|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-316 |
0e+00 |
|
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: 650.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVIS 80
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWGGPG--PNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQ 158
Cdd:cd19143 81 TKIFWGGGGppPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 159 ITEAWGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGaIPSDSRFALENYKNL 238
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNG-IPEGSRLALPGYEWL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 239 ANRS--LVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTPIVLDKIEQV 316
Cdd:cd19143 240 KDRKeeLGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-309 |
5.28e-171 |
|
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: 476.31 E-value: 5.28e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRelGWRRSDIVISTKIFWG-GP 88
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPtGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 89 GPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADR 168
Cdd:cd19074 79 GPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 169 LDLVGPIVEQPEYNMFARHKvETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAI-PSDSRFALENYKNLANRSLVDDV 247
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREI-EEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPpPSRSRATDEDNRDKKRRLLTDEN 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219795 248 LRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDviPLLTPIV 309
Cdd:cd19074 238 LEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASG--VKLSPEV 297
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-307 |
1.03e-137 |
|
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: 392.58 E-value: 1.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 3 YKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVISTK 82
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEA 162
Cdd:cd19141 82 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 163 WGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGaIPSDSRFALENYKNLANRS 242
Cdd:cd19141 162 YSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDG-VPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 243 LVDDVLR---KVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTP 307
Cdd:cd19141 241 LSEEGRRqqaKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTP 308
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-321 |
1.31e-129 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 372.78 E-value: 1.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVIS 80
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQIT 160
Cdd:cd19160 83 TKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 161 EAWGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNkGAIPSDSRFALENYKNLAN 240
Cdd:cd19160 163 EAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYD-GRVPDTCRAAVKGYQWLKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 241 RSLVDDVLR---KVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTPIVLDKIEQVI 317
Cdd:cd19160 242 KVQSEEGKKqqaKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALL 321
|
....
gi 15219795 318 QSKP 321
Cdd:cd19160 322 GNKP 325
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-321 |
9.48e-128 |
|
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: 367.58 E-value: 9.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWvTFGN---QLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRelGWRRSDI 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 78 VISTKIFW-GGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSA 156
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 157 QQITEAWGAADrlDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGA-IPSDSRFALeny 235
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDR-SAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGAtFPEGDRAAT--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 236 kNLANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIplLTPIVLDKIEQ 315
Cdd:COG0667 232 -NFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLE--LSAEDLAALDA 308
|
....*.
gi 15219795 316 VIQSKP 321
Cdd:COG0667 309 ALAAVP 314
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-321 |
1.02e-127 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 367.83 E-value: 1.02e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVIS 80
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQIT 160
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 161 EAWGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGaIPSDSRFALENYKNLAN 240
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSRASLKCYQWLKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 241 RSLVDDVLRKVSGLK---PIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTPIVLDKIEQVI 317
Cdd:cd19159 240 RIVSEEGRKQQNKLKdlsPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 319
|
....
gi 15219795 318 QSKP 321
Cdd:cd19159 320 RNKP 323
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
3-317 |
2.87e-124 |
|
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.
Pssm-ID: 213602 [Multi-domain] Cd Length: 317 Bit Score: 358.86 E-value: 2.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 3 YKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVISTK 82
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEA 162
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 163 WGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNkGAIPSDSRFALENYKNLANRS 242
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYD-SGIPPYSRATLKGYQWLKDKI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 243 LVDDVLR---KVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTPIVLDKIEQVI 317
Cdd:TIGR01293 240 LSEEGRRqqaRLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-321 |
2.79e-119 |
|
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: 346.69 E-value: 2.79e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVIS 80
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQIT 160
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 161 EAWGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGaIPSDSRFALENYKNLAN 240
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG-IPPYSRASLKGYQWLKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 241 RSLVDDVLR---KVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTPIVLDKIEQVI 317
Cdd:cd19158 240 KILSEEGRRqqaKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSIL 319
|
....
gi 15219795 318 QSKP 321
Cdd:cd19158 320 GNKP 323
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-314 |
2.64e-114 |
|
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: 333.39 E-value: 2.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAwVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVIS 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWG-GPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQI 159
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 160 TEAWGAADRLDLVGPIVEQPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFALENYKNLa 239
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERARYQA- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219795 240 nRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIplLTPIVLDKIE 314
Cdd:cd19087 235 -RYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT--LTPELLAEID 306
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-321 |
2.37e-111 |
|
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: 326.34 E-value: 2.37e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVIS 80
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWGGpGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQIT 160
Cdd:cd19142 81 TKIYWSY-GSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 161 EAWGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTG-KYNKGAIPSDSRFALENYKNLA 239
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGiSEETRRLVTKLSFKSSKYKVGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 240 NRSLVDDVLR----KVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLTPIVLDKIEQ 315
Cdd:cd19142 240 DGNGIHEETRrashKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELER 319
|
....*.
gi 15219795 316 VIQSKP 321
Cdd:cd19142 320 ILDNKP 325
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-316 |
4.18e-102 |
|
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: 302.61 E-value: 4.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAwVTFG---------NQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElg 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 72 wRRSDIVISTKI-FWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWG 150
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 151 TSEWSAQQITEAWGAADRLDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGA-IPSDSR 229
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGR-DLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQpAPEGSR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 230 FALENYKNLA-NRSLVDDVlrkVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIplLTPI 308
Cdd:cd19091 236 LRRTGFDFPPvDRERGYDV---VDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLS--LTPE 310
|
....*...
gi 15219795 309 VLDKIEQV 316
Cdd:cd19091 311 EIARLDKV 318
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-301 |
5.50e-101 |
|
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: 299.50 E-value: 5.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 2 QYKNLGKSGLKVSTLSFGAWvTFGNQ------LDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwRRS 75
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 76 DIVISTKIFWG-GPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEW 154
Cdd:cd19079 79 EVVIATKVYFPmGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAWGAADRLDLVGPIVEQPEYNMFARHKvETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFALEN 234
Cdd:cd19079 159 YAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219795 235 YKNLANRSLVDDVLRKVsglKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19079 238 LKYDYFTEADKEIVDRV---EEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-301 |
4.52e-90 |
|
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: 271.40 E-value: 4.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 6 LGKSGLKVSTLSFGAWVtFGNQLDVKEAKSILQCCRDHGVNFFDNAEVY-------ANGRAEEIMGQAIRELGwRRSDIV 78
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 79 ISTKIFWGgPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQ 158
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 159 ITEAWGAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFALENYKNL 238
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEAAKRY 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219795 239 ANrslvDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19081 239 LN----ERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL 297
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-314 |
1.85e-88 |
|
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: 267.08 E-value: 1.85e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWV---TFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVISTK--IF 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwg 164
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 165 aadrLDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAI--PSDSRFALENYKnlanRS 242
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLER-EIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTfpPDDRRSRFPFFR----GE 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219795 243 LVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIplLTPIVLDKIE 314
Cdd:cd19084 227 NFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWE--LTEEELKEID 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-304 |
2.17e-85 |
|
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: 259.50 E-value: 2.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 3 YKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVY--ANGRAEEIMGQAI-RELGWRRSDIVI 79
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILkRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 80 STKIFWG-GPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQ 158
Cdd:cd19089 81 STKAGYGmWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 159 ITEawgAADRLDLVG--PIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFAleNYK 236
Cdd:cd19089 161 ARR---AIALLRELGvpLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAA--ESK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 237 NLANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPL 304
Cdd:cd19089 235 FLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDF 302
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-297 |
1.89e-77 |
|
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: 236.65 E-value: 1.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 14 STLSFGAWvTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwRRSDIVISTKI-FWGGPGPND 92
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 93 KGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDLV 172
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 173 GPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyknlanrslvddvlrkvs 252
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15219795 253 glkpiadelgvtLAQLAIAWCASNPNVSSVITGATRESQIQENMK 297
Cdd:cd06660 200 ------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-317 |
3.50e-76 |
|
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: 235.28 E-value: 3.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGAWvTFGNQLDV---KEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVISTKIfWGGPGPND 92
Cdd:pfam00248 1 IGLGTW-QLGGGWGPiskEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 93 KGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrldlV 172
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 173 GPIVEQPEYNMFaRHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIP-SDSRFALENYKNLANRSLVDDvlrkv 251
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKgPGERRRLLKKGTPLNLEALEA----- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 252 sgLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDviPLLTPIVLDKIEQVI 317
Cdd:pfam00248 229 --LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-316 |
2.56e-75 |
|
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: 233.25 E-value: 2.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 13 VSTLSFGAWV-----TFGNQlDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVISTKIFWGG 87
Cdd:cd19085 1 VSRLGLGCWQfgggyWWGDQ-DDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVSPDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 88 PGPNDkglsrkhIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwGAAD 167
Cdd:cd19085 77 LTPED-------VRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEA-LDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 168 RLDLVgpiveQPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGA--IPSDSR------FALENYKNla 239
Cdd:cd19085 149 RIDSN-----QLPYNLLWRA-IEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfPPGDARtrlfrhFEPGAEEE-- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219795 240 nrslvddVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIplLTPIVLDKIEQV 316
Cdd:cd19085 221 -------TFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLE--LSPSVLERLDEI 288
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-300 |
1.81e-74 |
|
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: 231.52 E-value: 1.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 2 QYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYA--NGRAEEIMGQAIRE-LGWRRSDIV 78
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 79 ISTK---IFWGGPgPNDKGlSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWS 155
Cdd:cd19151 81 ISTKagyTMWPGP-YGDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 156 AQQITEAwgAADRLDLVGP-IVEQPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGaIPSDSRFALEN 234
Cdd:cd19151 159 PEEAREA--AAILKDLGTPcLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNG-IPEDSRAAKGS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 235 yKNLANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD 300
Cdd:cd19151 235 -SFLKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-307 |
2.04e-73 |
|
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: 229.03 E-value: 2.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 6 LGKSGLKVSTLSFGAwVTFGNQ----LDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVIST 81
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 82 KIFWG--GPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQI 159
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 160 TEAWGAADRLDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSR----FALENY 235
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLER-TPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEakgvTVGFGK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219795 236 KNLANRSLVDDVLRkvsglkpIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIplLTP 307
Cdd:cd19080 238 LTERNWAIVDVVAA-------VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLT--LSP 300
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-300 |
3.63e-69 |
|
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: 218.09 E-value: 3.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 2 QYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYA--NGRAEEIMGQAIRE-LGWRRSDIV 78
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdFAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 79 ISTKI---FWggPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWS 155
Cdd:cd19150 81 ISTKAgydMW--PGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 156 AQQITEAwgAADRLDLVGP-IVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYnKGAIPSDSRFALEn 234
Cdd:cd19150 159 PERTREA--AAILRELGTPlLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKY-LNGIPEGSRASKE- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 235 yKNLANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD 300
Cdd:cd19150 235 -RSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALD 299
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-301 |
3.28e-67 |
|
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: 213.29 E-value: 3.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 3 YKNLGKSGLKVSTLSFGAWV----TFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIV 78
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 79 ISTK--IFWGGPGPND----------KGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWA 146
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 147 FYWGTSEWSAQQITEAwGAADRLDLVgpiveQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKG--AI 224
Cdd:cd19149 158 RAIGASNVSVEQIKEY-VKAGQLDII-----QEKYSMLDR-GIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDreFD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219795 225 PSDSRFALENYKnLANRSLVDDVLRKvsgLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19149 231 AGDARSGIPWFS-PENREKVLALLEK---WKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-316 |
5.34e-66 |
|
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: 210.50 E-value: 5.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 13 VSTLSFGAwVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYA-------NGRAEEIMGQAIRELGwRRSDIVISTKI-- 83
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 ---FWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPD------------------ASTPIEETVRAMNYVID 142
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 143 KGWAFYWGTSEWSAQQITEAWGAADRLDLVGPIVEQPEYNMFARHKVEtEFLPLYTNHGIGLTTWSPLASGVLTGKYNKG 222
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEE-GLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 223 AI-PSDSRFALenYKNLANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19094 238 AArPEGGRLNL--FPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDV 315
|
330
....*....|....*
gi 15219795 302 IplLTPIVLDKIEQV 316
Cdd:cd19094 316 P--LSDELLAEIDAV 328
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
6-301 |
8.44e-65 |
|
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: 206.89 E-value: 8.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 6 LGKSGLKVSTLSFGAWVTFGNQL--DVKEA--KSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgWRRSDIVIST 81
Cdd:cd19083 4 LGKSDIDVNPIGLGTNAVGGHNLypNLDEEegKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKE--YNRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 82 KifwGGP--GPNDKGL--SRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQ 157
Cdd:cd19083 82 K---GAHkfGGDGSVLnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 158 QITEAwGAADRLDLVgpiveQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFalENYKN 237
Cdd:cd19083 159 QLKEA-NKDGYVDVL-----QGEYNLLQR-EAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDL--RNDKP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219795 238 LANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19083 230 LFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV 293
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-317 |
9.91e-65 |
|
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: 206.37 E-value: 9.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 13 VSTLSFGAWVT--------FGNQlDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVISTK-- 82
Cdd:cd19102 1 LTTIGLGTWAIggggwgggWGPQ-DDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKG---LRDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQItea 162
Cdd:cd19102 77 LLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 163 wgaaDRLDLVGPI-VEQPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFALENYKNLANR 241
Cdd:cd19102 154 ----KRCQAIHPIaSLQPPYSLLRRG-IEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVASLPADDWRRRSPFFQE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 242 SLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVipLLTPIVLDKIEQVI 317
Cdd:cd19102 229 PNLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-300 |
6.37e-63 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 203.30 E-value: 6.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYA--NGRAEEIMGQAIRE-LGWRRSDI 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdFAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 78 VISTKI---FWggPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEW 154
Cdd:PRK09912 93 IISTKAgydMW--PGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEawgAADRLD--LVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGaIPSDSRFAL 232
Cdd:PRK09912 171 SPERTQK---MVELLRewKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG-IPQDSRMHR 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 233 ENYK--NLANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD 300
Cdd:PRK09912 247 EGNKvrGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALN 316
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-313 |
1.79e-61 |
|
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: 198.21 E-value: 1.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 2 QYKNLGKSGLKVSTLSFGAW--VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVI 79
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 80 STKifWG---GPGPNDKGL--SRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEW 154
Cdd:cd19076 78 ATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAwgAAdrldlVGPIVE-QPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKgaiPSDS----- 228
Cdd:cd19076 156 SADTIRRA--HA-----VHPITAvQSEYSLWTR-DIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKS---PEDLpeddf 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 229 -----RFALENYKnlANRSLVDDVlrkvsglKPIADELGVTLAQLAIAWC-ASNPNVSSvITGATRESQIQENMKAVDVI 302
Cdd:cd19076 225 rrnnpRFQGENFD--KNLKLVEKL-------EAIAAEKGCTPAQLALAWVlAQGDDIVP-IPGTKRIKYLEENVGALDVV 294
|
330
....*....|.
gi 15219795 303 plLTPIVLDKI 313
Cdd:cd19076 295 --LTPEELAEI 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-314 |
2.90e-61 |
|
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: 197.46 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAW---VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAireLGWRRSDIVISTKIFW- 85
Cdd:cd19078 1 GLEVSAIGLGCMgmsHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEA---LKPFRDQVVIATKFGFk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 -GGPGPNDKGL--SRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEA 162
Cdd:cd19078 78 iDGGKPGPLGLdsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 163 WGaadrldlVGPIVE-QPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAI--PSD-----SRFALEN 234
Cdd:cd19078 158 HA-------VCPVTAvQSEYSMMWRE-PEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfdEGDdraslPRFTPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 235 YKnlANRSLVdDVLRKvsglkpIADELGVTLAQLAIAWC-ASNPNVSSvITGATRESQIQENMKAVDVIplLTPIVLDKI 313
Cdd:cd19078 230 LE--ANQALV-DLLKE------FAEEKGATPAQIALAWLlAKKPWIVP-IPGTTKLSRLEENIGAADIE--LTPEELREI 297
|
.
gi 15219795 314 E 314
Cdd:cd19078 298 E 298
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-316 |
9.56e-61 |
|
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: 196.24 E-value: 9.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGA--WVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGqairELGWRRSDIVISTKIfwggPGPNDK 93
Cdd:cd19075 3 IILGTmtFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLG----ELGLGERGFKIDTKA----NPGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 94 GLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDLVG 173
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 174 PIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKY-NKGAIPSDSRFALEN-----YKNLANRSLVDDV 247
Cdd:cd19075 155 PTVYQGMYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkYSEDKAGGGRFDPNNalgklYRDRYWKPSYFEA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219795 248 LRKVsglKPIADELGVTLAQLAIAWCASNPNVSS-----VITGATRESQIQENMKAVDVIPLLTPIVlDKIEQV 316
Cdd:cd19075 234 LEKV---EEAAEKEGISLAEAALRWLYHHSALDGekgdgVILGASSLEQLEENLAALEKGPLPEEVV-KAIDEA 303
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-301 |
1.87e-56 |
|
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: 184.74 E-value: 1.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 12 KVSTLSFGAWvTFGNQL-------DVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwRRSDIVISTKiF 84
Cdd:cd19093 1 EVSPLGLGTW-QWGDRLwwgygeyGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATK-F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WGGPGPndkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDA-STPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAW 163
Cdd:cd19093 78 APLPWR----LTRRSVVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 164 GAADRLDlVGPIVEQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFALENYKNLANRSL 243
Cdd:cd19093 154 KALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 244 VDDVLRKvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVDV 301
Cdd:cd19093 233 LLDALEE------IAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW 282
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-298 |
1.29e-55 |
|
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: 180.75 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 11 LKVSTLSFGAWvTFGNQ----LDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVISTKI--F 84
Cdd:cd19086 1 LEVSEIGFGTW-GLGGDwwgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRP-DASTPIEETVRAMNYVIDKGWAFYWGtseWSAQQITEAW 163
Cdd:cd19086 77 FDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYG---VSVGDPEEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 164 GAADRLDLVgpiVEQPEYNMFaRHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKynkgaipsdsrfalenyknlanrsl 243
Cdd:cd19086 154 AALRRGGID---VVQVIYNLL-DQRPEEELFPLAEEHGVGVIARVPLASGLLTGK------------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15219795 244 vddvlrkvsglkpiadelgvtLAQLAIAWCASNPNVSSVITGATRESQIQENMKA 298
Cdd:cd19086 205 ---------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-300 |
1.97e-54 |
|
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: 178.58 E-value: 1.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQL----DVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRelGWRRSDIVISTKIFw 85
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSkdysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 ggpgPNdkGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGA 165
Cdd:cd19072 78 ----PD--HLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 166 ADRldlvGPIV-EQPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKgaipsdsrfalenyknlanrslv 244
Cdd:cd19072 152 LKK----GPIVaNQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS----------------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 245 ddvlrkvSGLKPIADELGVTLAQLAIAWCASNPNVsSVITGATRESQIQENMKAVD 300
Cdd:cd19072 204 -------PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-301 |
3.34e-46 |
|
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: 158.10 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 8 KSGLKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVISTK---IF 84
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WGGPGPNDKG---LSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQIte 161
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQI-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 162 AWGAAdRLDLvgPIV-EQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKynkgaipsdsrfALENYKNLAn 240
Cdd:cd19092 159 ELLQS-YLDQ--PLVtNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGG------------FDERFQRLR- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219795 241 rslvdDVLRKvsglkpIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19092 223 -----AALEE------LAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-302 |
6.60e-45 |
|
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: 155.16 E-value: 6.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQ---LDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwRRSDIVISTK--IF 84
Cdd:cd19148 1 DLPVSRIALGTWAIGGWMwggTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKvgLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQIteawg 164
Cdd:cd19148 80 WDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQM----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 165 aaDRLDLVGPI-VEQPEYNMFARHkVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKG-------AIPSDSRFALENYk 236
Cdd:cd19148 155 --ETFRKVAPLhTVQPPYNLFERE-IEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDtkfegddLRRTDPKFQEPRF- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15219795 237 nlanrslvDDVLRKVSGLKPIADE-LGVTLAQLAIAWCASNPNVSSVITGATRESQI------------QENMKAVDVI 302
Cdd:cd19148 231 --------SQYLAAVEELDKLAQErYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLdavdevfgwslnDEDMKEIDAI 301
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
24-300 |
6.80e-44 |
|
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: 152.32 E-value: 6.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 24 FGNQLDVKEAKSILQCCRDHGVNFFDNAEVYAN----GRAEEIMGQAIRELGwRRSDIVISTKifwGG-PGPNDKG---L 95
Cdd:cd19082 10 FGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhPDLEDMSrsrL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 96 SRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDLVGPI 175
Cdd:cd19082 86 SPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 176 VEQPEYNMfARHKVET-----------EFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDsrFALENYKNLANRslv 244
Cdd:cd19082 166 ASSPQWSL-ARPNEPPwpgptlvamdeEMRAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDS--ELRRVYYSEENF--- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 245 dDVLRKVSGLkpiADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD 300
Cdd:cd19082 240 -ERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-299 |
4.73e-41 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 143.49 E-value: 4.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWVTFGnqldvkEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRelGWRRSDIVIS 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPR------ESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALK--GLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIFWGgpgpnDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPI---EETVRAMNYVIDKGWAFYWGTSEWSAQ 157
Cdd:cd19105 73 TKASPR-----LDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSTHDNM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 158 QitEAWGAA---DRLDLVgpiveQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLtgkynkgaIPSDSRFALEN 234
Cdd:cd19105 148 A--EVLQAAiesGWFDVI-----MVAYNFLNQPAELEEALAAAAEKGIGVVAMKTLAGGYL--------QPALLSVLKAK 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219795 235 yknlanrslvddvlrkvsglkpiadelGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAV 299
Cdd:cd19105 213 ---------------------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-327 |
1.59e-40 |
|
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: 144.12 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAW---VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRELGWRRSDI 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 78 VISTKIFWGGPGPNDKGLSR---KHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEW 154
Cdd:cd19144 79 FLATKFGIEKNVETGEYSVDgspEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAWGaadrldlVGPIVE-QPEYNMFAR--HKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKgaiPSD---- 227
Cdd:cd19144 159 SAETLRRAHA-------VHPIAAvQIEYSPFSLdiERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRS---PDDfeeg 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 228 ------SRFALENYKnlANRSLVDdvlrkvsGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19144 229 dfrrmaPRFQAENFP--KNLELVD-------KIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV 299
|
330 340
....*....|....*....|....*.
gi 15219795 302 ipLLTPIVLDKIEQVIQSKPKRPESY 327
Cdd:cd19144 300 --KLTEEEEKEIREIAEEAEVVGERY 323
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-301 |
3.29e-40 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 141.73 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWggp 88
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAASGVPREELFVTTKV-W--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 89 gPNDkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRPdASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADr 168
Cdd:COG0656 69 -NDN--HGYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 169 ldlVGPIVEQPEYNMFARhkvETEFLPLYTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyknlanRSLVDDVL 248
Cdd:COG0656 144 ---VKPAVNQVELHPYLQ---QRELLAFCREHGIVVEAYSPLGRG---------------------------KLLDDPVL 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15219795 249 RKvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVDV 301
Cdd:COG0656 191 AE------IAEKHGKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFDF 235
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-316 |
5.93e-40 |
|
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: 142.79 E-value: 5.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 2 QYKNLGKSGLKVSTLSFGA------WVTfGNQldvKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELgwrRS 75
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGggigglMGR-TTR---EEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 76 DIVISTKIFWGGPGPNDKGlsrKHIVEGTKASLKRLDMDYVDVLYCH---RPDASTPIEET------------VRAMNYV 140
Cdd:cd19104 74 GPYITTKVRLDPDDLGDIG---GQIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTlsttdvlglggvADAFERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 141 IDKGWAFYWGTSEWSAQQITEAWGAADRLDLVgpiveQPEYNMFARHKVET-----------EFLPLYTNHGIGLTTWSP 209
Cdd:cd19104 151 RSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLLNPSAAEArprgwsaqdygGIIDAAAEHGVGVMGIRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 210 LASGVLTGKYNKGAIPSDSRFalenyknlanrSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRE 289
Cdd:cd19104 226 LAAGALTTSLDRGREAPPTSD-----------SDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNR 294
|
330 340
....*....|....*....|....*..
gi 15219795 290 SQIQENMKAVDVIPlLTPIVLDKIEQV 316
Cdd:cd19104 295 EELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-301 |
2.77e-39 |
|
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: 139.31 E-value: 2.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWvTFGNQL-DVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgwRRSDIVISTKIFwgg 87
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPaKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 88 pgPNDKglSRKHIVEGTKASLKRLDMDYVDVLYCHRPdASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAAD 167
Cdd:cd19138 80 --PSNA--SRQGTVRACERSLRRLGTDYLDLYLLHWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 168 RLDLVgpiVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKynkgaipsdsrfalenyknlanrslvddV 247
Cdd:cd19138 155 GGNCA---ANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQGGLLRR----------------------------G 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15219795 248 LRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSvITGATRESQIQENMKAVDV 301
Cdd:cd19138 203 LLENPTLKEIAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAAADL 255
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-301 |
5.75e-39 |
|
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: 138.12 E-value: 5.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 13 VSTLSFGAW-----VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAireLGWRRSDIVISTKIFWGG 87
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEA---LHPYPDDVVIATKGGLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 88 PGPNDKGL--SRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwGA 165
Cdd:cd19088 78 TGPGWWGPdgSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA-RA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 166 ADRLDLVgpiveQPEYNMFARHKVETefLPLYTNHGIGLTTWSPLASGVLtgkynkgaipsdsrfalenyknLANRSLVD 245
Cdd:cd19088 157 IVRIVSV-----QNRYNLANRDDEGV--LDYCEAAGIAFIPWFPLGGGDL----------------------AQPGGLLA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15219795 246 DVlrkvsglkpiADELGVTLAQLAIAWC-ASNPNVsSVITGATRESQIQENMKAVDV 301
Cdd:cd19088 208 EV----------AARLGATPAQVALAWLlARSPVM-LPIPGTSSVEHLEENLAAAGL 253
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-300 |
8.63e-39 |
|
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: 138.84 E-value: 8.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAwVTFGN---QLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELgwRRSDI 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGI--PRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 78 VISTKI-FWGGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCH----RPDASTPIEETVRAMNYVIDKGWAFYWGts 152
Cdd:cd19163 78 YLATKVgRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 153 ewsaqqITeawgaADRLDLVGPIVEQPEYnmfarhKVET---------------EFLPLYTNHGIGLTTWSPLASGVLTg 217
Cdd:cd19163 156 ------IT-----GYPLDVLKEVLERSPV------KIDTvlsychytlndtsllELLPFFKEKGVGVINASPLSMGLLT- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 218 kyNKGaiPSDSRFALENYKNLANRSLVddvlrkvsglkpIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMK 297
Cdd:cd19163 218 --ERG--PPDWHPASPEIKEACAKAAA------------YCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLE 281
|
...
gi 15219795 298 AVD 300
Cdd:cd19163 282 AAE 284
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-298 |
3.01e-38 |
|
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: 136.21 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 14 STLSFGAWVTFGNQLDV--KEAKSILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRELgwRRSDIVISTKIFWGGPGPN 91
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPseAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGL--RRDDLFIATKVGTHGEGGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 92 D-KGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSewSAQQITEAWGAADRLD 170
Cdd:cd19095 77 DrKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS--GDGEELEAAIASGVFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 171 LVgpiveQPEYNMFARHkvETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDSRFALEnyknlanrslvddvlrk 250
Cdd:cd19095 155 VV-----QLPYNVLDRE--EEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPE----------------- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15219795 251 vsglkPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKA 298
Cdd:cd19095 211 -----FAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
6-307 |
1.98e-37 |
|
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: 135.64 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 6 LGKSGLKVSTLSFGAW---VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELgwRRSDIVISTK 82
Cdd:cd19145 5 LGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDG--PREKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 I---FWGGPGPNDKGlSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQI 159
Cdd:cd19145 83 FgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 160 TEAWGaadrldlVGPIVE-QPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDS-------RFA 231
Cdd:cd19145 162 RRAHA-------VHPITAvQLEWSLWTR-DIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSdvrkshpRFQ 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 232 LENYKNlaNRSLvddvLRKVSGLkpiADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVipLLTP 307
Cdd:cd19145 234 GENLEK--NKVL----YERVEAL---AKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSV--KLTK 298
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-299 |
1.85e-36 |
|
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: 132.29 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 14 STLSFG-AWVTFG-NQLDVKEAKSILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRElgWRRSDIVISTKIfwgGPGPN 91
Cdd:cd19090 1 SALGLGtAGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAE--LPREPLVLSTKV---GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 92 DKG-LSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTP-----IEETVRAMNYVIDKGWAFYWG----TSEWSAQQITE 161
Cdd:cd19090 74 DTAdYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWvdilaPGGALEALLELKEEGLIKHIGlgggPPDLLRRAIET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 162 awGAAD------RLDLVgpiveqpeynmfaRHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDsrfaleny 235
Cdd:cd19090 154 --GDFDvvltanRYTLL-------------DQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTY-------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219795 236 knlanRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAV 299
Cdd:cd19090 211 -----RWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAA 269
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-314 |
5.19e-36 |
|
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: 131.59 E-value: 5.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGA----WVtfGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAE---EIMGQAIRELGWRRSDIVIST 81
Cdd:cd19077 1 NGKLVGPIGLGLmgltWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlKLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 82 KifwGG--PGPNDKGLSRKHIVEGTKASLKRLDM-DYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQ 158
Cdd:cd19077 79 K---GGldPDTLRPDGSPEAVRKSIENILRALGGtKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 159 ITEAwgAAdrldlVGPIVE-QPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGA-IPSD------SRF 230
Cdd:cd19077 156 IRRA--HA-----VHPIAAvEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLAdIPEGdfrrhlDRF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 231 ALENY-KNLAnrslvddvlrKVSGLKPIADELGVTLAQLAIAWCASNPNVSSV-ITGATRESQIQENMKAVDVipLLTPI 308
Cdd:cd19077 229 NGENFeKNLK----------LVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDE 296
|
....*.
gi 15219795 309 VLDKIE 314
Cdd:cd19077 297 ELKEIN 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-300 |
4.58e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 126.29 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 24 FGNQLDVKEAKSILQCCRDHGVNFFDNAEVYA-------NGRAEEIMGQAIRELGwRRSDIVISTKIFWGGPGPND---- 92
Cdd:cd19752 10 FGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVGAGPRDPDGgpes 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 93 -KGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDL 171
Cdd:cd19752 89 pEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 172 VGPIVEQPEYNMF-----ARHKVE----TEFLPLYTNHG-IGLTTWSPLAsgvltgkynKGAIPSDSRFALENYKNLANR 241
Cdd:cd19752 169 AEFSAIQQRHSYLrprpgADFGVQrivtDELLDYASSRPdLTLLAYSPLL---------SGAYTRPDRPLPEQYDGPDSD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 242 slvddvlRKVSGLKPIADELGVTLAQLAIAW-CASNPNVSSVItGATRESQIQENMKAVD 300
Cdd:cd19752 240 -------ARLAVLEEVAGELGATPNQVVLAWlLHRTPAIIPLL-GASTVEQLEENLAALD 291
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-301 |
1.30e-32 |
|
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: 121.22 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFWGGPGPNDkgl 95
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTKVWRDHLRPED--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 96 srkhIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrldlVGPI 175
Cdd:cd19073 73 ----LKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 176 VEQPEYNMFArhkVETEFLPLYTNHGIGLTTWSPLASGVLtgkynkgaipsdsrfalenyknlanrsLVDDVLRKvsglk 255
Cdd:cd19073 145 VNQVEFHPFL---YQAELLEYCRENDIVITAYSPLARGEV---------------------------LRDPVIQE----- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15219795 256 pIADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMKAVDV 301
Cdd:cd19073 190 -IAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIFDW 232
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-301 |
1.30e-32 |
|
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: 121.91 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQL----DVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgWRRSDIVISTKIFw 85
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTpdysRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 ggpgpnDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwga 165
Cdd:cd19137 78 ------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 166 adRLDLVGPIV-EQPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLtgkynkgaipsdsrfalenyknLANRSlv 244
Cdd:cd19137 149 --ISKSQTPIVcNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE----------------------KTNRT-- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15219795 245 ddvlrkvsgLKPIADELGVTLAQLAIAWCASNPNVSSvITGATRESQIQENMKAVDV 301
Cdd:cd19137 203 ---------LEEIAKNYGKTIAQIALAWLIQKPNVVA-IPKAGRVEHLKENLKATEI 249
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-318 |
3.63e-32 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 122.65 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAwVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYA-------NGRAEEIMGQAIRELGwR 73
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetQGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 74 RSDIVISTKIfwGGPGP-NDKG------LSRKHIVEGTKASLKRLDMDYVDVLYCHRPDAST-----------------P 129
Cdd:PRK10625 79 REKLIIASKV--SGPSRnNDKGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsapavS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 130 IEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSP 209
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNR-SFEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 210 LASGVLTGKYNKGAIPSDSRFALENYknlANRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRE 289
Cdd:PRK10625 236 LAFGTLTGKYLNGAKPAGARNTLFSR---FTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTM 312
|
330 340
....*....|....*....|....*....
gi 15219795 290 SQIQENMKAVDVIplLTPIVLDKIEQVIQ 318
Cdd:PRK10625 313 EQLKTNIESLHLT--LSEEVLAEIEAVHQ 339
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
16-303 |
3.75e-32 |
|
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: 121.56 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGAwVTFGN---QLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwrRSDIVISTKIFW-----GG 87
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRllvplQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 88 PGPNDKGL---SRKHIV------EGTKA----SLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGwafYWGTSEW 154
Cdd:cd19152 80 VEPTFEPGfwnPLPFDAvfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKGA---FRALEEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAWGA-ADRLDLVGPIVE--QPEYNMFAR------HKVETEFLPLYTNHGIGLTTWSPLASGVLTGkynkgaip 225
Cdd:cd19152 157 REEGVIKAIGLgVNDWEVILRILEeaDLDWVMLAGrytlldHSAARELLPECEKRGVKVVNAGPFNSGFLAG-------- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15219795 226 sDSRFALENYknlanRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDV-IP 303
Cdd:cd19152 229 -GDNFDYYEY-----GPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATeIP 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-318 |
1.80e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 121.08 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 1 MQYKNLGKSGLKVSTLSFGAWvtFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRElgwRRSDIVIS 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM--RLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIfwgGPGPNDKGLSRKHIvegtKASLKRLDMDYVDVLYCHRPDASTPIEETVR---AMNYV---IDKGWAFYWGTSEW 154
Cdd:COG1453 74 TKL---PPWVRDPEDMRKDL----EESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggALEALekaKAEGKIRHIGFSTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAWGAADRLDLVgpiveQPEYN-MFARHKVETEFLPLYTNHGIGLTTWSPLASGvltgkynkgaipsdsrfale 233
Cdd:COG1453 147 GSLEVIKEAIDTGDFDFV-----QLQYNyLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG-------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 234 nykNLANRSlvDDVLRKVsglkpiadELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD-VIPlLTPIVLDK 312
Cdd:COG1453 202 ---RLANPP--EKLVELL--------CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnLEP-LTEEELAI 267
|
....*.
gi 15219795 313 IEQVIQ 318
Cdd:COG1453 268 LERLAE 273
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-314 |
5.05e-31 |
|
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: 117.36 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWggpg 89
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKV-W---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 90 PNDkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrl 169
Cdd:cd19140 72 PDN--YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 170 dlvGPIV-EQPEYNMFARhkvETEFLPLYTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyknlanRSLVDDVL 248
Cdd:cd19140 148 ---APLFtNQVEYHPYLD---QRKLLDAAREHGIALTAYSPLARG---------------------------EVLKDPVL 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 249 RKvsglkpIADELGVTLAQLAIAWCASNPNVsSVITGATRESQIQENMKAVDVIplLTPIVLDKIE 314
Cdd:cd19140 195 QE------IGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDFT--LSDEEMARIA 251
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-304 |
4.02e-29 |
|
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: 112.62 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 26 NQLDVKEAKSILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRelgwRRSDIVISTKIfwgGPGPNDKGLSRKHIVEGTK 105
Cdd:cd19097 21 GKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLK----RLDKFKIITKL---PPLKEDKKEDEAAIEASVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 106 ASLKRLDMDYVDVLYCHRP-DASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWgAADRLDLVgpiveQPEYNMF 184
Cdd:cd19097 92 ASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKAL-ESFKIDII-----QLPFNIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 185 ARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKgaIPSDSRFALENYKNLANrslvddvlrkvsglkpIADELGVT 264
Cdd:cd19097 166 DQRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDK--LPAKFAPAKPLLKKLHE----------------LAKKLGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15219795 265 LAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPL 304
Cdd:cd19097 228 PLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-327 |
5.39e-29 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 113.67 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAwVTFGNQ-------LDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwRRSDIVISTK 82
Cdd:cd19146 8 GVRVSPLCLGA-MSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFWG----GPGP---NDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEWS 155
Cdd:cd19146 86 YTTGyrrgGPIKiksNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 156 AQQITEAWGAADRLDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVL---TGKYNKGAIPSDSRFAL 232
Cdd:cd19146 166 AWVVSKANAYARAHGLTQFVVYQGHWSAAFR-DFERDILPMCEAEGMALAPWGVLGQGQFrteEEFKRRGRSGRKGGPQT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 233 ENYknlanrslvddvlRKVS-GLKPIADELGVTLAQLAIAWC-ASNPNVSSVITGATREsQIQENMKAVDVIplLTPIVL 310
Cdd:cd19146 245 EKE-------------RKVSeKLEKVAEEKGTAITSVALAYVmHKAPYVFPIVGGRKVE-HLKGNIEALGIS--LSDEEI 308
|
330
....*....|....*..
gi 15219795 311 DKIEQVIQSKPKRPESY 327
Cdd:cd19146 309 QEIEDAYPFDVGFPMNF 325
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-297 |
2.54e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 106.80 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 3 YKNLGKSGLKVSTLSFGAWVTFGnqLDVKEAKSILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRElgwRRSDIVISTK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR--LSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IfwggpGPNDKGLSRKHIVEgtkaSLKRLDMDYVDVLYCHRPDASTPIEETVR---AMNYVI---DKGWAFYWG-TSEWS 155
Cdd:cd19100 74 T-----GARDYEGAKRDLER----SLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggALEALLeakEEGKIRFIGiSGHSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 156 AQqiteAWGAADR--LDLVgpiveQPEYNMFARH--KVETEFLPLYTNHGIGLTTWSPLASGVLTGKynkgaipsdsrfa 231
Cdd:cd19100 145 EV----LLRALETgeFDVV-----LFPINPAGDHidSFREELLPLAREKGVGVIAMKVLAGGRLLSG------------- 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 232 lenyknlanrslvddvlrkvsglkpiadelGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMK 297
Cdd:cd19100 203 ------------------------------DPLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-316 |
1.08e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 106.65 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 11 LKVSTLSFGAW----------VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgWRRSDIVIS 80
Cdd:cd19103 2 KKLPKIALGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIfwggpGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDastpieETVRAMNYVID---KGWAFYWGTSEWSAQ 157
Cdd:cd19103 80 TKF-----TPQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPA------DVERWTPELIPllkSGKVKHVGVSNHNLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 158 QITEawgAADRLDLVGPIVE--QPEYNMFARHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYNKG-AIPSDSRFAlEN 234
Cdd:cd19103 149 EIKR---ANEILAKAGVSLSavQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKhPLPEGSGRA-ET 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 235 YknlanRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSsvITGATRESQIQENMKAVDVIplLTPIVLDKIE 314
Cdd:cd19103 225 Y-----NPLLPQLEELTAVMAEIGAKHGASIAQVAIAWAIAKGTTP--IIGVTKPHHVEDAARAASIT--LTDDEIKELE 295
|
..
gi 15219795 315 QV 316
Cdd:cd19103 296 QL 297
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
32-300 |
1.09e-26 |
|
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: 106.67 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 32 EAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRelGWRRSDIVISTKI---------FWGGPGPNDKGLSRKHIVE 102
Cdd:cd19162 20 EAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgaaGRPAGADRRFDFSADGIRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 103 GTKASLKRLDMDYVDVLYCHRPD--ASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwGAADRLDLVgpiveqpe 180
Cdd:cd19162 98 SIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLRA-ARRADVDVV-------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 181 ynMFA------RHKVETEFLPLYTNHGIGLTTWSPLASGVL-TGKynkgaiPSDSRFaleNYknlanRSLVDDVLRKVSG 253
Cdd:cd19162 169 --MVAgrytllDRRAATELLPLCAAKGVAVVAAGVFNSGILaTDD------PAGDRY---DY-----RPATPEVLARARR 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15219795 254 LKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD 300
Cdd:cd19162 233 LAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
31-303 |
1.84e-26 |
|
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: 106.26 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 31 KEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwrRSDIVISTK----------------IFWGGPGPN--D 92
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKvgrllkparegsvpdpNGFVDPLPFeiV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 93 KGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGW--------------AFYWGTSEWsaQQ 158
Cdd:cd19161 98 YDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERHHFAQLMSGGfkaleelkkagvikAFGLGVNEV--QI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 159 ITEAWGAADrLDLvgpIVEQPEYNMFARHKVEtEFLPLYTNHGIGLTTWSPLASGVLTgkynKGAIPsDSRFaleNYknl 238
Cdd:cd19161 176 CLEALDEAD-LDC---FLLAGRYSLLDQSAEE-EFLPRCEQRGTSLVIGGVFNSGILA----TGTKS-GAKF---NY--- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 239 anRSLVDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD-VIP 303
Cdd:cd19161 240 --GDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQtDIP 303
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-300 |
3.55e-26 |
|
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: 104.18 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 14 STLSFGAW---VTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRElgWRRSDIVISTKIFWGGPGP 90
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 91 NDKglSRKHIvegtKASLKRLDMDYVDVLYCHRPDAST---------PIEETVRAMnyviDKGWAFYWG-TSEWSAQQIT 160
Cdd:cd19096 79 AED--FRRIL----EESLKRLGVDYIDFYLLHGLNSPEwlekarkggLLEFLEKAK----KEGLIRHIGfSFHDSPELLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 161 EAWgAADRLDLVgpiveQPEYNMFARHKVETEFLPLYT-NHGIGLTTWSPLASGVLtgkynkGAIPSDSRFALENYKnla 239
Cdd:cd19096 149 EIL-DSYDFDFV-----QLQYNYLDQENQAGRPGIEYAaKKGMGVIIMEPLKGGGL------ANNPPEALAILCGAP--- 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219795 240 nrslvddvlrkvsglkpiadelgVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVD 300
Cdd:cd19096 214 -----------------------LSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-317 |
4.39e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 105.37 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 42 DHGVNFFDNAEVYanGRAEEIMGQAIRELGW---RRSDIVISTKIFwggPGPNDKGLSRKHIVEGTKASLKRLDMDYVDV 118
Cdd:cd19101 34 DAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWV---PDPGELTMTRAYVEAAIDRSLKRLGVDRLDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 119 LYCHRPDASTP-IEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwgaadrLDLVGPIV-EQPEYNMFARhKVETEFLPL 196
Cdd:cd19101 109 VQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREI------LDAGVPIVsNQVQYSLLDR-RPENGMAAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 197 YTNHGIGLTTWSPLASGVLTGKYnKGAiPSDSRFALEN-----YKNLANR----SLVDDVLRKvsgLKPIADELGVTLAQ 267
Cdd:cd19101 182 CEDHGIKLLAYGTLAGGLLSEKY-LGV-PEPTGPALETrslqkYKLMIDEwggwDLFQELLRT---LKAIADKHGVSIAN 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15219795 268 LAIAWCASNPNVSSVITGATRESQIQENMKAVDVipLLTPIVLDKIEQVI 317
Cdd:cd19101 257 VAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF--RLDDEDRAAIDAVL 304
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-300 |
9.96e-26 |
|
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: 102.95 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFWGGPGPndkgl 95
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAYGN---EAEVGEAIRESGVPREELFITTKLWPTDHGY----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 96 srKHIVEGTKASLKRLDMDYVDVLYCHRP------DASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrl 169
Cdd:cd19071 71 --ERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 170 dlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyknlaNRSLVDDvlr 249
Cdd:cd19071 147 --IKPAVNQIELHPYLQQKELVEFC---KEHGIVVQAYSPLGRG--------------------------RRPLLDD--- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15219795 250 kvSGLKPIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19071 193 --PVLKEIAKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDVFD 239
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-297 |
6.71e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 102.40 E-value: 6.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 11 LKVSTLSFGAWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIREL----GWRRSDIVISTK---I 83
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVVIVTKagyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 FWGGPGPNDKGLSRKHIVEGTK-----------------------ASLKRLDMDYVDVLYCHRPDASTP----------I 130
Cdd:cd19099 81 PGDGDEPLRPLKYLEEKLGRGLidvadsaglrhcispayledqieRSLKRLGLDTIDLYLLHNPEEQLLelgeeefydrL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 131 EETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDLVGPIVEQPEYNmfaRHKVETEFLPLytnhgiglttwSPL 210
Cdd:cd19099 161 EEAFEALEEAVAEGKIRYYGISTWDGFRAPPALPGHLSLEKLVAAAEEVGGD---NHHFKVIQLPL-----------NLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 211 ASGVLTGKyNKGAIPSDSRFALENYKNL---ANRSL-VDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVSSVITGA 286
Cdd:cd19099 227 EPEALTEK-NTVKGEALSLLEAAKELGLgviASRPLnQGQLLGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGM 305
|
330
....*....|.
gi 15219795 287 TRESQIQENMK 297
Cdd:cd19099 306 RRPEHVDENLA 316
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-318 |
3.67e-23 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 97.54 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 3 YKNLGKSGLKVSTLSFGAwVTFGNQL-DVKEAKSIlQCCR---DHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIV 78
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGSVFgPVSEEDAI-ASVReafRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 79 ISTKIFWGGPGPNdkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDAST---PIEETVRAMNYVIDKGWAFYWGTSEWS 155
Cdd:PLN02587 79 VSTKCGRYGEGFD---FSAERVTKSVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESGKVRFIGITGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 156 AQQITEAwgaadrLDLVGP-----IVEQPEYNMfaRHKVETEFLPLYTNHGIGLTTWSPLASGVLTGKYnkgaiPSDSRF 230
Cdd:PLN02587 156 LAIFTYV------LDRVPPgtvdvILSYCHYSL--NDSSLEDLLPYLKSKGVGVISASPLAMGLLTENG-----PPEWHP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 231 ALENYKnLANRSLVDDVLRKvsglkpiadelGVTLAQLAIAWCASNPNVSSVITGATRESQIQENMKAVDVIPLLT--PI 308
Cdd:PLN02587 223 APPELK-SACAAAATHCKEK-----------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSGidEE 290
|
330
....*....|
gi 15219795 309 VLDKIEQVIQ 318
Cdd:PLN02587 291 LLSEVEAILA 300
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-322 |
3.12e-22 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 93.84 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFG---AW-VTFGNQLDVKEAKSILQCCRdHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFW 85
Cdd:cd19120 1 GSKIPAIAFGtgtAWyKSGDDDIQRDLVDSVKLALK-AGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 GGpgpndkglsrKHIVEGTKASLKRLDMDYVDVLYCHRP----DASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITE 161
Cdd:cd19120 77 GI----------KDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 162 AWGAADrldlVGPIVEQPEYNMFARHKvETEFLPLYTNHGIGLTTWSPLASgvLTgkynkgaipsdsRFAlenyknlanR 241
Cdd:cd19120 147 LLDTAK----IKPAVNQIEFHPYLYPQ-QPALLEYCREHGIVVSAYSPLSP--LT------------RDA---------G 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 242 SLVDDVLRKvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVDviPLLTPIVLDKIEQVIQSKP 321
Cdd:cd19120 199 GPLDPVLEK------IAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAFD--FELTEEEVEEIDKAGKQKH 268
|
.
gi 15219795 322 K 322
Cdd:cd19120 269 F 269
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-305 |
6.00e-22 |
|
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: 93.75 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 6 LGKSGLKVSTLSFGAWV---TFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGWRRSDIVISTK 82
Cdd:cd19153 5 LEIALGNVSPVGLGTAAlggVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFWGGPGPNDkgLSRKHIVEGTKASLKRLDMDYVDVLYCHR---PDASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQI 159
Cdd:cd19153 85 VGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 160 TEawgAADRLDLVGPIVEQPEYNMFARHKVETEFLPLYTN-HGIGLTTWSPLASGVLTGKYNKGAIPSDSrfALENYKNL 238
Cdd:cd19153 163 TR---ATRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRgAGPHVINASPLSMGLLTSQGPPPWHPASG--ELRHYAAA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 239 ANRslvddvlrkvsglkpIADELGVTLAQLAIAWCASNPN-VSSVITGATRESQIQENMKAVDVIPLL 305
Cdd:cd19153 238 ADA---------------VCASVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSMLAAVDAVASL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
49-301 |
9.44e-20 |
|
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: 86.64 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 49 DNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFWggpgpndKGLSRKHIVEGTKASLKRLDMDYVDVLYCH--RPDA 126
Cdd:cd19139 32 DTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWI-------DNLSKDKLLPSLEESLEKLRTDYVDLTLIHwpSPND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 127 STPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwgaadrLDLVGP---IVEQPEYNMFARHKVETEFLplyTNHGIG 203
Cdd:cd19139 102 EVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEA------IAVVGAgaiATNQIELSPYLQNRKLVAHC---KQHGIH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 204 LTTWSPLASGvltgkynkgaipsdsrfalenyknlanRSLVDDVLRKvsglkpIADELGVTLAQLAIAWCASNPnvSSVI 283
Cdd:cd19139 173 VTSYMTLAYG---------------------------KVLDDPVLAA------IAERHGATPAQIALAWAMARG--YAVI 217
|
250
....*....|....*...
gi 15219795 284 TGATRESQIQENMKAVDV 301
Cdd:cd19139 218 PSSTKREHLRSNLLALDL 235
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
9-314 |
7.76e-19 |
|
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: 85.26 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFG------AWVTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANGRAEEIMGQAIRELGwRRSDIVISTK 82
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFW--------GGPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNYVIDKGWAFYWGTSEW 154
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAWGAADRLDLVGPIVEQPEYNMFARhKVETEFLPLYTNHGIGLTTWSPLASGVLtgkynkgaipsDSRFALEN 234
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNR-DFERDIIPMARHFGMALAPWDVLGGGKF-----------QSKKAVEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 235 YK--NLANRSLV------DDVLRKVSGLKPIADELGV-TLAQLAIAWCASN-PNVSSVItGATRESQIQENMKAVDVIpl 304
Cdd:cd19147 233 RKknGEGLRSFVggteqtPEEVKISEALEKVAEEHGTeSVTAIALAYVRSKaPNVFPLV-GGRKIEHLKDNIEALSIK-- 309
|
330
....*....|
gi 15219795 305 LTPIVLDKIE 314
Cdd:cd19147 310 LTPEEIEYLE 319
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-300 |
8.71e-18 |
|
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: 81.78 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIREL----GWRRSDIVISTKIFw 85
Cdd:cd19111 1 GFPMPVIGLGTY-----QSPPEEVRAAVDYALFVGYRHIDTALSYQN---EKAIGEALKWWlkngKLKREEVFITTKLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 ggpgpnDKGLSRKHIVEGTKASLKRLDMDYVDVLYCH-------------RPDASTPIEETVRAMNYVIDKGWAFYWGTS 152
Cdd:cd19111 72 ------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 153 EWSAQQITEAWGAAdrldLVGPIVEQPEYNMFARHKvetEFLPLYTNHGIGLTTWSPLASGVLTGKYNKGAIPSDsrfaL 232
Cdd:cd19111 146 NFNPRQINKILAYA----KVKPSNLQLECHAYLQQR---ELRKFCNKKNIVVTAYAPLGSPGRANQSLWPDQPDL----L 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 233 ENYKNLAnrslvddvlrkvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19111 215 EDPTVLA-----------------IAKELDKTPAQVLLRFVLQRGTG--VLPKSTNKERIEENFEVFD 263
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-300 |
1.30e-17 |
|
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: 81.69 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 8 KSGLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIREL----GWRRSDIVISTKI 83
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLYQN---EEAIGEALAELleegVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 FWGGPGPNDkglsrkhIVEGTKASLKRLDMDYVDVLYCHRP-------------------DASTPIEETVRAMNYVIDKG 144
Cdd:cd19154 79 WTHEHAPED-------VEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 145 WAFYWGTSEWSAQQITEAWGAAdrldLVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASgvlTGKYNkgAI 224
Cdd:cd19154 152 LTKAIGVSNFNNDQIQRILDNA----RVKPHNNQVECHLYFPQKELVEFC---KKHNISVTSYATLGS---PGRAN--FT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 225 PSDSRFALENyknlanrsLVDDVLrkvsgLKPIADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMKAVD 300
Cdd:cd19154 220 KSTGVSPAPN--------LLQDPI-----VKAIAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIKENFNIFD 280
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-301 |
3.44e-16 |
|
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: 77.03 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWGGPG 89
Cdd:cd19131 7 GNTIPQLGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTKL-WNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 90 PNDKGLsrkhivEGTKASLKRLDMDYVDVLYCHRPdasTPIE----ETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGA 165
Cdd:cd19131 78 GYDSTL------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 166 ADrldlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyknlanRSLVD 245
Cdd:cd19131 149 TG----VVPVVNQIELHPRFQQRELRAFH---AKHGIQTESWSPLGQG---------------------------GLLSD 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 246 DVLRKvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVDV 301
Cdd:cd19131 195 PVIGE------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDF 242
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-320 |
2.44e-15 |
|
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: 74.73 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAW-VTFGNQLdVKEAKSILqccrDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWGGP 88
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEV-VNAVKTAL----KNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 89 GPNDKGLsrkhivEGTKASLKRLDMDYVDVLYCHRPdASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADr 168
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 169 ldlVGPIVEQPEYnmfarHK--VETEFLPLYTNHGIGLTTWSPLASGVLtgkynkgaipsdsrfaLENyknlanrslvdD 246
Cdd:cd19157 150 ---IVPMVNQVEF-----HPrlTQKELRDYCKKQGIQLEAWSPLMQGQL----------------LDN-----------P 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219795 247 VlrkvsgLKPIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVDVipLLTPIVLDKIEQVIQSK 320
Cdd:cd19157 195 V------LKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENADVFDF--ELSQEDMDKIDALNENL 258
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-301 |
6.49e-15 |
|
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: 73.71 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIREL----GWRRSDIVISTKIfWggpgPN 91
Cdd:cd19128 4 LGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYGN---EAFIGIAFSEIfkdgGVKREDLFITSKL-W----PT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 92 DkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRP-------------------DASTPIEETVRAMNYVIDKGWAFYWGTS 152
Cdd:cd19128 71 M--HQPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 153 EWSAQQITEAWGAADrldlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLAsgvltGKYNKGAipsdsrfal 232
Cdd:cd19128 149 NYSTKLLTDLLNYCK----IKPFMNQIECHPYFQNDKLIKFC---IENNIHVTAYRPLG-----GSYGDGN--------- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 233 enyknlanrslvdDVLRKVSGLKPIADELGVTLAQLAIAWCASN-PNVSSVITGATRESQIQENMKAVDV 301
Cdd:cd19128 208 -------------LTFLNDSELKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDL 264
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
44-301 |
1.04e-14 |
|
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: 73.21 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 44 GVNFFDNAEVYANgraEEIMGQAIREL----GWRRSDIVISTKIFWGGPGPNDkglsrkhIVEGTKASLKRLDMDYVDVL 119
Cdd:cd19123 38 GYRHIDCAAIYGN---EAEIGAALAEVfkegKVKREDLWITSKLWNNSHAPED-------VLPALEKTLADLQLDYLDLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 120 YCHRP------------------DASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLDLVG-----PIV 176
Cdd:cd19123 108 LMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATARIKPAVNqvelhPYL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 177 EQPEYNMFARHKveteflplytnhGIGLTTWSPLASGVLtgkynkgaiPSDSRFALENyknlanRSLVDDVLRKvsglkp 256
Cdd:cd19123 188 QQPELLAFCRDN------------GIHLTAYSPLGSGDR---------PAAMKAEGEP------VLLEDPVINK------ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15219795 257 IADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMKAVDV 301
Cdd:cd19123 235 IAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPERIQQNLEAAEV 277
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
49-301 |
1.17e-14 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 72.75 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 49 DNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWggpgpnDKGLSRKHIVEGTKASLKRLDMDYVDVLYCH--RPDA 126
Cdd:PRK11172 34 DTAQIYDN---EAAVGQAIAESGVPRDELFITTKI-W------IDNLAKDKLIPSLKESLQKLRTDYVDLTLIHwpSPND 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 127 STPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAwgaadrLDLVGP---IVEQPEYNMFARHKVETEFLplyTNHGIG 203
Cdd:PRK11172 104 EVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA------IAAVGAeniATNQIELSPYLQNRKVVAFA---KEHGIH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 204 LTTWSPLASGvltgkynkgaipsdsrfalenyknlanRSLVDDVLRKvsglkpIADELGVTLAQLAIAWCASNPnvSSVI 283
Cdd:PRK11172 175 VTSYMTLAYG---------------------------KVLKDPVIAR------IAAKHNATPAQVILAWAMQLG--YSVI 219
|
250
....*....|....*...
gi 15219795 284 TGATRESQIQENMKAVDV 301
Cdd:PRK11172 220 PSSTKRENLASNLLAQDL 237
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-300 |
1.82e-14 |
|
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: 72.05 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQLdVKEAKSILQCcrdhGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFWGGPG 89
Cdd:cd19127 6 GVEMPALGLGVFQTPPEET-ADAVATALAD----GYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWISDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 90 pNDKGLsrkhivEGTKASLKRLDMDYVDVLYCHRPdASTPIEETV---RAMNYVIDKGWAFYWGTSEWSAQQITEawgAA 166
Cdd:cd19127 78 -YDKAL------RGFDASLRRLGLDYVDLYLLHWP-VPNDFDRTIqayKALEKLLAEGRVRAIGVSNFTPEHLER---LI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 167 DRLDLVgPIVEQPEYNMFARHKVETEFlplYTNHGIGLTTWSPLAsGVLTgkYNKGAIPsdsrfalenyknlANRSLVDD 246
Cdd:cd19127 147 DATTVV-PAVNQVELHPYFSQKDLRAF---HRRLGIVTQAWSPIG-GVMR--YGASGPT-------------GPGDVLQD 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15219795 247 VLrkvsgLKPIADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMKAVD 300
Cdd:cd19127 207 PT-----ITGLAEKYGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFD 253
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-300 |
2.28e-14 |
|
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: 71.70 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTfgnqLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWGGPG 89
Cdd:cd19126 6 GTRMPWLGLGVFQT----PDGDETERAVQTALENGYRSIDTAAIYKN---EEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 90 PNDKGLSRKHivegtkASLKRLDMDYVDVLYCHRPdASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrl 169
Cdd:cd19126 78 RARRTEDAFQ------ESLDRLGLDYVDLYLIHWP-GKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 170 dlVGPIVEQPEYNMFARHKVETEFLPLytnHGIGLTTWSPLASGVLtgkynkgaipsdsrfalenyknLANRSLVDdvlr 249
Cdd:cd19126 149 --VVPAVNQVEFHPYLTQKELRGYCKS---KGIVVEAWSPLGQGGL----------------------LSNPVLAA---- 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15219795 250 kvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19126 198 -------IGEKYGKSAAQVVLRWDIQHGVV--TIPKSVHASRIKENADIFD 239
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
13-122 |
4.22e-14 |
|
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: 71.54 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 13 VSTLSFGAwVTFGNQL--DVKEAK--SILQCCRDHGVNFFDNAEVYanGRAEEIMGQAIREL--GWRRSDIVISTKIfwG 86
Cdd:cd19164 13 LPPLIFGA-ATFSYQYttDPESIPpvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALrdEFPRDTYFIITKV--G 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 15219795 87 GPGPNDKGLSRKHIVEGTKASLKRLDMDYVDVLYCH 122
Cdd:cd19164 88 RYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLH 123
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-318 |
7.60e-14 |
|
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: 70.76 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQLDVKEAksILQCCRdHGVNFFDNAEVYAngrAEEIMGQAIRE-----LGWRRSDIVISTKI 83
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEDIKAA--VLEAIE-VGYRHFDTAAAYG---TEEALGEALAEalrlgLVKSRDELFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 fWggpgPNDkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTP----------------IEETVRAMNYVIDKGWAF 147
Cdd:cd19124 75 -W----CSD--AHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 148 YWGTSEWSAQQITEAWGAADrldlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLasgvltgkynkGAIpsd 227
Cdd:cd19124 148 AIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNPAWQQKKLREFC---KANGIHVTAYSPL-----------GAP--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 228 srfaleNYKNLANRSLVDDVLRKvsglkpIADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMKAVDVipLLTP 307
Cdd:cd19124 207 ------GTKWGSNAVMESDVLKE------IAAAKGKTVAQVSLRWVYEQG--VSLVVKSFNKERMKQNLDIFDW--ELTE 270
|
330
....*....|.
gi 15219795 308 IVLDKIEQVIQ 318
Cdd:cd19124 271 EDLEKISEIPQ 281
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
29-300 |
9.84e-14 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 69.97 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 29 DVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWR----RSDIVISTKIfwggpGPNDKGLSRKHivEGT 104
Cdd:cd19136 13 GEEEVRQAVDAALKAGYRLIDTASVYRN---EADIGKALRDLLPKyglsREDIFITSKL-----APKDQGYEKAR--AAC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 105 KASLKRLDMDYVDVLYCHRP-----DASTPIE-----ETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrldlVGP 174
Cdd:cd19136 83 LGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE----VPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 175 IVEQPEYNmfaRHKVETEFLPLYTNHGIGLTTWSPLASGVLTgkynkgaipsdsrfALENyknlanrslvDDVLRkvsgl 254
Cdd:cd19136 159 AVNQVEFH---PHLVQKELLKFCKDHGIHLQAYSSLGSGDLR--------------LLED----------PTVLA----- 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15219795 255 kpIADELGVTLAQLAIAWCASNpNVsSVITGATRESQIQENMKAVD 300
Cdd:cd19136 207 --IAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENIKVFD 248
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-300 |
9.87e-14 |
|
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: 70.24 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgNQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWGGPG 89
Cdd:cd19156 6 GVEMPRLGLGVW----RVQDGAEAENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIRESGVPREEVFVTTKL-WNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 90 PNDKGLSrkhiveGTKASLKRLDMDYVDVLYCHRPDASTPIeETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADrl 169
Cdd:cd19156 78 GYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGKFK-DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 170 dlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASGVLtgkynkgaipsdsrfaLENYKnlanrslvddvlr 249
Cdd:cd19156 149 --VAPMVNQIELHPLLTQEPLRKFC---KEKNIAVEAWSPLGQGKL----------------LSNPV------------- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15219795 250 kvsgLKPIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19156 195 ----LKAIGKKYGKSAAQVIIRWDIQHGII--TIPKSVHEERIQENFDVFD 239
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-300 |
1.93e-13 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 69.36 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQLD--VKEAKsilqccrDHGVNFFDNAEVYANgraEEIMGQAIREL-----GWRRSDIVIST 81
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGaaVKIAL-------KAGYRHLDLAKVYQN---QHEVGQALKELlkeepGVKREDLFITS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 82 KIfWggpgpNDKGlSRKHIVEGTKASLKRLDMDYVDVLYCHRP------------------------DASTPIEETVRAM 137
Cdd:cd19118 73 KL-W-----NNSH-RPEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltavptnggevdlDLSVSLVDTWKAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 138 NYVIDKGWAFYWGTSEWSA---QQITEAWGaadrldlVGPIVEQPEynmfaRHKV--ETEFLPLYTNHGIGLTTWSPLas 212
Cdd:cd19118 146 VELKKTGKVKSIGVSNFSIdhlQAIIEETG-------VVPAVNQIE-----AHPLllQDELVDYCKSKNIHITAYSPL-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 213 gvltGKYNKGAIPsdsrfalenyknlanrsLVDDvlrkvSGLKPIADELGVTLAQLAIAWCASNPNvsSVITGATRESQI 292
Cdd:cd19118 212 ----GNNLAGLPL-----------------LVQH-----PEVKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRI 263
|
....*...
gi 15219795 293 QENMKAVD 300
Cdd:cd19118 264 RSNFEQVE 271
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-296 |
5.77e-13 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 67.60 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQL-DVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWggp 88
Cdd:cd19133 6 GVEMPILGFGVF-----QIpDPEECERAVLEAIKAGYRLIDTAAAYGN---EEAVGRAIKKSGIPREELFITTKL-W--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 89 gPNDKGLsrkhivEGTKA----SLKRLDMDYVDVLYCHRPDAStpIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWG 164
Cdd:cd19133 74 -IQDAGY------EKAKKaferSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLIL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 165 AADrldlVGPIVEQPEYNMFARHKVETEFLPLYtnhGIGLTTWSPLASGvltgkynkgaipsdsrfalenYKNLANrslv 244
Cdd:cd19133 145 HNE----VKPAVNQIETHPFNQQIEAVEFLKKY---GVQIEAWGPFAEG---------------------RNNLFE---- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15219795 245 DDVLRKvsglkpIADELGVTLAQLAIAWcasnpNVSS---VITGATRESQIQENM 296
Cdd:cd19133 193 NPVLTE------IAEKYGKSVAQVILRW-----LIQRgivVIPKSVRPERIAENF 236
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-316 |
6.45e-13 |
|
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: 68.14 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 8 KSGLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELG----WRRSDIVISTKI 83
Cdd:cd19125 6 NTGAKIPAVGLGTW-----QADPGVVGNAVKTAIKEGYRHIDCAAIYGN---EKEIGKALKKLFedgvVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 FWGGPGPNDkglsrkhIVEGTKASLKRLDMDYVDVLYCHRPDA--------------STPIEETVRAMNYVIDKGWAFYW 149
Cdd:cd19125 78 WCTDHAPED-------VPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepeevlPPDIPSTWKAMEKLVDSGKVRAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 150 GTSEWSAQQITEAWGAAdrldLVGPIVEQPEYNMFARhkvETEFLPLYTNHGIGLTTWSPLASgvltgkynkgaipSDSR 229
Cdd:cd19125 151 GVSNFSVKKLEDLLAVA----RVPPAVNQVECHPGWQ---QDKLHEFCKSKGIHLSAYSPLGS-------------PGTT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 230 FAlenYKNLANRSLVDDvlrkvsglkpIADELGVTLAQLAIAWCASNPNvsSVITGATRESQIQENMKAVDV-IPLLTPI 308
Cdd:cd19125 211 WV---KKNVLKDPIVTK----------VAEKLGKTPAQVALRWGLQRGT--SVLPKSTNEERIKENIDVFDWsIPEEDFA 275
|
....*...
gi 15219795 309 VLDKIEQV 316
Cdd:cd19125 276 KFSSIEQQ 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-300 |
7.50e-13 |
|
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: 67.35 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQLDvkeakSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFwggp 88
Cdd:cd19135 9 NGVEMPILGLGTSHSGGYSHE-----AVVYALKECGYRHIDTAKRYGC---EELLGKAIKESGVPREDLFLTTKLW---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 89 gPNDKGLSRkhIVEGTKASLKRLDMDYVDVLYCHRPDASTP-------IEETVRAMNYVIDKGWAFYWGTSEWSAQ---Q 158
Cdd:cd19135 77 -PSDYGYES--TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEhleQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 159 ITEAWGaadrldlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyKNL 238
Cdd:cd19135 154 LLEDCS-------VVPHVNQVEFHPFQNPVELIEYC---RDNNIVFEGYCPLAKG----------------------KAL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219795 239 ANRSLVDdvlrkvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19135 202 EEPTVTE-----------LAKKYQKTPAQILIRWSIQNGVV--TIPKSTKEERIKENCQVFD 250
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-272 |
1.45e-12 |
|
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: 66.52 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfwggPG 89
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL----PG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 90 pNDKGlsRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIE-ETVRAMNYVIDKGWAFYWGTSEWSAQQIteawgaaDR 168
Cdd:cd19132 72 -RHHG--YEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHL-------DR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 169 L-DLVG--PIVEQPE-YNMFARhkveTEFLPLYTNHGIGLTTWSPLASGvltgkynkgaipsdsrfalenyknlaNRSLV 244
Cdd:cd19132 142 LiDETGvtPAVNQIElHPYFPQ----AEQRAYHREHGIVTQSWSPLGRG--------------------------SGLLD 191
|
250 260
....*....|....*....|....*...
gi 15219795 245 DDVLRKvsglkpIADELGVTLAQLAIAW 272
Cdd:cd19132 192 EPVIKA------IAEKHGKTPAQVVLRW 213
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
44-300 |
4.72e-12 |
|
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: 65.26 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 44 GVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfwggpGPNDKGLSRKhiVEGTKASLKRLDMDYVDVLYCHR 123
Cdd:cd19134 37 GYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGFTAS--QAACRASLERLGLDYVDLYLIHW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 124 PDAST-PIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGaadrLDLVGPIVEQ----PEYNMFARHKVETEflplyt 198
Cdd:cd19134 107 PAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLID----LTFFTPAVNQielhPLLNQAELRKVNAQ------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 199 nHGIGLTTWSPLASGVLtgkynkgaipsdsrfaLENyknlanrslvDDVLRkvsglkpIADELGVTLAQLAIAWCASNPN 278
Cdd:cd19134 177 -HGIVTQAYSPLGVGRL----------------LDN----------PAVTA-------IAAAHGRTPAQVLLRWSLQLGN 222
|
250 260
....*....|....*....|..
gi 15219795 279 VssVITGATRESQIQENMKAVD 300
Cdd:cd19134 223 V--VISRSSNPERIASNLDVFD 242
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
24-304 |
6.64e-12 |
|
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: 65.17 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 24 FGNQL-DVKEAKSILQCCRDHGVNFFDNAEVYangRAEEIMGQAIREL----GWRRSDIVISTKIfWggpgpndkglSRK 98
Cdd:cd19129 11 FGTLIpDPSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTKL-W----------NTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 99 HIVEGTK----ASLKRLDMDYVDVLYCHRPDASTPIEE--------------------TVRAMNYVIDKGWAFYWGTSEW 154
Cdd:cd19129 77 HRPERVKpafeASLKRLQLDYLDLYLIHTPFAFQPGDEqdprdangnviyddgvtlldTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 155 SAQQITEAWGAADrldlVGPIVEQPEYNMFARhkvETEFLPLYTNHGIGLTTWSPLASGVLTGkynkgaipsdsrfalen 234
Cdd:cd19129 157 SLEKLREIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPK----------------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 235 yknlanrsLVDDVLrkvsgLKPIADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMkavDVIPL 304
Cdd:cd19129 213 --------LLEDPV-----ITAIARRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIRENF---DISTL 264
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-300 |
1.22e-11 |
|
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: 64.33 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQldVKEA-KSILQCcrdhGVNFFDNAEVYANgraEEIMGQAIRE-----LGWRRSDIVISTK 82
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQ--VKAAvKYALDA----GYRHIDCAAVYGN---EQEVGEALKEkvgpgKAVPREDLFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 IFWGGPGPNDkglsrkhiVEGT-KASLKRLDMDYVDVLYCHRPDA-------------------STPIEETVRAMNYVID 142
Cdd:cd19106 74 LWNTKHHPED--------VEPAlRKTLKDLQLDYLDLYLIHWPYAfergdnpfpknpdgtirydSTHYKETWKAMEKLVD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 143 KGWAFYWGTSEWSAQQITEAWGAADrldlVGPIVEQPEYNmfaRHKVETEFLPLYTNHGIGLTTWSPLASgvltgkynkg 222
Cdd:cd19106 146 KGLVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECH---PYLAQNELIAHCKARGLVVTAYSPLGS---------- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 223 aipSDSRFALENyknlanrslvDDVLRKVSGLKPIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19106 209 ---PDRPWAKPD----------EPVLLEEPKVKALAKKYNKSPAQILLRWQVQRGVV--VIPKSVTPSRIKQNIQVFD 271
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-297 |
1.33e-11 |
|
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: 64.06 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQLdvkeAKSILQCCRDhGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWGgp 88
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNEV----AKAVEAALKA-GYRHIDTAAIYGN---EEEVGQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 89 gpndkgLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIEETVRAMNY----VIDKGWAFY--W------------- 149
Cdd:cd19117 79 ------TWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDdgtkDHEPDWDFIktWelmqklpatgkvk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 150 --GTSEWS--------AQQITEAWGAADRLDLvGPIVEQPEYNMFARHKveteflplytnhGIGLTTWSPLASgvltgky 219
Cdd:cd19117 153 aiGVSNFSiknlekllASPSAKIVPAVNQIEL-HPLLPQPKLVDFCKSK------------GIHATAYSPLGS------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219795 220 nkgaipsdsrfalenyknlANRSLVDDVLrkvsgLKPIADELGVTLAQLAIAWCASNPnvSSVITGATRESQIQENMK 297
Cdd:cd19117 213 -------------------TNAPLLKEPV-----IIKIAKKHGKTPAQVIISWGLQRG--YSVLPKSVTPSRIESNFK 264
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-313 |
4.03e-11 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 62.93 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRElgW------RRSDIVISTKI 83
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRN---EAAIGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 FWGGpgpndkglSRKHIVEGT-KASLKRLDMDYVDVLYCHRP---------------------DASTPIEETVRAMNYVI 141
Cdd:cd19155 79 PPGG--------NRREKVEKFlLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 142 DKGWAFYWGTSEWSAQQITEAWGAADrldlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASGVLTGKYNK 221
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFC---STHSITVTAYAPLGSPGAAHFSPG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 222 GAIPSDSRFalenyknlanrSLVDDvlrkvSGLKPIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVDV 301
Cdd:cd19155 224 TGSPSGSSP-----------DLLQD-----PVVKAIAERHGKSPAQVLLRWLMQRGVV--VIPKSTNAARIKENFQVFDF 285
|
330
....*....|..
gi 15219795 302 ipLLTPIVLDKI 313
Cdd:cd19155 286 --ELTEADMAKL 295
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-295 |
4.45e-11 |
|
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: 62.68 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQlDVKEAksiLQCCRDHGVNFFDNAEVYANgraEEIMGQAIREL----GWRRSDIVISTKIf 84
Cdd:cd19116 7 DGNEIPAIALGTWKLKDDE-GVRQA---VKHAIEAGYRHIDTAYLYGN---EAEVGEAIREKiaegVVKREDLFITTKL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WggpgpNDKGlSRKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPIE----------------ETVRAMNYVIDKGWAFY 148
Cdd:cd19116 79 W-----NSYH-EREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNdsesngdgslsdidylETWRGMEDLVKLGLTRS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 149 WGTSEWSAQQITEAWgaadRLDLVGPIVEQPEYNmfarhkveteflPLYTN---------HGIGLTTWSPLasgvltGKY 219
Cdd:cd19116 153 IGVSNFNSEQINRLL----SNCNIKPAVNQIEVH------------PTLTQeklvaycqsNGIVVMAYSPF------GRL 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219795 220 NKgaipsdsRFALENYKNLANRSLVDdvlrkvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQEN 295
Cdd:cd19116 211 VP-------RGQTNPPPRLDDPTLVA-----------IAKKYGKTTAQIVLRYLIDRGVV--PIPKSSNKKRIKEN 266
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-327 |
4.09e-10 |
|
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: 60.05 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQLDVKEAKSI----------LQCCRDHGVNFFDNAEVYanGRAEEIMGQAIRELGWRRSDIVI 79
Cdd:cd19098 4 GLGLAALGRPGYINLGHAADLGSGRSVeamrahthavLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 80 STKifWG----------GPGPNDKGLSRKHI---VEGTKASLKrldmDYVDVLYCHRPDASTPI---EETVRAMNYVIDK 143
Cdd:cd19098 82 GSK--WGytytadwqvdAAVHEVKDHSLARLlkqWEETRSLLG----KHLDLYQIHSATLESGVledADVLAALAELKAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 144 GWAFywGTSEWSAQQ---ITEAWGAA---DRL-DLVgpiveQPEYNMFarhkvETEFLP-LYTNH--GIGLTTWSPLASG 213
Cdd:cd19098 156 GVKI--GLSLSGPQQaetLRRALEIEidgARLfDSV-----QATWNLL-----EQSAGEaLEEAHeaGMGVIVKEALANG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 214 VLTGkynkgaipsdsrfalenyknlANRSLVDDVLRKVsgLKPIADELGVTLAQLAIAWCASNPNVSSVITGATRESQIQ 293
Cdd:cd19098 224 RLTD---------------------RNPSPELAPLMAV--LKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLR 280
|
330 340 350
....*....|....*....|....*....|....
gi 15219795 294 ENMKAVDVIplLTPIVLDKIEQVIQSkpkrPESY 327
Cdd:cd19098 281 SNLRALDVS--LDLELLAALADLAEP----PEDY 308
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-212 |
6.12e-09 |
|
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: 56.00 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIREL---GWRRSDIVISTKIfW 85
Cdd:cd19121 8 TGASIPAVGLGTW-----QAKAGEVKAAVAHALKIGYRHIDGALCYQN---EDEVGEGIKEAiagGVKREDLFVTTKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 GgpgpndkgLSRKHIVEGTKASLKRLDMDYVDVLYCH----------------RPDASTPIE------ETVRAMNYVIDK 143
Cdd:cd19121 79 S--------TYHRRVELCLDRSLKSLGLDYVDLYLVHwpvllnpngnhdlfptLPDGSRDLDwdwnhvDTWKQMEKVLKT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15219795 144 GWAFYWGTSEWSAQQITEAWGAADrldlVGPIVEQPEYNMFARhkvETEFLPLYTNHGIGLTTWSPLAS 212
Cdd:cd19121 151 GKTKAIGVSNYSIPYLEELLKHAT----VVPAVNQVENHPYLP---QQELVDFCKEKGILIEAYSPLGS 212
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-301 |
1.03e-08 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 55.71 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGawvTFGNQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIREL-----GWRRSDIVISTKI 83
Cdd:cd19122 5 NGVKIPAVGFG---TFANEGAKGETYAAVTKALDVGYRHLDCAWFYLN---EDEVGDAVRDFlkenpSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 FWGGPGPNDkglsrkhIVEGTKASLKRLDMDYVDVLYCHRP------DASTPI-----------------EETVRAMNYV 140
Cdd:cd19122 79 WNHLHEPED-------VKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAMEEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 141 IDKGWAFYWGTSEWSAQQITEAWGAADrldlVGPIVEQPEYNMFARHKvetEFLPLYTNHGIGLTTWSPLASgvltgkyn 220
Cdd:cd19122 152 YESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGS-------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 221 KGAIPSDSRFALENyknlanrslvddvlrkvSGLKPIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:cd19122 217 QNQVPSTGERVSEN-----------------PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIE 277
|
.
gi 15219795 301 V 301
Cdd:cd19122 278 L 278
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
16-300 |
1.09e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 55.46 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 16 LSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIfWggpgpNDKgl 95
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIYKN---EEGVGKALKEASVAREELFITTKL-W-----NDD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 96 sRKHIVEGTKASLKRLDMDYVDVLYCHRPDAstPIEETVRAMNYVID---KGWAFYWGTSEWSA---QQITEAWGaadrl 169
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETG----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 170 dlVGPIVEQPE-YNMFARHKVETeflpLYTNHGIGLTTWSPLASGvltgkyNKGAIPSdsrfalenyknlanrslvdDVL 248
Cdd:PRK11565 154 --VTPVINQIElHPLMQQRQLHA----WNATHKIQTESWSPLAQG------GKGVFDQ-------------------KVI 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15219795 249 RKvsglkpIADELGVTLAQLAIAWCASNPNVssVITGATRESQIQENMKAVD 300
Cdd:PRK11565 203 RD------LADKYGKTPAQIVIRWHLDSGLV--VIPKSVTPSRIAENFDVFD 246
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-300 |
2.62e-08 |
|
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: 54.41 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgRAE--EIMGQAIRELGWRRSDIVISTKIfWG 86
Cdd:cd19112 7 SGHKMPVIGLGVW-----RMEPGEIKELILNAIKIGYRHFDCAADYKN-EKEvgEALAEAFKTGLVKREDLFITTKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 87 gpgpNDKGlsrkHIVEGTKASLKRLDMDYVDVLYCHRP-----------------------DASTPIEETVRAMNYVIDK 143
Cdd:cd19112 80 ----SDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 144 GWAFYWGTSEWsaqqitEAWGAADRL--DLVGPIVEQPE-YNMFARHkvetEFLPLYTNHGIGLTTWSPLASGvltgkyn 220
Cdd:cd19112 152 GLVRSIGISNY------DIFLTRDCLaySKIKPAVNQIEtHPYFQRD----SLVKFCQKHGISVTAHTPLGGA------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 221 kgaipsdsrfaLENYKNLANRSLVDDVLrkvsgLKPIADELGVTLAQLAIAWcaSNPNVSSVITGATRESQIQENMKAVD 300
Cdd:cd19112 215 -----------AANAEWFGSVSPLDDPV-----LKDLAKKYGKSAAQIVLRW--GIQRNTAVIPKSSKPERLKENIDVFD 276
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
42-224 |
1.28e-07 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 51.84 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 42 DHGVNFFDNAEVYANgraEEIMGQAIRELGWRRSDIVISTKIFWGGPGPNDkglSRKHIVEgtkaSLKRLDMDYVDVLYC 121
Cdd:cd19130 34 EVGYRHIDTAAIYGN---EEGVGAAIAASGIPRDELFVTTKLWNDRHDGDE---PAAAFAE----SLAKLGLDQVDLYLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 122 HRP-DASTPIEETVRAMNYVIDKGWAFYWGTSEWSAQQITEAWGAADRLdlvgPIVEQPEYNMFARHKVETEFLplyTNH 200
Cdd:cd19130 104 HWPtPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVV----PAVNQIELHPAYQQRTIRDWA---QAH 176
|
170 180
....*....|....*....|....
gi 15219795 201 GIGLTTWSPLASGVLTGKYNKGAI 224
Cdd:cd19130 177 DVKIEAWSPLGQGKLLGDPPVGAI 200
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-300 |
2.92e-07 |
|
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: 51.29 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYANgraEEIMGQ----AIRELGWRRSDIVISTKIF 84
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGN---EKEVGEgvnrAIDEGLVKREELFLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 85 WGGPGPndkglsrKHIVEGTKASLKRLDMDYVDVLYCHRPDA-------------------------STPIEETVRAMNY 139
Cdd:cd19113 79 NNFHDP-------KNVETALNKTLSDLKLDYVDLFLIHFPIAfkfvpieekyppgfycgdgdnfvyeDVPILDTWKALEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 140 VIDKGWAFYWGTSEWSAQQITEAWGAADrldlVGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWsplasgvltgky 219
Cdd:cd19113 152 LVDAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHHPYLQQPKLIEYA---QKAGITITAY------------ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 220 nkgaipsdSRFALENYKNLAN-RSLVDDVLRKVSGLKPIADELGVTLAQLAIAWcASNPNVsSVITGATRESQIQENMKA 298
Cdd:cd19113 213 --------SSFGPQSFVELNQgRALNTPTLFEHDTIKSIAAKHNKTPAQVLLRW-ATQRGI-AVIPKSNLPERLLQNLSV 282
|
..
gi 15219795 299 VD 300
Cdd:cd19113 283 ND 284
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-300 |
7.58e-06 |
|
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: 47.03 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWVTFGNQldVKEA--KSIlqccrDHGVNFFDNAEVYANgraEEIMGQAI----RELGWRRSDIVISTKI 83
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQ--VTEAvkVAI-----DAGYRHIDCAYVYQN---ENEVGEAIqekiKEQVVKREDLFIVSKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 84 FwggPGPNDKGLSRkhivEGTKASLKRLDMDYVDVLYCHRP------DASTPIEE-------------TVRAMNYVIDKG 144
Cdd:cd19107 71 W---CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPtgfkpgKELFPLDEsgnvipsdttfldTWEAMEELVDEG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 145 WAFYWGTSEWSAQQIteawgaaDRLdLVGP-IVEQPEYNMFARHKVET-EFLPLYTN-HGIGLTTWSPLASgvltgKYNK 221
Cdd:cd19107 144 LVKAIGVSNFNHLQI-------ERI-LNKPgLKYKPAVNQIECHPYLTqEKLIQYCQsKGIVVTAYSPLGS-----PDRP 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15219795 222 GAIPSDSrfalenyknlanrSLVDDvlrkvSGLKPIADELGVTLAQLAIAWCASNpNVsSVITGATRESQIQENMKAVD 300
Cdd:cd19107 211 WAKPEDP-------------SLLED-----PKIKEIAAKHNKTTAQVLIRFPIQR-NL-VVIPKSVTPERIAENFKVFD 269
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-213 |
8.20e-06 |
|
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: 46.72 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWVTFGNQLDVKEA--KSILQccrdhGVNFFDNAEVYAngrAEEIMGQAIREL----GWRRSDIVISTK 82
Cdd:cd19119 8 TGASIPALGLGTASPHEDRAEVKEAveAAIKE-----GYRHIDTAYAYE---TEDFVGEAIKRAiddgSIKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 83 I---FWggpgpndkglsrKHIVEGTKASLKRLDMDYVDVLYCHRPDASTPI-EETVRAMNYVIDKGWAFYWGTSEW--SA 156
Cdd:cd19119 80 VwptFY------------DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDsDDSGKPFTPVNDDGKTRYAASGDHitTY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219795 157 QQITEAW--GAADRLDL----------------VGPIVEQPEYNMFARHKVETEFLplyTNHGIGLTTWSPLASG 213
Cdd:cd19119 148 KQLEKIYldGRAKAIGVsnysivylerlikeckVVPAVNQVELHPHLPQMDLRDFC---FKHGILVTAYSPLGSH 219
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-300 |
1.52e-05 |
|
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: 45.87 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 9 SGLKVSTLSFGAWvtfgnqldvKEAKSIlqcCRDH-------GVNFFDNAEVYANGR-AEEIMGQAIRELGWRRSDIVIS 80
Cdd:cd19115 9 SGYDMPLVGFGLW---------KVNNDT---CADQvynaikaGYRLFDGACDYGNEVeAGQGVARAIKEGIVKREDLFIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 81 TKIfWGGPgpNDKglsrKHIVEGTKASLKRLDMDYVDVLYCHRPDA------------------------STPIEETVRA 136
Cdd:cd19115 77 SKL-WNTF--HDG----ERVEPICRKQLADWGIDYFDLFLIHFPIAlkyvdpavryppgwfydgkkvefsNAPIQETWTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 137 MNYVIDKGWAFYWGTSEWSAQQITEAWgaadRLDLVGPIVEQPEYNMFArhkVETEFLPLYTNHGIGLTTWSPLasGVLt 216
Cdd:cd19115 150 MEKLVDKGLARSIGVSNFSAQLLMDLL----RYARIRPATLQIEHHPYL---TQPRLVKYAQKEGIAVTAYSSF--GPQ- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 217 gkynkgaipSDSRFALENYKNLAnrSLVD-DVLRKvsglkpIADELGVTLAQLAIAWcASNPNVsSVITGATRESQIQEN 295
Cdd:cd19115 220 ---------SFLELDLPGAKDTP--PLFEhDVIKS------IAEKHGKTPAQVLLRW-ATQRGI-AVIPKSNNPKRLAQN 280
|
....*
gi 15219795 296 MKAVD 300
Cdd:cd19115 281 LDVTG 285
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-272 |
2.24e-05 |
|
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: 45.24 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 10 GLKVSTLSFGAWvtfgnQLDVKEAKSILQCCRDHGVNFFDNAEVYAN----GRAeeiMGQAIRELGWRRSDIVISTKIfW 85
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGNeaevGRG---IRKAIQEGLVKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 86 ggpgpnDKGLSRKHIVEGTKASLKRLDMDYVDVLYCHRPDA-------------------------STPIEETVRAMNYV 140
Cdd:cd19114 72 ------NNFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 141 IDKGWAFYWGTSEWSAQQIteawgaadrLDL-----VGPIVEQPEYNMFARHKvetEFLPLYTNHGIGLTTWSPLASGVL 215
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLI---------LDLltyakIKPAVLQIEHHPYLQQK---RLIDWAKKQGIQITAYSSFGNAVY 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15219795 216 TgkynkgaipsdsRFALENyKNLANrslvddvLRKVSGLKPIADELGVTLAQLAIAW 272
Cdd:cd19114 214 T------------KVTKHL-KHFTN-------LLEHPVVKKLADKHKRDTGQVLLRW 250
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
42-132 |
4.67e-04 |
|
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: 41.45 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219795 42 DHGVNFFDNAEVYANgraEEIMGQAIR---ELGW-RRSDIVISTKIfWGGpgpndkgLSRKHIVE-GTKASLKRLDMDYV 116
Cdd:cd19108 38 DAGFRHIDSAYLYQN---EEEVGQAIRskiADGTvKREDIFYTSKL-WCT-------FHRPELVRpALEKSLKKLQLDYV 106
|
90
....*....|....*.
gi 15219795 117 DVLYCHRPDASTPIEE 132
Cdd:cd19108 107 DLYLIHFPVALKPGEE 122
|
|
| |
