|
Name |
Accession |
Description |
Interval |
E-value |
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
3-268 |
0e+00 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 568.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIATNQIELSPYLQN 162
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYLQN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTD 242
Cdd:PRK11172 162 RKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDA 241
|
250 260
....*....|....*....|....*.
gi 881124778 243 DDMAQIAALERNGREVDPAGLAPKWD 268
Cdd:PRK11172 242 EDMAAIAALDRNGRLVSPEGLAPEWD 267
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
4-251 |
6.22e-169 |
|
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: 466.83 E-value: 6.22e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLEDS 83
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIATNQIELSPYLQNR 163
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 164 KLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDD 243
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDAD 240
|
....*...
gi 881124778 244 DMAQIAAL 251
Cdd:cd19139 241 DMAAIAAL 248
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
4-261 |
7.75e-137 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 385.95 E-value: 7.75e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLEDS 83
Cdd:COG0656 5 IPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAAFEES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPAPDngvPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGkDAIATNQIELSPYLQNR 163
Cdd:COG0656 85 LERLGLDYLDLYLIHWPGPG---PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG-VKPAVNQVELHPYLQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 164 KLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDD 243
Cdd:COG0656 161 ELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDE 240
|
250
....*....|....*....
gi 881124778 244 DMAQIAALERNGRE-VDPA 261
Cdd:COG0656 241 DMAAIDALDRGERLgPDPD 259
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
4-248 |
1.40e-115 |
|
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: 331.54 E-value: 1.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLEDS 83
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDaIATNQIELSPYLQNR 163
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPT--VPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP-IAVNQVEFHPFLYQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 164 KLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDD 243
Cdd:cd19073 158 ELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 881124778 244 DMAQI 248
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
3-251 |
1.45e-110 |
|
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: 319.20 E-value: 1.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19140 7 RIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASVEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDaIATNQIELSPYLQN 162
Cdd:cd19140 87 SLRKLRTDYVDLLLLHWPNKD--VPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAP-LFTNQVEYHPYLDQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAM-QLGYSVIPSSTKRENLASNLLAQTLRLT 241
Cdd:cd19140 164 RKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIFDFTLS 243
|
250
....*....|
gi 881124778 242 DDDMAQIAAL 251
Cdd:cd19140 244 DEEMARIAAL 253
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
4-249 |
1.50e-109 |
|
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: 316.35 E-value: 1.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLEDS 83
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPAPDNGVP-----LATFmTALADAQAKGLTRRIGISNFNIALTKEaIAAVGKDAIATNQIELSP 158
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKEGGskearLETW-RALEELVDEGLVRSIGVSNFNVEHLEE-LLAAARIKPAVNQIELHP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 159 YLQNRKLVEFLNAEGIHVTSYMTLA--YGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQ 236
Cdd:cd19071 159 YLQQKELVEFCKEHGIVVQAYSPLGrgRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVF 238
|
250
....*....|...
gi 881124778 237 TLRLTDDDMAQIA 249
Cdd:cd19071 239 DFELSEEDMAAID 251
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
4-258 |
2.83e-86 |
|
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: 259.27 E-value: 2.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAA----SGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEvfkeGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPA----------------PDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAA 143
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPValkkgvgfpesgedllSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 144 vGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYG------------KVLGDPVLGAIAKRHDATPAQVALAW 211
Cdd:cd19123 172 -ARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaegepVLLEDPVINKIAEKHGASPAQVLIAW 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 881124778 212 AMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREV 258
Cdd:cd19123 251 AIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
2-252 |
9.52e-84 |
|
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: 251.14 E-value: 9.52e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLE 81
Cdd:cd19131 8 NTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTLRAFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 82 DSLRKLRTDYVDLTLIHWPAPDNGVPLATFmTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKdAIATNQIELSPYLQ 161
Cdd:cd19131 88 ESLRKLGLDYVDLYLIHWPVPAQDKYVETW-KALIELKKEGRVKSIGVSNFTIEHLQRLIDETGV-VPVVNQIELHPRFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 162 NRKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLT 241
Cdd:cd19131 166 QRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELD 245
|
250
....*....|.
gi 881124778 242 DDDMAQIAALE 252
Cdd:cd19131 246 ADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
3-253 |
3.88e-81 |
|
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: 244.49 E-value: 3.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19132 6 QIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEALRTIEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDNGVPLATFmTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKdAIATNQIELSPYLQN 162
Cdd:cd19132 86 SLYRLGLDYVDLYLIHWPNPSRDLYVEAW-QALIEAREEGLVRSIGVSNFLPEHLDRLIDETGV-TPAVNQIELHPYFPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLVEFLNAEGIHVTSYMTLAYG-KVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLT 241
Cdd:cd19132 164 AEQRAYHREHGIVTQSWSPLGRGsGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELS 243
|
250
....*....|..
gi 881124778 242 DDDMAQIAALER 253
Cdd:cd19132 244 DEDMAAIAALDR 255
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
4-251 |
2.42e-80 |
|
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: 242.92 E-value: 2.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQ-VVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAAS----GVSRDALFLTTKIWVDNYAPDKLVP 78
Cdd:cd19136 1 MPILGLGTFRLRGEeEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 79 SLEDSLRKLRTDYVDLTLIHWPA--------PDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEaIAAVGKDAIA 150
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGvqglkpsdPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEE-LLKYCEVPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 151 TNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYG--KVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKREN 228
Cdd:cd19136 160 VNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGdlRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPER 239
|
250 260
....*....|....*....|...
gi 881124778 229 LASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19136 240 IAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-252 |
8.95e-79 |
|
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: 239.55 E-value: 8.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASG----VSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19125 11 IPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDHAPEDVPPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPA----------PDNGVPL---ATF--MTALADaqaKGLTRRIGISNFNIALTKEaIAAV 144
Cdd:cd19125 91 LEKTLKDLQLDYLDLYLIHWPVrlkkgahmpePEEVLPPdipSTWkaMEKLVD---SGKVRAIGVSNFSVKKLED-LLAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSY-------MTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGY 217
Cdd:cd19125 167 ARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYsplgspgTTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRGT 246
|
250 260 270
....*....|....*....|....*....|....*
gi 881124778 218 SVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALE 252
Cdd:cd19125 247 SVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIE 281
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
4-251 |
4.46e-76 |
|
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: 231.69 E-value: 4.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG-QVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19133 9 MPILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKAKKAFER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDngvplaTFMT--ALADAQAKGLTRRIGISNFN------IALTKEAIAAVgkdaiatNQI 154
Cdd:cd19133 89 SLKRLGLDYLDLYLIHQPFGD------VYGAwrAMEELYKEGKIRAIGVSNFYpdrlvdLILHNEVKPAV-------NQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 155 ELSPYLQNRKLVEFLNAEGIHVTSYMTLAYGK--VLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASN 232
Cdd:cd19133 156 ETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAEN 235
|
250
....*....|....*....
gi 881124778 233 LLAQTLRLTDDDMAQIAAL 251
Cdd:cd19133 236 FDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
2-256 |
4.42e-75 |
|
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: 230.25 E-value: 4.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKG-QVVIDSVRNALELGYRAIDTAQIYGNEAEVGEA----IAASGVSRDALFLTTKIWVDNYAPDKL 76
Cdd:cd19116 9 NEIPAIALGTWKLKDdEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNSYHEREQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 77 VPSLEDSLRKLRTDYVDLTLIHWP----------APDNGVP-----LATFmTALADAQAKGLTRRIGISNFNIALTKeAI 141
Cdd:cd19116 89 EPALRESLKRLGLDYVDLYLIHWPvafkenndseSNGDGSLsdidyLETW-RGMEDLVKLGLTRSIGVSNFNSEQIN-RL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 142 AAVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAY---------GKVLGDPVLGAIAKRHDATPAQVALAWA 212
Cdd:cd19116 167 LSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRlvprgqtnpPPRLDDPTLVAIAKKYGKTTAQIVLRYL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 881124778 213 MQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGR 256
Cdd:cd19116 247 IDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQR 290
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-256 |
1.25e-74 |
|
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: 228.43 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLK-GQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19157 10 MPWLGLGVFKVEeGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDSTLKAFEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDNGVplATFmTALADAQAKGLTRRIGISNFNIALTKEaIAAVGKDAIATNQIELSPYLQN 162
Cdd:cd19157 90 SLERLGLDYLDLYLIHWPVKGKYK--ETW-KALEKLYKDGRVRAIGVSNFQVHHLED-LLADAEIVPMVNQVEFHPRLTQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTD 242
Cdd:cd19157 166 KELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQ 245
|
250
....*....|....
gi 881124778 243 DDMAQIAALERNGR 256
Cdd:cd19157 246 EDMDKIDALNENLR 259
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-252 |
6.18e-74 |
|
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: 226.16 E-value: 6.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLK-GQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19126 9 MPWLGLGVFQTPdGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDNgvpLATFMTALADAQAKGLTRRIGISNFNIALTKEaIAAVGKDAIATNQIELSPYLQN 162
Cdd:cd19126 89 SLDRLGLDYVDLYLIHWPGKDK---FIDTWKALEKLYASGKVKAIGVSNFQEHHLEE-LLAHADVVPAVNQVEFHPYLTQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTD 242
Cdd:cd19126 165 KELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSE 244
|
250
....*....|
gi 881124778 243 DDMAQIAALE 252
Cdd:cd19126 245 DDMTAIDALN 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-257 |
8.82e-74 |
|
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: 227.29 E-value: 8.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIA---ASGV-SRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19154 12 MPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAellEEGVvKREDLFITTKLWTHEHAPEDVEEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPAP-----------DNG------VPLATFMTALADAQAKGLTRRIGISNFNIALTkEAIA 142
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHAPAAfkddegesgtmENGmsihdaVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQI-QRIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 143 AVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAY---------------GKVLGDPVLGAIAKRHDATPAQV 207
Cdd:cd19154 171 DNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspaPNLLQDPIVKAIAEKHGKTPAQV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 881124778 208 ALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGRE 257
Cdd:cd19154 251 LLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
2-252 |
1.26e-73 |
|
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: 225.56 E-value: 1.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLE 81
Cdd:cd19130 8 NSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEPAAAFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 82 DSLRKLRTDYVDLTLIHWPAPDNGVPLATFmTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKdAIATNQIELSPYLQ 161
Cdd:cd19130 88 ESLAKLGLDQVDLYLVHWPTPAAGNYVHTW-EAMIELRAAGRTRSIGVSNFLPPHLERIVAATGV-VPAVNQIELHPAYQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 162 NRKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLT 241
Cdd:cd19130 166 QRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLT 245
|
250
....*....|.
gi 881124778 242 DDDMAQIAALE 252
Cdd:cd19130 246 DTEIAAIDALD 256
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
4-248 |
2.64e-71 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 219.79 E-value: 2.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG---------QVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIaaSGVSRDALFLTTKIWVDNY 71
Cdd:cd19072 4 VPVLGLGTWGIGGgmskdysddKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 72 APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIAT 151
Cdd:cd19072 82 KYDDVIKAAKESLKRLGTDYIDLYLIHWPNPS--IPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 152 NQIELSpyLQNR----KLVEFLNAEGIHVTSYMTLAYGKVLGD---PVLGAIAKRHDATPAQVALAWAMQL-GYSVIPSS 223
Cdd:cd19072 160 NQVEYN--LFDReeesGLLPYCQKNGIAIIAYSPLEKGKLSNAkgsPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKA 237
|
250 260
....*....|....*....|....*
gi 881124778 224 TKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19072 238 SNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
3-250 |
1.26e-70 |
|
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: 218.26 E-value: 1.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKGQV------VIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKl 76
Cdd:cd19120 5 PAIAFGTGTAWYKSGDddiqrdLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIKDPRE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 77 vpSLEDSLRKLRTDYVDLTLIHWP--APDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEaIAAVGKDAIATNQI 154
Cdd:cd19120 84 --ALRKSLAKLGVDYVDLYLIHSPffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEE-LLDTAKIKPAVNQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 155 ELSPYLQNR--KLVEFLNAEGIHVTSYMTLA--YGKVLG--DPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKREN 228
Cdd:cd19120 161 EFHPYLYPQqpALLEYCREHGIVVSAYSPLSplTRDAGGplDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEER 240
|
250 260
....*....|....*....|..
gi 881124778 229 LASNLLAQTLRLTDDDMAQIAA 250
Cdd:cd19120 241 MKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
4-251 |
3.66e-68 |
|
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: 211.88 E-value: 3.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLEDS 83
Cdd:cd19127 9 MPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRGFDAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKdAIATNQIELSPYLQNR 163
Cdd:cd19127 89 LRRLGLDYVDLYLLHWPVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTV-VPAVNQVELHPYFSQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 164 KLVEFLNAEGIHVTSYMTL------------AYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLAS 231
Cdd:cd19127 168 DLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAE 247
|
250 260
....*....|....*....|
gi 881124778 232 NLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19127 248 NIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
2-251 |
6.49e-68 |
|
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: 211.89 E-value: 6.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIA-----ASGVSRDALFLTTKIWVDNYAPDKL 76
Cdd:cd19118 5 NKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKellkeEPGVKREDLFITSKLWNNSHRPEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 77 VPSLEDSLRKLRTDYVDLTLIHWPA---------PDNGVPL--------------ATF--MTALadaQAKGLTRRIGISN 131
Cdd:cd19118 85 EPALDDTLKELGLDYLDLYLIHWPVafkptgdlnPLTAVPTnggevdldlsvslvDTWkaMVEL---KKTGKVKSIGVSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 132 FNIALTKEAIAAVGkDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL---AYGK--VLGDPVLGAIAKRHDATPAQ 206
Cdd:cd19118 162 FSIDHLQAIIEETG-VVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLplLVQHPEVKAIAAKLGKTPAQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 881124778 207 VALAWAMQLGYSVIPSSTKRENLASNLlaQTLRLTDDDMAQIAAL 251
Cdd:cd19118 241 VLIAWGIQRGHSVIPKSVTPSRIRSNF--EQVELSDDEFNAVTAL 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-251 |
3.41e-67 |
|
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: 209.49 E-value: 3.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLkGQVVIDSVRNAL-ELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19135 13 MPILGLGTSHS-GGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTKQAFEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDNGVP-----LATFMTALADAQAKGLTRRIGISNFNIALTKEAIAavgkDAIAT---NQI 154
Cdd:cd19135 92 SLKRLGVDYLDLYLLHWPDCPSSGKnvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLE----DCSVVphvNQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 155 ELSPYLQNRKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLL 234
Cdd:cd19135 168 EFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQ 247
|
250
....*....|....*..
gi 881124778 235 AQTLRLTDDDMAQIAAL 251
Cdd:cd19135 248 VFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
4-251 |
4.48e-67 |
|
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: 209.66 E-value: 4.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYApdKLVPSLEDS 83
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHR--RVEEALDQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPAP-----DNGVPLATFMTALADAQ--------------AKGLTRRIGISNFNIALTKEAIAAV 144
Cdd:cd19117 92 LKKLGLDYVDLYLMHWPVPldpdgNDFLFKKDDGTKDHEPDwdfiktwelmqklpATGKVKAIGVSNFSIKNLEKLLASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAI-ATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL--AYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIP 221
Cdd:cd19117 172 SAKIVpAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLP 251
|
250 260 270
....*....|....*....|....*....|
gi 881124778 222 SSTKRENLASNLlaQTLRLTDDDMAQIAAL 251
Cdd:cd19117 252 KSVTPSRIESNF--KLFTLSDEEFKEIDEL 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
4-261 |
1.18e-65 |
|
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: 206.85 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLK-GQVViDSVRNALELGYRAIDTAQIYGNEAEVGEAIAAS-----GVSRDALFLTTKIWVDNYAPDKLV 77
Cdd:cd19106 7 MPLIGLGTWKSKpGQVK-AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHHPEDVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 78 PSLEDSLRKLRTDYVDLTLIHWPA------------PDNGV------PLATF--MTALADaqaKGLTRRIGISNFNIALT 137
Cdd:cd19106 86 PALRKTLKDLQLDYLDLYLIHWPYafergdnpfpknPDGTIrydsthYKETWkaMEKLVD---KGLVKAIGLSNFNSRQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 138 KEaIAAVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL-----AYGK-----VLGDPVLGAIAKRHDATPAQV 207
Cdd:cd19106 163 DD-ILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrPWAKpdepvLLEEPKVKALAKKYNKSPAQI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 881124778 208 ALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREVDPA 261
Cdd:cd19106 242 LLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPM 295
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
5-251 |
4.48e-65 |
|
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: 204.29 E-value: 4.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAA----SGVSRDALFLTTKIWVDNYAPDKLVPSL 80
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 81 EDSLRKLRTDYVDLTLIHWP-----------------APDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIaA 143
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLL-N 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 144 VGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL----AYGK--VLGDPVLGAIAKRHDATPAQVALAWAMQL-- 215
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLggsyGDGNltFLNDSELKALATKYNTTPPQVIIAWHLQKwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 881124778 216 -GYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19128 241 kNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
4-252 |
1.76e-64 |
|
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: 202.88 E-value: 1.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGT--YRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIA---ASGV--SRDALFLTTKIWVDNYAPDKL 76
Cdd:cd19124 5 MPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSDAHPDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 77 VPSLEDSLRKLRTDYVDLTLIHWPA------------PDNGVPL---ATFmTALADAQAKGLTRRIGISNFNIALTKE-- 139
Cdd:cd19124 85 LPALKKSLRNLQLEYVDLYLIHWPVslkpgkfsfpieEEDFLPFdikGVW-EAMEECQRLGLTKAIGVSNFSCKKLQEll 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 140 AIAAVGKdaiATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL-AYGK------VLGDPVLGAIAKRHDATPAQVALAWA 212
Cdd:cd19124 164 SFATIPP---AVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgAPGTkwgsnaVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 881124778 213 MQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALE 252
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIP 280
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-256 |
2.35e-64 |
|
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: 201.98 E-value: 2.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLK-GQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLED 82
Cdd:cd19156 9 MPRLGLGVWRVQdGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYESTLAAFEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPAPDNGVPLatfMTALADAQAKGLTRRIGISNFNIALTKEAIAAVgKDAIATNQIELSPYLQN 162
Cdd:cd19156 89 SLEKLGLDYVDLYLIHWPVKGKFKDT---WKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSC-KVAPMVNQIELHPLLTQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTD 242
Cdd:cd19156 165 EPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTA 244
|
250
....*....|....
gi 881124778 243 DDMAQIAALERNGR 256
Cdd:cd19156 245 EEIRQIDGLNTDHR 258
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
2-256 |
2.75e-64 |
|
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: 202.01 E-value: 2.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNYAPDKLVPSLE 81
Cdd:cd19134 9 NTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTASQAACR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 82 DSLRKLRTDYVDLTLIHWPAPDNGVPLATFmTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAiATNQIELSPYLQ 161
Cdd:cd19134 89 ASLERLGLDYVDLYLIHWPAGREGKYVDSW-GGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTP-AVNQIELHPLLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 162 NRKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLT 241
Cdd:cd19134 167 QAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELT 246
|
250
....*....|....*
gi 881124778 242 DDDMAQIAALERNGR 256
Cdd:cd19134 247 ADHMDALDGLDDGTR 261
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
3-256 |
1.17e-63 |
|
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: 201.19 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIA---ASG-VSRDALFLTTKIWVDNYAPDKLVP 78
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 79 SLEDSLRKLRTDYVDLTLIHWPA-----------PDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEaIAAVGKD 147
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPCgfvnkkdkgerELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK-ILAYAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 148 AIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL-AYGKV-----------LGDPVLGAIAKRHDATPAQVALAWAMQL 215
Cdd:cd19111 162 KPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgSPGRAnqslwpdqpdlLEDPTVLAIAKELDKTPAQVLLRFVLQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 881124778 216 GYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGR 256
Cdd:cd19111 242 GTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-261 |
5.51e-63 |
|
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: 200.02 E-value: 5.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASG----VSRDALFLTTKIWvdNYAPDKLVPS 79
Cdd:cd19112 11 MPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLW--NSDHGHVIEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPAP---------------------DNGVPLATFMTALADAQAKGLTRRIGISNFNIALTK 138
Cdd:cd19112 89 CKDSLKKLQLDYLDLYLVHFPVAtkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIFLTR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 139 EaIAAVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLA--------YGKV--LGDPVLGAIAKRHDATPAQVA 208
Cdd:cd19112 169 D-CLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaaanaewFGSVspLDDPVLKDLAKKYGKSAAQIV 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 881124778 209 LAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREVDPA 261
Cdd:cd19112 248 LRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
2-256 |
6.98e-62 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 196.06 E-value: 6.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAASGVSRDALFLTTKIWVDNY-APDKlvpSL 80
Cdd:PRK11565 13 NVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHkRPRE---AL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 81 EDSLRKLRTDYVDLTLIHWPAPDNGvplaTFMTA---LADAQAKGLTRRIGISNFNIALTKEAIAAVGKdAIATNQIELS 157
Cdd:PRK11565 90 EESLKKLQLDYVDLYLMHWPVPAID----HYVEAwkgMIELQKEGLIKSIGVCNFQIHHLQRLIDETGV-TPVINQIELH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 158 PYLQNRKLVEFLNAEGIHVTSYMTLAYG--KVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLA 235
Cdd:PRK11565 165 PLMQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDV 244
|
250 260
....*....|....*....|.
gi 881124778 236 QTLRLTDDDMAQIAALERNGR 256
Cdd:PRK11565 245 FDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-268 |
9.32e-62 |
|
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: 196.90 E-value: 9.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGE----AIAASGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEgvnrAIDEGLVKREELFLTSKLWNNFHDPKNVETA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWP-------------------APDN----GVPLATFMTALADAQAKGLTRRIGISNFNIAL 136
Cdd:cd19113 91 LNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgDGDNfvyeDVPILDTWKALEKLVDAGKIKSIGVSNFPGAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 137 TKEAI-AAVGKDAIAtnQIELSPYLQNRKLVEFLNAEGIHVTSY--------MTLAYGKVLGDPVL------GAIAKRHD 201
Cdd:cd19113 171 ILDLLrGATIKPAVL--QIEHHPYLQQPKLIEYAQKAGITITAYssfgpqsfVELNQGRALNTPTLfehdtiKSIAAKHN 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881124778 202 ATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREVDPaglapkWD 268
Cdd:cd19113 249 KTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDP------WD 309
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-248 |
4.26e-60 |
|
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: 191.31 E-value: 4.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRL-----KGQVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASgvsRDALFLTTKIWVDNYAP 73
Cdd:cd19138 9 TKVPALGQGTWYMgedpaKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLPSNASR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 74 DKLVPSLEDSLRKLRTDYVDLTLIHWPApdnGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIATNQ 153
Cdd:cd19138 86 QGTVRACERSLRRLGTDYLDLYLLHWRG---GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCAANQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 154 IELSpyLQNR----KLVEFLNAEGIHVTSYMTLAYGKVLG-----DPVLGAIAKRHDATPAQVALAWAMQLGYSV-IPSS 223
Cdd:cd19138 163 VLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLRrglleNPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKS 240
|
250 260
....*....|....*....|....*
gi 881124778 224 TKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19138 241 GSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
4-245 |
3.52e-57 |
|
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: 183.54 E-value: 3.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG---------QVVIDSVRNALELGYRAIDTAQIYG---NEAEVGEAIaaSGVSRDALFLTTKIWVDNY 71
Cdd:cd19137 4 IPALGLGTWGIGGfltpdysrdEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAI--KDFPREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 72 APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDaIAT 151
Cdd:cd19137 82 RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPN--IPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTP-IVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 152 NQIELSPY---LQNRKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYSV-IPSSTKRE 227
Cdd:cd19137 159 NQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGRVE 238
|
250
....*....|....*...
gi 881124778 228 NLASNLLAQTLRLTDDDM 245
Cdd:cd19137 239 HLKENLKATEIKLSEEEM 256
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
8-251 |
5.70e-57 |
|
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: 184.05 E-value: 5.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 8 GLGTYRLKGQV-------VIDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAASGVSRDALFLTTKI------WVDNY 71
Cdd:pfam00248 2 GLGTWQLGGGWgpiskeeALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 72 APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAvGKDAIAT 151
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPD--TPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTK-GKIPIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 152 NQIELSPY--LQNRKLVEFLNAEGIHVTSYMTLAYGKVLG---------------------------DPVLGAIAKRHDA 202
Cdd:pfam00248 159 VQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleaLEALEEIAKEHGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 881124778 203 TPAQVALAWAMQ--LGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:pfam00248 239 SPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
4-245 |
8.05e-57 |
|
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: 183.12 E-value: 8.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIA---ASGVSRDALFLTTKIWvdNYAPDKLVPSL 80
Cdd:cd19121 12 IPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKeaiAGGVKREDLFVTTKLW--STYHRRVELCL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 81 EDSLRKLRTDYVDLTLIHWPAPDNGVPLATFMTALADAQ--------------------AKGLTRRIGISNFNIALTKEA 140
Cdd:cd19121 90 DRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSrdldwdwnhvdtwkqmekvlKTGKTKAIGVSNYSIPYLEEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 141 IAAvGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL--AYGKVLGDPVLGAIAKRHDATPAQVALAWAMQLGYS 218
Cdd:cd19121 170 LKH-ATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLISYQVARGAV 248
|
250 260
....*....|....*....|....*..
gi 881124778 219 VIPSSTKRENLASNLlaQTLRLTDDDM 245
Cdd:cd19121 249 VLPKSVTPDRIKSNL--EIIDLDDEDM 273
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-256 |
9.63e-55 |
|
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: 178.87 E-value: 9.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEA----IAASGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVlkkwIDSGKVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPAPDNG-------------------VPLATFMTALADAQAKGLTRRIGISNFNialtKEA 140
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPVGSLSkeddsgkldptgehkqdytTDLLDIWKAMEAQVDQGLTRSIGLSNFN----REQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 141 IAAVGKDAI---ATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL-----------------AYGKVLGDPVLGAIAKRH 200
Cdd:cd19155 168 MARILKNARikpANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPVVKAIAERH 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 881124778 201 DATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGR 256
Cdd:cd19155 248 GKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
4-256 |
1.17e-54 |
|
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: 178.58 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYR----LKGQVViDSVRNALELGYRAIDTAQIYGNEAEVGEAI----AASGVSRDALFLTTKIWVDNYAPDK 75
Cdd:cd19108 11 IPVLGFGTYApeevPKSKAL-EATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCTFHRPEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 76 LVPSLEDSLRKLRTDYVDLTLIHWPAP-----------DNGVPL-------ATF--MTALADAqakGLTRRIGISNFN-- 133
Cdd:cd19108 90 VRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfpkdENGKLIfdtvdlcATWeaMEKCKDA---GLAKSIGVSNFNrr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 134 ---IALTKEAIaavgKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYGK-----------VLGDPVLGAIAKR 199
Cdd:cd19108 167 qleMILNKPGL----KYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRdkewvdqnspvLLEDPVLCALAKK 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 881124778 200 HDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGR 256
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-262 |
4.77e-54 |
|
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: 177.23 E-value: 4.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGE----AIAASGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19115 13 MPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQgvarAIKEGIVKREDLFIVSKLWNTFHDGERVEPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPAP----------------DNG------VPLATFMTALADAQAKGLTRRIGISNFNIALT 137
Cdd:cd19115 93 CRKQLADWGIDYFDLFLIHFPIAlkyvdpavryppgwfyDGKkvefsnAPIQETWTAMEKLVDKGLARSIGVSNFSAQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 138 KEAIAAvGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTL--------------AYGKVLGDPVLGAIAKRHDAT 203
Cdd:cd19115 173 MDLLRY-ARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFgpqsfleldlpgakDTPPLFEHDVIKSIAEKHGKT 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 881124778 204 PAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREVDPAG 262
Cdd:cd19115 252 PAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNNPLN 310
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
4-248 |
2.20e-52 |
|
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: 172.26 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAI----AASGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMqevfKAGKIRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWP---AP---------------DNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEaI 141
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPfafQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLRE-I 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 142 AAVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYG---KVLGDPVLGAIAKRHDATPAQVALAWAMQLGYS 218
Cdd:cd19129 165 FEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAWAIQRGTA 244
|
250 260 270
....*....|....*....|....*....|
gi 881124778 219 VIPSSTKRENLASNLLAQTlrLTDDDMAQI 248
Cdd:cd19129 245 LLTTSKTPSRIRENFDIST--LPEDAMREI 272
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
2-259 |
1.72e-51 |
|
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: 170.37 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIPAFGLGTYRLKGQVVID----SVRNALELGYRAIDTAQIYGNEAEVGEA----IAASGVSRDALFLTTKIWVDNYAP 73
Cdd:cd19109 2 NSIPIIGLGTYSEPKTTPKGacaeAVKVAIDTGYRHIDGAYIYQNEHEVGQAirekIAEGKVKREDIFYCGKLWNTCHPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 74 DKLVPSLEDSLRKLRTDYVDLTLIH-----------WPAPDNGVPL-------ATF--MTALADAqakGLTRRIGISNFN 133
Cdd:cd19109 82 ELVRPTLERTLKVLQLDYVDLYIIEmpmafkpgdeiYPRDENGKWLyhktnlcATWeaLEACKDA---GLVKSIGVSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 134 -----IALTKEAIaavgKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYGK-----------VLGDPVLGAIA 197
Cdd:cd19109 159 rrqleLILNKPGL----KHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881124778 198 KRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREVD 259
Cdd:cd19109 235 KKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVE 296
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
4-256 |
1.76e-51 |
|
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: 170.29 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAA----SGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEkikeQVVKREDLFIVSKLWCTFHEKGLVKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPA------------------PDNGVPLATF--MTALADAqakGLTRRIGISNFNIALTKE 139
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnviPSDTTFLDTWeaMEELVDE---GLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 140 AIAAVG-KDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLA-----YGK-----VLGDPVLGAIAKRHDATPAQVA 208
Cdd:cd19107 161 ILNKPGlKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 881124778 209 LAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGR 256
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
4-260 |
2.30e-51 |
|
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: 170.05 E-value: 2.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVG----EAIAASGVSRDALFLTTKIWVDNYAPDKLVPS 79
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPAPDNGV-PLATFMTALADAQAK----------------------GLTRRIGISNFNIAL 136
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAAYVdPAENYPFLWKDKELKkfpleqspmqecwremeklvdaGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 137 TKEAIAaVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLA-------------YGKVLGDPVLGAIAKRHDAT 203
Cdd:cd19114 164 ILDLLT-YAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkhlkhFTNLLEHPVVKKLADKHKRD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 881124778 204 PAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGREVDP 260
Cdd:cd19114 243 TGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDP 299
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
4-251 |
5.47e-51 |
|
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: 169.20 E-value: 5.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRL---KGQV----VIDSVRNALELGYRAIDTAQIYGN-EAE--VGEAIAasGVSRDALFLTTKI------- 66
Cdd:COG0667 13 VSRLGLGTMTFggpWGGVdeaeAIAILDAALDAGINFFDTADVYGPgRSEelLGEALK--GRPRDDVVIATKVgrrmgpg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 -WVDNYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIA-AV 144
Cdd:COG0667 91 pNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPD--TPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAiAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAIATNQIELSpyLQNRK----LVEFLNAEGIHVTSYMTLAYG----KVLGDP------------------------- 191
Cdd:COG0667 169 GLPPIVAVQNEYS--LLDRSaeeeLLPAARELGVGVLAYSPLAGGlltgKYRRGAtfpegdraatnfvqgylternlalv 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881124778 192 -VLGAIAKRHDATPAQVALAWAMQLGY--SVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:COG0667 247 dALRAIAAEHGVTPAQLALAWLLAQPGvtSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
1-256 |
3.16e-48 |
|
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: 161.67 E-value: 3.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 1 MNPIPAFGLGTYRLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAIAAS----GVSRDALFLTTKIWVDNYAPDKL 76
Cdd:cd19110 1 MEDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKikegVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 77 VPSLEDSLRKLRTDYVDLTLIHWP----APDNGVPL----------ATFM---TALADAQAKGLTRRIGISNFNIALTKE 139
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPmgfkPGEPDLPLdrsgmvipsdTDFLdtwEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 140 AIAAVG-KDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYG----KVLGDPVLGAIAKRHDATPAQVALAWAMQ 214
Cdd:cd19110 161 LLNKPGlRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGScegvDLIDDPVIQRIAKKHGKSPAQILIRFQIQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 881124778 215 LGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALERNGR 256
Cdd:cd19110 241 RNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLR 282
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
4-248 |
1.25e-47 |
|
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: 160.06 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG---------QVVIDSVRNALELGYRAIDTAQIYGN-EAE--VGEAIAASgvsRDALFLTTKIWVDNY 71
Cdd:cd19085 1 VSRLGLGCWQFGGgywwgdqddEESIATIHAALDAGINFFDTAEAYGDgHSEevLGKALKGR---RDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 72 APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAiAAVGKdaIAT 151
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD--VPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEA-LDAGR--IDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 152 NQIelsPY-LQNR----KLVEFLNAEGIHVTSYMTLAYG---------------------KVLGDP-----------VLG 194
Cdd:cd19085 153 NQL---PYnLLWRaieyEILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlFRHFEPgaeeetfealeKLK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 881124778 195 AIAKRHDATPAQVALAWAMQLGY--SVIPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19085 230 EIADELGVTMAQLALAWVLQQPGvtSVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-245 |
5.13e-44 |
|
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: 150.73 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTY--RLKGQVVIDSVRNALELGYRAIDTAQIYGNEAEVGEAI----AASGVSRDALFLTTKIWVDNYapDKLV 77
Cdd:cd19119 12 IPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIkraiDDGSIKREELFITTKVWPTFY--DEVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 78 PSLEDSLRKLRTDYVDLTLIHWPAP------DNGVPL-----------------ATFMTALADAQAKGLTRRIGISNFNI 134
Cdd:cd19119 90 RSLDESLKALGLDYVDLLLVHWPVCfekdsdDSGKPFtpvnddgktryaasgdhITTYKQLEKIYLDGRAKAIGVSNYSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 135 ALTKEAIAAVgKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYGK--VLGDPVLGAIAKRHDATPAQVALAWA 212
Cdd:cd19119 170 VYLERLIKEC-KVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGapNLKNPLVKKIAEKYNVSTGDILISYH 248
|
250 260 270
....*....|....*....|....*....|...
gi 881124778 213 MQLGYSVIPSSTKRENLASNLlaQTLRLTDDDM 245
Cdd:cd19119 249 VRQGVIVLPKSLKPVRIVSNG--KIVSLTKEDL 279
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
5-233 |
3.05e-43 |
|
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: 146.89 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGTYRLKGQV----VIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASGVsRDALFLTTKI--------WVD 69
Cdd:cd06660 1 SRLGLGTMTFGGDGdeeeAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGghppggdpSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 70 NYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAV---GK 146
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPS--TPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAkahGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 147 DAIATNQIELS---PYLQNRKLVEFLNAEGIHVTSYMTLAYGkvlgdpvlgaiakrhdatPAQVALAWAMQLGY--SVIP 221
Cdd:cd06660 158 PGFAAVQPQYSlldRSPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFvtVPIV 219
|
250
....*....|..
gi 881124778 222 SSTKRENLASNL 233
Cdd:cd06660 220 GARSPEQLEENL 231
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
4-248 |
8.85e-43 |
|
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: 147.29 E-value: 8.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG--------QVVIDSVRNALELGYRAIDTAQIYGN-EAE--VGEAIaasGVSRDALFLTTKIWVD--- 69
Cdd:cd19084 4 VSRIGLGTWAIGGtwwgevddQESIEAIKAAIDLGINFFDTAPVYGFgHSEeiLGKAL---KGRRDDVVIATKCGLRwdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 70 ------NYAPDKLVPSLEDSLRKLRTDYVDLTLIHWpaPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAA 143
Cdd:cd19084 81 gkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHW--PDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 144 VGkdaIATNQIELSPYLQN--RKLVEFLNAEGIHVTSYMTLAYG----KVLGDP-------------------------- 191
Cdd:cd19084 159 GP---IVSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQGlltgKYKKEPtfppddrrsrfpffrgenfeknleiv 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 192 -VLGAIAKRHDATPAQVALAWAMQ--LGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19084 236 dKLKEIAEKYGKSLAQLAIAWTLAqpGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
4-251 |
1.29e-42 |
|
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: 147.00 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQV--VIDSVRNALELGYRAIDTAQIYGNEAEVGEAI-----AASGVSRDALFLTTKIWVDNYAPDKL 76
Cdd:cd19122 9 IPAVGFGTFANEGAKgeTYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVrdflkENPSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 77 VPSLEDSLRKLRTDYVDLTLIHWP-------------APDNGVPLATFMT--------ALADAQAKGLTRRIGISNFNIA 135
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPiaaekndqrspklGPDGKYVILKDLTenpeptwrAMEEIYESGKAKAIGVSNWTIP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 136 LTKEaIAAVGKDAIATNQIELSPYLQNRKLVEFLNAEGIHVTSYMTLAYG--------KVLGDPVLGAIAKRHDATPAQV 207
Cdd:cd19122 169 GLKK-LLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQnqvpstgeRVSENPTLNEVAEKGGYSLAQV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 881124778 208 ALAWAMQLGYSVIPSSTKRENLASNLlaQTLRLTDDDMAQIAAL 251
Cdd:cd19122 248 LIAWGLRRGYVVLPKSSTPSRIESNF--KSIELSDEDFEAINQV 289
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
4-248 |
3.17e-38 |
|
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: 135.43 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTY-----------RLKGQVVIDSVRNALELGYRAIDTAQIYGN-EAE--VGEAIAASGVsRDALFLTTKIWVD 69
Cdd:cd19093 2 VSPLGLGTWqwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgRSErlLGRFLKELGD-RDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 70 NY--APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPdNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKD 147
Cdd:cd19093 81 PWrlTRRSVVKALKASLERLGLDSIDLYQLHWPGP-WYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 148 --AIATNQIE---LSPYLQNRKLVEFLNAEGIHVTSYMTLAYGKVLG------------------------DPV---LGA 195
Cdd:cd19093 160 gvPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGkyspenpppggrrrlfgrknlekvQPLldaLEE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 881124778 196 IAKRHDATPAQVALAWAMQLGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19093 240 IAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
4-241 |
6.96e-38 |
|
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: 133.50 E-value: 6.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVV----------IDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAASGvsrDALFLTTKI---- 66
Cdd:cd19088 1 VSRLGYGAMRLTGPGIwgppadreeaIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 -----WVDNYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPapDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAI 141
Cdd:cd19088 78 tgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI--DPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 142 AAVGkdaIATNQIELSP-YLQNRKLVEFLNAEGIHVTSYMTLAYGKVLGD-PVLGAIAKRHDATPAQVALAWAMQLG--Y 217
Cdd:cd19088 156 AIVR---IVSVQNRYNLaNRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPgGLLAEVAARLGATPAQVALAWLLARSpvM 232
|
250 260
....*....|....*....|....
gi 881124778 218 SVIPSSTKRENLASNLLAQTLRLT 241
Cdd:cd19088 233 LPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
7-241 |
1.92e-34 |
|
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: 125.36 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 7 FGLGTYRLKG-----QVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASGVSRDALFLTTK-----------IW 67
Cdd:cd19092 9 LVLGCMRLADwgesaEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirlgddprpGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 68 VDNY--APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPdngvplatFM------TALADAQAKGLTRRIGISNFN---IAL 136
Cdd:cd19092 89 IKHYdtSKEHILASVEGSLKRLGTDYLDLLLLHRPDP--------LMdpeevaEAFDELVKSGKVRYFGVSNFTpsqIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 137 TKEAIaavgKDAIATNQIELSPY----LQNRKLvEFLNAEGIHVTSYMTLAYGKVLGDP---------VLGAIAKRHDAT 203
Cdd:cd19092 161 LQSYL----DQPLVTNQIELSLLhteaIDDGTL-DYCQLLDITPMAWSPLGGGRLFGGFderfqrlraALEELAEEYGVT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 881124778 204 PAQVALAWAMQLGYSVIP--SSTKRENLASNLLAQTLRLT 241
Cdd:cd19092 236 IEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELT 275
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-251 |
3.14e-34 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 125.48 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG------------QVVIDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAASgvsRDALFLTTK--- 65
Cdd:cd19102 1 LTTIGLGTWAIGGggwgggwgpqddRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL---RDRPIVATKcgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 66 IWVDN------YAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKe 139
Cdd:cd19102 78 LWDEEgrirrsLKPASIRAECEASLRRLGVDVIDLYQIHWPDPD--EPIEEAWGALAELKEEGKVRAIGVSNFSVDQMK- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 140 AIAAVGkdAIATNQIELSpyLQNR----KLVEFLNAEGIHVTSYMTLAYG---------KVLGDP--------------- 191
Cdd:cd19102 155 RCQAIH--PIASLQPPYS--LLRRgieaEILPFCAEHGIGVIVYSPMQSGlltgkmtpeRVASLPaddwrrrspffqepn 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881124778 192 ---------VLGAIAKRHDATPAQVALAWAMQLG--YSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19102 231 larnlalvdALRPIAERHGRTVAQLAIAWVLRRPevTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
9-241 |
3.99e-34 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 124.88 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 9 LGTYRLKG-----QVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASGVSRDALFLTTK--IWVDNYAPDKLVP 78
Cdd:COG4989 18 LGCMRLGEwdlspAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTKcgIRLPSEARDNRVK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 79 -----------SLEDSLRKLRTDYVDLTLIHWPAPdngvplatFM------TALADAQAKGLTRRIGISNFN---IALTK 138
Cdd:COG4989 98 hydtskehiiaSVEGSLRRLGTDYLDLLLLHRPDP--------LMdpeevaEAFDELKASGKVRHFGVSNFTpsqFELLQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 139 EAIaavgKDAIATNQIELSPY----LQNRKLvEFLNAEGIHVTSYMTLAYGKVLGDP---------VLGAIAKRHDATPA 205
Cdd:COG4989 170 SAL----DQPLVTNQIELSLLhtdaFDDGTL-DYCQLNGITPMAWSPLAGGRLFGGFdeqfprlraALDELAEKYGVSPE 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 881124778 206 QVALAWAMQLGYSVIP--SSTKRENLASNLLAQTLRLT 241
Cdd:COG4989 245 AIALAWLLRHPAGIQPviGTTNPERIKAAAAALDIELT 282
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
28-248 |
1.56e-30 |
|
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: 115.77 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 28 ELGYRAIDTAQIYGN----------EAEVGEAIAASGvSRDALFLTTKI----WVDNY--APDKLVPSLEDSLRKLRTDY 91
Cdd:cd19081 37 DAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRG-KRDRVVIATKVgfpmGPNGPglSRKHIRRAVEASLRRLQTDY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 92 VDLTLIHWpaPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAavgkdaiATNQIELSPY--------LQNR 163
Cdd:cd19081 116 IDLYQAHW--DDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALE-------LSRQHGLPRYvslqpeynLVDR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 164 KLVEF-----LNAEGIHVTSYMTLAYG-------------------------------KVLGdpVLGAIAKRHDATPAQV 207
Cdd:cd19081 187 ESFEGellplCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakrylnerglRILD--ALDEVAAEHGATPAQV 264
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 881124778 208 ALAWAMQLGY--SVIPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19081 265 ALAWLLARPGvtAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
2-251 |
9.40e-30 |
|
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: 113.67 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 2 NPIpafGLGTY---------RLKGQVVIDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAasGVSRDALFLTTK---- 65
Cdd:cd19083 12 NPI---GLGTNavgghnlypNLDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLK--EYNRNEVVIATKgahk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 66 -----IWVDNyAPDKLVPSLEDSLRKLRTDYVDLTLIHWpaPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEA 140
Cdd:cd19083 87 fggdgSVLNN-SPEFLRSAVEKSLKRLNTDYIDLYYIHF--PDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 141 IAAVGKDAIatnQIELSpyLQNRK----LVEFLNAEGIHVTSYMTLAYGKVLG--------------------------- 189
Cdd:cd19083 164 NKDGYVDVL---QGEYN--LLQREaeedILPYCVENNISFIPYFPLASGLLAGkytkdtkfpdndlrndkplfkgerfse 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881124778 190 --DPV--LGAIAKRHDATPAQVALAWAMQ--LGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19083 239 nlDKVdkLKSIADEKGVTVAHLALAWYLTrpAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
5-235 |
3.99e-28 |
|
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: 108.09 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGTYRLKGQVVIDS-------VRNALELGYRAIDTAQIYGN-EAEVGEAIaaSGVSRDALFLTTKIW--------V 68
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSeaeaarlLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGthgeggrdR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 69 DNYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNialtKEAIAAVGKDA 148
Cdd:cd19095 79 KDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDD--ELTGEVLETLEDLKAAGKVRYIGVSGDG----EELEAAIASGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 149 IATNQIELSPYLQ-NRKLVEFLNAEGIHVTSYMTLAYG----KVLGDP-------VLGAIAKRHDATPAQVALAWAMQ-- 214
Cdd:cd19095 153 FDVVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGrlrrRVRRRPlyadyarRPEFAAEIGGATWAQAALRFVLShp 232
|
250 260
....*....|....*....|.
gi 881124778 215 LGYSVIPSSTKRENLASNLLA 235
Cdd:cd19095 233 GVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
20-248 |
4.86e-28 |
|
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: 108.84 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 20 IDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAASgvsRDALFLTTK---IWVD-------NYAPDKLVPSLEDSLRK 86
Cdd:cd19076 35 IATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR---RDEVVIATKfgiVRDPgsgfrgvDGRPEYVRAACEASLKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 87 LRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAiAAVGKdaIATNQIELSpyLQNRklv 166
Cdd:cd19076 112 LGTDVIDLYYQHRVDPN--VPIEETVGAMAELVEEGKVRYIGLSEASADTIRRA-HAVHP--ITAVQSEYS--LWTR--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 167 eflNAE----------GIHVTSYMTLAYGKVLG----------------DP---------------VLGAIAKRHDATPA 205
Cdd:cd19076 182 ---DIEdevlptcrelGIGFVAYSPLGRGFLTGaikspedlpeddfrrnNPrfqgenfdknlklveKLEAIAAEKGCTPA 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 881124778 206 QVALAWAMQLGYSV--IPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19076 259 QLALAWVLAQGDDIvpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
23-248 |
1.03e-26 |
|
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: 105.74 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 23 VRNALELGYRAIDTAQIYGN-EAE--VGEAIAASGVsRDALFLTTKIwvdnYAPDKLVP------------SLEDSLRKL 87
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgASEeiLGRALKEFAP-RDEVVIATKV----YFPMGDGPngrglsrkhimaEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 88 RTDYVDLTLIHWpaPDNGVPLATFMTALADAQAKGLTRRIGISN-----FNIALtkeaiaavgkdAIATNQiELSPY--L 160
Cdd:cd19079 116 GTDYIDLYQIHR--WDYETPIEETLEALHDVVKSGKVRYIGASSmyawqFAKAL-----------HLAEKN-GWTKFvsM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 161 QN----------RKLVEFLNAEGIHVTSYMTLAYGKVLGDPV------------------------------LGAIAKRH 200
Cdd:cd19079 182 QNhynllyreeeREMIPLCEEEGIGVIPWSPLARGRLARPWGdtterrrsttdtaklkydyfteadkeivdrVEEVAKER 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 881124778 201 DATPAQVALAWAMQLGYSVIP--SSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19079 262 GVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
4-253 |
2.75e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 105.29 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG---QVVIDSVRNALELGYRAIDTAQIYGN-EAEVGEAIaaSGVsRDALFLTTKI--WVDNyaPDKLV 77
Cdd:COG1453 13 VSVLGFGGMRLPRkdeEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKAL--KGP-RDKVILATKLppWVRD--PEDMR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 78 PSLEDSLRKLRTDYVDLTLIH-------WPAP--DNGVplatfMTALADAQAKGLTRRIGISNFN-IALTKEAIAAvgkD 147
Cdd:COG1453 88 KDLEESLKRLQTDYIDLYLIHglnteedLEKVlkPGGA-----LEALEKAKAEGKIRHIGFSTHGsLEVIKEAIDT---G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 148 AIATNQIELSPYLQN----RKLVEFLNAEGIHVTSyM-TLAYGKVLGDP-VLGAIAkRHDATPAQVALAWAMQLGY--SV 219
Cdd:COG1453 160 DFDFVQLQYNYLDQDnqagEEALEAAAEKGIGVII-MkPLKGGRLANPPeKLVELL-CPPLSPAEWALRFLLSHPEvtTV 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 881124778 220 IPSSTKRENLASNL--LAQTLRLTDDDMAQIAALER 253
Cdd:COG1453 238 LSGMSTPEQLDENLktADNLEPLTEEELAILERLAE 273
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-233 |
1.01e-25 |
|
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: 101.51 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 8 GLGTYRLkGQVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAasGVSRDALFLTTKIWV--DNYAPDKLVPSLED 82
Cdd:cd19105 17 GFGGGGL-PRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPrlDKKDKAELLKSVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIH---WPAPD--NGVPLAtfmtALADAQAKGLTRRIGISnfnialTKEAIAAVGKDAIATNQIEL- 156
Cdd:cd19105 94 SLKRLQTDYIDIYQLHgvdTPEERllNEELLE----ALEKLKKEGKVRFIGFS------THDNMAEVLQAAIESGWFDVi 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 157 ----SPYLQNRKLVEFLNA---EGIHVTSYMTLAYGKvlGDPVLGAIAKRHDATPAQVALAWAMQLGY--SVIPSSTKRE 227
Cdd:cd19105 164 mvayNFLNQPAELEEALAAaaeKGIGVVAMKTLAGGY--LQPALLSVLKAKGFSLPQAALKWVLSNPRvdTVVPGMRNFA 241
|
....*.
gi 881124778 228 NLASNL 233
Cdd:cd19105 242 ELEENL 247
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
4-250 |
2.22e-25 |
|
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: 101.97 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG---------QVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASgvsRDALFLTTK---IW- 67
Cdd:cd19149 11 ASVIGLGTWAIGGgpwwggsddNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglRWd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 68 ---------------VDNYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNF 132
Cdd:cd19149 88 reggsfffvrdgvtvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVE--TPIEETMEALEELKRQGKIRAIGASNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 133 NIALTKEAIAAVGKDAIatnQIELSpyLQNRK----LVEFLNAEGIHVTSYMTLAYG----KVLGDPVLGA--------- 195
Cdd:cd19149 166 SVEQIKEYVKAGQLDII---QEKYS--MLDRGiekeLLPYCKKNNIAFQAYSPLEQGlltgKITPDREFDAgdarsgipw 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881124778 196 ------------------IAKRHDATPAQVALAWAM-QLGY-SVIPSSTKRENLASNLLAQTLRLTDDDMAQIAA 250
Cdd:cd19149 241 fspenrekvlallekwkpLCEKYGCTLAQLVIAWTLaQPGItSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
34-248 |
2.08e-24 |
|
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: 99.22 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 34 IDTAQIYGN---EAEVGEAIAASgvsRDALFLTTKiWVDNYAPDK----------LVPSLEDSLRKLRTDYVDLTLIHWp 100
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN---RDRIVLATK-YTMNRRPGDpnaggnhrknLRRSVEASLRRLQTDYIDLLYVHA- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 101 aPDNGVPLATFMTALADAQAKGLTRRIGISNFN--IALTKEAIA-AVGKDAIATNQIELSpyLQNR----KLVEFLNAEG 173
Cdd:cd19080 123 -WDFTTPVEEVMRALDDLVRAGKVLYVGISDTPawVVARANTLAeLRGWSPFVALQIEYS--LLERtperELLPMARALG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 174 IHVTSYMTLAYGKVLGD------------------------------PVLGAIAKRHDATPAQVALAWAMQLGYSVIPS- 222
Cdd:cd19080 200 LGVTPWSPLGGGLLTGKyqrgeegrageakgvtvgfgklternwaivDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIi 279
|
250 260
....*....|....*....|....*..
gi 881124778 223 -STKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19080 280 gARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-233 |
2.47e-24 |
|
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: 97.55 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG---QVVIDSVRNALELGYRAIDTAQIYGN-EAEVGEAIAasGVsRDALFLTTKIWVDNYapDKLVPS 79
Cdd:cd19100 11 VSRLGFGGGPLGRlsqEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALK--GR-RDKVFLATKTGARDY--EGAKRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 80 LEDSLRKLRTDYVDLTLIHWPAPDNGVPLATF----MTALADAQAKGLTRRIGISNFNIALtkeAIAAVGKDAIATNQIE 155
Cdd:cd19100 86 LERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggaLEALLEAKEEGKIRFIGISGHSPEV---LLRALETGEFDVVLFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 156 LSP-YLQNR----KLVEFLNAEGIHVTSyMtlaygKVLGDpvlGAIAKRHDATPAQvALAWAMQLGY--SVIPSSTKREN 228
Cdd:cd19100 163 INPaGDHIDsfreELLPLAREKGVGVIA-M-----KVLAG---GRLLSGDPLDPEQ-ALRYALSLPPvdVVIVGMDSPEE 232
|
....*
gi 881124778 229 LASNL 233
Cdd:cd19100 233 LDENL 237
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-248 |
2.97e-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: 98.84 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 20 IDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAASgvsRDALFLTTKIWVDNYAPDKLVP-----------SLEDSLR 85
Cdd:cd19078 28 IELIRKAVELGITFFDTAEVYGpytNEELVGEALKPF---RDQVVIATKFGFKIDGGKPGPLgldsrpehirkAVEGSLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 86 KLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIatnQIELSpyLQNRK- 164
Cdd:cd19078 105 RLQTDYIDLYYQHRVDPN--VPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVCPVTAV---QSEYS--MMWREp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 165 ---LVEFLNAEGIHVTSYMTLAYGKVLG--DP-----------------------------VLGAIAKRHDATPAQVALA 210
Cdd:cd19078 178 ekeVLPTLEELGIGFVPFSPLGKGFLTGkiDEntkfdegddraslprftpealeanqalvdLLKEFAEEKGATPAQIALA 257
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 881124778 211 WAM-QLGYSV-IPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19078 258 WLLaKKPWIVpIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
23-248 |
7.67e-24 |
|
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: 98.07 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 23 VRNALELGYRAIDTAQIYGN-EAEV--GEAIAASgvsRDALFLTTKI--WVDNyAPD-------KLVPSLEDSLRKLRTD 90
Cdd:cd19091 45 VDIALDAGINFFDTADVYSEgESEEilGKALKGR---RDDVLIATKVrgRMGE-GPNdvglsrhHIIRAVEASLKRLGTD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 91 YVDLTLIHWpaPDNGVPLATFMTALADAQAKGLTRRIGISNFNI--ALTKEAIA-AVGKDAIATNQIELSpyLQNR---- 163
Cdd:cd19091 121 YIDLYQLHG--FDALTPLEETLRALDDLVRQGKVRYIGVSNFSAwqIMKALGISeRRGLARFVALQAYYS--LLGRdleh 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 164 KLVEFLNAEGIHVTSYMTLAYG-----------------------------KVLGDPV---LGAIAKRHDATPAQVALAW 211
Cdd:cd19091 197 ELMPLALDQGVGLLVWSPLAGGllsgkyrrgqpapegsrlrrtgfdfppvdRERGYDVvdaLREIAKETGATPAQVALAW 276
|
250 260 270
....*....|....*....|....*....|....*....
gi 881124778 212 AMQLGY--SVIPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19091 277 LLSRPTvsSVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
8-235 |
1.90e-23 |
|
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: 95.24 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 8 GLGTYRLKGQV--------VIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASgvsRDALFLTTKI---------W 67
Cdd:cd19086 7 GFGTWGLGGDWwgdvddaeAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR---RDKVVIATKFgnrfdggpeR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 68 VDNYAPDKLVPSLEDSLRKLRTDYVDLTLIH-WPAPDNGVPLAtfMTALADAQAKGLTRRIGISnfnIALTKEAIAAVGK 146
Cdd:cd19086 84 PQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDEL--FEALEKLKQEGKIRAYGVS---VGDPEEALAALRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 147 DAIATNQIELSPYLQN--RKLVEFLNAEGIHVTSYMTLAYGKVLGdpvlgaiakrhdaTPAQVALAWAmqLGY----SVI 220
Cdd:cd19086 159 GGIDVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPLASGLLTG-------------KLAQAALRFI--LSHpavsTVI 223
|
250
....*....|....*
gi 881124778 221 PSSTKRENLASNLLA 235
Cdd:cd19086 224 PGARSPEQVEENAAA 238
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
4-248 |
2.40e-23 |
|
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: 96.74 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLK---GQVVIDSVR-----NALELGYRAIDTAQIYG-NEAEVGEAIAASGVSRDALFLTTKI-------- 66
Cdd:cd19144 13 VPALGFGAMGLSafyGPPKPDEERfavldAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFgieknvet 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 ---WVDNyAPDKLVPSLEDSLRKLRTDYVDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAA 143
Cdd:cd19144 93 geySVDG-SPEYVKKACETSLKRLGVDYIDLYYQH--RVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 144 vgkDAIATNQIELSPYLQN--RKLVEFLNA---EGIHVTSYMTLAYGKVLGD---------------------------- 190
Cdd:cd19144 170 ---HPIAAVQIEYSPFSLDieRPEIGVLDTcreLGVAIVAYSPLGRGFLTGAirspddfeegdfrrmaprfqaenfpknl 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881124778 191 ---PVLGAIAKRHDATPAQVALAWAMQLGYSV--IPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19144 247 elvDKIKAIAKKKNVTAGQLTLAWLLAQGDDIipIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
27-235 |
3.52e-23 |
|
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: 95.70 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 27 LELGYRAIDTAQIYGN-------EAEVGEAIAASGVsRDALFLTTK--------IWVDNYAPDKLVPSLEDSLRKLRTDY 91
Cdd:cd19082 27 VELGGNFIDTARVYGDwvergasERVIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 92 VDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIA---AVGKDAIATNQIELS------PYLQN 162
Cdd:cd19082 106 IDLYFLH--RDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAyakAHGLPGFAASSPQWSlarpnePPWPG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 RKLV-------EFLNAEGIHVTSYMTLAYG-----------------KVLGDPV-------LGAIAKRHDATPAQVALAW 211
Cdd:cd19082 184 PTLVamdeemrAWHEENQLPVFAYSSQARGffskraaggaeddselrRVYYSEEnferlerAKELAEEKGVSPTQIALAY 263
|
250 260
....*....|....*....|....*.
gi 881124778 212 AMQLGYSVIP--SSTKRENLASNLLA 235
Cdd:cd19082 264 VLNQPFPTVPiiGPRTPEQLRDSLAA 289
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-250 |
5.55e-23 |
|
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: 95.35 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 12 YRLKGQVVIDSVRNALELGYRAIDTAQIYGN-EAEVGEAIA---ASGVSRDALFLTTKiWVDNYAPDKLVPS-----LED 82
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKrlrRERDAADDVQIHTK-WVPDPGELTMTRAyveaaIDR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 83 SLRKLRTDYVDLTLIHWPapDNGVPlaTFMTA---LADAQAKGLTRRIGISNFNIALTKEAIAAVGKdaIATNQIELS-- 157
Cdd:cd19101 97 SLKRLGVDRLDLVQFHWW--DYSDP--GYLDAakhLAELQEEGKIRHLGLTNFDTERLREILDAGVP--IVSNQVQYSll 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 158 ---PylqNRKLVEFLNAEGIHVTSYMTLAYG----KVLGDP---------------------------------VLGAIA 197
Cdd:cd19101 171 drrP---ENGMAALCEDHGIKLLAYGTLAGGllseKYLGVPeptgpaletrslqkyklmidewggwdlfqellrTLKAIA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 881124778 198 KRHDATPAQVALAWAMQ---LGySVIPSSTKRENLASNLLAQTLRLTDDDMAQIAA 250
Cdd:cd19101 248 DKHGVSIANVAVRWVLDqpgVA-GVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
8-135 |
8.37e-23 |
|
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: 94.68 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 8 GLGTYRLKG--------QVVIDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAASGVsRDALFLTTKI---WVD---- 69
Cdd:cd19148 8 ALGTWAIGGwmwggtdeKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYGK-RDRVVIATKVgleWDEggev 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881124778 70 --NYAPDKLVPSLEDSLRKLRTDYVDLTLIHWpaPDNGVPL---ATFMTALADAqakGLTRRIGISNFNIA 135
Cdd:cd19148 87 vrNSSPARIRKEVEDSLRRLQTDYIDLYQVHW--PDPLVPIeetAEALKELLDE---GKIRAIGVSNFSPE 152
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
8-243 |
1.91e-21 |
|
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: 91.11 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 8 GLGTYRLKGQVVIDS-----VRNALELGYRAIDTAQIYGN---EAEVGEAIAasGVSRDALFLTTKIwvdnYAP------ 73
Cdd:cd19074 8 SLGTWLTFGGQVDDEdakacVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKV----FWPtgpgpn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 74 DK------LVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEA---IAAV 144
Cdd:cd19074 82 DRglsrkhIFESIHASLKRLQLDYVDIYYCHRYDPE--TPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAhdlARQF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAIATNQIELSpYLQNRK---LVEFLNAEGIHVTSYMTLAYGkVL------GDPV----------------------- 192
Cdd:cd19074 160 GLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQG-LLtgkyrdGIPPpsrsratdednrdkkrrlltden 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 881124778 193 ------LGAIAKRHDATPAQVALAWAMQ--LGYSVIPSSTKRENLASNLLAQTLRLTDD 243
Cdd:cd19074 238 lekvkkLKPIADELGLTLAQLALAWCLRnpAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-246 |
2.37e-21 |
|
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: 90.78 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG-----QVVIDSVRNALELGYRAIDTAQIYGN-----EAEVGEAIAASGVS-RDALFLTTKIWVD--- 69
Cdd:cd19089 11 LPAISLGLWHNFGdytspEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPyRDELVISTKAGYGmwp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 70 ----NYAPDK-LVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAV 144
Cdd:cd19089 91 gpygDGGSRKyLLASLDQSLKRMGLDYVDIFYHHRYDPD--TPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAI--ATNQIELSpyLQNR----KLVEFLNAEGIHVTSYMTLAYG----KVLGDP----------------------- 191
Cdd:cd19089 169 RELGVplIIHQPRYS--LLDRwaedGLLEVLEEAGIGFIAFSPLAQGlltdKYLNGIppdsrraaeskflteealtpekl 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881124778 192 ----VLGAIAKRHDATPAQVALAWAMQLGY--SVIPSSTKRENLASNLLA-QTLRLTDDDMA 246
Cdd:cd19089 247 eqlrKLNKIAAKRGQSLAQLALSWVLRDPRvtSVLIGASSPSQLEDNVAAlKNLDFSEEELA 308
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
5-130 |
2.64e-21 |
|
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: 90.31 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGTYRL---KGQV----VIDSVRNALELGYRAIDTAQIYGN-EAEVGEAIAasGVSRDALFLTTKI-----WVDNY 71
Cdd:cd19090 1 SALGLGTAGLggvFGGVdddeAVATIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881124778 72 APDKLVPSLEDSLRKLRTDYVDLTLIH---WPAPDNGVPLATFMTALADAQAKGLTRRIGIS 130
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGGALEALLELKEEGLIKHIGLG 140
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
3-248 |
6.07e-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: 89.61 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKG-------QVVIDSVRNALELGYRAIDTAQIYG------NEAEVGEAIAASGVSRDALFLTTKIWVD 69
Cdd:cd19077 4 LVGPIGLGLMGLTWrpnptpdEEAFETMKAALDAGSNLWNGGEFYGppdphaNLKLLARFFRKYPEYADKVVLSVKGGLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 70 NYA------PDKLVPSLEDSLRKLR-TDYVDltlIHWPAP-DNGVPLATFMTALADAQAKGLTRRIGISNFNiALTKEAI 141
Cdd:cd19077 84 PDTlrpdgsPEAVRKSIENILRALGgTKKID---IFEPARvDPNVPIEETIKALKELVKEGKIRGIGLSEVS-AETIRRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 142 AAVGKdaIATNQIELSPY----LQNrKLVEFLNAEGIHVTSYMTLAYG------KVLGDP-------------------- 191
Cdd:cd19077 160 HAVHP--IAAVEVEYSLFsreiEEN-GVLETCAELGIPIIAYSPLGRGlltgriKSLADIpegdfrrhldrfngenfekn 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881124778 192 -----VLGAIAKRHDATPAQVALAWAMQLGYSV---IPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19077 237 lklvdALQELAEKKGCTPAQLALAWILAQSGPKiipIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
7-253 |
1.05e-20 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 88.87 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 7 FGLGTYRLKGQVV----------IDSVRNALELGYRAIDTAQIYG----NEAeVGEAIAASgvsRDALFLTTKI------ 66
Cdd:PRK10376 20 LGYGAMQLAGPGVfgppkdrdaaIAVLREAVALGVNHIDTSDFYGphvtNQL-IREALHPY---PDDLTIVTKVgarrge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 ---WVDNYAPDKLVPSLEDSLRKLRTDYVDLT------LIHWPAPDngvPLATFMTALADAQAKGLTRRIGISNFNIALT 137
Cdd:PRK10376 96 dgsWLPAFSPAELRRAVHDNLRNLGLDVLDVVnlrlmgDGHGPAEG---SIEEPLTVLAELQRQGLVRHIGLSNVTPTQV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 138 KEA--IAAVgkdAIATNQIELSpYLQNRKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAIAKRHDATPAQVALAWAMQL 215
Cdd:PRK10376 173 AEArkIAEI---VCVQNHYNLA-HRADDALIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQR 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 881124778 216 GYS--VIPSSTKRENLASNLLAQTLRLTDDDMAQIAALER 253
Cdd:PRK10376 249 SPNilLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
20-248 |
9.00e-20 |
|
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: 86.72 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 20 IDSVRNALELGYRAIDTAQIYG---NEAEVGEAIaaSGVSRDALFLTTKI---WVDNYA------PDKLVPSLEDSLRKL 87
Cdd:cd19145 36 IALIHHAFNSGVTFLDTSDIYGpntNEVLLGKAL--KDGPREKVQLATKFgihEIGGSGvevrgdPAYVRAACEASLKRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 88 RTDYVDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISnfnialtkEAIAAVGKDA-----IATNQIELSPYLQN 162
Cdd:cd19145 114 DVDYIDLYYQH--RIDTTVPIEITMGELKKLVEEGKIKYIGLS--------EASADTIRRAhavhpITAVQLEWSLWTRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 163 --RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVL-------------------------------GAIAKRHDATPAQVAL 209
Cdd:cd19145 184 ieEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLeellensdvrkshprfqgenleknkvlyervEALAKKKGCTPAQLAL 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 881124778 210 AWAMQLGYSV--IPSSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19145 264 AWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-251 |
6.20e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 84.31 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 26 ALELGYRAIDTAQIYG---NEAEVGEAIAAsgVSRDALFLTTK---IWVDNYApDKLVPSLEDSLRKLRTDYVDLTLIHW 99
Cdd:cd19103 41 AMAAGLNLWDTAAVYGmgaSEKILGEFLKR--YPREDYIISTKftpQIAGQSA-DPVADMLEGSLARLGTDYIDIYWIHN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 100 PApdnGVPLATfmTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIATNQIELSPYLQNRK-----LVEFLNAEGI 174
Cdd:cd19103 118 PA---DVERWT--PELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAVQNHYSLLYRSseeagILDYCKENGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 175 HVTSYMTL-----------------------AYGKVLGD-----PVLGAIAKRHDATPAQVALAWAMQLGYSVIPSSTKR 226
Cdd:cd19103 193 TFFAYMVLeqgalsgkydtkhplpegsgraeTYNPLLPQleeltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKP 272
|
250 260
....*....|....*....|....*
gi 881124778 227 ENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19103 273 HHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-235 |
1.48e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 83.15 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 27 LELGYRAIDTAQIY--------GNEAE--VGEAIAASGVsRDALFLTTKI---------WVDNY---APDKLVPSLEDSL 84
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvGGESErlIGRWLKDRGN-RDDVVIATKVgagprdpdgGPESPeglSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 85 RKLRTDYVDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNF---NIALTKEAIAAVGKDAIATNQIELSpYLQ 161
Cdd:cd19752 106 RRLGTDYIDLYYAH--VDDRDTPLEETLEAFNELVKAGKVRAIGASNFaawRLERARQIARQQGWAEFSAIQQRHS-YLR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 162 NR-------------KLVEFLNAEG-IHVTSYMTLAYG------KVLGDP-----------VLGAIAKRHDATPAQVALA 210
Cdd:cd19752 183 PRpgadfgvqrivtdELLDYASSRPdLTLLAYSPLLSGaytrpdRPLPEQydgpdsdarlaVLEEVAGELGATPNQVVLA 262
|
250 260
....*....|....*....|....*..
gi 881124778 211 WAMQLGYSVIP--SSTKRENLASNLLA 235
Cdd:cd19752 263 WLLHRTPAIIPllGASTVEQLEENLAA 289
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
26-251 |
6.49e-18 |
|
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: 81.46 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 26 ALELGYRAIDTAQIYGN---EAEVGEAIAASgvsRDALFLTTKIwVDNYAPD---------KLVPSLEDSLRKLRTDYVD 93
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKV-FGPMGDDpndrglsrrHIRRAVEASLRRLQTDYID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 94 LTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNF---NIALTKEAIAAVGKDAIATNQielSPY-LQNRKL-VEF 168
Cdd:cd19087 115 LYQMH--HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFaawQIAKAQGIAARRGLLRFVSEQ---PMYnLLKRQAeLEI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 169 L---NAEGIHVTSYMTLA-------YGKVLGDPV------------------------LGAIAKRHDATPAQVALAWAMQ 214
Cdd:cd19087 190 LpaaRAYGLGVIPYSPLAgglltgkYGKGKRPESgrlveraryqarygleeyrdiaerFEALAAEAGLTPASLALAWVLS 269
|
250 260 270
....*....|....*....|....*....|....*....
gi 881124778 215 --LGYSVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19087 270 hpAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
26-253 |
1.01e-17 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 81.44 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 26 ALELGYRAIDTAQIYG----------NEAEVGEAIAASGvSRDALFLTTKI----------WVDNYAPDK--LVPSLEDS 83
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVsgpsrnndkgIRPNQALDRknIREALHDS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPA-PDN--------------GVPLATFMTALADAQAKGLTRRIGISN---FNIALTKEAIAAVG 145
Cdd:PRK10625 118 LKRLQTDYLDLYQVHWPQrPTNcfgklgyswtdsapAVSLLETLDALAEQQRAGKIRYIGVSNetaFGVMRYLHLAEKHD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 146 KDAIATNQielSPY-LQNRK----LVEFLNAEGIHVTSYMTLAYGKVLGDPVLGA------------------------- 195
Cdd:PRK10625 198 LPRIVTIQ---NPYsLLNRSfevgLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAkpagarntlfsrftrysgeqtqkav 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881124778 196 -----IAKRHDATPAQVALAWAMQLGY--SVIPSSTKRENLASNLLAQTLRLTDDDMAQIAALER 253
Cdd:PRK10625 275 aayvdIAKRHGLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
5-212 |
8.41e-17 |
|
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: 77.60 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGTYRL--KGQVVIDS------VRNALELGYRAIDTAQIYGN---EAEVGEAIaaSGVSRDALFLTTKI--WVDNY 71
Cdd:cd19096 1 SVLGFGTMRLpeSDDDSIDEekaiemIRYAIDAGINYFDTAYGYGGgksEEILGEAL--KEGPREKFYLATKLppWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 72 APD--KLvpsLEDSLRKLRTDYVDLTLIHWP--------APDNGVplatfMTALADAQAKGLTRRIGISnF--NIALTKE 139
Cdd:cd19096 79 AEDfrRI---LEESLKRLGVDYIDFYLLHGLnspewlekARKGGL-----LEFLEKAKKEGLIRHIGFS-FhdSPELLKE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881124778 140 AIAAVGKDAIatnQIELS----PYLQNRKLVEFLNAEGIHVtSYMTLAYGKVLGD--PVLGAIAKRHDATPAQVALAWA 212
Cdd:cd19096 150 ILDSYDFDFV---QLQYNyldqENQAGRPGIEYAAKKGMGV-IIMEPLKGGGLANnpPEALAILCGAPLSPAEWALRFL 224
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
19-169 |
1.65e-15 |
|
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: 74.62 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 19 VIDSVRNALELGYRAIDTAQIYGN-EAEVGEAIAA--SGVSRDALFLTTK-----IWVDNYAPDKLVPSLEDSLRKLRTD 90
Cdd:cd19164 36 PVDIVRRALELGIRAFDTSPYYGPsEIILGRALKAlrDEFPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 91 YVDLTLIH--WPAPDNGVPLAtfMTALADAQAKGLTRRIGISNFNI-ALTKEAIAA---VGK--DAIatnqieLSpY--- 159
Cdd:cd19164 116 YLDLVYLHdvEFVADEEVLEA--LKELFKLKDEGKIRNVGISGYPLpVLLRLAELArttAGRplDAV------LS-Ychy 186
|
170
....*....|.
gi 881124778 160 -LQNRKLVEFL 169
Cdd:cd19164 187 tLQNTTLLAYI 197
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-233 |
2.83e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 74.28 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 6 AFGLGTYRL-----KGQVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEA----IAASGVSRDALFLTTKI------- 66
Cdd:cd19099 5 SLGLGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKAlrelIEKGGIKRDEVVIVTKAgyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 --------WVDNYA------------------PDKLVPSLEDSLRKLRTDYVDLTLIHWP----APDNGVPLATFM---- 112
Cdd:cd19099 85 deplrplkYLEEKLgrglidvadsaglrhcisPAYLEDQIERSLKRLGLDTIDLYLLHNPeeqlLELGEEEFYDRLeeaf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 113 TALADAQAKGLTRRIGIS-----------NFNIALTKEAIAAvgKDAIATN------QIELSPYLQ------------NR 163
Cdd:cd19099 165 EALEEAVAEGKIRYYGIStwdgfrappalPGHLSLEKLVAAA--EEVGGDNhhfkviQLPLNLLEPealtekntvkgeAL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881124778 164 KLVEFLNAEGIHVTSYMTLAYGKVLGDPVLGAI-AKRHDATPAQVALAWA-MQLGY-SVIPSSTKRENLASNL 233
Cdd:cd19099 243 SLLEAAKELGLGVIASRPLNQGQLLGELRLADLlALPGGATLAQRALQFArSTPGVdSALVGMRRPEHVDENL 315
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
3-132 |
5.26e-15 |
|
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: 73.36 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 3 PIPAFGLGTYRLKG-QVVIDSVRNAL----ELGYRAIDTAQIYGN---EAEVGEAIAA-SGVSRDalfltTKI---WVDN 70
Cdd:cd19075 1 PKIILGTMTFGSQGrFTTAEAAAELLdaflERGHTEIDTARVYPDgtsEELLGELGLGeRGFKID-----TKAnpgVGGG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881124778 71 YAPDKLVPSLEDSLRKLRTDYVDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNF 132
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLH--APDRSTPLEETLAAIDELYKEGKFKEFGLSNY 135
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
26-251 |
6.90e-15 |
|
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: 72.98 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 26 ALELGYRAIDTAQIY--------GNEAE--VGEAIAASGvSRDALFLTTKI--------WVDNYAP----DKLVPSLEDS 83
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetQGRTEeiIGSWLKKKG-NRDKVVLATKVagpgegitWPRGGGTrldrENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 84 LRKLRTDYVDLTLIHWPA----------------PDNGVPLATFMTALADAQAKGLTRRIGISN---FNIALTKEAIAAV 144
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDrytplfgggyytepseEEDSVSFEEQLEALGELVKAGKIRHIGLSNetpWGVMKFLELAEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAIATNQIELSpyLQNRK----LVEFLNAEGIHVTSYMTLAYG----KVLGDP------------------------- 191
Cdd:cd19094 186 GLPRIVSIQNPYS--LLNRNfeegLAEACHRENVGLLAYSPLAGGvltgKYLDGAarpeggrlnlfpgymaryrspqale 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881124778 192 ---VLGAIAKRHDATPAQVALAWAMQLGY--SVIPSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19094 264 avaEYVKLARKHGLSPAQLALAWVRSRPFvtSTIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-185 |
9.76e-15 |
|
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: 72.57 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 6 AFGLGTYRLKGQ--------VVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASGVSRDALFLTTKI-----WVD 69
Cdd:cd19153 14 PVGLGTAALGGVygdgleqdEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdSEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 70 NYAPDKLVPSLEDSLRKLRTDYVDLTLIH-------WPAPDNGVPlatfmtALADAQAKGLTRRIGISNFNIaltkEAIA 142
Cdd:cd19153 94 DYSAERVRASVATSLERLHTTYLDVVYLHdiefvdyDTLVDEALP------ALRTLKDEGVIKRIGIAGYPL----DTLT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 881124778 143 AVGKD-AIATNQIELSpY----LQNRKLVEFL----NAEGIHVTSYMTLAYG 185
Cdd:cd19153 164 RATRRcSPGSLDAVLS-YchltLQDARLESDApglvRGAGPHVINASPLSMG 214
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-215 |
2.21e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 71.02 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 15 KGQVVIDSVRN----ALELGYRAIDTAQIYGNeAEvgEAIAASGVSRDALFLTTKI----WVDNYAPDKLVPSLEDSLRK 86
Cdd:cd19097 20 SGKPSEKEAKKileyALKAGINTLDTAPAYGD-SE--KVLGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 87 LRTDYVDLTLIHWPApDNGVPLATFMTALADAQAKGLTRRIGISNFNIaltKEAIAAVGKDAIATNQIELSPY---LQNR 163
Cdd:cd19097 97 LKVDSLDGLLLHNPD-DLLKHGGKLVEALLELKKEGLIRKIGVSVYSP---EELEKALESFKIDIIQLPFNILdqrFLKS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881124778 164 KLVEFLNAEG--IHVTS-------YMTLAYGKVLGDPV------LGAIAKRHDATPAQVALAWAMQL 215
Cdd:cd19097 173 GLLAKLKKKGieIHARSvflqgllLMEPDKLPAKFAPAkpllkkLHELAKKLGLSPLELALGFVLSL 239
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
20-233 |
1.85e-13 |
|
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: 68.73 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 20 IDSVRNALELGYRAIDTAQIYGN---EAEVGEAIaaSGVSRDALFLTTKI------WVD--NYAPDKLVPSLEDSLRKLR 88
Cdd:cd19163 36 IRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL--KGIPRDSYYLATKVgrygldPDKmfDFSAERITKSVEESLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 89 TDYVDLTLIHWP--APDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAI--AAVGKDAIATnqielspY----L 160
Cdd:cd19163 114 LDYIDIIQVHDIefAPSLDQILNETLPALQKLKEEGKVRFIGITGYPLDVLKEVLerSPVKIDTVLS-------YchytL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 161 QNR---KLVEFLNAEGIHVTSYMTLAygkvlgdpvLGAIAKR-----HDATP--------------------AQVALAWA 212
Cdd:cd19163 187 NDTsllELLPFFKEKGVGVINASPLS---------MGLLTERgppdwHPASPeikeacakaaaycksrgvdiSKLALQFA 257
|
250 260
....*....|....*....|...
gi 881124778 213 MQL--GYSVIPSSTKRENLASNL 233
Cdd:cd19163 258 LSNpdIATTLVGTASPENLRKNL 280
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-251 |
4.44e-13 |
|
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: 67.68 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 23 VRNALELGYRAIDTAQIYGN-EAEV--GEAIaaSGVSrDALFLTTKIWVDNYAPD----KLVPSLEDSLRKLRTDYVDLT 95
Cdd:cd19104 38 VRRALDLGINFFDTAPSYGDgKSEEnlGRAL--KGLP-AGPYITTKVRLDPDDLGdiggQIERSVEKSLKRLKRDSVDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 96 LIH-WPAPDNGVPLATFMT------------ALADAQAKGLTRRIGISNF-NIALTKEAIAAVGKDAIAT--NQIELSPY 159
Cdd:cd19104 115 QLHnRIGDERDKPVGGTLSttdvlglggvadAFERLRSEGKIRFIGITGLgNPPAIRELLDSGKFDAVQVyyNLLNPSAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 160 LQN---------RKLVEFLNAEGIHVTSYMTLAYGKVLGDPVLG----------------------AIAKRHDATPAQVA 208
Cdd:cd19104 195 EARprgwsaqdyGGIIDAAAEHGVGVMGIRVLAAGALTTSLDRGreapptsdsdvaidfrraaafrALAREWGETLAQLA 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 881124778 209 L--AWAMQLGYSVIPSSTKRENLASNLLAQTL-RLTDDDMAQIAAL 251
Cdd:cd19104 275 HrfALSNPGVSTVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
34-248 |
6.68e-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: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 34 IDTAQIY-GNEAE--VGEAIAASGvSRDALFLTTK--IWVDNYAPDK------------LVPSLEDSLRKLRTDYVDLTL 96
Cdd:cd19146 52 IDTANNYqGEESErwVGEWMASRG-NRDEMVLATKytTGYRRGGPIKiksnyqgnhaksLRLSVEASLKKLQTSYIDILY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 97 IHWpaPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAV------------GKDAIATNQIElspylqnRK 164
Cdd:cd19146 131 VHW--WDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYArahgltqfvvyqGHWSAAFRDFE-------RD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 165 LVEFLNAEGIHVTSYMTLAYGKVLGDP------------------------VLGAIAKRHDATPAQVALAWAMQLGYSVI 220
Cdd:cd19146 202 ILPMCEAEGMALAPWGVLGQGQFRTEEefkrrgrsgrkggpqtekerkvseKLEKVAEEKGTAITSVALAYVMHKAPYVF 281
|
250 260 270
....*....|....*....|....*....|
gi 881124778 221 P--SSTKRENLASNLLAQTLRLTDDDMAQI 248
Cdd:cd19146 282 PivGGRKVEHLKGNIEALGISLSDEEIQEI 311
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
4-214 |
1.99e-12 |
|
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: 65.89 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVviDSVRNALELGYRAIDT-------AQIYGNEAEVGEA----IAASGVS--RDALFLTTK----I 66
Cdd:cd19151 12 LPAISLGLWHNFGDV--DRYENSRAMLRRAFDLgithfdlANNYGPPPGSAEEnfgrILKEDLKpyRDELIISTKagytM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 WVDNY----APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDNgvPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIA 142
Cdd:cd19151 90 WPGPYgdwgSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPET--PLEETMGALDQIVRQGKALYVGISNYPPEEAREAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 143 AVgKDAIATNQIELSPY-LQNR----KLVEFLNAEGIHVTSYMTLAYGKVL-----GDPV-------------------- 192
Cdd:cd19151 168 IL-KDLGTPCLIHQPKYsMFNRwveeGLLDVLEEEGIGCIAFSPLAQGLLTdrylnGIPEdsraakgssflkpeqiteek 246
|
250 260
....*....|....*....|....*...
gi 881124778 193 ------LGAIAKRHDATPAQVALAWAMQ 214
Cdd:cd19151 247 lakvrrLNEIAQARGQKLAQMALAWVLR 274
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
15-248 |
2.95e-12 |
|
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: 65.31 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 15 KGQVVIDSVRNALELGYRA----IDTAQIYGN-EAEV--GEAIAASGVSRDALFLTTKI---WVDNYAPDK------LVP 78
Cdd:cd19143 25 GNQVDVDEAKECMKAAYDAgvnfFDNAEVYANgQSEEimGQAIKELGWPRSDYVVSTKIfwgGGGPPPNDRglsrkhIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 79 SLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIA-AVGKDAIA--TNQIE 155
Cdd:cd19143 105 GTKASLKRLQLDYVDLVFCHRPDPA--TPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEiADRLGLIPpvMEQPQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 156 LSPYLQNRKLVEFL---NAEGIHVTSYMTLAYG---------------------KVLGDPV-------------LGAIAK 198
Cdd:cd19143 183 YNLFHRERVEVEYAplyEKYGLGTTTWSPLASGlltgkynngipegsrlalpgyEWLKDRKeelgqekiekvrkLKPIAE 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 881124778 199 RHDATPAQVALAWAMQLGY--SVIPSSTKRENLASNLLA-QTL-RLTDDDMAQI 248
Cdd:cd19143 263 ELGCSLAQLAIAWCLKNPNvsTVITGATKVEQLEENLKAlEVLpKLTPEVMEKI 316
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
4-248 |
1.92e-11 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 63.47 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQV-VIDS----VRNALELGYRAIDTAQIYG-----NEAEVGEAIAAS-GVSRDALFLTTK----IWV 68
Cdd:PRK09912 25 LPALSLGLWHNFGHVnALESqraiLRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDfAAYRDELIISTKagydMWP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 69 DNYAPDK----LVPSLEDSLRKLRTDYVDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAV 144
Cdd:PRK09912 105 GPYGSGGsrkyLLASLDQSLKRMGLEYVDIFYSH--RVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAIATNQIELSPYLQNR-----KLVEFLNAEGIHVTSYMTLAYGKVLGD----------------------------- 190
Cdd:PRK09912 183 REWKIPLLIHQPSYNLLNRwvdksGLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdsrmhregnkvrgltpkmltea 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881124778 191 -----PVLGAIAKRHDATPAQVALAWAMQLG--YSVIPSSTKRENLASNLLA-QTLRLTDDDMAQI 248
Cdd:PRK09912 263 nlnslRLLNEMAQQRGQSMAQMALSWLLKDErvTSVLIGASRAEQLEENVQAlNNLTFSTEELAQI 328
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
4-246 |
8.79e-11 |
|
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: 60.93 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKG-----QVVIDSVRNALELGYRAIDTAQIYG-----NEAEVGEAIAASGVS-RDALFLTTK----IWV 68
Cdd:cd19150 12 LPALSLGLWHNFGddtplETQRAILRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGyRDELIISTKagydMWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 69 DNY----APDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDNgvPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAV 144
Cdd:cd19150 92 GPYgewgSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDT--PLEETMGALDHAVRSGKALYVGISSYSPERTREAAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 145 GKDAIATNQIELSPYLQNR-----KLVEFLNAEGIHVTSYMTLAYG----KVL-GDP----------------------- 191
Cdd:cd19150 170 RELGTPLLIHQPSYNMLNRwveesGLLDTLQELGVGCIAFTPLAQGlltdKYLnGIPegsraskerslspkmlteanlns 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 192 --VLGAIAKRHDATPAQVALAWAMQLG--YSVIPSSTKRENLASNLLA-QTLRLTDDDMA 246
Cdd:cd19150 250 irALNEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEENVGAlDNLTFSADELA 309
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
28-252 |
2.98e-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: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 28 ELGYRAIDTAQIYGNEAE---VGEAIAASGvSRDALFLTTKIWVD------------NYAPD---KLVPSLEDSLRKLRT 89
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRK-NRDQIVIATKFTTDykayevgkgkavNYCGNhkrSLHVSVRDSLRKLQT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 90 DYVDLTLIHWpaPDNGVPLATFMTALADAQAKGLTRRIGISN---FNIALTKEAIAAVGKDAIATNQ------------- 153
Cdd:cd19147 124 DWIDILYVHW--WDYTTSIEEVMDSLHILVQQGKVLYLGVSDtpaWVVSAANYYATAHGKTPFSVYQgrwnvlnrdferd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 154 ---------IELSPY-------LQNRKLVEFLNAEGIHVTSYMT---LAYGKVLGDPVLGAIAKRH-DATPAQVALAWAM 213
Cdd:cd19147 202 iipmarhfgMALAPWdvlgggkFQSKKAVEERKKNGEGLRSFVGgteQTPEEVKISEALEKVAEEHgTESVTAIALAYVR 281
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 881124778 214 QLGYSVIPS--STKRENLASNLLAQTLRLTDDdmaQIAALE 252
Cdd:cd19147 282 SKAPNVFPLvgGRKIEHLKDNIEALSIKLTPE---EIEYLE 319
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
5-149 |
4.68e-09 |
|
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: 55.83 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGT------YRLKGQVVIDSVRNALELGYRAIDTAQIYG---NEAEVGEAIAasGVSRDALFLTTKI--------- 66
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 -------WVDNYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKE 139
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170
....*....|
gi 881124778 140 AIAAVGKDAI 149
Cdd:cd19162 159 AARRADVDVV 168
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
5-98 |
3.66e-08 |
|
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: 53.48 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGTYRLKG-------QVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAAsgVSRDALFLTTKI-------- 66
Cdd:cd19161 1 SELGLGTAGLGNlytavsnADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 881124778 67 ---------WVD--------NYAPDKLVPSLEDSLRKLRTDYVDLTLIH 98
Cdd:cd19161 79 egsvpdpngFVDplpfeivyDYSYDGIMRSFEDSLQRLGLNRIDILYVH 127
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
20-185 |
8.78e-08 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 52.09 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 20 IDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASGVSRDALFLTTKI--WVD--NYAPDKLVPSLEDSLRKLRTDYV 92
Cdd:PLN02587 34 IASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCgrYGEgfDFSAERVTKSVDESLARLQLDYV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 93 DLTLIH---WPAPDNGVplATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDAIA------------TNQIELS 157
Cdd:PLN02587 114 DILHCHdieFGSLDQIV--NETIPALQKLKESGKVRFIGITGLPLAIFTYVLDRVPPGTVDvilsychyslndSSLEDLL 191
|
170 180
....*....|....*....|....*...
gi 881124778 158 PYLQNRklveflnaeGIHVTSYMTLAYG 185
Cdd:PLN02587 192 PYLKSK---------GVGVISASPLAMG 210
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
5-243 |
4.97e-07 |
|
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: 49.92 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 5 PAFGLGT------YR-LKGQVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAasGVSRDALFLTTKI-------- 66
Cdd:cd19152 1 PKLGFGTaplgnlYEaVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR--ELGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 67 ----------WVD-------NYAPDKLVPSLEDSLRKLRTDYVDLTLIHWPAPDNG-----VPLATFMT----ALADAQA 120
Cdd:cd19152 79 eveptfepgfWNPlpfdavfDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAgaesdEHFAQAIKgafrALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 121 KGLTRRIGI-SNFNIALTKeAIAAVGKD----AIATNQIELSPYlqnRKLVEFLNAEGIHV--------------TSYMT 181
Cdd:cd19152 159 EGVIKAIGLgVNDWEVILR-ILEEADLDwvmlAGRYTLLDHSAA---RELLPECEKRGVKVvnagpfnsgflaggDNFDY 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 182 LAYGKVlGDPVL------GAIAKRHDATPAQVALAWAMQ--LGYSVIPSSTKRENLASNLLAQTLRLTDD 243
Cdd:cd19152 235 YEYGPA-PPELIarrdriEALCEQHGVSLAAAALQFALAppAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
4-235 |
6.57e-07 |
|
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: 49.70 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRNAL-----ELGYRAIDTAQIYG-NEAEV--GEAIAASGVSRDALFLTTKIWVDNYAPDK 75
Cdd:cd19158 13 VSCLGLGTWVTFGGQITDEMAEHLmtlayDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWGGKAETE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 76 -------LVPSLEDSLRKLRTDYVDLTLIHWPAPDngVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDA 148
Cdd:cd19158 93 rglsrkhIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 149 IATNQIELSPY--LQNRK----LVEFLNAEGIHVTSYMTLAYGKVLG---------------------DPVLG------- 194
Cdd:cd19158 171 LIPPICEQAEYhmFQREKvevqLPELFHKIGVGAMTWSPLACGIVSGkydsgippysraslkgyqwlkDKILSeegrrqq 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 881124778 195 -------AIAKRHDATPAQVALAWAMQLG--YSVIPSSTKRENLASNLLA 235
Cdd:cd19158 251 aklkelqAIAERLGCTLPQLAIAWCLRNEgvSSVLLGASNAEQLMENIGA 300
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
4-98 |
7.08e-07 |
|
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: 49.38 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTY-----RLKGQVVIDSVRNALELGYRAIDTAQIYGN---EAEVGEAIAASGVSRDALFLTTKIWVDNYAPDK 75
Cdd:cd19142 13 VSNVGLGTWstfstAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYGSEER 92
|
90 100
....*....|....*....|....*....
gi 881124778 76 ------LVPSLEDSLRKLRTDYVDLTLIH 98
Cdd:cd19142 93 glsrkhIIESVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-251 |
2.09e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 45.03 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 19 VIDSVRNAlelGYRAIDTAQIYGN-EAEVGEAIAASGVSRDALFLTTK---IWVDNYAPDKLVPSLED-SLRKLRT---- 89
Cdd:cd19098 40 VLDAAWAA---GVRYFDAARSYGRaEEFLGSWLRSRNIAPDAVFVGSKwgyTYTADWQVDAAVHEVKDhSLARLLKqwee 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 90 ------DYVDLTLIHWPAPDNGV-PLATFMTALADAQAKGltRRIGISNFNI--------ALTKEAIAAVGKDAI-AT-N 152
Cdd:cd19098 117 trsllgKHLDLYQIHSATLESGVlEDADVLAALAELKAEG--VKIGLSLSGPqqaetlrrALEIEIDGARLFDSVqATwN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 153 QIELSPylqnRKLVEFLNAEGIHVTSYMTLAYGKVLGDP----------VLGAIAKRHDATPAQVALAWAMQLGYS--VI 220
Cdd:cd19098 195 LLEQSA----GEALEEAHEAGMGVIVKEALANGRLTDRNpspelaplmaVLKAVADRLGVTPDALALAAVLAQPFVdvVL 270
|
250 260 270
....*....|....*....|....*....|.
gi 881124778 221 PSSTKRENLASNLLAQTLRLTDDDMAQIAAL 251
Cdd:cd19098 271 SGAATPEQLRSNLRALDVSLDLELLAALADL 301
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
4-235 |
3.42e-05 |
|
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: 44.36 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 4 IPAFGLGTYRLKGQVVIDSVRN-----ALELGYRAIDTAQIY-GNEAEV--GEAIAASGVSRDALFLTTKIWVDNYAPDK 75
Cdd:cd19141 12 VSCLGLGTWVTFGSQISDEVAEelvtlAYENGINLFDTAEVYaAGKAEIvlGKILKKKGWRRSSYVITTKIFWGGKAETE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 76 -------LVPSLEDSLRKLRTDYVDLTLIHwpAPDNGVPLATFMTALADAQAKGLTRRIGISNFNIALTKEAIAAVGKDA 148
Cdd:cd19141 92 rglsrkhIIEGLKASLERLQLEYVDIVFAN--RPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881124778 149 IATNQIELSPY-LQNRKLVEFLNAE-----GIHVTSYMTLAYGKVLG---DPV--------------------------- 192
Cdd:cd19141 170 LIPPIVEQAEYhLFQREKVEMQLPElfhkiGVGAMTWSPLACGILSGkydDGVpeysraslkgyqwlkekilseegrrqq 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 881124778 193 -----LGAIAKRHDATPAQVALAWAMQLG--YSVIPSSTKRENLASNLLA 235
Cdd:cd19141 250 aklkeLQIIADRLGCTLPQLAIAWCLKNEgvSSVLLGASSTEQLYENLQA 299
|
|
| |
