDDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 170 LESFLSIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGGRIEHGTDELALKVRKKLVEMAEKYESNIESIA 249
Cdd:cd19092 161 LQSYLDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRAALEELAEEYGVTIEAIA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1391131612 250 VAWIVKLGA--LPLIGTLEEKRIRNIVNSFSVKLDHQDWYELY 290
Cdd:cd19092 241 LAWLLRHPAriQPILGTTNPERIRSAVKALDIELTREEWYEIY 283
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-286 |
3.86e-54 |
|
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: 178.45 E-value: 3.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYGFWRW-EKESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVV 79
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEAL--KGRPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 80 LFSKCGVNIPDSSkpeirvSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGV 159
Cdd:COG0667 79 IATKVGRRMGPGP------NGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 160 SNFSVYQ----HQLLESFlsIPVVSNHIDLNLLNTSALDnGALDYVKQKYMRPLAVSPLGGGR----------------- 218
Cdd:COG0667 153 SNYSAEQlrraLAIAEGL--PPIVAVQNEYSLLDRSAEE-ELLPAARELGVGVLAYSPLAGGLltgkyrrgatfpegdra 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391131612 219 ----IEHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVKLG--ALPLIGTLEEKRIRNIVNSFSVKLDHQDW 286
Cdd:COG0667 230 atnfVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDL 303
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-289 |
2.59e-49 |
|
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: 165.56 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 17 IYGFWRWE-KESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKCGVNIPDSskpe 95
Cdd:pfam00248 2 GLGTWQLGgGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPW---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 96 irvsHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLS 175
Cdd:pfam00248 78 ----PSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 176 IPVVSNHIDLNLLNtSALDNGALDYVKQKYMRPLAVSPLGGG------------------RIEHGTDELALKVRKKLVEM 237
Cdd:pfam00248 154 IPIVAVQVEYNLLR-RRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrRLLKKGTPLNLEALEALEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1391131612 238 AEKYESNIESIAVAWIVK--LGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:pfam00248 233 AKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-289 |
7.90e-45 |
|
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: 153.84 E-value: 7.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 10 GPKVSPAIYGFW-----RWEKESANSLKDMdqiVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKC 84
Cdd:cd19084 1 DLKVSRIGLGTWaiggtWWGEVDDQESIEA---IKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVIATKC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 85 GVNIPDSSKpeirvSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSV 164
Cdd:cd19084 75 GLRWDGGKG-----VTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 165 YQHQLLESFlsIPVVSNHIDLNLLNTSAlDNGALDYVKQKYMRPLAVSPLGGG----RIEHGTD---------------- 224
Cdd:cd19084 150 EQLEEARKY--GPIVSLQPPYSMLEREI-EEELLPYCRENGIGVLPYGPLAQGlltgKYKKEPTfppddrrsrfpffrge 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391131612 225 --ELALKVRKKLVEMAEKYESNIESIAVAWIV--KLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19084 227 nfEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLaqPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-217 |
4.66e-44 |
|
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: 149.98 E-value: 4.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 14 SPAIYGFWRWEkeSANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLAnKSFKRSDVVLFSKCGvNIPDSSK 93
Cdd:cd06660 1 SRLGLGTMTFG--GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLK-GRGNRDDVVIATKGG-HPPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 94 PEIRVSHvdssaKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ----HQL 169
Cdd:cd06660 77 SRSRLSP-----EHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERlaeaLAY 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391131612 170 LESFLSIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGG 217
Cdd:cd06660 152 AKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG 199
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-285 |
4.64e-42 |
|
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: 145.83 E-value: 4.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 12 KVSPAIYGFW----RWEKESANSLKDMDQIVHLcLELGINTFDHADRYGKYSCESLFGKVLANksFKRSDVVLFSKcgVN 87
Cdd:cd19072 3 EVPVLGLGTWgiggGMSKDYSDDKKAIEALRYA-IELGINLIDTAEMYGGGHAEELVGKAIKG--FDREDLFITTK--VS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 88 IPDSSKPEIRvshvdssakhitTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ- 166
Cdd:cd19072 78 PDHLKYDDVI------------KAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEEl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 167 HQLLESFLSIPVVSNHIDLNLLNTSALDnGALDYVKQKYMRPLAVSPLGGGRIehgtdeLALKVRKKLVEMAEKYESNIE 246
Cdd:cd19072 146 EEAQSYLKKGPIVANQVEYNLFDREEES-GLLPYCQKNGIAIIAYSPLEKGKL------SNAKGSPLLDEIAKKYGKTPA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1391131612 247 SIAVAWIVKL-GALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19072 219 QIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
19-295 |
3.56e-39 |
|
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: 138.87 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 19 GFWRWEKESANSLKdmdqIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKCGVNipdsskpeirv 98
Cdd:cd19085 14 GYWWGDQDDEESIA----TIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGR---RDDVVIATKVSPD----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 99 shvDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVyqhQLLESFLS-IP 177
Cdd:cd19085 76 ---NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGP---AQLEEALDaGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 178 VVSNHIDLNLLNTSAlDNGALDYVKQKYMRPLAVSPLGGG-----------------RIEH------GTDELALKVRKKL 234
Cdd:cd19085 150 IDSNQLPYNLLWRAI-EYEILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdaRTRLfrhfepGAEEETFEALEKL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391131612 235 VEMAEKYESNIESIAVAWIVKLGAL--PLIGTLEEKRIRNIVNSFSVKLDHQDWYELYHTTRP 295
Cdd:cd19085 229 KEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-289 |
5.86e-35 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 128.11 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 12 KVSPAIYGFWRW-----EKESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKvLANKSFKRSDVVLFSKcgv 86
Cdd:cd19093 1 EVSPLGLGTWQWgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGR-FLKELGDRDEVVIATK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 87 nipdsskpeIRVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVL-ALEKLKSSGKVKNIGVSNFSVY 165
Cdd:cd19093 77 ---------FAPLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMdGLADAVEEGLVRAVGVSNYSAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 166 Q----HQLLESfLSIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLG---------------GGRIEHGTDEL 226
Cdd:cd19093 148 QlrraHKALKE-RGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenpppGGRRRLFGRKN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391131612 227 ALKVR---KKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19093 227 LEKVQpllDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
6-285 |
3.53e-34 |
|
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: 126.54 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 6 LSDAGPKVSPAIYG--------FWRWEKESANSLKDMDQivhlCLELGINTFDHADRYGKYSCESLFGKVLanKSF-KRS 76
Cdd:cd19079 5 LGNSGLKVSRLCLGcmsfgdpkWRPWVLDEEESRPIIKR----ALDLGINFFDTANVYSGGASEEILGRAL--KEFaPRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 77 DVVLFSKCGVNIPDSSKPEIrvshvdSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKN 156
Cdd:cd19079 79 EVVIATKVYFPMGDGPNGRG------LSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 157 IGVSNFSVYQ-HQLL--------ESFLSipvVSNHidLNLLNTSAldngaldyvkQKYMRPLAV---------SPLGGGR 218
Cdd:cd19079 153 IGASSMYAWQfAKALhlaekngwTKFVS---MQNH--YNLLYREE----------EREMIPLCEeegigvipwSPLARGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 219 I---------------------EHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVK--LGALPLIGTLEEKRIRNIVN 275
Cdd:cd19079 218 LarpwgdtterrrsttdtaklkYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSkpGVTAPIVGATKLEHLEDAVA 297
|
330
....*....|
gi 1391131612 276 SFSVKLDHQD 285
Cdd:cd19079 298 ALDIKLSEEE 307
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-285 |
8.27e-34 |
|
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: 123.75 E-value: 8.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRWEKEsanslkDMDQIVHLCLELGINTFDHADRYGkysCESLFGKVLANKSFKRSDVVLFSKcgvnipdssk 93
Cdd:cd19071 2 PLIgLGTYKLKPE------ETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESGVPREELFITTK---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 94 peirVSHVDSSAKHITTSVENSLRNLQTDYLDVFLL------DQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQH 167
Cdd:cd19071 63 ----LWPTDHGYERVREALEESLKDLGLDYLDLYLIhwpvpgKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 168 QLLESFLSIPVVSNHIDLNLLNTsalDNGALDYVKQKYMRPLAVSPLGGGRIEHGTDELalkvrkkLVEMAEKYESNIES 247
Cdd:cd19071 139 EELLAAARIKPAVNQIELHPYLQ---QKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPV-------LKEIAKKYGKTPAQ 208
|
250 260 270
....*....|....*....|....*....|....*...
gi 1391131612 248 IAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19071 209 VLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEED 246
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-282 |
1.23e-33 |
|
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: 124.63 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 10 GPKVSPAIYGFWRWEkESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVVLFSKCGVNIP 89
Cdd:cd19074 1 GLKVSELSLGTWLTF-GGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKAL--KGWPRESYVISTKVFWPTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 90 DSskpeirVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ--- 166
Cdd:cd19074 78 PG------PNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQiae 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 167 -HQLLESFLSIPVVSNHIDLNLLNTSALDNgaldyVKQKYMRP----LAVSPLGGG----RIEHG--------------- 222
Cdd:cd19074 152 aHDLARQFGLIPPVVEQPQYNMLWREIEEE-----VIPLCEKNgiglVVWSPLAQGlltgKYRDGipppsrsratdednr 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391131612 223 -------TDELALKVrKKLVEMAEKYESNIESIAVAWIV--KLGALPLIGTLEEKRIRNIVNSFSVKLD 282
Cdd:cd19074 227 dkkrrllTDENLEKV-KKLKPIADELGLTLAQLALAWCLrnPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-254 |
7.75e-33 |
|
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: 123.11 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYG-------FWRWEKESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsf 73
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggGGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 74 kRSDVVLFSKCGVNIPDSskpeirVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGK 153
Cdd:cd19091 79 -RDDVLIATKVRGRMGEG------PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 154 VKNIGVSNFSVYQhqlLESFLSI-------PVVSNHIDLNLLNTSaLDNGALDYVKQKYMRPLAVSPLGGGR-------- 218
Cdd:cd19091 152 VRYIGVSNFSAWQ---IMKALGIserrglaRFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLlsgkyrrg 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1391131612 219 -------IEHGT--------DELALKVRKKLVEMAEKYESNIESIAVAWIV 254
Cdd:cd19091 228 qpapegsRLRRTgfdfppvdRERGYDVVDALREIAKETGATPAQVALAWLL 278
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-266 |
1.41e-31 |
|
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: 119.60 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYGFWRW-----EKESAnslkdmdQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkR 75
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFggrtdEETSF-------AIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR---R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 76 SDVVLFSKCGVniPDSSKPEIRvshvDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVK 155
Cdd:cd19087 71 DDIVLATKVFG--PMGDDPNDR----GLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 156 NIGVSNFSVYQ----------HQLLeSFLSI-PV---VSNHIDLNLLnTSALDNGaldyvkqkymrpLAV---SPLGGG- 217
Cdd:cd19087 145 YIGVSNFAAWQiakaqgiaarRGLL-RFVSEqPMynlLKRQAELEIL-PAARAYG------------LGVipySPLAGGl 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391131612 218 --------------RIEHGTDELALKVRKKLVEMAEKYES-------NIESIAVAWIVKLGAL--PLIG--TLE 266
Cdd:cd19087 211 ltgkygkgkrpesgRLVERARYQARYGLEEYRDIAERFEAlaaeaglTPASLALAWVLSHPAVtsPIIGprTLE 284
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-289 |
9.76e-30 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 114.35 E-value: 9.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 11 PKVSPAIYGFWRWEKESA-------NSL--KDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVVLf 81
Cdd:cd19103 2 KKLPKIALGTWSWGSGGAggdqvfgNHLdeDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFL--KRYPREDYII- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 82 skcgvnipdSSK--PEIRvshvDSSAKHITTSVENSLRNLQTDYLDVFLLDqlDPlSDLESTVLALEKLKSSGKVKNIGV 159
Cdd:cd19103 79 ---------STKftPQIA----GQSADPVADMLEGSLARLGTDYIDIYWIH--NP-ADVERWTPELIPLLKSGKVKHVGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 160 SNFSVYQHQLLESFL-----SIPVVSNHidLNLLNTSALDNGALDYVKQK------YM--------------RPLavsPL 214
Cdd:cd19103 143 SNHNLAEIKRANEILakagvSLSAVQNH--YSLLYRSSEEAGILDYCKENgitffaYMvleqgalsgkydtkHPL---PE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391131612 215 GGGRIEHGTDELAlKVRK---KLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19103 218 GSGRAETYNPLLP-QLEEltaVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKEL 294
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-285 |
2.74e-29 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 111.59 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAIyGFWRWEKESANSLkdmdQIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgvnipdsskp 94
Cdd:cd19073 2 PAL-GLGTWQLRGDDCA----NAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTK----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 95 eIRVSHVDssAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFL 174
Cdd:cd19073 63 -VWRDHLR--PEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDIS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 175 SIPVVSNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGGRIEHgtDELalkvrkkLVEMAEKYESNIESIAVAWI 253
Cdd:cd19073 140 PLPIAVNQVEFHpFLYQAEL----LEYCRENDIVITAYSPLARGEVLR--DPV-------IQEIAEKYDKTPAQVALRWL 206
|
250 260 270
....*....|....*....|....*....|..
gi 1391131612 254 VKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19073 207 VQKGIVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
15-285 |
9.38e-29 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 110.53 E-value: 9.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRWEKEsanslkDMDQIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgVNIPDSSK 93
Cdd:COG0656 6 PALgLGTWQLPGE------EAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAASGVPREELFVTTK--VWNDNHGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 94 PEIRvshvdssakhitTSVENSLRNLQTDYLDVFLLDQldPLS-DLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLES 172
Cdd:COG0656 75 DDTL------------AAFEESLERLGLDYLDLYLIHW--PGPgPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 173 FLSIPVVSNHIDLNLLNTsalDNGALDYVKQKYMRPLAVSPLGGGRI-EHGTdelalkvrkkLVEMAEKYESNIESIAVA 251
Cdd:COG0656 141 ETGVKPAVNQVELHPYLQ---QRELLAFCREHGIVVEAYSPLGRGKLlDDPV----------LAEIAEKHGKTPAQVVLR 207
|
250 260 270
....*....|....*....|....*....|....*
gi 1391131612 252 WIVKLGALPLIGTLEEKRIR-NIvNSFSVKLDHQD 285
Cdd:COG0656 208 WHLQRGVVVIPKSVTPERIReNL-DAFDFELSDED 241
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
32-204 |
1.91e-28 |
|
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: 109.49 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 32 KDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKCGvNIPDSSKPEIRvshvDSSAKHITTS 111
Cdd:cd19086 24 AEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGR---RDKVVIATKFG-NRFDGGPERPQ----DFSPEYIREA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 112 VENSLRNLQTDYLDVFLLdQLDPLSDLESTVL--ALEKLKSSGKVKNIGVS-NFSVYQHQLLESFLsIPVVSnhIDLNLL 188
Cdd:cd19086 96 VEASLKRLGTDYIDLYQL-HNPPDEVLDNDELfeALEKLKQEGKIRAYGVSvGDPEEALAALRRGG-IDVVQ--VIYNLL 171
|
170
....*....|....*.
gi 1391131612 189 NTSALDnGALDYVKQK 204
Cdd:cd19086 172 DQRPEE-ELFPLAEEH 186
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-214 |
3.94e-28 |
|
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: 110.09 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 16 AIYGfWRW----EKESANSLkdmdqivHLCLELGINTFDHADRYGKYSCESLFGKVLANKSfKRSDVVLFSKCGVNIpDS 91
Cdd:cd19148 13 AIGG-WMWggtdEKEAIETI-------HKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKVGLEW-DE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 92 SKPEIRvshvDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQhqlLE 171
Cdd:cd19148 83 GGEVVR----NSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQ---ME 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391131612 172 SFLSI-PVVSNHIDLNLLNtSALDNGALDYVKQKYMRPLAVSPL 214
Cdd:cd19148 156 TFRKVaPLHTVQPPYNLFE-REIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-282 |
5.97e-28 |
|
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: 108.46 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 18 YGFWRWEKESANSL-KDMDQ---IVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSfkrSDVVLFSKCGvnipdSSK 93
Cdd:cd19088 6 YGAMRLTGPGIWGPpADREEaiaVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP---DDVVIATKGG-----LVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 94 PEIRVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESF 173
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 174 LSIPVVSNHidLNLLNTSalDNGALDYVKQKYMRPLAVSPLGGGRI-EHGTDelalkvrkkLVEMAEKYESNIESIAVAW 252
Cdd:cd19088 158 VRIVSVQNR--YNLANRD--DEGVLDYCEAAGIAFIPWFPLGGGDLaQPGGL---------LAEVAARLGATPAQVALAW 224
|
250 260 270
....*....|....*....|....*....|..
gi 1391131612 253 IVKLGA--LPLIGTLEEKRIRNIVNSFSVKLD 282
Cdd:cd19088 225 LLARSPvmLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-285 |
1.85e-27 |
|
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: 108.51 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 3 KIYLSDAGPKVSPAIYGFWRWEKESANS-LKDMDQI--VHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVV 79
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGPWWGgSDDNESIrtIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 80 LFSKCGVNIPDSSKPEIRVS-----HVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKV 154
Cdd:cd19149 78 LATKCGLRWDREGGSFFFVRdgvtvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 155 KNIGVSNFSVYQhqlLESFLSI-PVVSNHIDLNLLNtSALDNGALDYVKQKYMRPLAVSPLGGG---------RIEHGTD 224
Cdd:cd19149 158 RAIGASNVSVEQ---IKEYVKAgQLDIIQEKYSMLD-RGIEKELLPYCKKNNIAFQAYSPLEQGlltgkitpdREFDAGD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391131612 225 ELALKV------RKKLVEM-------AEKYESNIESIAVAWIVKLGALP--LIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19149 234 ARSGIPwfspenREKVLALlekwkplCEKYGCTLAQLVIAWTLAQPGITsaLCGARKPEQAEENAKAGDIRLSAED 309
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
36-271 |
2.42e-27 |
|
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: 107.64 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 36 QIVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVVLFSKCGVNIPDSSKpeirvsHVDSSAKHITTSVENS 115
Cdd:cd19163 37 RTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYLATKVGRYGLDPDK------MFDFSAERITKSVEES 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 116 LRNLQTDYLDVF---------LLDQLdplsdLESTVLALEKLKSSGKVKNIGVSNFSV-YQHQLLE-SFLSIPVVSNHID 184
Cdd:cd19163 109 LKRLGLDYIDIIqvhdiefapSLDQI-----LNETLPALQKLKEEGKVRFIGITGYPLdVLKEVLErSPVKIDTVLSYCH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 185 LNLLNTSALDngALDYVKQKYMRPLAVSPLG-------GGRIEH-GTDELaLKVRKKLVEMAEKYESNIESIAVAWIVKL 256
Cdd:cd19163 184 YTLNDTSLLE--LLPFFKEKGVGVINASPLSmgllterGPPDWHpASPEI-KEACAKAAAYCKSRGVDISKLALQFALSN 260
|
250
....*....|....*..
gi 1391131612 257 GALP--LIGTLEEKRIR 271
Cdd:cd19163 261 PDIAttLVGTASPENLR 277
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-289 |
4.12e-27 |
|
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: 107.30 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 5 YLSDAGPKVSPAIYGFWR--WEKESANSLKDMDQIVhlclELGINTFDHADRYGKY-------SCESLFGKVLAnKSFKR 75
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVfgWTADEETSFALLDAFV----DAGGNFIDTADVYSAWvpgnaggESETIIGRWLK-SRGKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 76 SDVVLFSKCGVnipdsskpEIRVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVK 155
Cdd:cd19081 76 DRVVIATKVGF--------PMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 156 NIGVSNFSVYQHQ---------LLESFLSI-----------------PVVSNHiDLNLLNTSALDNGALdyvKQKYMR-- 207
Cdd:cd19081 148 YIGASNYSAWRLQealelsrqhGLPRYVSLqpeynlvdresfegellPLCREE-GIGVIPYSPLAGGFL---TGKYRSea 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 208 PLAVSPLGGGRIEHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVKLGAL--PLIG--TLEEkrIRNIVNSFSVKLDH 283
Cdd:cd19081 224 DLPGSTRRGEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVtaPIAGarTVEQ--LEDLLAAAGLRLTD 301
|
....*.
gi 1391131612 284 QDWYEL 289
Cdd:cd19081 302 EEVARL 307
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
42-269 |
6.48e-27 |
|
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: 105.73 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKYSCESLFGKvlANKSFKRSDVVLFSKcgvnipdsskpeirVSHVDSSAKHITTSVENSLRNLQT 121
Cdd:cd19137 36 IELGYTHIDTAEMYGGGHTEELVGK--AIKDFPREDLFIVTK--------------VWPTNLRYDDLLRSLQNSLRRLDT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 122 DYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNLLNTSALDNGALDYV 201
Cdd:cd19137 100 DYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEDRDPERDGLLEYC 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391131612 202 KQKYMRPLAVSPLGGGriehgtdelALKVRKKLVEMAEKYESNIESIAVAWIVK---LGALPLIGTLEEKR 269
Cdd:cd19137 180 QKNGITVVAYSPLRRG---------LEKTNRTLEEIAKNYGKTIAQIALAWLIQkpnVVAIPKAGRVEHLK 241
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-218 |
1.19e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 104.97 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 10 GPKVSPAIYGfwrwekeSANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVVLFSKcgVNIP 89
Cdd:cd19105 10 GLKVSRLGFG-------GGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATK--ASPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 90 DSSKpeirvshvdsSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDL---ESTVLALEKLKSSGKVKNIGVSNFSvYQ 166
Cdd:cd19105 79 LDKK----------DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSTHD-NM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391131612 167 HQLLESFLSipvvSNHIDL-----NLLNTSALDNGALDYVKQKYMRPLAVSPLGGGR 218
Cdd:cd19105 148 AEVLQAAIE----SGWFDVimvayNFLNQPAELEEALAAAAEKGIGVVAMKTLAGGY 200
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-255 |
5.14e-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: 104.65 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRwEKESANSLKDMDQIVHLCLELGINTFDHADRYGKY--SCESLFGKVLA-NKSFKRSDVVLFSKCGVNIPD 90
Cdd:cd19089 12 PAIsLGLWH-NFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPpgSAEENFGRILKrDLRPYRDELVISTKAGYGMWP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 91 SskPEIRVShvdsSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ---- 166
Cdd:cd19089 91 G--PYGDGG----SRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKarra 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 167 HQLLESfLSIPVVSNHIDLNLLNTSAlDNGALDYVKQKYMRPLAVSPLGGG-----------------------RIEHGT 223
Cdd:cd19089 165 IALLRE-LGVPLIIHQPRYSLLDRWA-EDGLLEVLEEAGIGFIAFSPLAQGlltdkylngippdsrraaeskflTEEALT 242
|
250 260 270
....*....|....*....|....*....|..
gi 1391131612 224 DELALKVRkKLVEMAEKYESNIESIAVAWIVK 255
Cdd:cd19089 243 PEKLEQLR-KLNKIAAKRGQSLAQLALSWVLR 273
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
30-218 |
6.90e-26 |
|
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: 103.08 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 30 SLKDMDQIVHLCLELGINTFDHADRYGkySCESLFGKVLAnkSFKRSDVVLFSKCGVNIPDSSkpeirvSHVDSSAKHIT 109
Cdd:cd19095 18 SEAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALA--GLRRDDLFIATKVGTHGEGGR------DRKDFSPAAIR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 110 TSVENSLRNLQTDYLDVFLLDQLdPLSDLESTVL-ALEKLKSSGKVKNIGVSNFsvyqHQLLESFLSipvvSNHIDL--- 185
Cdd:cd19095 88 ASIERSLRRLGTDYIDLLQLHGP-SDDELTGEVLeTLEDLKAAGKVRYIGVSGD----GEELEAAIA----SGVFDVvql 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1391131612 186 --NLLNTSALDngALDYVKQKYMRPLAVSPLGGGR 218
Cdd:cd19095 159 pyNVLDREEEE--LLPLAAEAGLGVIVNRPLANGR 191
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
15-289 |
2.23e-25 |
|
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: 101.94 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRWEkESANSLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKcgvnipdssk 93
Cdd:cd19138 12 PALgQGTWYMG-EDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGR---RDKVFLVSK---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 94 peirVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLsDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESF 173
Cdd:cd19138 78 ----VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV-PLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 174 L-SIPVVSNHIDLNLLNtSALDNGALDYVKQKYMRPLAVSPLG-GGRIEHGTDElalkvRKKLVEMAEKYESNIESIAVA 251
Cdd:cd19138 153 PgGGNCAANQVLYNLGS-RGIEYDLLPWCREHGVPVMAYSPLAqGGLLRRGLLE-----NPTLKEIAARHGATPAQVALA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1391131612 252 WIVKLG---ALPLIGTLEekRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19138 227 WVLRDGnviAIPKSGSPE--HARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
42-285 |
4.64e-25 |
|
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: 100.80 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKCGVNipdsskpeirvshvDSSAKHITTSVENSLRNLQT 121
Cdd:cd19140 31 LELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKVWPD--------------NYSPDDFLASVEESLRKLRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 122 DYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLN-LLNTSALdngaLDY 200
Cdd:cd19140 94 DYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHpYLDQRKL----LDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 201 VKQKYMRPLAVSPLGGGRIEhgTDELalkvrkkLVEMAEKYESNIESIAVAWIV---KLGALPliGTLEEKRIRNIVNSF 277
Cdd:cd19140 170 AREHGIALTAYSPLARGEVL--KDPV-------LQEIGRKHGKTPAQVALRWLLqqeGVAAIP--KATNPERLEENLDIF 238
|
....*...
gi 1391131612 278 SVKLDHQD 285
Cdd:cd19140 239 DFTLSDEE 246
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
6-289 |
6.79e-25 |
|
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: 101.14 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 6 LSDAGPKVSPAIYG------FW--RWEKESANSLkdmdqivHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSD 77
Cdd:cd19076 5 LGTQGLEVSALGLGcmgmsaFYgpADEEESIATL-------HRALELGVTFLDTADMYGPGTNEELLGKALKDR---RDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 78 VVLFSKCGVNIPDSSKPEIrvshVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNI 157
Cdd:cd19076 75 VVIATKFGIVRDPGSGFRG----VDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 158 GVSNFS---------VYQHQLLESFLSipvvsnhidlnlLNTSALDNGALDYVKQKYMRPLAVSPLG----GGRIEhGTD 224
Cdd:cd19076 151 GLSEASadtirrahaVHPITAVQSEYS------------LWTRDIEDEVLPTCRELGIGFVAYSPLGrgflTGAIK-SPE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 225 ELA-------------------LKVRKKLVEMAEKYESNIESIAVAWIVKLGA--LPLIGTLEEKRIRNIVNSFSVKLDH 283
Cdd:cd19076 218 DLPeddfrrnnprfqgenfdknLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDdiVPIPGTKRIKYLEENVGALDVVLTP 297
|
....*.
gi 1391131612 284 QDWYEL 289
Cdd:cd19076 298 EELAEI 303
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
36-239 |
7.12e-25 |
|
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: 100.71 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 36 QIVHLCLELGINTFDHADRYGKysCESLFGKVLANKsfKRSDVVLFSKCGvniPDSSKpeirvsHVDSSAKHITTSVENS 115
Cdd:cd19090 24 ATIRAALDLGINYIDTAPAYGD--SEERLGLALAEL--PREPLVLSTKVG---RLPED------TADYSADRVRRSVEES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 116 LRNLQTDYLDVFLL-----DQLDPLSDLESTVLALEKLKSSGKVKNIGVsnfSVYQHQLLESFLS---IPVVSNHIDLNL 187
Cdd:cd19090 91 LERLGRDRIDLLMIhdperVPWVDILAPGGALEALLELKEEGLIKHIGL---GGGPPDLLRRAIEtgdFDVVLTANRYTL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 188 LNTSALDNgALDYVKQKYMRPLAVSPLGGG--------RIEHGTDELALKVRKKLVEMAE 239
Cdd:cd19090 168 LDQSAADE-LLPAAARHGVGVINASPLGMGllagrppeRVRYTYRWLSPELLDRAKRLYE 226
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
32-164 |
2.44e-24 |
|
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: 99.61 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 32 KDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKCGVNI-PDSSKPEIRvshvDSSAKHITT 110
Cdd:cd19078 25 EEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF---RDQVVIATKFGFKIdGGKPGPLGL----DSRPEHIRK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1391131612 111 SVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSV 164
Cdd:cd19078 98 AVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGV 151
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
37-255 |
3.59e-24 |
|
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: 99.42 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 37 IVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVVLFSKCGVNIPDSSkpeirvSHVDSSAKHITTSVENSL 116
Cdd:cd19083 38 LVREALDNGVNLLDTAFIYGLGRSEELVGEVL--KEYNRNEVVIATKGAHKFGGDG------SVLNNSPEFLRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 117 RNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNhiDLNLLNTSALdNG 196
Cdd:cd19083 110 KRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVLQG--EYNLLQREAE-ED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 197 ALDYVKQKYMR-----PLAVSPLGGGRIEHGT-DELALKVRK----------------KLVEMAEKYESNIESIAVAWIV 254
Cdd:cd19083 187 ILPYCVENNISfipyfPLASGLLAGKYTKDTKfPDNDLRNDKplfkgerfsenldkvdKLKSIADEKGVTVAHLALAWYL 266
|
.
gi 1391131612 255 K 255
Cdd:cd19083 267 T 267
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-282 |
3.69e-22 |
|
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: 93.07 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 10 GPKVsPAI-YG--FWRWEKESANSLKDMDQIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKCGV 86
Cdd:cd19120 1 GSKI-PAIaFGtgTAWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 87 NIPDsskpeirvshvdssakhITTSVENSLRNLQTDYLDVFLL------DQLDPlsDLESTVLALEKLKSSGKVKNIGVS 160
Cdd:cd19120 77 GIKD-----------------PREALRKSLAKLGVDYVDLYLIhspffaKEGGP--TLAEAWAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 161 NFSVyQH--QLLESFLSIPVVsNHIDLNLLNTsALDNGALDYVKQKYMRPLAVSPLGGgrIEHGTDELALKVRKKLvemA 238
Cdd:cd19120 138 NFRI-EDleELLDTAKIKPAV-NQIEFHPYLY-PQQPALLEYCREHGIVVSAYSPLSP--LTRDAGGPLDPVLEKI---A 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1391131612 239 EKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLD 282
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELT 253
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-225 |
9.29e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 91.39 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 30 SLKDMDQIVHLCLELGINTFDHADRYGKysCESLFGKVLANKsfkRSDVVLFSKCGVNIPDSSKPEIrvshvdssakhit 109
Cdd:cd19100 25 SQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKGR---RDKVFLATKTGARDYEGAKRDL------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 110 tsvENSLRNLQTDYLDVFLLDQLDPLSDLESTVL------ALEKLKSSGKVKNIGVSNFSVYQHQ-LLESFLsipvvsnh 182
Cdd:cd19100 87 ---ERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggaleALLEAKEEGKIRFIGISGHSPEVLLrALETGE-------- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391131612 183 IDLNLLNTSALDNGALDYVKQKYmrPLAVS---------PLGGGRIEHGTDE 225
Cdd:cd19100 156 FDVVLFPINPAGDHIDSFREELL--PLAREkgvgviamkVLAGGRLLSGDPL 205
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-241 |
2.33e-21 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 92.57 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYGFWRWEKesaNSLKDMDQIVHLCLELGINTFDHADRYGKysCESLFGKVLANKsfkRSDVVL 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPR---KDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKGP---RDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 81 FSKCGVNIPDsskpeirvshvdssAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVL------ALEKLKSSGKV 154
Cdd:COG1453 73 ATKLPPWVRD--------------PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 155 KNIGVSNfsvyqHQLLESFLSIpVVSNHID-----LNLLNT-SALDNGALDYVKQKYMrPLAV-SPLGGGRIEHGTDELA 227
Cdd:COG1453 139 RHIGFST-----HGSLEVIKEA-IDTGDFDfvqlqYNYLDQdNQAGEEALEAAAEKGI-GVIImKPLKGGRLANPPEKLV 211
|
250
....*....|....*.
gi 1391131612 228 LKVRKKL--VEMAEKY 241
Cdd:COG1453 212 ELLCPPLspAEWALRF 227
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-290 |
3.22e-21 |
|
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: 91.15 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 9 AGPKVSPAIYGF----WRWEKES---ANslkdmdQIVHLCLELGINTFDHADRYG---KYSCESLFGKVLANKSFKRSDV 78
Cdd:cd19077 1 NGKLVGPIGLGLmgltWRPNPTPdeeAF------ETMKAALDAGSNLWNGGEFYGppdPHANLKLLARFFRKYPEYADKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 79 VLFSKCGVNiPDSSKPeirvshvDSSAKHITTSVENSLRNL-QTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNI 157
Cdd:cd19077 75 VLSVKGGLD-PDTLRP-------DGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 158 GVSNFSvyqHQLLESFLSI-PVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGG------------------- 217
Cdd:cd19077 147 GLSEVS---AETIRRAHAVhPIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGlltgriksladipegdfrr 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391131612 218 ---RIEHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVKLGA---LPLIGTLEEKRIRNIVNSFSVKLDHQDWYELY 290
Cdd:cd19077 224 hldRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
15-255 |
9.66e-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: 90.15 E-value: 9.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRwEKESANSLKDMDQIVHLCLELGINTFDHADRYGKY--SCESLFGKVLAnKSFK--RSDVVLFSKCGVNIP 89
Cdd:cd19151 13 PAIsLGLWH-NFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPpgSAEENFGRILK-EDLKpyRDELIISTKAGYTMW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 90 DSSKPEIrvshvdSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQ- 168
Cdd:cd19151 91 PGPYGDW------GSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEARe 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 169 ---LLESfLSIPVVSNHIDLNLLNtSALDNGALDYVKQKYMRPLAVSPLGGGRI-----------------------EHG 222
Cdd:cd19151 165 aaaILKD-LGTPCLIHQPKYSMFN-RWVEEGLLDVLEEEGIGCIAFSPLAQGLLtdrylngipedsraakgssflkpEQI 242
|
250 260 270
....*....|....*....|....*....|...
gi 1391131612 223 TDELALKVRkKLVEMAEKYESNIESIAVAWIVK 255
Cdd:cd19151 243 TEEKLAKVR-RLNEIAQARGQKLAQMALAWVLR 274
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-217 |
5.92e-20 |
|
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: 87.73 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 38 VHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKCGVnIPDSSKPeIRVSHvdsSAKHITTSVENSLR 117
Cdd:cd19102 32 IRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCGL-LWDEEGR-IRRSL---KPASIRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 118 NLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQhqlLESFLSI-PVVSNHIDLNLLNtSALDNG 196
Cdd:cd19102 104 RLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQ---MKRCQAIhPIASLQPPYSLLR-RGIEAE 179
|
170 180
....*....|....*....|.
gi 1391131612 197 ALDYVKQKYMRPLAVSPLGGG 217
Cdd:cd19102 180 ILPFCAEHGIGVIVYSPMQSG 200
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-192 |
6.30e-20 |
|
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: 88.09 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 32 KDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLankSFKRSDVVLFSKCGVNIPDSskpeirvshvDSSAKHITTS 111
Cdd:cd19104 32 EEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRAL---KGLPAGPYITTKVRLDPDDL----------GDIGGQIERS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 112 VENSLRNLQTDYLDVFLL-----DQLDPLSDLESTVL----------ALEKLKSSGKVKNIGVSNFSVYQ--HQLLES-- 172
Cdd:cd19104 99 VEKSLKRLKRDSVDLLQLhnrigDERDKPVGGTLSTTdvlglggvadAFERLRSEGKIRFIGITGLGNPPaiRELLDSgk 178
|
170 180
....*....|....*....|
gi 1391131612 173 FLSIPVVsnhidLNLLNTSA 192
Cdd:cd19104 179 FDAVQVY-----YNLLNPSA 193
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
35-271 |
1.62e-19 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 85.84 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 35 DQIVHLCLELGINTFDHADRYGkysCESLFGKVLANKSFKRSDVVLFSKcgvnipdsskpeirVSHVDSSAKHITTSVEN 114
Cdd:cd19135 29 EAVVYALKECGYRHIDTAKRYG---CEELLGKAIKESGVPREDLFLTTK--------------LWPSDYGYESTKQAFEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 115 SLRNLQTDYLDVFLLDQLDPLSD-------LESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNL 187
Cdd:cd19135 92 SLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHVNQVEFHP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 188 LNTsalDNGALDYVKQKYMRPLAVSPLGGGRiehgtdelALKvRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEE 267
Cdd:cd19135 172 FQN---PVELIEYCRDNNIVFEGYCPLAKGK--------ALE-EPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKE 239
|
....
gi 1391131612 268 KRIR 271
Cdd:cd19135 240 ERIK 243
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-219 |
3.10e-19 |
|
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: 84.92 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 26 ESANSLKDMDQ---IVHLCLELGINTFDHADRYGKYSCESLFGKVLanKSFKRSDVVLFSKCGVNIpDSSKPEIRvshvd 102
Cdd:cd19096 12 ESDDDSIDEEKaieMIRYAIDAGINYFDTAYGYGGGKSEEILGEAL--KEGPREKFYLATKLPPWS-VKSAEDFR----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 103 ssaKHIttsvENSLRNLQTDYLDVFLLDQLDpLSDLESTVL------ALEKLKSSGKVKNIGVS---NFSVYQhQLLESF 173
Cdd:cd19096 84 ---RIL----EESLKRLGVDYIDFYLLHGLN-SPEWLEKARkgglleFLEKAKKEGLIRHIGFSfhdSPELLK-EILDSY 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391131612 174 lsiPVVSNHIDLNLLNTSALDN-GALDYVKQKYMRPLAVSPLGGGRI 219
Cdd:cd19096 155 ---DFDFVQLQYNYLDQENQAGrPGIEYAAKKGMGVIIMEPLKGGGL 198
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
33-217 |
3.34e-19 |
|
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: 85.66 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 33 DMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKCGvnipdsskpEIRVSHVDSSAKHITTSV 112
Cdd:cd19153 34 EAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVG---------RYRDSEFDYSAERVRASV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 113 ENSLRNLQTDYLDVFLLDQ---LDPLSDLESTVLALEKLKSSGKVKNIGVSNFSV-YQHQLLE--SFLSIPVVSNHIDLN 186
Cdd:cd19153 105 ATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLdTLTRATRrcSPGSLDAVLSYCHLT 184
|
170 180 190
....*....|....*....|....*....|.
gi 1391131612 187 LLNtSALDNGALDYVKQKYMRPLAVSPLGGG 217
Cdd:cd19153 185 LQD-ARLESDAPGLVRGAGPHVINASPLSMG 214
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
32-289 |
3.61e-19 |
|
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: 85.56 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 32 KDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKvlANKSFKRSDVVLFSKCGVNIPDSSKPEIRvshvdSSAKHITTS 111
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGK--ALKDGPREKVQLATKFGIHEIGGSGVEVR-----GDPAYVRAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 112 VENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVyqHQLLESFLSIPVVSNHIDLNLLnTS 191
Cdd:cd19145 106 CEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASA--DTIRRAHAVHPITAVQLEWSLW-TR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 192 ALDNGALDYVKQKYMRPLAVSPLGGG-------RIEHGTDELALK---------------VRKKLVEMAEKYESNIESIA 249
Cdd:cd19145 183 DIEEEIIPTCRELGIGIVPYSPLGRGffagkakLEELLENSDVRKshprfqgenleknkvLYERVEALAKKKGCTPAQLA 262
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1391131612 250 VAWIVKLG--ALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19145 263 LAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
27-283 |
6.38e-19 |
|
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: 85.31 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 27 SANSLKDMDQIVHLCLELGINTFDHADRY---------GKysCESLFGKVLANKSfKRSDVVLFSK-CGVNiPDSSKPEI 96
Cdd:cd19094 13 EQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqGR--TEEIIGSWLKKKG-NRDKVVLATKvAGPG-EGITWPRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 97 RVSHVDssAKHITTSVENSLRNLQTDYLDVFLL------------------DQLDPLSDLESTVLALEKLKSSGKVKNIG 158
Cdd:cd19094 89 GGTRLD--RENIREAVEGSLKRLGTDYIDLYQLhwpdrytplfgggyytepSEEEDSVSFEEQLEALGELVKAGKIRHIG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 159 VSN---FSVYQ-HQLLESFLSIPVVSNHIDLNLLN---------TSALDNGALdyvkqkymrpLAVSPLGGG-------- 217
Cdd:cd19094 167 LSNetpWGVMKfLELAEQLGLPRIVSIQNPYSLLNrnfeeglaeACHRENVGL----------LAYSPLAGGvltgkyld 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 218 ---RIEHG------------TDELALKVRKKLVEMAEKYESNIESIAVAWI--VKLGALPLIGTLEEKRIRNIVNSFSVK 280
Cdd:cd19094 237 gaaRPEGGrlnlfpgymaryRSPQALEAVAEYVKLARKHGLSPAQLALAWVrsRPFVTSTIIGATTLEQLKENIDAFDVP 316
|
...
gi 1391131612 281 LDH 283
Cdd:cd19094 317 LSD 319
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
15-285 |
6.62e-19 |
|
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: 84.77 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRWEKESANslkdmdQIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSF----KRSDVVLFSK--CGVN 87
Cdd:cd19123 13 PALgLGTWKSKPGEVG------QAVKQALEAGYRHIDCAAIYGN---EAEIGAALAEVFKegkvKREDLWITSKlwNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 88 IPDSSKPeirvshvdssakhittSVENSLRNLQTDYLDVFLL----------------DQLDPLSD--LESTVLALEKLK 149
Cdd:cd19123 84 APEDVLP----------------ALEKTLADLQLDYLDLYLMhwpvalkkgvgfpesgEDLLSLSPipLEDTWRAMEELV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 150 SSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGG---RIEHGTDE 225
Cdd:cd19123 148 DKGLCRHIGVSNFSVKKLEDLLATARIKPAVNQVELHpYLQQPEL----LAFCRDNGIHLTAYSPLGSGdrpAAMKAEGE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 226 LALKVRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19123 224 PVLLEDPVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASD 283
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
36-252 |
7.97e-19 |
|
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: 84.64 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 36 QIVHLCLELGINTFDHADRYGKysCESLFGKVLAN--KSFKRSDVVLFSKCGvnipdsskpEIRVSHVDSSAKHITTSVE 113
Cdd:cd19164 38 DIVRRALELGIRAFDTSPYYGP--SEIILGRALKAlrDEFPRDTYFIITKVG---------RYGPDDFDYSPEWIRASVE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 114 NSLRNLQTDYLDVFLLDQLDPLSDLEstVLA----LEKLKSSGKVKNIGVSNF------SVYQHQLLESFLSIPVVSNHI 183
Cdd:cd19164 107 RSLRRLHTDYLDLVYLHDVEFVADEE--VLEalkeLFKLKDEGKIRNVGISGYplpvllRLAELARTTAGRPLDAVLSYC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 184 DLNLLNTSAL-------DNGALDYVkqkymrpLAVSPLG-------GGRIEH-GTDELALKVrKKLVEMAEKYESNIESI 248
Cdd:cd19164 185 HYTLQNTTLLayipkflAAAGVKVV-------LNASPLSmgllrsqGPPEWHpASPELRAAA-AKAAEYCQAKGTDLADV 256
|
....
gi 1391131612 249 AVAW 252
Cdd:cd19164 257 ALRY 260
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
42-299 |
1.11e-18 |
|
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: 84.42 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKYscESLFGKVLANKSFKRSDVVLFSKCGVNIPdsskPEIRVSHVDSSAKHITTSVENSLRNLQT 121
Cdd:cd19144 44 FELGCTFWDTADIYGDS--EELIGRWFKQNPGKREKIFLATKFGIEKN----VETGEYSVDGSPEYVKKACETSLKRLGV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 122 DYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVyqHQLLESFLSIPVVSNHIDLNLLNTSALDN--GALD 199
Cdd:cd19144 118 DYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSA--ETLRRAHAVHPIAAVQIEYSPFSLDIERPeiGVLD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 200 YVKQKYMRPLAVSPLG----GGRIEHGTDELALKVRKKLVEMA-EKYESN------IESIA-----------VAWIVKLG 257
Cdd:cd19144 196 TCRELGVAIVAYSPLGrgflTGAIRSPDDFEEGDFRRMAPRFQaENFPKNlelvdkIKAIAkkknvtagqltLAWLLAQG 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1391131612 258 A--LPLIGTLEEKRIRNIVNSFSVKLDHQDWYELYHTTRPAPIV 299
Cdd:cd19144 276 DdiIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEVV 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
35-174 |
1.95e-18 |
|
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: 84.05 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 35 DQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKcgvnIPDSSKPEIRvshvDSSAKHITTSVEN 114
Cdd:cd19142 34 EEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTK----IYWSYGSEER----GLSRKHIIESVRA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 115 SLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSvyQHQLLESFL 174
Cdd:cd19142 106 SLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWS--PVEIMEAFS 163
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-285 |
3.57e-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: 82.64 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 13 VSPAIYGFWRW------EKESANSLKDMDQIVhlclELGINTFDHADRYGkySCESLFG---KVLANKSFKRSDVVLFSK 83
Cdd:cd19101 2 ISRVINGMWQLsgghggIRDEDAAVRAMAAYV----DAGLTTFDCADIYG--PAEELIGefrKRLRRERDAADDVQIHTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 84 CgvnIPDSSKPEIRVSHVDSSakhittsVENSLRNLQTDYLDvfLL-----DQLDPlsDLESTVLALEKLKSSGKVKNIG 158
Cdd:cd19101 76 W---VPDPGELTMTRAYVEAA-------IDRSLKRLGVDRLD--LVqfhwwDYSDP--GYLDAAKHLAELQEEGKIRHLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 159 VSNFSVyQHqlLESFLS--IPVVSNHIDLNLLNTSALdNGALDYVKQKYMRPLAVSPLGGG-------------RIEHGT 223
Cdd:cd19101 142 LTNFDT-ER--LREILDagVPIVSNQVQYSLLDRRPE-NGMAALCEDHGIKLLAYGTLAGGllsekylgvpeptGPALET 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 224 ----------DE-----LALKVRKKLVEMAEKYESNIESIAVAWIVK---LGAlPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19101 218 rslqkyklmiDEwggwdLFQELLRTLKAIADKHGVSIANVAVRWVLDqpgVAG-VIVGARNSEHIDDNVRAFSFRLDDED 296
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-204 |
4.53e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 81.80 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 30 SLKDMDQIVHLCLELGINTFDHADRYGkySCESLFGKVLANKSfkrsDVVLFSKCGVNIPDSSKPEirvshvdssaKHIT 109
Cdd:cd19097 24 SEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKRLD----KFKIITKLPPLKEDKKEDE----------AAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 110 TSVENSLRNLQTDYLDVFLL-DQLDPLSDLESTVLALEKLKSSGKVKNIGVsnfSVYQHQLLESFLSIPvvsnHID---- 184
Cdd:cd19097 88 ASVEASLKRLKVDSLDGLLLhNPDDLLKHGGKLVEALLELKKEGLIRKIGV---SVYSPEELEKALESF----KIDiiql 160
|
170 180
....*....|....*....|.
gi 1391131612 185 -LNLLNTSALDNGALDYVKQK 204
Cdd:cd19097 161 pFNILDQRFLKSGLLAKLKKK 181
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
42-285 |
4.91e-18 |
|
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: 81.47 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgVNIPDSSkpeirvshvDSSAKhitTSVENSLRNLQT 121
Cdd:cd19133 33 IKAGYRLIDTAAAYGN---EEAVGRAIKKSGIPREELFITTK--LWIQDAG---------YEKAK---KAFERSLKRLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 122 DYLDVFLLDQldPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQ-LLESFLSIPVVsNHIDLNLLNTSaldNGALDY 200
Cdd:cd19133 96 DYLDLYLIHQ--PFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVdLILHNEVKPAV-NQIETHPFNQQ---IEAVEF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 201 VKQKYMRPLAVSPLGGGRIEHGTDELalkvrkkLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVK 280
Cdd:cd19133 170 LKKYGVQIEAWGPFAEGRNNLFENPV-------LTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFE 242
|
....*
gi 1391131612 281 LDHQD 285
Cdd:cd19133 243 LSDED 247
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-267 |
7.51e-18 |
|
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: 81.83 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 14 SPAIYGF----WRWEKESANSLkdMDQIVhlclELGINTFDHA----DRYGKYSCESLFGKVLANKSfKRSDVVLFSKCG 85
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFAL--LDAFV----ELGGNFIDTArvygDWVERGASERVIGEWLKSRG-NRDKVVIATKGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 86 vnIPDSSKPEI-RVSHVDssakhITTSVENSLRNLQTDYLDVFLL--DQLD-PLSDLestVLALEKLKSSGKVKNIGVSN 161
Cdd:cd19082 74 --HPDLEDMSRsRLSPED-----IRADLEESLERLGTDYIDLYFLhrDDPSvPVGEI---VDTLNELVRAGKIRAFGASN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 162 FSV----------YQHQlLESFLsipVVSNHIDLNLLN--------TSALDNGALDYVKQKYMRPLAVSPLGGG----RI 219
Cdd:cd19082 144 WSTeriaeanayaKAHG-LPGFA---ASSPQWSLARPNeppwpgptLVAMDEEMRAWHEENQLPVFAYSSQARGffskRA 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391131612 220 EHGTDELALKVR-----------KKLVEMAEKYESNIESIAVAWIV--KLGALPLIG--TLEE 267
Cdd:cd19082 220 AGGAEDDSELRRvyyseenferlERAKELAEEKGVSPTQIALAYVLnqPFPTVPIIGprTPEQ 282
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-255 |
1.53e-17 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 81.57 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYGFWRwEKESANSLKDMDQIVHLCLELGINTFDHADRYGKY--SCESLFGKVLaNKSFK--RS 76
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWH-NFGHVNALESQRAILRKAFDLGITHFDLANNYGPPpgSAEENFGRLL-REDFAayRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 77 DVVLFSKCGVNI---PDSSkpeirvshvDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGK 153
Cdd:PRK09912 91 ELIISTKAGYDMwpgPYGS---------GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 154 VKNIGVSNFSVYQHQLLESFL---SIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGGRI----------- 219
Cdd:PRK09912 162 ALYVGISSYSPERTQKMVELLrewKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLtgkylngipqd 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1391131612 220 --------------EHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVK 255
Cdd:PRK09912 242 srmhregnkvrgltPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLK 291
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-263 |
2.75e-17 |
|
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: 80.07 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 30 SLKDMDQIVhlclELGINTFDHADRYGKY-------SCESLFGKVLANKSfKRSDVVLFSKCGVNIPD-SSKPEIRVShv 101
Cdd:cd19752 19 SFAILDRYV----AAGGNFLDTANNYAFWteggvggESERLIGRWLKDRG-NRDDVVIATKVGAGPRDpDGGPESPEG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 102 dSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ---------HQLLES 172
Cdd:cd19752 92 -LSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRlerarqiarQQGWAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 173 FLSIP-----VVSNHiDLNLLNTSALDNGALDYVKQ-KYMRPLAVSPLGGGRI--------EHGTDELALKVRKKLVEMA 238
Cdd:cd19752 171 FSAIQqrhsyLRPRP-GADFGVQRIVTDELLDYASSrPDLTLLAYSPLLSGAYtrpdrplpEQYDGPDSDARLAVLEEVA 249
|
250 260
....*....|....*....|....*..
gi 1391131612 239 EKYESNIESIAVAWIV--KLGALPLIG 263
Cdd:cd19752 250 GELGATPNQVVLAWLLhrTPAIIPLLG 276
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
38-225 |
8.40e-17 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 79.05 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 38 VHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKCGVnipdsskpeiRVSHVDSSAKHITTSVENSLR 117
Cdd:PLN02587 37 VREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKCGR----------YGEGFDFSAERVTKSVDESLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 118 NLQTDYLDVFL--------LDQLdplsdLESTVLALEKLKSSGKVKNIGVSN--FSVYQHQLLEsflsipVVSNHIDLNL 187
Cdd:PLN02587 107 RLQLDYVDILHchdiefgsLDQI-----VNETIPALQKLKESGKVRFIGITGlpLAIFTYVLDR------VPPGTVDVIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391131612 188 ------LNTSALDnGALDYVKQKYMRPLAVSPLGGGRI-EHGTDE 225
Cdd:PLN02587 176 sychysLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLtENGPPE 219
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
38-285 |
1.02e-16 |
|
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: 78.46 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 38 VHLCLELGINTFDHADRYGKyscESLFGKVLAN-------KSfkRSDVVLFSKcgvnipdsskpeIRVShvDSSAKHITT 110
Cdd:cd19124 26 VLEAIEVGYRHFDTAAAYGT---EEALGEALAEalrlglvKS--RDELFVTSK------------LWCS--DAHPDLVLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 111 SVENSLRNLQTDYLDVFLL-----------------DQLDPLsDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESF 173
Cdd:cd19124 87 ALKKSLRNLQLEYVDLYLIhwpvslkpgkfsfpieeEDFLPF-DIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 174 LSIPVVSNHIDLNLlntsALDNGAL-DYVKQKYMRPLAVSPLGGGRIEHGTDE-LALKVrkkLVEMAEKYESNIESIAVA 251
Cdd:cd19124 166 ATIPPAVNQVEMNP----AWQQKKLrEFCKANGIHVTAYSPLGAPGTKWGSNAvMESDV---LKEIAAAKGKTVAQVSLR 238
|
250 260 270
....*....|....*....|....*....|....
gi 1391131612 252 WIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19124 239 WVYEQGVSLVVKSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
18-255 |
1.31e-16 |
|
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: 77.95 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 18 YGFWRWEKESAnslkdmDQIVHLCLELGINTFDHADRYGKyscESLFGKVLA----NKSFKRSDVVLFSKCGvniPDSSK 93
Cdd:cd19128 6 FGTYKITESES------KEAVKNAIKAGYRHIDCAYYYGN---EAFIGIAFSeifkDGGVKREDLFITSKLW---PTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 94 PEirvshvdssakHITTSVENSLRNLQTDYLDVFL---------LDQLDPLSD----------LESTVLALEKLKSSGKV 154
Cdd:cd19128 74 PE-----------NVKEQLLITLQDLQLEYLDLFLihwplafdmDTDGDPRDDnqiqslskkpLEDTWRAMEQCVDEKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 155 KNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNLLntsaLDNGAL-DYVKQKYMRPLAVSPLGGgriEHGTDELALKVRKK 233
Cdd:cd19128 143 KNIGVSNYSTKLLTDLLNYCKIKPFMNQIECHPY----FQNDKLiKFCIENNIHVTAYRPLGG---SYGDGNLTFLNDSE 215
|
250 260
....*....|....*....|..
gi 1391131612 234 LVEMAEKYESNIESIAVAWIVK 255
Cdd:cd19128 216 LKALATKYNTTPPQVIIAWHLQ 237
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
36-290 |
2.90e-16 |
|
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: 77.32 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 36 QIVHLCLELGINTFDHADRYGKyscESLFGKVLANK----SFKRSDVVLFSKCGVNipdsskpeirvSHvdsSAKHITTS 111
Cdd:cd19116 29 QAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREKiaegVVKREDLFITTKLWNS-----------YH---EREQVEPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 112 VENSLRNLQTDYLDVFLL------------DQLDPLSDLESTVL----ALEKLKSSGKVKNIGVSNFSVYQHQ-LLESFL 174
Cdd:cd19116 92 LRESLKRLGLDYVDLYLIhwpvafkenndsESNGDGSLSDIDYLetwrGMEDLVKLGLTRSIGVSNFNSEQINrLLSNCN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 175 SIPVVsNHIDLNLlntsALDNGAL-DYVKQKYMRPLAVSPLGGGRIEHGTDELALKVRKKLVEMAEKYESNIESIAVAWI 253
Cdd:cd19116 172 IKPAV-NQIEVHP----TLTQEKLvAYCQSNGIVVMAYSPFGRLVPRGQTNPPPRLDDPTLVAIAKKYGKTTAQIVLRYL 246
|
250 260 270
....*....|....*....|....*....|....*..
gi 1391131612 254 VKLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYELY 290
Cdd:cd19116 247 IDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALN 283
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-267 |
3.57e-16 |
|
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: 77.26 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 6 LSDAGPKVSPAIYG---F---WRWEKESANSLKDMDQIVhlclELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVV 79
Cdd:cd19080 3 LGRSGLRVSPLALGtmtFgteWGWGADREEARAMFDAYV----EAGGNFIDTANNYTNGTSERLLGEFIAGN---RDRIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 80 LFSKCGVNiPDSSKPeirvSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGV 159
Cdd:cd19080 76 LATKYTMN-RRPGDP----NAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 160 SNFS---VYQHQLLESF--LSiPVVSNHIDLNLLNTSaLDNGALDYVKQKYMRPLAVSPLGGG----------RIEHGT- 223
Cdd:cd19080 151 SDTPawvVARANTLAELrgWS-PFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGlltgkyqrgeEGRAGEa 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391131612 224 ----------DELALKVRKKLVEMAEKYESNIESIAVAWIVK--LGALPLIG--TLEE 267
Cdd:cd19080 229 kgvtvgfgklTERNWAIVDVVAAVAEELGRSAAQVALAWVRQkpGVVIPIIGarTLEQ 286
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-160 |
5.37e-16 |
|
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: 76.97 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 36 QIVHLCLELGINTFDHADRYGKYSCESLFGKVL----ANKSFKRSDVVLFSKCG---------------VNIPDSSKPEI 96
Cdd:cd19099 25 EALKAALDSGINVIDTAINYRGGRSERLIGKALreliEKGGIKRDEVVIVTKAGyipgdgdeplrplkyLEEKLGRGLID 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391131612 97 RVSHVDS----SAKHITTSVENSLRNLQTDYLDVFLLD----QLDPLSD------LESTVLALEKLKSSGKVKNIGVS 160
Cdd:cd19099 105 VADSAGLrhciSPAYLEDQIERSLKRLGLDTIDLYLLHnpeeQLLELGEeefydrLEEAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
47-285 |
8.99e-16 |
|
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: 75.17 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 47 NTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKcgvnipdsskpeirVSHVDSSAKHITTSVENSLRNLQTDYLDV 126
Cdd:cd19126 35 NGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTK--------------LWNDDQRARRTEDAFQESLDRLGLDYVDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 127 FLLDQldPLSD-LESTVLALEKLKSSGKVKNIGVSNFSVyqHQLLESFLSIPVVS--NHIDLN-LLNTSALdngaLDYVK 202
Cdd:cd19126 101 YLIHW--PGKDkFIDTWKALEKLYASGKVKAIGVSNFQE--HHLEELLAHADVVPavNQVEFHpYLTQKEL----RGYCK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 203 QKYMRPLAVSPLGGGRiehgtdelaLKVRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLD 282
Cdd:cd19126 173 SKGIVVEAWSPLGQGG---------LLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELS 243
|
...
gi 1391131612 283 HQD 285
Cdd:cd19126 244 EDD 246
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-166 |
1.21e-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: 75.71 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 1 MEKIYLSDAGPKVSPAIYGFWRWEKESANsLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVL 80
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVD-VDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 81 FSKC---GVNIPDSSKpeirvshvDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNI 157
Cdd:cd19143 80 STKIfwgGGGPPPNDR--------GLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYW 151
|
....*....
gi 1391131612 158 GVSNFSVYQ 166
Cdd:cd19143 152 GTSEWSAQQ 160
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
37-263 |
3.42e-15 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 74.41 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 37 IVHLCLELGINTFDHADRYGKY--SCESLFGKVLANK-SFKRSDVVLFSKCGVNIPDSSKPEIrvshvdSSAKHITTSVE 113
Cdd:cd19150 35 ILRTAFDLGITHFDLANNYGPPpgSAEENFGRILREDfAGYRDELIISTKAGYDMWPGPYGEW------GSRKYLLASLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 114 NSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLS---IPVVSNHIDLNLLNT 190
Cdd:cd19150 109 QSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRelgTPLLIHQPSYNMLNR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 191 SALDNGALDYVKQKYMRPLAVSPLGGG----------------------RIEHGTDELALKVRkKLVEMAEKYESNIESI 248
Cdd:cd19150 189 WVEESGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsraskerslSPKMLTEANLNSIR-ALNEIAQKRGQSLAQM 267
|
250
....*....|....*..
gi 1391131612 249 AVAWIVKLGALP--LIG 263
Cdd:cd19150 268 ALAWVLRDGRVTsaLIG 284
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
110-285 |
3.70e-15 |
|
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: 74.19 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 110 TSVENSLRNLQTDYLDVFLL---------DQLDPLS----------DLESTVLALEKLKSSGKVKNIGVSNFSvyqHQLL 170
Cdd:cd19108 92 PALEKSLKKLQLDYVDLYLIhfpvalkpgEELFPKDengklifdtvDLCATWEAMEKCKDAGLAKSIGVSNFN---RRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 171 ESFLSIP-----VVSNHIDLNL-LNTSALdngaLDYVKQKYMRPLAVSPLGGGRIEHGTDE-----LALKVrkkLVEMAE 239
Cdd:cd19108 169 EMILNKPglkykPVCNQVECHPyLNQSKL----LDFCKSKDIVLVAYSALGSQRDKEWVDQnspvlLEDPV---LCALAK 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391131612 240 KYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19108 242 KHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSED 287
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
18-285 |
4.31e-15 |
|
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: 73.56 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 18 YGFWRWEKESANSlkdmdqIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgvnipdsskpeIR 97
Cdd:cd19131 15 LGVWQVSNDEAAS------AVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTK------------LW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 98 VSHV--DSSAKhittSVENSLRNLQTDYLDVFLLDQLDPLSDLE-STVLALEKLKSSGKVKNIGVSNFSVYQHQ-LLESF 173
Cdd:cd19131 74 NSDQgyDSTLR----AFDESLRKLGLDYVDLYLIHWPVPAQDKYvETWKALIELKKEGRVKSIGVSNFTIEHLQrLIDET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 174 LSIPVVsNHIDLN-LLNTSALDngalDYVKQKYMRPLAVSPLGGGRIehgtdeLALKVRKKLvemAEKYESNIESIAVAW 252
Cdd:cd19131 150 GVVPVV-NQIELHpRFQQRELR----AFHAKHGIQTESWSPLGQGGL------LSDPVIGEI---AEKHGKTPAQVVIRW 215
|
250 260 270
....*....|....*....|....*....|...
gi 1391131612 253 IVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19131 216 HLQNGLVVIPKSVTPSRIAENFDVFDFELDADD 248
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
51-289 |
1.42e-14 |
|
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: 72.38 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 51 HADRYGKYSCESLFGKVLaNKSF-----KRSDVVLFSKcgvnipdsskpeIRVSHVDSSAkhITTSVENSLRNLQTDYLD 125
Cdd:cd19125 40 HIDCAAIYGNEKEIGKAL-KKLFedgvvKREDLFITSK------------LWCTDHAPED--VPPALEKTLKDLQLDYLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 126 VFLL----------DQLDPLS----DLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNLLNTs 191
Cdd:cd19125 105 LYLIhwpvrlkkgaHMPEPEEvlppDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARVPPAVNQVECHPGWQ- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 192 alDNGALDYVKQKYMRPLAVSPLG-GGRIEHGTDELALKVrkkLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRI 270
Cdd:cd19125 184 --QDKLHEFCKSKGIHLSAYSPLGsPGTTWVKKNVLKDPI---VTKVAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERI 258
|
250
....*....|....*....
gi 1391131612 271 RNIVNSFSVKLDHQDWYEL 289
Cdd:cd19125 259 KENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
113-285 |
2.57e-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: 71.27 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 113 ENSLRNLQTDYLDVFLLDQldPLSDL-ESTVLALEKLKSSGKVKNIGVSNFSVYQHQ-LLESFLSIPVVsNHIDLN-LLN 189
Cdd:cd19157 88 EASLERLGLDYLDLYLIHW--PVKGKyKETWKALEKLYKDGRVRAIGVSNFQVHHLEdLLADAEIVPMV-NQVEFHpRLT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 190 TSALdngaLDYVKQKYMRPLAVSPLGGGRIehgtdeLALKVrkkLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKR 269
Cdd:cd19157 165 QKEL----RDYCKKQGIQLEAWSPLMQGQL------LDNPV---LKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHR 231
|
170
....*....|....*.
gi 1391131612 270 IRNIVNSFSVKLDHQD 285
Cdd:cd19157 232 IIENADVFDFELSQED 247
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
58-289 |
4.56e-14 |
|
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: 71.29 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 58 YSCESLFGKVLAN----KSFKRSDVVLFSKCGvnipdsskpeirvSHVDSSAKhITTSVENSLRNLQTDYLDVFLL---- 129
Cdd:cd19154 48 YQNEEAIGEALAElleeGVVKREDLFITTKLW-------------THEHAPED-VEEALRESLKKLQLEYVDLYLIhapa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 130 ---DQLDPLS------------DLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNLlntsald 194
Cdd:cd19154 114 afkDDEGESGtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHL------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 195 ngaldYVKQKYMRPL---------AVSPLGG-GRIEHGTDELALKVRKKL-----VEMAEKYESNIESIAVAWIVKLGAL 259
Cdd:cd19154 187 -----YFPQKELVEFckkhnisvtSYATLGSpGRANFTKSTGVSPAPNLLqdpivKAIAEKHGKTPAQVLLRYLLQRGIA 261
|
250 260 270
....*....|....*....|....*....|
gi 1391131612 260 PLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19154 262 VIPKSATPSRIKENFNIFDFSLSEEDMATL 291
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
38-271 |
5.18e-14 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 70.90 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 38 VHLCLELGINTFDHADRYGKyscESLFGKVLAN-----KSFKRSDVVLFSKCGVNipdSSKPEirvshvdssakHITTSV 112
Cdd:cd19118 26 VKIALKAGYRHLDLAKVYQN---QHEVGQALKEllkeePGVKREDLFITSKLWNN---SHRPE-----------YVEPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 113 ENSLRNLQTDYLDVFLL---------DQLDPLS-----------DLESTVL----ALEKLKSSGKVKNIGVSNFSV-YQH 167
Cdd:cd19118 89 DDTLKELGLDYLDLYLIhwpvafkptGDLNPLTavptnggevdlDLSVSLVdtwkAMVELKKTGKVKSIGVSNFSIdHLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 168 QLLESFLSIPVVsNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGGRIehgtDELALKVRKKLVEMAEKYESNIE 246
Cdd:cd19118 169 AIIEETGVVPAV-NQIEAHpLLLQDEL----VDYCKSKNIHITAYSPLGNNLA----GLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260
....*....|....*....|....*
gi 1391131612 247 SIAVAWIVKLGALPLIGTLEEKRIR 271
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIR 264
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
111-286 |
8.14e-14 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 70.34 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 111 SVENSLRNLQTDYLDVFLL---------DQLDP----------LSDL----ESTVLALEKLKSSGKVKNIGVSNFSVYQH 167
Cdd:cd19122 91 SIDNSLKNLKLDYIDLFLVhwpiaaeknDQRSPklgpdgkyviLKDLtenpEPTWRAMEEIYESGKAKAIGVSNWTIPGL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 168 QLLESFLSIPVVSNHIDLNLLntsaLDNGAL-DYVKQKYMRPLAVSPLGGGRIEHGTDElalKVR--KKLVEMAEKYESN 244
Cdd:cd19122 171 KKLLSFAKVKPHVNQIEIHPF----LPNEELvDYCFSNDILPEAYSPLGSQNQVPSTGE---RVSenPTLNEVAEKGGYS 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1391131612 245 IESIAVAWIVKLGALPLIGTLEEKRIRNivNSFSVKLDHQDW 286
Cdd:cd19122 244 LAQVLIAWGLRRGYVVLPKSSTPSRIES--NFKSIELSDEDF 283
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
31-285 |
8.82e-14 |
|
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: 69.69 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 31 LKDMDQI--VHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgVNIPDSSKPEIRvshvdssakhi 108
Cdd:cd19139 11 LKDDVVIdsVRTALELGYRHIDTAQIYDN---EAAVGQAIAESGVPRDELFITTK--IWIDNLSKDKLL----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 109 tTSVENSLRNLQTDYLDVFLLDQLDP--LSDLESTVLALEKLKSSGKVKNIGVSNFSVyqhQLLESFLSIP----VVSNH 182
Cdd:cd19139 75 -PSLEESLEKLRTDYVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTI---ALLDEAIAVVgagaIATNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 183 IDLNLLntsaLDNGAL-DYVKQKYMRPLAVSPLGGGRIehGTDELalkvrkkLVEMAEKYESNIESIAVAWIVKLGALPL 261
Cdd:cd19139 151 IELSPY----LQNRKLvAHCKQHGIHVTSYMTLAYGKV--LDDPV-------LAAIAERHGATPAQIALAWAMARGYAVI 217
|
250 260
....*....|....*....|....
gi 1391131612 262 IGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19139 218 PSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
37-160 |
1.93e-13 |
|
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: 69.31 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 37 IVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfKRSDVVLFSKCG--VNIPDSSKPEIRVSHVDSSAKHITTSVEN 114
Cdd:cd19162 24 TLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARH--PRAEYVVSTKVGrlLEPGAAGRPAGADRRFDFSADGIRRSIEA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1391131612 115 SLRNLQTDYLDVFLLDQLDP--LSDLESTVLALEKLKSSGKVKNIGVS 160
Cdd:cd19162 102 SLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
50-285 |
2.52e-13 |
|
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: 68.45 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 50 DHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgvnIPDSskpeirvshvDSSAKHITTSVENSLRNLQTDYLDVFLL 129
Cdd:cd19132 38 DTAFNYEN---EGAVGEAVRRSGVPREELFVTTK----LPGR----------HHGYEEALRTIEESLYRLGLDYVDLYLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 130 DQLDPLSDLE-STVLALEKLKSSGKVKNIGVSNFsvyqhqlLESFLS--------IPVVsNHIDLN-LLNTSALdngaLD 199
Cdd:cd19132 101 HWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNF-------LPEHLDrlidetgvTPAV-NQIELHpYFPQAEQ----RA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 200 YVKQKYMRPLAVSPLGGGriehgTDELALKVrkkLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSV 279
Cdd:cd19132 169 YHREHGIVTQSWSPLGRG-----SGLLDEPV---IKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDF 240
|
....*.
gi 1391131612 280 KLDHQD 285
Cdd:cd19132 241 ELSDED 246
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
18-285 |
2.63e-13 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 68.31 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 18 YGFWRWE--KESANSLKdmdqivhLCLELGintFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKcgvnipdsskpe 95
Cdd:cd19156 14 LGVWRVQdgAEAENAVK-------WAIEAG---YRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTK------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 96 irVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQldPLSD-LESTVLALEKLKSSGKVKNIGVSNFsvYQHQLLESFL 174
Cdd:cd19156 72 --LWNSDQGYESTLAAFEESLEKLGLDYVDLYLIHW--PVKGkFKDTWKAFEKLYKEKKVRAIGVSNF--HEHHLEELLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 175 SIPVVS--NHIDLN-LLNTSALDngalDYVKQKYMRPLAVSPLGGGRIehgtdelaLKvRKKLVEMAEKYESNIESIAVA 251
Cdd:cd19156 146 SCKVAPmvNQIELHpLLTQEPLR----KFCKEKNIAVEAWSPLGQGKL--------LS-NPVLKAIGKKYGKSAAQVIIR 212
|
250 260 270
....*....|....*....|....*....|....
gi 1391131612 252 WIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19156 213 WDIQHGIITIPKSVHEERIQENFDVFDFELTAEE 246
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
96-282 |
3.74e-13 |
|
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: 68.29 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 96 IRVSHVDSSAKHITTSVEN------------SLRNLQTDYLDVFLL---------------------DQLDPLSDLESTV 142
Cdd:cd19117 60 IKDSGVPREEIFITTKLWCtwhrrveealdqSLKKLGLDYVDLYLMhwpvpldpdgndflfkkddgtKDHEPDWDFIKTW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 143 LALEKLKSSGKVKNIGVSNFSV-YQHQLLESFLS--IPVVsNHIDLNLLNTSaldNGALDYVKQKYMRPLAVSPLGggri 219
Cdd:cd19117 140 ELMQKLPATGKVKAIGVSNFSIkNLEKLLASPSAkiVPAV-NQIELHPLLPQ---PKLVDFCKSKGIHATAYSPLG---- 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391131612 220 ehGTDELALKvRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLD 282
Cdd:cd19117 212 --STNAPLLK-EPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDE 271
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
9-289 |
8.98e-13 |
|
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: 67.45 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 9 AGPKVSPAIYGFW----RWE-------KESANSLkdMDQIVhlclELGINTFDHADRYGKYSCESLFGKVLANKSfKRSD 77
Cdd:cd19146 7 AGVRVSPLCLGAMsfgeAWKsmmgecdKETAFKL--LDAFY----EQGGNFIDTANNYQGEESERWVGEWMASRG-NRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 78 VVLFSKCGVNIPDSSKPEIRVSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNI 157
Cdd:cd19146 80 MVLATKYTTGYRRGGPIKIKSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 158 GVSN--------------------FSVYQHQLLESFLS-----IPvVSNHIDLNLLNTSALDNGALDYVKQKYMRplavs 212
Cdd:cd19146 160 GVSDtpawvvskanayarahgltqFVVYQGHWSAAFRDferdiLP-MCEAEGMALAPWGVLGQGQFRTEEEFKRR----- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391131612 213 pLGGGRIEHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVKLG--ALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19146 234 -GRSGRKGGPQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEI 311
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
33-166 |
9.25e-13 |
|
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: 67.20 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 33 DMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLAnksfKRSDVVLFSKCGVNIPDSSKPE-IRvshvdssakhitTS 111
Cdd:cd19075 21 AAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGL----GERGFKIDTKANPGVGGGLSPEnVR------------KQ 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1391131612 112 VENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ 166
Cdd:cd19075 85 LETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWE 139
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
31-234 |
2.41e-12 |
|
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: 65.73 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 31 LKDMDQIVHLCLELGINTFDHADRYGKyscESLFGKVL----ANKSFKRSDVVLFSKcgvnipdsskpeirVSHVDSSAK 106
Cdd:cd19136 14 EEEVRQAVDAALKAGYRLIDTASVYRN---EADIGKALrdllPKYGLSREDIFITSK--------------LAPKDQGYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 107 HITTSVENSLRNLQTDYLDVFL--------LDQLDPL-SDLES-TVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSI 176
Cdd:cd19136 77 KARAACLGSLERLGTDYLDLYLihwpgvqgLKPSDPRnAELRReSWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391131612 177 PVVSNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGGRIEHGTDELALKVRKKL 234
Cdd:cd19136 157 PPAVNQVEFHpHLVQKEL----LKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKY 211
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
96-285 |
3.77e-12 |
|
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: 65.12 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 96 IRVSHVDSSAKHITTSV--------------ENSLRNLQTDYLDVFLLDQLDPlSDLESTVL---ALEKLKSSGKVKNIG 158
Cdd:cd19127 55 IRRSGVDRSDIFVTTKLwisdygydkalrgfDASLRRLGLDYVDLYLLHWPVP-NDFDRTIQaykALEKLLAEGRVRAIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 159 VSNFSVyQH--QLLESFLSIPVVsNHIDLN-------LLNTSAldngALDYVKQkymrplAVSPLGGGRI---EHGTDEL 226
Cdd:cd19127 134 VSNFTP-EHleRLIDATTVVPAV-NQVELHpyfsqkdLRAFHR----RLGIVTQ------AWSPIGGVMRygaSGPTGPG 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391131612 227 ALKVRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19127 202 DVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAED 260
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
30-289 |
5.49e-12 |
|
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: 65.04 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 30 SLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKsfKRSDVVLFSKCG---VNIPDSSKPEIR--------V 98
Cdd:cd19161 18 SNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK--PRDEFVLSTKVGrllKPAREGSVPDPNgfvdplpfE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 99 SHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSD------------LESTVLALEKLKSSGKVK--NIGVSNFSV 164
Cdd:cd19161 96 IVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHgdrkerhhfaqlMSGGFKALEELKKAGVIKafGLGVNEVQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 165 YQhQLLESFlsipvvsnHIDL-------NLLNTSALDnGALDYVKQKYMRPLAVSPLGGGRIEHGTDELA--------LK 229
Cdd:cd19161 176 CL-EALDEA--------DLDCfllagrySLLDQSAEE-EFLPRCEQRGTSLVIGGVFNSGILATGTKSGAkfnygdapAE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391131612 230 VRKKLVEM---AEKYESNIESIAVAWIV--KLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19161 246 IISRVMEIekiCDAYNVPLAAAALQFPLrhPAVASVLTGARNPAQLRQNVEAFQTDIPEELWQAL 310
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
15-285 |
1.09e-11 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 64.43 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRWEKEsanslkDMDQIVHLCLELGINTFDHADRYGKyscESLFGKVLAnKSF-----KRSDVVLFSKCGvni 88
Cdd:cd19112 12 PVIgLGVWRMEPG------EIKELILNAIKIGYRHFDCAADYKN---EKEVGEALA-EAFktglvKREDLFITTKLW--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 89 pdsskpeirvshvDSSAKHITTSVENSLRNLQTDYLDVFLLD-----------------------QLDPLSDLESTVLAL 145
Cdd:cd19112 79 -------------NSDHGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 146 EKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNllntSALDNGALDYVKQKY-MRPLAVSPLGGGRI-EHGT 223
Cdd:cd19112 146 EKLVSAGLVRSIGISNYDIFLTRDCLAYSKIKPAVNQIETH----PYFQRDSLVKFCQKHgISVTAHTPLGGAAAnAEWF 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391131612 224 DELALKVRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19112 222 GSVSPLDDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKED 283
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
74-285 |
2.38e-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: 62.93 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 74 KRSDVVLFSKCGVNIPDssKPEIrvshvdssakhittSVENSLRNLQTDYLDVFLLD----------------------Q 131
Cdd:cd19121 67 KREDLFVTTKLWSTYHR--RVEL--------------CLDRSLKSLGLDYVDLYLVHwpvllnpngnhdlfptlpdgsrD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 132 LDPLSDLESTVLALEKLKSSGKVKNIGVSNFSV-YQHQLLESFLSIPVVsNHIDLN-LLNTSALdngaLDYVKQKYMRPL 209
Cdd:cd19121 131 LDWDWNHVDTWKQMEKVLKTGKTKAIGVSNYSIpYLEELLKHATVVPAV-NQVENHpYLPQQEL----VDFCKEKGILIE 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391131612 210 AVSPLGGGRIEHGTDElalkvrkKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNivNSFSVKLDHQD 285
Cdd:cd19121 206 AYSPLGSTGSPLISDE-------PVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKS--NLEIIDLDDED 272
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
35-163 |
2.98e-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: 62.85 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 35 DQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKcgvnIPDSSKPEirvSHVDSSAKHITTSVEN 114
Cdd:cd19141 33 EELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK----IFWGGKAE---TERGLSRKHIIEGLKA 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1391131612 115 SLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFS 163
Cdd:cd19141 106 SLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWS 154
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
42-290 |
7.39e-11 |
|
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: 61.75 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKyscESLFGKVLA----NKSFKRSDVVLFSKcgvnipdsskpeirVSHVDSSAKHITTSVENSLR 117
Cdd:cd19111 27 LFVGYRHIDTALSYQN---EKAIGEALKwwlkNGKLKREEVFITTK--------------LPPVYLEFKDTEKSLEKSLE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 118 NLQTDYLDVFLL-----------DQLDPL--SDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHID 184
Cdd:cd19111 90 NLKLPYVDLYLIhhpcgfvnkkdKGERELasSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAKVKPSNLQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 185 LNLLNTSaldNGALDYVKQKYMRPLAVSPLGG-GRIE--HGTDELALKVRKKLVEMAEKYESNIESIAVAWIVKLGALPL 261
Cdd:cd19111 170 CHAYLQQ---RELRKFCNKKNIVVTAYAPLGSpGRANqsLWPDQPDLLEDPTVLAIAKELDKTPAQVLLRFVLQRGTGVL 246
|
250 260
....*....|....*....|....*....
gi 1391131612 262 IGTLEEKRIRNIVNSFSVKLDHQDWYELY 290
Cdd:cd19111 247 PKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-173 |
9.97e-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: 61.64 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 6 LSDAGPKVSpaIYGFWRWEKESANSLKDM-DQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKc 84
Cdd:cd19158 6 LGKSGLRVS--CLGLGTWVTFGGQITDEMaEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 85 gvnIPDSSKPEirvSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSV 164
Cdd:cd19158 83 ---IFWGGKAE---TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 156
|
....*....
gi 1391131612 165 YqhQLLESF 173
Cdd:cd19158 157 M--EIMEAY 163
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
35-255 |
1.13e-10 |
|
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: 61.21 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 35 DQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVLFSKcgvnIPDSSKPEirvSHVDSSAKHITTSVEN 114
Cdd:cd19159 34 ERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK----LYWGGKAE---TERGLSRKHIIEGLKG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 115 SLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSNFSVYQ----HQLLESFLSIPVVSNHIDLNLLNT 190
Cdd:cd19159 107 SLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEimeaYSVARQFNMIPPVCEQAEYHLFQR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 191 SALDNGALDYVKQKYMRPLAVSPLG----GGRIEHGTDELA---------LKVR-------------KKLVEMAEKYESN 244
Cdd:cd19159 187 EKVEVQLPELYHKIGVGAMTWSPLAcgiiSGKYGNGVPESSraslkcyqwLKERivseegrkqqnklKDLSPIAERLGCT 266
|
250
....*....|.
gi 1391131612 245 IESIAVAWIVK 255
Cdd:cd19159 267 LPQLAVAWCLR 277
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
37-289 |
2.69e-10 |
|
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: 59.82 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 37 IVHLCLELGI-NTFDHADRYGKYSCESLFGK----VLANKSFKRSDVVLFSKCGVNIPDsskpeirvshvdssakHITTS 111
Cdd:cd19119 28 EVKEAVEAAIkEGYRHIDTAYAYETEDFVGEaikrAIDDGSIKREELFITTKVWPTFYD----------------EVERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 112 VENSLRNLQTDYLDVFLLDQLDPL-------------------------SDLESTVLALEKLKSSGKVKNIGVSNFS-VY 165
Cdd:cd19119 92 LDESLKALGLDYVDLLLVHWPVCFekdsddsgkpftpvnddgktryaasGDHITTYKQLEKIYLDGRAKAIGVSNYSiVY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 166 QHQLLESFLSIPVVsNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGGRIEHGTDELAlkvrkklVEMAEKYESN 244
Cdd:cd19119 172 LERLIKECKVVPAV-NQVELHpHLPQMDL----RDFCFKHGILVTAYSPLGSHGAPNLKNPLV-------KKIAEKYNVS 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1391131612 245 IESIAVAWIVKLGALPLIGTLEEKRIrnIVNSFSVKLDHQDWYEL 289
Cdd:cd19119 240 TGDILISYHVRQGVIVLPKSLKPVRI--VSNGKIVSLTKEDLQKL 282
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
6-255 |
3.27e-10 |
|
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: 60.00 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 6 LSDAGPKVSPAIYGFW-----RWEKESANSLkdmdqiVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSFKRSDVVL 80
Cdd:cd19160 8 LGKSGLRVSCLGLGTWvtfgsQISDETAEDL------LTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 81 FSKcgvnIPDSSKPEirvSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVS 160
Cdd:cd19160 82 TTK----IYWGGQAE---TERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 161 NFSVYQ----HQLLESFLSIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGGRIEHGTDE----------- 225
Cdd:cd19160 155 RWSAMEimeaYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGrvpdtcraavk 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1391131612 226 ----LALKVR-----------KKLVEMAEKYESNIESIAVAWIVK 255
Cdd:cd19160 235 gyqwLKEKVQseegkkqqakvKELHPIADRLGCTVAQLAIAWCLR 279
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
108-289 |
3.59e-09 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 56.89 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 108 ITTSVENSLRNLQTDYLDVFLLD--------QLD-PL----------SDLESTVLALEKLKSSGKVKNIGVSNFSvyqHQ 168
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHwpmgfkpgEPDlPLdrsgmvipsdTDFLDTWEAMEDLVIEGLVKNIGVSNFN---HE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 169 LLESFLSIP-----VVSNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGGriEHGTDELALKVRKKLvemAEKYE 242
Cdd:cd19110 157 QLERLLNKPglrvkPVTNQIECHpYLTQKKL----ISFCQSRNVSVTAYRPLGGS--CEGVDLIDDPVIQRI---AKKHG 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391131612 243 SNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19110 228 KSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
9-285 |
4.21e-09 |
|
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: 56.76 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 9 AGPKVSPAIYGFWRWEKESANSLKDMD-----QIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSfKRSDVVLFSK 83
Cdd:cd19147 6 AGIRVSPLILGAMSIGDAWSGFMGSMDkeqafELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 84 CGVNIPDSSKPEIR-VSHVDSSAKHITTSVENSLRNLQTDYLDVFLLDQLDPLSDLESTVLALEKLKSSGKVKNIGVSN- 161
Cdd:cd19147 85 FTTDYKAYEVGKGKaVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 162 -------------------FSVYQHQ--LLESFLS---IPvVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGG 217
Cdd:cd19147 165 pawvvsaanyyatahgktpFSVYQGRwnVLNRDFErdiIP-MARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGLRSF 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391131612 218 RIEHGTDELALKVRKKLVEMAEKY-ESNIESIAVAWIVKLG--ALPLIGTLEEKRIRNIVNSFSVKLDHQD 285
Cdd:cd19147 244 VGGTEQTPEEVKISEALEKVAEEHgTESVTAIALAYVRSKApnVFPLVGGRKIEHLKDNIEALSIKLTPEE 314
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
30-195 |
4.31e-09 |
|
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: 56.46 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 30 SLKDMDQIVHLCLELGINTFDHADRYGKYSCESLFGKVLANKSfkRSDVVLFSKCG-VNIPDSSKPEIRVSHVDSSAKH- 107
Cdd:cd19152 18 SDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGrLLVPLQEVEPTFEPGFWNPLPFd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 108 ---------ITTSVENSLRNLQTDYLD-VFLLDQLDPLSDLEST----------VLALEKLKSSGKVKNIGV-SNFSVYQ 166
Cdd:cd19152 96 avfdysydgILRSIEDSLQRLGLSRIDlLSIHDPDEDLAGAESDehfaqaikgaFRALEELREEGVIKAIGLgVNDWEVI 175
|
170 180 190
....*....|....*....|....*....|
gi 1391131612 167 HQLLESF-LSIPVVSNHidLNLLNTSALDN 195
Cdd:cd19152 176 LRILEEAdLDWVMLAGR--YTLLDHSAARE 203
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
61-285 |
8.02e-09 |
|
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: 55.85 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 61 ESLFGKVLANKSFKRSDVVLFSKC--GVNIPDSSKPEIRvshvdssakhittsveNSLRNLQTDYLDVFLL--------- 129
Cdd:cd19106 51 EALKEKVGPGKAVPREDLFVTSKLwnTKHHPEDVEPALR----------------KTLKDLQLDYLDLYLIhwpyaferg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 130 DQLDP----------LSDLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLN-LLNTSALdngaL 198
Cdd:cd19106 115 DNPFPknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVARIKPAVLQVECHpYLAQNEL----I 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 199 DYVKQKYMRPLAVSPLGG-GRIEHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSF 277
Cdd:cd19106 191 AHCKARGLVVTAYSPLGSpDRPWAKPDEPVLLEEPKVKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVF 270
|
....*...
gi 1391131612 278 SVKLDHQD 285
Cdd:cd19106 271 DFTLSPEE 278
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
42-257 |
1.62e-08 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 54.64 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKcgvnipdsskpeIRVSHVdsSAKHITTSVENSLRNLQT 121
Cdd:PRK11172 26 LELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTK------------IWIDNL--AKDKLIPSLKESLQKLRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 122 DYLDVFLLDQLDPLS--DLESTVLALEKLKSSGKVKNIGVSNFSVYQ-HQLLESFLSIPVVSNHIDLNLLntsaLDNGAL 198
Cdd:PRK11172 89 DYVDLTLIHWPSPNDevSVEEFMQALLEAKKQGLTREIGISNFTIALmKQAIAAVGAENIATNQIELSPY----LQNRKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391131612 199 -DYVKQK------YMrPLAVsplggGRIEHgtDELalkvrkkLVEMAEKYESNIESIAVAWIVKLG 257
Cdd:PRK11172 165 vAFAKEHgihvtsYM-TLAY-----GKVLK--DPV-------IARIAAKHNATPAQVILAWAMQLG 215
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
35-285 |
2.23e-08 |
|
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: 54.09 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 35 DQIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDvvLFSKCGVNIPDSSkpeirvshVDSSAKhittSVEN 114
Cdd:cd19134 27 ERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGE--LFVTTKLATPDQG--------FTASQA----ACRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 115 SLRNLQTDYLDVFLLD-QLDPLSDLESTVLALEKLKSSGKVKNIGVSNF-SVYQHQLLESFLSIPVVsNHIDLN-LLNTS 191
Cdd:cd19134 90 SLERLGLDYVDLYLIHwPAGREGKYVDSWGGLMKLREEGLARSIGVSNFtAEHLENLIDLTFFTPAV-NQIELHpLLNQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 192 ALD--NGALDYVKQKYmrplavSPLGGGR-IEHGTdelalkvrkkLVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEK 268
Cdd:cd19134 169 ELRkvNAQHGIVTQAY------SPLGVGRlLDNPA----------VTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPE 232
|
250
....*....|....*..
gi 1391131612 269 RIRNIVNSFSVKLDHQD 285
Cdd:cd19134 233 RIASNLDVFDFELTADH 249
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
111-281 |
4.29e-08 |
|
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: 53.65 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 111 SVENSLRNLQTDYLDVFLL---------DQLDPL----------SDLESTVLALEKLKSSGKVKNIGVSNFSVYQhqlLE 171
Cdd:cd19109 87 TLERTLKVLQLDYVDLYIIempmafkpgDEIYPRdengkwlyhkTNLCATWEALEACKDAGLVKSIGVSNFNRRQ---LE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 172 SFLSIP-----VVSNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLGGGRiehgtDELALKVR-------KKLVEMA 238
Cdd:cd19109 164 LILNKPglkhkPVSNQVECHpYFTQPKL----LEFCQQHDIVIVAYSPLGTCR-----DPIWVNVSspplledPLLNSIG 234
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391131612 239 EKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKL 281
Cdd:cd19109 235 KKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSL 277
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
38-285 |
7.55e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 52.38 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 38 VHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKCGvnipdsskpeirvshvDSSAKHITTSVENSLR 117
Cdd:PRK11565 34 IHKALEVGYRSIDTAAIYKN---EEGVGKALKEASVAREELFITTKLW----------------NDDHKRPREALEESLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 118 NLQTDYLDVFLLDQLDPLSDleSTVLA---LEKLKSSGKVKNIGVSNFSVYQHQ-LLESFLSIPVVsNHIDLN-LLNTSA 192
Cdd:PRK11565 95 KLQLDYVDLYLMHWPVPAID--HYVEAwkgMIELQKEGLIKSIGVCNFQIHHLQrLIDETGVTPVI-NQIELHpLMQQRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 193 LDN-GALDYVKQKYMRPLAVSplGGGRIEHgtdelalKVRKKLvemAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIR 271
Cdd:PRK11565 172 LHAwNATHKIQTESWSPLAQG--GKGVFDQ-------KVIRDL---ADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIA 239
|
250
....*....|....
gi 1391131612 272 NIVNSFSVKLDHQD 285
Cdd:PRK11565 240 ENFDVFDFRLDKDE 253
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
33-219 |
3.46e-07 |
|
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: 50.29 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 33 DMDQIVHLCLELGINTFDHADRYGKyscESLFGKVLANKSFKRSDVVLFSKCGvniPDSSKPEirvshvdssakHITTSV 112
Cdd:cd19130 24 DTQRAVATALEVGYRHIDTAAIYGN---EEGVGAAIAASGIPRDELFVTTKLW---NDRHDGD-----------EPAAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 113 ENSLRNLQTDYLDVFLLDQLDPLSDLE-STVLALEKLKSSGKVKNIGVSNFSV-YQHQLLESFLSIPVVsNHIDLNllnt 190
Cdd:cd19130 87 AESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFLPpHLERIVAATGVVPAV-NQIELH---- 161
|
170 180 190
....*....|....*....|....*....|
gi 1391131612 191 SALDN-GALDYVKQKYMRPLAVSPLGGGRI 219
Cdd:cd19130 162 PAYQQrTIRDWAQAHDVKIEAWSPLGQGKL 191
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
29-297 |
5.19e-07 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 50.24 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 29 NSLKDMDQIVHLCLELGINTFDHADRY-------GKYSCESLFGKVLAnKSFKRSDVVLFSKcgVNIP----DSSkpeIR 97
Cdd:PRK10625 27 NSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLA-KRGSREKLIIASK--VSGPsrnnDKG---IR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 98 VSHVdSSAKHITTSVENSLRNLQTDYLDVFLL------------------DQLDPLSDLEsTVLALEKLKSSGKVKNIGV 159
Cdd:PRK10625 101 PNQA-LDRKNIREALHDSLKRLQTDYLDLYQVhwpqrptncfgklgyswtDSAPAVSLLE-TLDALAEQQRAGKIRYIGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 160 SN---FSVYQH-QLLE-------------------SF-LSIPVVSNHIDLNLLNTSALDNGALdyvKQKYMRplAVSPLG 215
Cdd:PRK10625 179 SNetaFGVMRYlHLAEkhdlprivtiqnpysllnrSFeVGLAEVSQYEGVELLAYSCLAFGTL---TGKYLN--GAKPAG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 216 G-----GRIEHGTDELALKVRKKLVEMAEKYESNIESIAVAWIVK--LGALPLIGTLEEKRIRNIVNSFSVKLDHQ--DW 286
Cdd:PRK10625 254 ArntlfSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRqpFVASTLLGATTMEQLKTNIESLHLTLSEEvlAE 333
|
330
....*....|...
gi 1391131612 287 YELYHT--TRPAP 297
Cdd:PRK10625 334 IEAVHQvyTYPAP 346
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
42-271 |
7.02e-07 |
|
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: 49.76 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKyscESLFG----KVLANKSFKRSDVVLFSKCGVNipdSSKPEiRVShvdssakhitTSVENSLR 117
Cdd:cd19129 29 LEAGFRHFDCAERYRN---EAEVGeamqEVFKAGKIRREDLFVTTKLWNT---NHRPE-RVK----------PAFEASLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 118 NLQTDYLDVFLL---------DQLDPLSD-----------LESTVLALEKLKSSGKVKNIGVSNFSVYQ-HQLLESFLSI 176
Cdd:cd19129 92 RLQLDYLDLYLIhtpfafqpgDEQDPRDAngnviyddgvtLLDTWRAMERLVDEGRCKAIGLSDVSLEKlREIFEAARIK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 177 PVVSNHIDLNLLNTSALdngaLDYVKQKYMRPLAVSPLGggrieHGTDELALKvRKKLVEMAEKYESNIESIAVAWIVKL 256
Cdd:cd19129 172 PAVVQVESHPYLPEWEL----LDFCKNHGIVLQAFAPLG-----HGMEPKLLE-DPVITAIARRVNKTPAQVLLAWAIQR 241
|
250
....*....|....*
gi 1391131612 257 GALPLIGTLEEKRIR 271
Cdd:cd19129 242 GTALLTTSKTPSRIR 256
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
15-163 |
1.04e-06 |
|
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: 49.37 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 15 PAI-YGFWRWEKESANslkdmDQIvHLCLELGINTFDHADRYGKyscESLFG----KVLANKSFKRSDVVLFSKCGVNIP 89
Cdd:cd19113 12 PSVgFGCWKLDNATAA-----DQI-YQAIKAGYRLFDGAEDYGN---EKEVGegvnRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 90 DSskpeirvshvdssaKHITTSVENSLRNLQTDYLDVFLL------------------------DQLD----PLSDlesT 141
Cdd:cd19113 83 DP--------------KNVETALNKTLSDLKLDYVDLFLIhfpiafkfvpieekyppgfycgdgDNFVyedvPILD---T 145
|
170 180
....*....|....*....|..
gi 1391131612 142 VLALEKLKSSGKVKNIGVSNFS 163
Cdd:cd19113 146 WKALEKLVDAGKIKSIGVSNFP 167
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
19-289 |
1.51e-05 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 45.59 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 19 GFWRWEKEsanslkDMDQIVHLCLELGINTFDHADRYGKyscESLFGKVL----ANKSFKRSDVVLFSKC--GVNIPDSS 92
Cdd:cd19155 18 GTWQSSPE------EIETAVDTALEAGYRHIDTAYVYRN---EAAIGNVLkkwiDSGKVKREELFIVTKLppGGNRREKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 93 KPEIRvshvdssakhittsveNSLRNLQTDYLDVFLLD---------------------QLDPLSDLESTVLALEKLKSS 151
Cdd:cd19155 89 EKFLL----------------KSLEKLQLDYVDLYLIHfpvgslskeddsgkldptgehKQDYTTDLLDIWKAMEAQVDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 152 GKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDLNL-LNTSALdngaLDYVKQKYMRPLAVSPLGGGRIEHGTDELALKV 230
Cdd:cd19155 153 GLTRSIGLSNFNREQMARILKNARIKPANLQVELHVyLQQKDL----VDFCSTHSITVTAYAPLGSPGAAHFSPGTGSPS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391131612 231 RKK--------LVEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYEL 289
Cdd:cd19155 229 GSSpdllqdpvVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKL 295
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
42-185 |
3.35e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 44.58 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 42 LELGINTFDHADRYGKYSCESLFGKVLANKsfkRSDVVLFSKCG-VNIPDSSKPeirvshVDSSAKHITTSVENSLRNLQ 120
Cdd:PRK10376 50 VALGVNHIDTSDFYGPHVTNQLIREALHPY---PDDLTIVTKVGaRRGEDGSWL------PAFSPAELRRAVHDNLRNLG 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 121 TDYLDVFLL----DQLDPLS-DLESTVLALEKLKSSGKVKNIGVSNFSVYQHQLLESFLSIPVVSNHIDL 185
Cdd:PRK10376 121 LDVLDVVNLrlmgDGHGPAEgSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNL 190
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
113-215 |
5.87e-05 |
|
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: 43.95 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 113 ENSLRNLQTDYLDVFLL---------DQLDPL----------SDLESTVLALEKLKSSGKVKNIGVSNFSvyqHQLLESF 173
Cdd:cd19107 85 QKTLSDLKLDYLDLYLIhwptgfkpgKELFPLdesgnvipsdTTFLDTWEAMEELVDEGLVKAIGVSNFN---HLQIERI 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1391131612 174 LSIP-----VVSNHIDLN-LLNTSALdngaLDYVKQKYMRPLAVSPLG 215
Cdd:cd19107 162 LNKPglkykPAVNQIECHpYLTQEKL----IQYCQSKGIVVTAYSPLG 205
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
104-290 |
3.16e-04 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 41.77 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 104 SAKHITTSVENSLRNLQTDYLDVFLL------------DQLDPL-------------SDLESTVLALEKLKSSGKVKNIG 158
Cdd:cd19114 76 GKDHVREAFDRQLKDYGLDYIDLYLIhfpipaayvdpaENYPFLwkdkelkkfpleqSPMQECWREMEKLVDAGLVRNIG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 159 VSNFSVyqhQLLESFLSIPVVSNHIDLNLLNTSALDNGALDYVKQKYMRPLAVSPLGGGRIEHGTDELA----LKVRKKL 234
Cdd:cd19114 156 IANFNV---QLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKhftnLLEHPVV 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391131612 235 VEMAEKYESNIESIAVAWIVKLGALPLIGTLEEKRIRNIVNSFSVKLDHQDWYELY 290
Cdd:cd19114 233 KKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALY 288
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
18-163 |
1.91e-03 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 39.33 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 18 YGFWRWEKESAnslkdMDQIVHlCLELGINTFDHADRYGKySCESLFGKVLANKS--FKRSDVVLFSKCGVNIPDSSkpe 95
Cdd:cd19115 18 FGLWKVNNDTC-----ADQVYN-AIKAGYRLFDGACDYGN-EVEAGQGVARAIKEgiVKREDLFIVSKLWNTFHDGE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391131612 96 irvsHVDSSAKHittsvenSLRNLQTDYLDVFL------LDQLDP--------LSD----------LESTVLALEKLKSS 151
Cdd:cd19115 88 ----RVEPICRK-------QLADWGIDYFDLFLihfpiaLKYVDPavryppgwFYDgkkvefsnapIQETWTAMEKLVDK 156
|
170
....*....|..
gi 1391131612 152 GKVKNIGVSNFS 163
Cdd:cd19115 157 GLARSIGVSNFS 168
|
|
| |
