|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
14-332 |
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: 588.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGWLTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVIT 93
Cdd:cd19143 2 EYRRLGRSGLKVSALSFGSWVTFGNQV-DVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 94 TKVFFGAGTKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFE 173
Cdd:cd19143 81 TKIFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 174 IEHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTTFTSLAG 253
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076016 254 QLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKIDEI 332
Cdd:cd19143 241 DRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
22-325 |
2.05e-144 |
|
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: 409.67 E-value: 2.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKelGWDRSEYVITTKVFFGAG 101
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQV-DDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 102 TKlPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIA 181
Cdd:cd19074 78 PG-PNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 182 TKYNLIAPVADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTTFTSLAGQLQTPEGK 261
Cdd:cd19074 157 RQFGLIPPVVEQPQYNMLWREI-EEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEDNRDKKRRLLTD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076016 262 TQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEI 325
Cdd:cd19074 236 ENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGV--KLSPEV 297
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
14-325 |
8.31e-124 |
|
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: 357.91 E-value: 8.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGWLTYGNEGYDvEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVIT 93
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISD-EVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 94 TKVFFGAgtKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFE 173
Cdd:cd19141 80 TKIFWGG--KAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAME 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 174 IEHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLS-TTFTSLA 252
Cdd:cd19141 158 IMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASlKGYQWLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 253 GQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEI 325
Cdd:cd19141 238 EKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
14-333 |
1.96e-115 |
|
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: 336.77 E-value: 1.96e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGWlTYGNE--GYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKelGWDRSEYV 91
Cdd:COG0667 2 EYRRLGRSGLKVSRLGLGTM-TFGGPwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 92 ITTKVFFGAGTKlPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSA 171
Cdd:COG0667 79 IATKVGRRMGPG-PNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 172 FEIEHAHHIATkyNLIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDG--IPEGSRLSTTFT 249
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATNFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 250 SLAGqlqTPEGktqLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKI 329
Cdd:COG0667 235 QGYL---TERN---LALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAAL 306
|
....
gi 19076016 330 DEIL 333
Cdd:COG0667 307 DAAL 310
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
15-333 |
2.92e-114 |
|
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: 334.21 E-value: 2.92e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGWLTYGNEGYDvEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITT 94
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISD-EMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 95 KVFFGaGTKlPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEI 174
Cdd:TIGR01293 80 KIFWG-GKA-ETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 175 EHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLST-TFTSLAG 253
Cdd:TIGR01293 158 MEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLkGYQWLKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 254 QLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKIDEIL 333
Cdd:TIGR01293 238 KILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-337 |
3.74e-112 |
|
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: 329.25 E-value: 3.74e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 13 VPFRFLGRSGLKVSAFSLGGWLTYGNEGYDvEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVI 92
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISD-ETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKVFFGAGTKlpNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAF 172
Cdd:cd19160 82 TTKIYWGGQAE--TERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 173 EIEHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTT-FTSL 251
Cdd:cd19160 160 EIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKgYQWL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 252 AGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKIDE 331
Cdd:cd19160 240 KEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDA 319
|
....*.
gi 19076016 332 ILNFTP 337
Cdd:cd19160 320 LLGNKP 325
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
13-337 |
1.58e-111 |
|
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: 327.38 E-value: 1.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 13 VPFRFLGRSGLKVSAFSLGGWLTYGNEGYDvEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVI 92
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKVFFGAgtKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAF 172
Cdd:cd19159 80 TTKLYWGG--KAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 173 EIEHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLS-TTFTSL 251
Cdd:cd19159 158 EIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlKCYQWL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 252 AGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKIDE 331
Cdd:cd19159 238 KERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDN 317
|
....*.
gi 19076016 332 ILNFTP 337
Cdd:cd19159 318 ILRNKP 323
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
15-337 |
1.69e-103 |
|
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: 307.01 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGWLTYGNEGYDvEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITT 94
Cdd:cd19158 3 YRNLGKSGLRVSCLGLGTWVTFGGQITD-EMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 95 KVFFGAgtKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEI 174
Cdd:cd19158 82 KIFWGG--KAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 175 EHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTT-FTSLAG 253
Cdd:cd19158 160 MEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKgYQWLKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 254 QLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKIDEIL 333
Cdd:cd19158 240 KILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSIL 319
|
....
gi 19076016 334 NFTP 337
Cdd:cd19158 320 GNKP 323
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
18-327 |
8.10e-102 |
|
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: 302.20 E-value: 8.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 18 LGRSGLKVSAFSLGGWlTYGNEGY-----DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwDRSEYVI 92
Cdd:cd19079 5 LGNSGLKVSRLCLGCM-SFGDPKWrpwvlDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKVFFGAGtKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAF 172
Cdd:cd19079 83 ATKVYFPMG-DGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 173 EIEHAHHIATKYNLIAPVADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGipeGSRLSTTFTSLA 252
Cdd:cd19079 162 QFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDT---TERRRSTTDTAK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076016 253 GQLQ--TPEGKTQLDQVRqisKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILK 327
Cdd:cd19079 238 LKYDyfTEADKEIVDRVE---EVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLSEEEIK 309
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
15-332 |
4.98e-98 |
|
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: 292.55 E-value: 4.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGwLTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgwDRSEYVITT 94
Cdd:cd19087 3 YRTLGRTGLKVSRLCLGT-MNFGGRT-DEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 95 KVFFGAGTKlPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEI 174
Cdd:cd19087 78 KVFGPMGDD-PNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 175 EHAHHIATKYNLIAPVADQPQYNYLTRdHFEKDLLPLQQIYGYGATVWSPLKSGILTGKY--NDGIPEGSRLSTTFTSLA 252
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKR-QAELEILPAARAYGLGVIPYSPLAGGLLTGKYgkGKRPESGRLVERARYQAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 253 GQLQtpegkTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19087 236 YGLE-----EYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
15-332 |
2.49e-94 |
|
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: 283.35 E-value: 2.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGwLTYGNEGY--------DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgwD 86
Cdd:cd19091 3 YRTLGRSGLKVSELALGT-MTFGGGGGffgawggvDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 87 RSEYVITTKVFF--GAGtklPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYW 164
Cdd:cd19091 79 RDDVLIATKVRGrmGEG---PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 165 GTSEWSAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKY--NDGIPEGS 242
Cdd:cd19091 156 GVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 243 RLSTTftslAGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLT 322
Cdd:cd19091 235 RLRRT----GFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--SLT 308
|
330
....*....|
gi 19076016 323 PEILKKIDEI 332
Cdd:cd19091 309 PEEIARLDKV 318
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
15-337 |
2.62e-91 |
|
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: 275.88 E-value: 2.62e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGWLTYGNeGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITT 94
Cdd:cd19142 3 YRNLGKSGLRVSNVGLGTWSTFST-AISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 95 KVFFGAGtklPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEI 174
Cdd:cd19142 82 KIYWSYG---SEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 175 EHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTTF-TSLAG 253
Cdd:cd19142 159 MEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSsKYKVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 254 QLQTPEGKT---QLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKID 330
Cdd:cd19142 239 SDGNGIHEEtrrASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELE 318
|
....*..
gi 19076016 331 EILNFTP 337
Cdd:cd19142 319 RILDNKP 325
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
17-330 |
1.52e-83 |
|
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: 255.60 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 17 FLGRSGLKVSAFSLGGWlTYGnEGYDVEHTKNCLKQAWDLGINTFDTAEIYS-------NGNSETVMGKAIKELGwDRSE 89
Cdd:cd19081 1 PLGRTGLSVSPLCLGTM-VFG-WTADEETSFALLDAFVDAGGNFIDTADVYSawvpgnaGGESETIIGRWLKSRG-KRDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 90 YVITTKVFFGAGtklPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEW 169
Cdd:cd19081 78 VVIATKVGFPMG---PNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 170 SAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYN-DGIPEGSRLSTTF 248
Cdd:cd19081 155 SAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRsEADLPGSTRRGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 249 tslAGQLQTPEGKTQLDQVRQiskIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKK 328
Cdd:cd19081 235 ---AKRYLNERGLRILDALDE---VAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVAR 306
|
..
gi 19076016 329 ID 330
Cdd:cd19081 307 LD 308
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-327 |
4.71e-83 |
|
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: 254.10 E-value: 4.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGWLTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIY--SNGNSETVMGKAIKE-LGWDRSEYV 91
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYT-SPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 92 ITTKVFFGAGtKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSA 171
Cdd:cd19089 80 ISTKAGYGMW-PGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 172 FEIEHAHHIATKYNlIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTTFTSL 251
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDRW-AEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 252 AGQLQTPEgktQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDkLTPEILK 327
Cdd:cd19089 237 TEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD-FSEEELA 308
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-330 |
2.63e-82 |
|
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: 251.68 E-value: 2.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWlTYGNEGY---DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSEYVITTKV-- 96
Cdd:cd19084 1 DLKVSRIGLGTW-AIGGTWWgevDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVIATKCgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 -FFGAGTKLPNttgLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIE 175
Cdd:cd19084 77 rWDGGKGVTKD---LSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 176 HAHhiatkyNLIAPVADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGI---PEGSRLSTTFtsla 252
Cdd:cd19084 154 EAR------KYGPIVSLQPPYSMLEREI-EEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRRSRFPF---- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19076016 253 gqLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19084 223 --FRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
16-330 |
1.51e-75 |
|
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: 234.81 E-value: 1.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 16 RFLGRSGLKVSAFSLGGwLTYGNE---GYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgwDRSEYVI 92
Cdd:cd19080 1 RLLGRSGLRVSPLALGT-MTFGTEwgwGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKVFFGAGTKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAF 172
Cdd:cd19080 77 ATKYTMNRRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 173 EIEHAHHIATKYNLIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGipEGSRLSTTFTSLA 252
Cdd:cd19080 157 VVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTV 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19076016 253 GQLQTPEGKTQLDQVRQisKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19080 234 GFGKLTERNWAIVDVVA--AVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
15-315 |
2.18e-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: 231.91 E-value: 2.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGWLTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIYS--NGNSETVMGKAIKE--LGWdRSEY 90
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVD-RYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPY-RDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 91 VITTKvffgAGTKL---PNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTS 167
Cdd:cd19151 80 IISTK----AGYTMwpgPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 168 EWSAFEIEHAHHIATkyNLIAP-VADQPQYNYLTRdHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLST 246
Cdd:cd19151 156 NYPPEEAREAAAILK--DLGTPcLIHQPKYSMFNR-WVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076016 247 TFTSLAGQLQTPEgktQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAV 315
Cdd:cd19151 233 GSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGAL 298
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
30-333 |
2.85e-73 |
|
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: 228.35 E-value: 2.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 30 LGGW-LTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITTKVFFGAGtklPNTT 108
Cdd:pfam00248 3 LGTWqLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDG---PWPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 109 GLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHhiatKYNLIA 188
Cdd:pfam00248 80 GGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAL----TKGKIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 189 PVADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRlsttftsLAGQLQTPEGKTQLDQVR 268
Cdd:pfam00248 156 IVAVQVEYNLLRRRQ-EEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG-------ERRRLLKKGTPLNLEALE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076016 269 QISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKIDEIL 333
Cdd:pfam00248 228 ALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEF--PLSDEEVARIDELL 290
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
26-313 |
9.65e-73 |
|
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: 225.09 E-value: 9.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 26 SAFSLGGWlTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwDRSEYVITTKVFFGAGTKlP 105
Cdd:cd06660 1 SRLGLGTM-TFGGDG-DEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGGHPPGGD-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 106 NTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYN 185
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 186 LIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGiltgkyndgipegsrlsttftslagqlqtpegktqld 265
Cdd:cd06660 157 LPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19076016 266 qvrqiskiaeqigatPSQLALAWTLKNPYVSTTILGASKPEQIVENVK 313
Cdd:cd06660 200 ---------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
14-319 |
2.89e-71 |
|
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: 224.26 E-value: 2.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGWLTYGNEGyDVEHTKNCLKQAWDLGINTFDTAEIYS--NGNSETVMGKAIKE-LGWDRSEY 90
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDT-PLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdFAGYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 91 VITTKvffgAGTKL---PNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTS 167
Cdd:cd19150 80 IISTK----AGYDMwpgPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 168 EWSAFEIEHAHHIATKYNlIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTT 247
Cdd:cd19150 156 SYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076016 248 fTSLAGQLQTPEgktQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFID 319
Cdd:cd19150 235 -RSLSPKMLTEA---NLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLT 302
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
11-331 |
4.31e-68 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 217.16 E-value: 4.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 11 KNVPFRFLGRSGLKVSAFSLGGWLTYG-NEGYDVEHTknCLKQAWDLGINTFDTAEIYS--NGNSETVMGKAIKE-LGWD 86
Cdd:PRK09912 11 GQMQYRYCGKSGLRLPALSLGLWHNFGhVNALESQRA--ILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdFAAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 87 RSEYVITTKvffgAGTKL---PNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFY 163
Cdd:PRK09912 89 RDELIISTK----AGYDMwpgPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 164 WGTSEWSAFEIEHAHHIATKYNlIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSR 243
Cdd:PRK09912 165 VGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 244 LSTTFTSLAGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIdKLTP 323
Cdd:PRK09912 244 MHREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL-TFST 322
|
....*...
gi 19076016 324 EILKKIDE 331
Cdd:PRK09912 323 EELAQIDQ 330
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
55-332 |
6.97e-63 |
|
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: 202.40 E-value: 6.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 55 DLGINTFDTAEIYSNGNSETVMGkaikELGWDRSEYVITTKVFFGagtklpNTTGLSRKHIIEGLNASLKRLGLPYVDVI 134
Cdd:cd19075 31 ERGHTEIDTARVYPDGTSEELLG----ELGLGERGFKIDTKANPG------VGGGLSPENVRKQLETSLKRLKVDKVDVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 135 MAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDHfEKDLLPLQQI 214
Cdd:cd19075 101 YLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITRQV-ETELFPCLRK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 215 YGYGATVWSPLKSGILTGKYNDG--IPEGSRLSTTfTSLAGQLQTPEGK-TQLDQVRQISKIAEQIGATPSQLALAWT-- 289
Cdd:cd19075 180 LGIRFYAYSPLAGGFLTGKYKYSedKAGGGRFDPN-NALGKLYRDRYWKpSYFEALEKVEEAAEKEGISLAEAALRWLyh 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19076016 290 ---LKNPYVSTTILGASKPEQIVENVKAVEfIDKLTPEILKKIDEI 332
Cdd:cd19075 259 hsaLDGEKGDGVILGASSLEQLEENLAALE-KGPLPEEVVKAIDEA 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
22-333 |
4.48e-62 |
|
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: 200.15 E-value: 4.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLG--GwLTYGnEGY--DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSEYVITTKVF 97
Cdd:cd19078 1 GLEVSAIGLGcmG-MSHG-YGPppDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF---RDQVVIATKFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 98 FGAGTKLPNTTGL--SRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIE 175
Cdd:cd19078 76 FKIDGGKPGPLGLdsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 176 HAHHiatkynlIAPV-ADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNdgipEGSRL-STTFTSLAG 253
Cdd:cd19078 156 RAHA-------VCPVtAVQSEYSMMWREP-EKEVLPTLEELGIGFVPFSPLGKGFLTGKID----ENTKFdEGDDRASLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 254 QLqTPEG-KTQLDQVRQISKIAEQIGATPSQLALAWTL-KNPYVsTTILGASKPEQIVENVKAVEFIdkLTPEILKKIDE 331
Cdd:cd19078 224 RF-TPEAlEANQALVDLLKEFAEEKGATPAQIALAWLLaKKPWI-VPIPGTTKLSRLEENIGAADIE--LTPEELREIED 299
|
..
gi 19076016 332 IL 333
Cdd:cd19078 300 AL 301
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-333 |
3.04e-61 |
|
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: 197.90 E-value: 3.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 31 GGWLTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSEYVITTKVFFGAGTKLPNTTGL 110
Cdd:cd19102 13 GGGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCGLLWDEEGRIRRSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 111 SRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAhhiatkyNLIAPV 190
Cdd:cd19102 90 KPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRC-------QAIHPI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 191 AD-QPQYNYLTRdHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYN---------DGIPEGSRlsttftslagQLQTPEG 260
Cdd:cd19102 163 ASlQPPYSLLRR-GIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTpervaslpaDDWRRRSP----------FFQEPNL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 261 KTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKIDEIL 333
Cdd:cd19102 232 ARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
25-332 |
1.14e-60 |
|
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: 196.27 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 25 VSAFSLGGWLTYGNEGY---DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSEYVITTKVFFGag 101
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWgdqDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGR---RDDVVIATKVSPD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 102 tklpnttGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIA 181
Cdd:cd19085 76 -------NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 182 TkynliaPVADQPQYNYLTRdHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDG--IPEGSRLSTTFtsLAGQLQTpE 259
Cdd:cd19085 149 R------IDSNQLPYNLLWR-AIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAedFPPGDARTRLF--RHFEPGA-E 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 260 GKTqLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19085 219 EET-FEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-331 |
7.42e-60 |
|
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: 194.80 E-value: 7.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLG-----GWLTYGneGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSE 89
Cdd:cd19149 1 YRKLGKSGIEASVIGLGtwaigGGPWWG--GSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---RDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 90 YVITTK------------VFFGAGTKLPNTtgLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQ 157
Cdd:cd19149 76 VVLATKcglrwdreggsfFFVRDGVTVYKN--LSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 158 DGKAFYWGTSEWSAFEIEHAHhiatKYNLIApvADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDG 237
Cdd:cd19149 154 QGKIRAIGASNVSVEQIKEYV----KAGQLD--IIQEKYSMLDRGI-EKELLPYCKKNNIAFQAYSPLEQGLLTGKITPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 238 ---IPEGSRLSTTFTSlagqlqtPEGKTQ-LDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVK 313
Cdd:cd19149 227 refDAGDARSGIPWFS-------PENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAK 299
|
330
....*....|....*...
gi 19076016 314 AVEFidKLTPEILKKIDE 331
Cdd:cd19149 300 AGDI--RLSAEDIATMRS 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-329 |
2.45e-58 |
|
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: 190.50 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLG--GwLT--YGneGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSE 89
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmG-MSafYG--PADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDR---RDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 90 YVITTKvfFGAgTKLPNTTGL----SRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWG 165
Cdd:cd19076 75 VVIATK--FGI-VRDPGSGFRgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 166 TSEWSAFEIEHAHHiatkynlIAPV-ADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKYN--DGIPEGS 242
Cdd:cd19076 152 LSEASADTIRRAHA-------VHPItAVQSEYSLWTRD-IEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKspEDLPEDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 243 rlsttFTSLAGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKN-----PyvsttILGASKPEQIVENVKAVEf 317
Cdd:cd19076 224 -----FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQgddivP-----IPGTKRIKYLEENVGALD- 292
|
330
....*....|..
gi 19076016 318 iDKLTPEILKKI 329
Cdd:cd19076 293 -VVLTPEELAEI 303
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
53-332 |
3.43e-58 |
|
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: 190.85 E-value: 3.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 53 AWDLGINTFDTAEIYS-------NGNSETVMGKAIKELGwDRSEYVITTKVFfGAGTKLP----NTTGLSRKHIIEGLNA 121
Cdd:cd19094 27 AFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVA-GPGEGITwprgGGTRLDRENIREAVEG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 122 SLKRLGLPYVDVIMAHRPD------------------PSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATK 183
Cdd:cd19094 105 SLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 184 YNLIAPVADQPQYNYLTRdHFEKDL--------LPLQqiygygatVWSPLKSGILTGKYNDG--IPEGSRLsTTFTSLAG 253
Cdd:cd19094 185 LGLPRIVSIQNPYSLLNR-NFEEGLaeachrenVGLL--------AYSPLAGGVLTGKYLDGaaRPEGGRL-NLFPGYMA 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076016 254 QLQTPegkTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIdkLTPEILKKIDEI 332
Cdd:cd19094 255 RYRSP---QALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVP--LSDELLAEIDAV 328
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
22-330 |
4.74e-57 |
|
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: 185.90 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEGYDVEHTKN---CLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKelGWDRSEYVITTKVff 98
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDKKaieALRYAIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFITTKV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 99 gagtklpNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAH 178
Cdd:cd19072 77 -------SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 179 HIATKYnliAPVADQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKyndgipegsrlsttftslagqlqtp 258
Cdd:cd19072 150 SYLKKG---PIVANQVEYNLFDREE-ESGLLPYCQKNGIAIIAYSPLEKGKLSNA------------------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076016 259 egktqlDQVRQISKIAEQIGATPSQLALAWTLKNPYVsTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19072 201 ------KGSPLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALGW--ELSEEDLQRLD 263
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
18-332 |
1.34e-56 |
|
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: 186.09 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 18 LGRSGLKVSAFSLGGWLTYGNEGY---DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgWDRSEYVITT 94
Cdd:cd19083 4 LGKSDIDVNPIGLGTNAVGGHNLYpnlDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKE--YNRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 95 K---VFFGAGTKLPNttglSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSA 171
Cdd:cd19083 82 KgahKFGGDGSVLNN----SPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 172 FEIEHAHHiATKYNLIapvadQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDG--IPEGSrlsttFT 249
Cdd:cd19083 158 EQLKEANK-DGYVDVL-----QGEYNLLQREA-EEDILPYCVENNISFIPYFPLASGLLAGKYTKDtkFPDND-----LR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 250 SLAGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKI 329
Cdd:cd19083 226 NDKPLFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFI 303
|
...
gi 19076016 330 DEI 332
Cdd:cd19083 304 DAL 306
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
18-324 |
6.00e-51 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 171.10 E-value: 6.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 18 LGRSGLKVSAFSLGGWlTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITTKvf 97
Cdd:COG4989 6 LGASGLSVSRIVLGCM-RLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTK-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 98 fgAGTKLPNTTG--------LSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEW 169
Cdd:COG4989 83 --CGIRLPSEARdnrvkhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 170 SAFEIEH-AHHIATKynliaPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDgipegsrlsttf 248
Cdd:COG4989 161 TPSQFELlQSALDQP-----LVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGGFDE------------ 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 249 tslagqlQTPEGKTQLDqvrqisKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPE 324
Cdd:COG4989 224 -------QFPRLRAALD------ELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDI--ELTRE 284
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
23-314 |
9.66e-51 |
|
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: 168.81 E-value: 9.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 23 LKVSAFSLGGWlTYGNEGY---DVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgwDRSEYVITTKVFFG 99
Cdd:cd19086 1 LEVSEIGFGTW-GLGGDWWgdvDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFGNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 100 AGTKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSV-PMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHah 178
Cdd:cd19086 77 FDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVlDNDELFEALEKLKQEGKIRAYGVSVGDPEEALA-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 179 hiATKYNLIAPVadQPQYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGKyndgipegsrlsttftslagqlqtp 258
Cdd:cd19086 155 --ALRRGGIDVV--QVIYNLLDQRP-EEELFPLAEEHGVGVIARVPLASGLLTGK------------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 259 egktqldqvrqiskiaeqigatPSQLALAWTLKNPYVSTTILGASKPEQIVENVKA 314
Cdd:cd19086 205 ----------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
24-330 |
3.10e-50 |
|
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: 169.33 E-value: 3.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 24 KVSAFSLGGW-----LTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwDRSEYVITTKVFf 98
Cdd:cd19093 1 EVSPLGLGTWqwgdrLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKFA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 99 gagtKLPNTtgLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVP-MEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHA 177
Cdd:cd19093 79 ----PLPWR--LTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSqIEALMDGLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 178 HHiATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYN-DGIPEGSRlsttftslaGQLQ 256
Cdd:cd19093 153 HK-ALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSpENPPPGGR---------RRLF 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 257 TPEGKTQLDQVRQ-ISKIAEQIGATPSQLALAWTL-KNPYVsttILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19093 223 GRKNLEKVQPLLDaLEEIAEKYGKTPAQVALNWLIaKGVVP---IPGAKNAEQAEENAGALGW--RLSEEEVAELD 293
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-317 |
6.68e-47 |
|
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: 160.41 E-value: 6.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWlTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITTK--VFF 98
Cdd:cd19092 2 EGLEVSRLVLGCM-RLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 99 GAgTKLPNTTG---LSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIE 175
Cdd:cd19092 81 GD-DPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 176 hahhiATKYNLIAP-VADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLksgiltgkyndgipEGSRLSTTFTSLAGQ 254
Cdd:cd19092 160 -----LLQSYLDQPlVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPL--------------GGGRLFGGFDERFQR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 255 LqtpegktqldqVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEF 317
Cdd:cd19092 221 L-----------RAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
21-332 |
1.56e-43 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 150.59 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGgwlTYGNEGydvEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVffga 100
Cdd:COG0656 1 NGVEIPALGLG---TWQLPG---EEAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAASGVPREELFVTTKV---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 101 gtklpNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPsVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHI 180
Cdd:COG0656 68 -----WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGP-GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 181 ATkynlIAPVADQPQYN-YLTrdhfEKDLLPLQQIYGYGATVWSPLKSGILtgkyndgipegsrlsttftslagqLQTPE 259
Cdd:COG0656 142 TG----VKPAVNQVELHpYLQ----QRELLAFCREHGIVVEAYSPLGRGKL------------------------LDDPV 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 260 gktqldqvrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:COG0656 190 ----------LAEIAEKHGKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-315 |
2.13e-43 |
|
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: 150.04 E-value: 2.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 13 VPFRFLGRSGLKVSAFSLGGwltygneGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKelGWDRSEYVI 92
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG-------GGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALK--GLRRDKVFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKVFFGAGTKlpnttglSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVP---MEEVVRAFTQLIQDGKAFYWGTSEw 169
Cdd:cd19105 72 ATKASPRLDKK-------DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEErllNEELLEALEKLKKEGKVRFIGFST- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 170 safeiehaHHIATkyNLIAPVAD-------QPQYNYLTRDHFEKDLLPLQQiygygatvwsplKSGIltgkyndGIpegs 242
Cdd:cd19105 144 --------HDNMA--EVLQAAIEsgwfdviMVAYNFLNQPAELEEALAAAA------------EKGI-------GV---- 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 243 rlsTTFTSLAGQLQTPEGKTQLdqvrqiskiaEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAV 315
Cdd:cd19105 191 ---VAMKTLAGGYLQPALLSVL----------KAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-316 |
9.19e-43 |
|
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: 149.79 E-value: 9.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 50 LKQAWDLGINTFDTAEIYS-------NGNSETVMGKAIKELGwDRSEYVITTKVFFG---AGTKLPNTTGLSRKHIIEGL 119
Cdd:cd19752 23 LDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVGAGprdPDGGPESPEGLSAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 120 NASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYNLIAPVADQPQYNYL 199
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 200 TRDH---FEKDLLPLQQIYGYGA-----TVW--SPLKSGILTgkyNDGIPegsrlsttftsLAGQLQTPEGKTQLdqvRQ 269
Cdd:cd19752 182 RPRPgadFGVQRIVTDELLDYASsrpdlTLLaySPLLSGAYT---RPDRP-----------LPEQYDGPDSDARL---AV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19076016 270 ISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVE 316
Cdd:cd19752 245 LEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
21-330 |
1.19e-42 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 148.55 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWlTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgwDRSEYVITTKVffga 100
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 101 gtkLPntTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDpSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHI 180
Cdd:cd19138 79 ---LP--SNASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 181 ATKYNLiapVADQPQYNyLTRDHFEKDLLPLQQIYGYGATVWSPLKSGiltGKYNDGIPEGSRLsttftslagqlqtpeg 260
Cdd:cd19138 153 PGGGNC---AANQVLYN-LGSRGIEYDLLPWCREHGVPVMAYSPLAQG---GLLRRGLLENPTL---------------- 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 261 ktqldqvrqiSKIAEQIGATPSQLALAWTLKNPYVsTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19138 210 ----------KEIAARHGATPAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
22-333 |
1.88e-42 |
|
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: 149.38 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNE--GYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwDRSEYVITTKV--- 96
Cdd:cd19148 1 DLPVSRIALGTWAIGGWMwgGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKVgle 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 FFGAGTKLPNTtglSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEh 176
Cdd:cd19148 80 WDEGGEVVRNS---SPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQME- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 177 ahhiatKYNLIAPVAD-QPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNdgipegsrLSTTFT-----S 250
Cdd:cd19148 156 ------TFRKVAPLHTvQPPYNLFERE-IEKDVLPYARKHNIVTLAYGALCRGLLSGKMT--------KDTKFEgddlrR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 251 LAGQLQTPEGKTQLDQVRQISKIA-EQIGATPSQLALAWTLKNPYVSTTILGASKPEQIvenvKAVEFID--KLTPEILK 327
Cdd:cd19148 221 TDPKFQEPRFSQYLAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL----DAVDEVFgwSLNDEDMK 296
|
....*.
gi 19076016 328 KIDEIL 333
Cdd:cd19148 297 EIDAIL 302
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
22-330 |
1.03e-41 |
|
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: 146.18 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEGYDV---EHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgWDRSEYVITTKVFf 98
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDYsrdEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 99 gagtklpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAh 178
Cdd:cd19137 78 --------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 179 hiaTKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKyndgipegsrlsttftslagqlqtp 258
Cdd:cd19137 149 ---ISKSQTPIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN------------------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076016 259 egktqldqvRQISKIAEQIGATPSQLALAWTLKNPYVsTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19137 201 ---------RTLEEIAKNYGKTIAQIALAWLIQKPNV-VAIPKAGRVEHLKENLKATEI--KLSEEEMKLLD 260
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
42-316 |
5.19e-41 |
|
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: 145.00 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 42 DVEHTKNCLKQAWDLGINTFDTAEIYSN----GNSETVMGKAIKELGwDRSEYVITTKvffGAGTKLPNTTG--LSRKHI 115
Cdd:cd19082 15 DEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGHPDLEDMSRsrLSPEDI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 116 IEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYNLIAPVADQPQ 195
Cdd:cd19082 91 RADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 196 YN---------------YLT---RDHFEKDLLPLqqiygygaTVWSPLKSGILTGKYNDGIPEGSRLSTTFTSlagqlqt 257
Cdd:cd19082 171 WSlarpneppwpgptlvAMDeemRAWHEENQLPV--------FAYSSQARGFFSKRAAGGAEDDSELRRVYYS------- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19076016 258 PEGKTQLDQVRQiskIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVE 316
Cdd:cd19082 236 EENFERLERAKE---LAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-332 |
5.68e-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: 143.35 E-value: 5.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 13 VPFRFLGRSGLKVSAFSLGGW---LTYGNEGYDvEHTKNCLKQAWDLGINTFDTAEIYsnGNSETVMGKAIKELGWDRSE 89
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPD-EERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 90 YVITTKVffgaGTKLPNTTGL-----SRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYW 164
Cdd:cd19144 78 IFLATKF----GIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 165 GTSEWSAFEIEHAHHiatkynlIAPV-ADQPQYNYLTRDHFEKDLLPLQQIYGYGATV--WSPLKSGILTGKYN--DGIP 239
Cdd:cd19144 154 GLSECSAETLRRAHA-------VHPIaAVQIEYSPFSLDIERPEIGVLDTCRELGVAIvaYSPLGRGFLTGAIRspDDFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 240 EGSrlsttFTSLAGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFid 319
Cdd:cd19144 227 EGD-----FRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV-- 299
|
330
....*....|...
gi 19076016 320 KLTPEILKKIDEI 332
Cdd:cd19144 300 KLTEEEEKEIREI 312
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
18-329 |
6.34e-40 |
|
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: 142.57 E-value: 6.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 18 LGRSGLKVSAFSLGGWLTYGNEGYDVEHTK--NCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEyvITTK 95
Cdd:cd19145 5 LGSQGLEVSAQGLGCMGLSGDYGAPKPEEEgiALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQ--LATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 VffgaGTKLPNTTGLSRK----HIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSA 171
Cdd:cd19145 83 F----GIHEIGGSGVEVRgdpaYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 172 FEIEHAHhiatkynLIAPV-ADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGKYN-DGIPEGSRLSTTFT 249
Cdd:cd19145 159 DTIRRAH-------AVHPItAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKlEELLENSDVRKSHP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 250 SLAGQlqtpegktQLDQVRQ----ISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEI 325
Cdd:cd19145 231 RFQGE--------NLEKNKVlyerVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSV--KLTKED 300
|
....
gi 19076016 326 LKKI 329
Cdd:cd19145 301 LKEI 304
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-332 |
1.27e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 139.71 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 16 RFLGRSGLKVSAFSLGGwltyGNEGYDVEHTKN-----CLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwdRSEY 90
Cdd:cd19104 3 RRFGRTGLKVSELTFGG----GGIGGLMGRTTReeqiaAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 91 VITTKVFFGAGTkLPNTTGlsrkHIIEGLNASLKRLGLPYVDVIMAH---RPDPSVPM------------EEVVRAFTQL 155
Cdd:cd19104 76 YITTKVRLDPDD-LGDIGG----QIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVggtlsttdvlglGGVADAFERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 156 IQDGKAFYWGTSEWS-------AFEIEHAHHIATKYNLI------APVADQPQYNYltrdhfeKDLLPLQQIYGYGATVW 222
Cdd:cd19104 151 RSEGKIRFIGITGLGnppaireLLDSGKFDAVQVYYNLLnpsaaeARPRGWSAQDY-------GGIIDAAAEHGVGVMGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 223 SPLKSGILTGKYNDGIPEGSRLSTTFTslagqlqtpegkTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGA 302
Cdd:cd19104 224 RVLAAGALTTSLDRGREAPPTSDSDVA------------IDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGV 291
|
330 340 350
....*....|....*....|....*....|
gi 19076016 303 SKPEQIVENVKAVEFiDKLTPEILKKIDEI 332
Cdd:cd19104 292 KNREELEEAVAAEAA-GPLPAENLARLEAL 320
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
26-314 |
1.28e-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: 137.75 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 26 SAFSLGGWLTYGNEGY-DVEHTKNCLKQAWDLGINTFDTAEIYsnGNSETVMGKAIKELgwDRSEYVITTKVffgaGTKL 104
Cdd:cd19095 1 SVLGLGTSGIGRVWGVpSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGL--RRDDLFIATKV----GTHG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 105 PNTTGL---SRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTsewSAFEIEHAHHIA 181
Cdd:cd19095 73 EGGRDRkdfSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGV---SGDGEELEAAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 182 TkynliaPVAD--QPQYNYLTRDhfEKDLLPLQQIYGYGATVWSPLKSGILTGKyndgipegsrlsttftslagqlqTPE 259
Cdd:cd19095 150 S------GVFDvvQLPYNVLDRE--EEELLPLAAEAGLGVIVNRPLANGRLRRR-----------------------VRR 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19076016 260 GKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKA 314
Cdd:cd19095 199 RPLYADYARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
21-332 |
1.37e-37 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 137.68 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGwLTYGNEGYDVE-HTKncLKQAWDLGINTFDTAEIY-------SNGNSETVMGKAIKELGwDRSEYVI 92
Cdd:PRK10625 9 SSLEVSTLGLGT-MTFGEQNSEADaHAQ--LDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRG-SREKLII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKVffgAGTKLPNTTG------LSRKHIIEGLNASLKRLGLPYVDVIMAHRPD-----------------PSVPMEEVV 149
Cdd:PRK10625 85 ASKV---SGPSRNNDKGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPAVSLLETL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 150 RAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGI 229
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 230 LTGKY-NDGIPEGSR--LSTTFTSLAGQlqtpegKTQLdQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPE 306
Cdd:PRK10625 241 LTGKYlNGAKPAGARntLFSRFTRYSGE------QTQK-AVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTME 313
|
330 340
....*....|....*....|....*.
gi 19076016 307 QIVENVKAVEFIdkLTPEILKKIDEI 332
Cdd:PRK10625 314 QLKTNIESLHLT--LSEEVLAEIEAV 337
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
26-326 |
3.10e-37 |
|
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: 134.60 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 26 SAFSLGG-WLTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYsnGNSETVMGKAIKElgWDRSEYVITTKVffgaGTKL 104
Cdd:cd19090 1 SALGLGTaGLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAE--LPREPLVLSTKV----GRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 105 PNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEE-----VVRAFTQLIQDGKAFYWGTSEWSAFEieHAHH 179
Cdd:cd19090 73 EDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPPDL--LRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 180 IAT-KYNLIAPVADqpqYNYLTRDHFEkDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRlsttftslagqlqtP 258
Cdd:cd19090 151 IETgDFDVVLTANR---YTLLDQSAAD-ELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYR--------------W 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19076016 259 EGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEIL 326
Cdd:cd19090 213 LSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEG--PLPEELW 278
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
50-317 |
1.13e-35 |
|
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: 130.03 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 50 LKQAWDLGINTFDTAEIYSNGNSETVMGKAIKelGWDRSeYVITTKVffGAGTKLPNTTGL--SRKHIIEGLNASLKRLG 127
Cdd:cd19088 30 LRRALELGVNFIDTADSYGPDVNERLIAEALH--PYPDD-VVIATKG--GLVRTGPGWWGPdgSPEYLRQAVEASLRRLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 128 LPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVadQPQYNYLTRDHFekD 207
Cdd:cd19088 105 LDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR----IVSV--QNRYNLANRDDE--G 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 208 LLPLQQIYGYGATVWSPLKSGiltgkyndGIPEGSRLsttftslagqlqtpegktqldqvrqISKIAEQIGATPSQLALA 287
Cdd:cd19088 177 VLDYCEAAGIAFIPWFPLGGG--------DLAQPGGL-------------------------LAEVAARLGATPAQVALA 223
|
250 260 270
....*....|....*....|....*....|
gi 19076016 288 WTLKNPYVSTTILGASKPEQIVENVKAVEF 317
Cdd:cd19088 224 WLLARSPVMLPIPGTSSVEHLEENLAAAGL 253
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
14-332 |
1.60e-35 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 132.25 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGW-LTYGNEgydvEHTKNCLKQAWDLGINTFDTAEIYsnGNSETVMGKAIKElgwDRSEYVI 92
Cdd:COG1453 2 QYRRLGKTGLEVSVLGFGGMrLPRKDE----EEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TtkvffgagTKLPNTTGlSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVR------AFTQLIQDGKafywgt 166
Cdd:COG1453 73 A--------TKLPPWVR-DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGK------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 167 sewsafeIEHA----HHiatKYNLIAPVAD-------QPQYNYL-TRDHFEKDLLPLQQIYGYGATVWSPLKsgiltgky 234
Cdd:COG1453 138 -------IRHIgfstHG---SLEVIKEAIDtgdfdfvQLQYNYLdQDNQAGEEALEAAAEKGIGVIIMKPLK-------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 235 ndgipegsrlsttftslAGQLQTPEGKtqldqvrqISKIAEQiGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKA 314
Cdd:COG1453 200 -----------------GGRLANPPEK--------LVELLCP-PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKT 253
|
330
....*....|....*...
gi 19076016 315 VEFIDKLTPEILKKIDEI 332
Cdd:COG1453 254 ADNLEPLTEEELAILERL 271
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
14-317 |
3.01e-33 |
|
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: 124.59 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGwLTYGNE--GYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwDRSEYV 91
Cdd:cd19163 2 KYRKLGKTGLKVSKLGFGA-SPLGGVfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGI--PRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 92 ITTKVffGA-GTKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAH----RPDPSVPMEEVVRAFTQLIQDGKAFYWGT 166
Cdd:cd19163 79 LATKV--GRyGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 167 sewsafeiehahhiaTKYNL--IAPVADQPQ--------YNYLT-RDHFEKDLLPLQQIYGYGATVWSPLKSGILTgkyN 235
Cdd:cd19163 157 ---------------TGYPLdvLKEVLERSPvkidtvlsYCHYTlNDTSLLELLPFFKEKGVGVINASPLSMGLLT---E 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 236 DGIPEGSRLsttftslagqlqTPEGKtqlDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAV 315
Cdd:cd19163 219 RGPPDWHPA------------SPEIK---EACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
..
gi 19076016 316 EF 317
Cdd:cd19163 284 EE 285
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
49-330 |
2.29e-32 |
|
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: 122.35 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 49 CLKQAWDLGINTFDTAEIYSNG---NSETVMGKAIKELGWDRSEYVITTKVFFGAGTKLPNTtglSRKHIIEGLNASLKR 125
Cdd:cd19077 30 TMKAALDAGSNLWNGGEFYGPPdphANLKLLARFFRKYPEYADKVVLSVKGGLDPDTLRPDG---SPEAVRKSIENILRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 126 LG-LPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHiatkynlIAPVAD-QPQYNYLTRDH 203
Cdd:cd19077 107 LGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHA-------VHPIAAvEVEYSLFSREI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 204 FEKDLLPLQQIYGYGATVWSPLKSGILTGKY--NDGIPEGS--RLSTTFtslagqlqTPEG-KTQLDQVRQISKIAEQIG 278
Cdd:cd19077 180 EENGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEGDfrRHLDRF--------NGENfEKNLKLVDALQELAEKKG 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19076016 279 ATPSQLALAWTLKNPyvSTTIL---GASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19077 252 CTPAQLALAWILAQS--GPKIIpipGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
20-332 |
6.09e-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: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 20 RSGLKVSAFSLGGWLTYGNEGYDVehtkncLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFFg 99
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEECTRA------VEHALELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKVWP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 100 agtklpntTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHH 179
Cdd:cd19140 73 --------DNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 180 IATkynliAP-VADQPQYN-YLTRDhfekDLLPLQQIYGYGATVWSPLKSGILtgkyndgipegsrlsttftslagqLQT 257
Cdd:cd19140 145 LSE-----APlFTNQVEYHpYLDQR----KLLDAAREHGIALTAYSPLARGEV------------------------LKD 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076016 258 PEgktqldqvrqISKIAEQIGATPSQLALAWTLKNPYVStTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19140 192 PV----------LQEIGRKHGKTPAQVALRWLLQQEGVA-AIPKATNPERLEENLDIFDF--TLSDEEMARIAAL 253
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-313 |
8.36e-31 |
|
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: 118.57 E-value: 8.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 23 LKVSAFSLGGWLTYGNEGYDVEHtKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKEL----GWDRSEYVITTKV-- 96
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEY-REALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVVIVTKAgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 FFGAGTKLPNT---------TGLSRKHIIEG-------------LNASLKRLGLPYVDVIMAHRPDPSVP---------- 144
Cdd:cd19099 80 IPGDGDEPLRPlkyleeklgRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefydr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 145 MEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYNLIAPVADQPQYNyltRDHFEKDLLPLQQIYGYGATVWSP 224
Cdd:cd19099 160 LEEAFEALEEAVAEGKIRYYGISTWDGFRAPPALPGHLSLEKLVAAAEEVGGD---NHHFKVIQLPLNLLEPEALTEKNT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 225 LKSG---ILTGKYNDGIpegsrlsTTFTS---LAGQLqtpegktqLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTT 298
Cdd:cd19099 237 VKGEalsLLEAAKELGL-------GVIASrplNQGQL--------LGELRLADLLALPGGATLAQRALQFARSTPGVDSA 301
|
330
....*....|....*
gi 19076016 299 ILGASKPEQIVENVK 313
Cdd:cd19099 302 LVGMRRPEHVDENLA 316
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
27-330 |
2.97e-29 |
|
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: 112.96 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 27 AFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVffgagtklpN 106
Cdd:cd19071 3 LIGLGTYKLKPEE------TAEAVLAALEAGYRHIDTAAAYGN---EAEVGEAIRESGVPREELFITTKL---------W 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 107 TTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPS------VPMEEVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHI 180
Cdd:cd19071 65 PTDHGYERVREALEESLKDLGLDYLDLYLIHWPVPGkeggskEARLETWRALEELVDEGLVRSIGVSN---FNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 181 aTKYNLIAPVADQPQYN-YLTRD-----HFEKDLLPlqqiygygaTVWSPLKSGILTGKYNDgipegsrlsttftslagq 254
Cdd:cd19071 142 -LAAARIKPAVNQIELHpYLQQKelvefCKEHGIVV---------QAYSPLGRGRRPLLDDP------------------ 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 255 lqtpegktqldqvrQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19071 194 --------------VLKEIAKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
27-330 |
7.82e-29 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 111.59 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 27 AFSLGGWLTYGNEGYDVehtkncLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfgagtklpn 106
Cdd:cd19073 3 ALGLGTWQLRGDDCANA------VKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTKVW--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 107 TTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHiATKYNL 186
Cdd:cd19073 65 RDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSN---FTIELLEE-ALDISP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 187 IAPVADQPQYNYLtrdHFEKDLLPLQQIYGYGATVWSPLksgiltgkyndgipegsrlsttftslagqlqtpeGKTQLDQ 266
Cdd:cd19073 141 LPIAVNQVEFHPF---LYQAELLEYCRENDIVITAYSPL----------------------------------ARGEVLR 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076016 267 VRQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19073 184 DPVIQEIAEKYDKTPAQVALRWLVQKGIV--VIPKASSEDHLKENLAIFDW--ELTSEDVAKID 243
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
22-337 |
2.61e-28 |
|
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: 112.13 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVS-----AFSLGGWLTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwDRSEYVITTKv 96
Cdd:cd19146 8 GVRVSplclgAMSFGEAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 fFGAGTKL-------PNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEW 169
Cdd:cd19146 86 -YTTGYRRggpikikSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 170 SAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSgiltgkyndgipegsrlsttft 249
Cdd:cd19146 165 PAWVVSKANAYARAHGLTQFVVYQGHWSAAFRD-FERDILPMCEAEGMALAPWGVLGQ---------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 250 slaGQLQTPEGKTQLDQV-----------RQIS----KIAEQIGATPSQLALAWTL-KNPYVsTTILGASKPEQIVENVK 313
Cdd:cd19146 222 ---GQFRTEEEFKRRGRSgrkggpqtekeRKVSekleKVAEEKGTAITSVALAYVMhKAPYV-FPIVGGRKVEHLKGNIE 297
|
330 340
....*....|....*....|....
gi 19076016 314 AVEFidKLTPEILKKIDEILNFTP 337
Cdd:cd19146 298 ALGI--SLSDEEIQEIEDAYPFDV 319
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
44-317 |
3.31e-28 |
|
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: 111.55 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 44 EHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwdRSEYVITTKV----------------FFGAGTKLPNT 107
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVgrllvplqeveptfepGFWNPLPFDAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 108 TGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDG-------------KAFYWGTSEWSAFE- 173
Cdd:cd19152 98 FDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKGAfraleelreegviKAIGLGVNDWEVILr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 174 -IEHAHH----IATKYNLIapvaDQPQynyltrdhfEKDLLPLQQIYGYGATVWSPLKSGILTGkyndgipegsrlSTTF 248
Cdd:cd19152 178 iLEEADLdwvmLAGRYTLL----DHSA---------ARELLPECEKRGVKVVNAGPFNSGFLAG------------GDNF 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076016 249 TSLAGQLQTPEgktQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEF 317
Cdd:cd19152 233 DYYEYGPAPPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
27-332 |
7.91e-28 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 109.63 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 27 AFSLGGWLTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFFGAgtklpn 106
Cdd:cd19120 8 AFGTGTAWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTKVSPGI------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 107 ttglsrKHIIEGLNASLKRLGLPYVDVIMAHRP---DPSVP-MEEVVRAFTQLIQDGKAFYWGTSEWsafeieHAHHIAT 182
Cdd:cd19120 79 ------KDPREALRKSLAKLGVDYVDLYLIHSPffaKEGGPtLAEAWAELEALKDAGLVRSIGVSNF------RIEDLEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 183 --KYNLIAPVADQPQYN-YLTRDHfeKDLLPLQQiygygatvwsplKSGILTgkyndgipegsrlsTTFTSLAGQLQTPE 259
Cdd:cd19120 147 llDTAKIKPAVNQIEFHpYLYPQQ--PALLEYCR------------EHGIVV--------------SAYSPLSPLTRDAG 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076016 260 GKtqLDQVrqISKIAEQIGATPSQLALAWTL-KNPYVSTTilgASKPEQIVENVKAveFIDKLTPEILKKIDEI 332
Cdd:cd19120 199 GP--LDPV--LEKIAEKYGVTPAQVLLRWALqKGIVVVTT---SSKEERMKEYLEA--FDFELTEEEVEEIDKA 263
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
53-315 |
2.57e-27 |
|
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: 108.60 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 53 AWDLGINTFDTAEIYSNGNSETVMGKAIKelGWDRSEYVITTKV----FFGAGTKLPNTT---GLSRKHIIEGLNASLKR 125
Cdd:cd19162 28 AWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllEPGAAGRPAGADrrfDFSADGIRRSIEASLER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 126 LGLPYVDVIMAHRPDP--SVPMEEVVRAFTQLIQDG--KAFYWGTSEWSAfeiehahhiatkynLIAPVADQP------- 194
Cdd:cd19162 106 LGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGvvGAIGVGVTDWAA--------------LLRAARRADvdvvmva 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 195 -QYNYLTRDHfEKDLLPLQQIYGYGATVWSPLKSGILTGkyndGIPEGSRLSTTftslagqlQTPEgkTQLDQVRQISKI 273
Cdd:cd19162 172 gRYTLLDRRA-ATELLPLCAAKGVAVVAAGVFNSGILAT----DDPAGDRYDYR--------PATP--EVLARARRLAAV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19076016 274 AEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAV 315
Cdd:cd19162 237 CRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALL 278
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-334 |
5.46e-27 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 108.33 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 15 FRFLGRSGLKVSAFSLGGwLTYGNEGYDV--EHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVI 92
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGSVFGPVseEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 93 TTKV-FFGAGTKlpnttgLSRKHIIEGLNASLKRLGLPYVDVIMAH-----RPDPSVpmEEVVRAFTQLIQDGKAFYWGT 166
Cdd:PLN02587 80 STKCgRYGEGFD------FSAERVTKSVDESLARLQLDYVDILHCHdiefgSLDQIV--NETIPALQKLKESGKVRFIGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 167 SEWSAFeiehahhiATKYNL--IAP--VADQPQY-NYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKyndGIPEG 241
Cdd:PLN02587 152 TGLPLA--------IFTYVLdrVPPgtVDVILSYcHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTEN---GPPEW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 242 SRLSttftslagqlqtPEGKTqldQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKL 321
Cdd:PLN02587 221 HPAP------------PELKS---ACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETS 285
|
330
....*....|....*
gi 19076016 322 T--PEILKKIDEILN 334
Cdd:PLN02587 286 GidEELLSEVEAILA 300
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-330 |
9.15e-26 |
|
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: 104.91 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGwLTYGNE------GYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGwDRSEYVITT 94
Cdd:cd19147 6 AGIRVSPLILGA-MSIGDAwsgfmgSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 95 KVFF-----GAGT-KLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSE 168
Cdd:cd19147 84 KFTTdykayEVGKgKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 169 WSAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDhFEKDLLPLQQIYGYGATVWSPLKSGILTGK--YNDGIPEGSRLST 246
Cdd:cd19147 164 TPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRD-FERDIIPMARHFGMALAPWDVLGGGKFQSKkaVEERKKNGEGLRS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 247 TFTslaGQLQTPEgktQLDQVRQISKIAEQIG-ATPSQLALAWTL-KNPYVsTTILGASKPEQIVENVKAVEFidKLTPE 324
Cdd:cd19147 243 FVG---GTEQTPE---EVKISEALEKVAEEHGtESVTAIALAYVRsKAPNV-FPLVGGRKIEHLKDNIEALSI--KLTPE 313
|
....*.
gi 19076016 325 ILKKID 330
Cdd:cd19147 314 EIEYLE 319
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-331 |
1.60e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 103.95 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 31 GGWLTYGNEgYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgWDRSEYVITTKVffgagtkLPNTTGL 110
Cdd:cd19103 20 GGDQVFGNH-LDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKF-------TPQIAGQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 111 SRKHIIEGLNASLKRLGLPYVDVIMAHRPDpsvpmeEVVRAFTQLI---QDGKAFYWGTSEWSAFEIEHAHHIATKYNLi 187
Cdd:cd19103 90 SADPVADMLEGSLARLGTDYIDIYWIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAGV- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 188 aPV-ADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDG--IPEGSRLSTTFTSLAGQLqtpegkTQL 264
Cdd:cd19103 163 -SLsAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKhpLPEGSGRAETYNPLLPQL------EEL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19076016 265 DQVrqISKIAEQIGATPSQLALAWTL-KNpyvSTTILGASKPEQIVENVKAVEFidKLTPEILKKIDE 331
Cdd:cd19103 236 TAV--MAEIGAKHGASIAQVAIAWAIaKG---TTPIIGVTKPHHVEDAARAASI--TLTDDEIKELEQ 296
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-333 |
1.87e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 103.83 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 31 GGWLTYGNEGYDVEHTK--NCLKQAWDLGINTFDTAEIYsnGNSETVMGKAIKELGWDR---SEYVITTK-VFFgagtkl 104
Cdd:cd19101 8 GMWQLSGGHGGIRDEDAavRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRERdaaDDVQIHTKwVPD------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 105 PNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVP-MEEVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHIATk 183
Cdd:cd19101 80 PGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTN---FDTERLREILD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 184 yNLIAPVADQPQYNYLTRdHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNdGIPEGSRLSTTFTSLAGQLQTPE--GK 261
Cdd:cd19101 156 -AGVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEPTGPALETRSLQKYKLMIDewGG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076016 262 TQLDQ--VRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFidKLTPEILKKIDEIL 333
Cdd:cd19101 233 WDLFQelLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF--RLDDEDRAAIDAVL 304
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-316 |
1.93e-25 |
|
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: 102.64 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 26 SAFSLGG--WLTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKElgWDRSEYVITtkvffgagTK 103
Cdd:cd19096 1 SVLGFGTmrLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLA--------TK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 104 LPNTTGLSRKHIIEGLNASLKRLGLPYVDV-----IMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSewsaFeieHAh 178
Cdd:cd19096 71 LPPWSVKSAEDFRRILEESLKRLGVDYIDFyllhgLNSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFS----F---HD- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 179 hiatKYNLIAPVAD-------QPQYNYLTRDHFE-KDLLPLQQIYGYGATVWSPLKSGILtgkyndgipegsrlsttfts 250
Cdd:cd19096 143 ----SPELLKEILDsydfdfvQLQYNYLDQENQAgRPGIEYAAKKGMGVIIMEPLKGGGL-------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 251 lagqLQTPEgktqldqvrQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVE 316
Cdd:cd19096 199 ----ANNPP---------EALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-313 |
4.38e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 98.71 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 16 RFLGRSGLKVSAFSLGGWltyGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYsnGNSETVMGKAIKElgwDRSEYVITTK 95
Cdd:cd19100 2 RRLGRTGLKVSRLGFGGG---PLGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 vffgagtklpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAH----RPDPSVPMEE--VVRAFTQLIQDGKAFYWG-TSe 168
Cdd:cd19100 74 -----------TGARDYEGAKRDLERSLKRLGTDYIDLYQLHavdtEEDLDQVFGPggALEALLEAKEEGKIRFIGiSG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 169 wsafeieHAHHIATKynliapVAD-------QPQYNYLTR--DHFEKDLLPLQQIYGYGATVWSPLKSGILtgkyndgip 239
Cdd:cd19100 142 -------HSPEVLLR------ALEtgefdvvLFPINPAGDhiDSFREELLPLAREKGVGVIAMKVLAGGRL--------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076016 240 egsrlsttftsLAGQLQTPEgktqldqvrqiskiaeqigatpsqLALAWTLKNPYVSTTILGASKPEQIVENVK 313
Cdd:cd19100 200 -----------LSGDPLDPE------------------------QALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-316 |
6.19e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 96.06 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 50 LKQAWDLGINTFDTAEIYsnGNSETVMGKAIKELgwdrSEYVITTKVffgagTKLPNTTGLSRKHIIEGLNASLKRLGLP 129
Cdd:cd19097 32 LEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL-----PPLKEDKKEDEAAIEASVEASLKRLKVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 130 YVDVIMAHRP-DPSVPMEEVVRAFTQLIQDGKAFYWGTsewSAFEIEHAHHIATKYN--LIapvadQPQYNYLTRDHFEK 206
Cdd:cd19097 101 SLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGV---SVYSPEELEKALESFKidII-----QLPFNILDQRFLKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 207 DLLPLqqiygygatvwspLKS-------------GILTgkyndgiPEGSRLSTTFTSLAgqlqtpegktqlDQVRQISKI 273
Cdd:cd19097 173 GLLAK-------------LKKkgieiharsvflqGLLL-------MEPDKLPAKFAPAK------------PLLKKLHEL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19076016 274 AEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVE 316
Cdd:cd19097 221 AKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
50-324 |
3.00e-22 |
|
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: 95.09 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 50 LKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELgwDRSEYVITTKVffG--------AGTKLPN--TTGL--------S 111
Cdd:cd19161 26 LDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK--PRDEFVLSTKV--GrllkpareGSVPDPNgfVDPLpfeivydyS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 112 RKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEE-VVRAFTQLIQDG-------------KAFYWGTSEWSAFE--IE 175
Cdd:cd19161 102 YDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRkERHHFAQLMSGGfkaleelkkagviKAFGLGVNEVQICLeaLD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 176 HAHH----IATKYNLiapvadqpqynyLTRDHfEKDLLPLQQIYGYGATVWSPLKSGIL-TGK-------YNDGIPEgsr 243
Cdd:cd19161 182 EADLdcflLAGRYSL------------LDQSA-EEEFLPRCEQRGTSLVIGGVFNSGILaTGTksgakfnYGDAPAE--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 244 lsttftslagqlqtpegktQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENvkaVEFIDKLTP 323
Cdd:cd19161 246 -------------------IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQN---VEAFQTDIP 303
|
.
gi 19076016 324 E 324
Cdd:cd19161 304 E 304
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
22-334 |
1.58e-21 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 92.07 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLT-YGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfga 100
Cdd:cd19157 7 GVKMPWLGLGVFKVeEGSE------VVNAVKTALKNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKVW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 101 gtklpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVpMEEVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHI 180
Cdd:cd19157 75 ------NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSN---FQVHHLEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 181 ATKYNlIAPVADQPQYN-YLTrdhfEKDLLPLQQIYGYGATVWSPLKSGiltgkyndgipegsrlsttftslagqlqtpe 259
Cdd:cd19157 145 LADAE-IVPMVNQVEFHpRLT----QKELRDYCKKQGIQLEAWSPLMQG------------------------------- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076016 260 gktQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKIDEiLN 334
Cdd:cd19157 189 ---QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENADVFDF--ELSQEDMDKIDA-LN 255
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
25-332 |
1.74e-21 |
|
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: 91.65 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 25 VSAFSLGGWLTYGNEGYDVehtkncLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFFgagtkl 104
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDS------VRTALELGYRHIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWI------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 105 pntTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPS--VPMEEVVRAFTQLIQDGKAFYWGTSEWS------AFEIEH 176
Cdd:cd19139 66 ---DNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTialldeAIAVVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 177 AHHIATKYNLIAPVADQPQYNYLTRDHfekdllplqqiygygatvwsplksGILTgkyndgipegsrlsTTFTSLAgqlq 256
Cdd:cd19139 143 AGAIATNQIELSPYLQNRKLVAHCKQH------------------------GIHV--------------TSYMTLA---- 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 257 tpEGKTQLDQVrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19139 181 --YGKVLDDPV--LAAIAERHGATPAQIALAWAMARGYA--VIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
22-332 |
1.23e-20 |
|
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: 89.77 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEGYDVEHTknclkqAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFFgag 101
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADAVAT------ALADGYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 102 tklpntTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVpMEEVV---RAFTQLIQDGKAFYWGTSEwsaFEIEHAH 178
Cdd:cd19127 74 ------SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPND-FDRTIqayKALEKLLAEGRVRAIGVSN---FTPEHLE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 179 HIATKYNLIAPVADQPQYNYLTrdhfEKDLLPLQQIYGYGATVWSPLkSGILTgkYNDGIPEGSRlsttftslaGQLQTP 258
Cdd:cd19127 144 RLIDATTVVPAVNQVELHPYFS----QKDLRAFHRRLGIVTQAWSPI-GGVMR--YGASGPTGPG---------DVLQDP 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076016 259 egktqldqvrQISKIAEQIGATPSQLALAWTLKNPYVSttILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19127 208 ----------TITGLAEKYGKTPAQIVLRWHLQNGVSA--IPKSVHPERIAENIDIFDF--ALSAEDMAAIDAL 267
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
14-316 |
2.33e-20 |
|
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: 89.52 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 14 PFRFLGRSGLKVSAFSLGGWLTYGNEGYDVEHTK--NCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYV 91
Cdd:cd19153 1 FGETLEIALGNVSPVGLGTAALGGVYGDGLEQDEavAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 92 ITTKVffgaGTKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAH-----RPDPSVpmEEVVRAFTQLIQDGKAFYWGT 166
Cdd:cd19153 81 VATKV----GRYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHdiefvDYDTLV--DEALPALRTLKDEGVIKRIGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 167 SEWSAFEIEHahhiATKYNLIAPVADQPQYNYLT--RDHFEKDLLPLQQIYGYGATVWSPLKSGILTgkyndgiPEGSRl 244
Cdd:cd19153 155 AGYPLDTLTR----ATRRCSPGSLDAVLSYCHLTlqDARLESDAPGLVRGAGPHVINASPLSMGLLT-------SQGPP- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 245 stTFTSLAGQLQtpegktqlDQVRQISKIAEQIGATPSQLALAWTLKNPY-VSTTILGASKPEQIVENVKAVE 316
Cdd:cd19153 223 --PWHPASGELR--------HYAAAADAVCASVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
22-332 |
4.19e-20 |
|
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: 88.26 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGW-LTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfga 100
Cdd:cd19126 6 GTRMPWLGLGVFqTPDGDE------TERAVQTALENGYRSIDTAAIYKN---EEGVGEAIRESGVPREELFVTTKLW--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 101 gtklpNTTGLSRKhIIEGLNASLKRLGLPYVDVIMAHRPDPSvPMEEVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHI 180
Cdd:cd19126 74 -----NDDQRARR-TEDAFQESLDRLGLDYVDLYLIHWPGKD-KFIDTWKALEKLYASGKVKAIGVSN---FQEHHLEEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 181 ATKYNlIAPVADQPQYN-YLTRdhfeKDLLPLQQIYGYGATVWSPLksgiltgkyndgipegsrlsttftslagqlqtpe 259
Cdd:cd19126 144 LAHAD-VVPAVNQVEFHpYLTQ----KELRGYCKSKGIVVEAWSPL---------------------------------- 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076016 260 GKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19126 185 GQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVV--TIPKSVHASRIKENADIFDF--ELSEDDMTAIDAL 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
21-332 |
9.06e-20 |
|
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: 88.24 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEGydvehtKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL----GWDRSEYVITTKV 96
Cdd:cd19154 8 NGVKMPLIGLGTWQSKGAEG------ITAVRTALKAGYRLIDTAFLYQN---EEAIGEALAELleegVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 FFGAgtklpnttgLSRKHIIEGLNASLKRLGLPYVDVIMAHRP-------------------DPSVPMEEVVRAFTQLIQ 157
Cdd:cd19154 79 WTHE---------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 158 DGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQPQ-YNYLTrdhfEKDLLPLQQIYGYGATVWSPLKSgilTGKYND 236
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVEcHLYFP----QKELVEFCKKHNISVTSYATLGS---PGRANF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 237 GIPEGsrlsttftslagqlQTPEGKTQLDQVrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVE 316
Cdd:cd19154 219 TKSTG--------------VSPAPNLLQDPI--VKAIAEKHGKTPAQVLLRYLLQRGIA--VIPKSATPSRIKENFNIFD 280
|
330
....*....|....*.
gi 19076016 317 FidKLTPEILKKIDEI 332
Cdd:cd19154 281 F--SLSEEDMATLEEI 294
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
23-329 |
7.15e-19 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 85.08 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 23 LKVSAFSLGgwlTYGNEGYDVEHTkncLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfgagt 102
Cdd:PRK11172 1 MSIPAFGLG---TFRLKDQVVIDS---VKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIW----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 103 klpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPS--VPMEEVVRAFTQLIQDGKAFYWGTSEWS------AFEI 174
Cdd:PRK11172 67 ----IDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 175 EHAHHIATkyNLIapvadqpqynyltrdhfekDLLPLQQiygyGATVWSPLKS-GILTgkyndgipegsrlsTTFTSLAg 253
Cdd:PRK11172 143 VGAENIAT--NQI-------------------ELSPYLQ----NRKVVAFAKEhGIHV--------------TSYMTLA- 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 254 qlqtpEGKTQLDQVrqISKIAEQIGATPSQLALAWTLKNPYvsTTILGASKPEQIVENVKAVEFidKLTPEILKKI 329
Cdd:PRK11172 183 -----YGKVLKDPV--IARIAAKHNATPAQVILAWAMQLGY--SVIPSSTKRENLASNLLAQDL--QLDAEDMAAI 247
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
22-332 |
7.24e-19 |
|
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: 84.88 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWltygnEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfgag 101
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDGAEAENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIRESGVPREEVFVTTKLW---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 102 tklpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSvPMEEVVRAFTQLIQDGKAFYWGTSEWsafeieHAHHIA 181
Cdd:cd19156 74 -----NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKG-KFKDTWKAFEKLYKEKKVRAIGVSNF------HEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 182 T--KYNLIAPVADQ----PQYNYLTRDHFEKDllplQQIygyGATVWSPLKSGILtgkyndgipegsrlsttftslagqL 255
Cdd:cd19156 142 EllKSCKVAPMVNQielhPLLTQEPLRKFCKE----KNI---AVEAWSPLGQGKL------------------------L 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076016 256 QTPEgktqldqvrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19156 191 SNPV----------LKAIGKKYGKSAAQVIIRWDIQHGII--TIPKSVHEERIQENFDVFDF--ELTAEEIRQIDGL 253
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
30-329 |
1.92e-18 |
|
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: 83.58 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 30 LGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFFGAGtklpnttg 109
Cdd:cd19131 15 LGVWQVSNDE------AASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTKLWNSDQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 110 lSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSV-PMEEVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHI--ATKynl 186
Cdd:cd19131 78 -GYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQdKYVETWKALIELKKEGRVKSIGVSN---FTIEHLQRLidETG--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 187 IAPVADQ----PQYNyltrdhfEKDLLPLQQIYGYGATVWSPLKSGiltgkyndgipegsrlsttftslaGQLQTPegkt 262
Cdd:cd19131 151 VVPVVNQielhPRFQ-------QRELRAFHAKHGIQTESWSPLGQG------------------------GLLSDP---- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076016 263 qldqvrQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKI 329
Cdd:cd19131 196 ------VIGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDF--ELDADDMQAI 252
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-330 |
2.05e-18 |
|
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: 83.47 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEGydvehtKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKvffgag 101
Cdd:cd19132 4 GTQIPAIGFGTYPLKGDEG------VEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTK------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 102 tkLPNttglsRKH----IIEGLNASLKRLGLPYVDVIMAHRPDPSVPME-EVVRAFTQLIQDGKAFYWGTSEwsaFEIEH 176
Cdd:cd19132 69 --LPG-----RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSN---FLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 177 AHHIATKYNlIAPVADQPQ-YNYLTRD-----HFEKDLLPlqqiygygaTVWSPL--KSGILTgkyndgipegsrlsttf 248
Cdd:cd19132 139 LDRLIDETG-VTPAVNQIElHPYFPQAeqrayHREHGIVT---------QSWSPLgrGSGLLD----------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 249 tslagqlqtpegktqlDQVrqISKIAEQIGATPSQLALAWTLKNPYVSttILGASKPEQIVENVKAVEFidKLTPEILKK 328
Cdd:cd19132 192 ----------------EPV--IKAIAEKHGKTPAQVVLRWHVQLGVVP--IPKSANPERQRENLAIFDF--ELSDEDMAA 249
|
..
gi 19076016 329 ID 330
Cdd:cd19132 250 IA 251
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
21-332 |
1.02e-17 |
|
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: 81.78 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEGYdvehtkNCLKQAWDLGINTFDTAEIYsnGNSETVmGKAIKELGWDRSEYVITTKVFfga 100
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNEVA------KAVEAALKAGYRHIDTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKLW--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 101 gtklpnttGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVP---------------------MEEVVRAFTQLIQDG 159
Cdd:cd19117 78 --------CTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWELMQKLPATG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 160 KAFYWGTSEWSAFEIEHAhhIATKYNLIAPVADQPQ-YNYLTRDHfekdLLPLQQIYGYGATVWSPLksgiltgkyndgi 238
Cdd:cd19117 150 KVKAIGVSNFSIKNLEKL--LASPSAKIVPAVNQIElHPLLPQPK----LVDFCKSKGIHATAYSPL------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 239 pegsrlsttftslaGQLQTPEGKTQLdqvrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEfi 318
Cdd:cd19117 211 --------------GSTNAPLLKEPV-----IIKIAKKHGKTPAQVIISWGLQRGYS--VLPKSVTPSRIESNFKLFT-- 267
|
330
....*....|....
gi 19076016 319 dkLTPEILKKIDEI 332
Cdd:cd19117 268 --LSDEEFKEIDEL 279
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
20-332 |
8.68e-17 |
|
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: 78.91 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 20 RSGLKVSAFSLGgwlTYGNEGYDVEHTKNCLKqawDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfg 99
Cdd:cd19135 8 SNGVEMPILGLG---TSHSGGYSHEAVVYALK---ECGYRHIDTAKRYGC---EELLGKAIKESGVPREDLFLTTKLW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 100 agtklPNTTGLSRkhIIEGLNASLKRLGLPYVDVIMAHRPDPSVP-------MEEVVRAFTQLIQDGKAFYWGTSEwsaF 172
Cdd:cd19135 77 -----PSDYGYES--TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSN---F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 173 EIEHAHHIATKYNlIAPVADQPQYNYLTRDhfekdllplQQIYGYgatvwspLKS-GILTGKYndgipegsrlsttftsl 251
Cdd:cd19135 147 LIEHLEQLLEDCS-VVPHVNQVEFHPFQNP---------VELIEY-------CRDnNIVFEGY----------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 252 agqlqTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKIDE 331
Cdd:cd19135 193 -----CPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVV--TIPKSTKEERIKENCQVFDF--SLSEEDMATLDS 263
|
.
gi 19076016 332 I 332
Cdd:cd19135 264 L 264
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-332 |
1.51e-16 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 78.69 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL---GWDRSEYVITTkvff 98
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEE------VRAAVDYALFVGYRHIDTALSYQN---EKAIGEALKWWlknGKLKREEVFIT---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 99 gagTKLPnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAH-------------RPDPSVPMEEVVRAFTQLIQDGKAFYWG 165
Cdd:cd19111 68 ---TKLP-PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 166 TSEWSAFEIEHahhiATKYNLIAPVADQPQYN-YLTrdhfEKDLLPLQQIYGYGATVWSPLKSgiltgkynDGIPEGSRL 244
Cdd:cd19111 144 LSNFNPRQINK----ILAYAKVKPSNLQLECHaYLQ----QRELRKFCNKKNIVVTAYAPLGS--------PGRANQSLW 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 245 STTFTSLAgqlqtpegktqlDQVrqISKIAEQIGATPSQLALAWTLKNpyvSTTILGAS-KPEQIVENVKAVEFidKLTP 323
Cdd:cd19111 208 PDQPDLLE------------DPT--VLAIAKELDKTPAQVLLRFVLQR---GTGVLPKStNKERIEENFEVFDF--ELTE 268
|
....*....
gi 19076016 324 EILKKIDEI 332
Cdd:cd19111 269 EHFKKLKTL 277
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
30-317 |
2.15e-15 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 30 LGGWLTygnegyDVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKvffgagtkLPNTtg 109
Cdd:PRK11565 20 LGVWQA------SNEEVITAIHKALEVGYRSIDTAAIYKN---EEGVGKALKEASVAREELFITTK--------LWND-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 110 lSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPsvPMEEVVRAFTQLI---QDGKAFYWGTSEwsaFEIEHAHHIATKYNl 186
Cdd:PRK11565 81 -DHKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIelqKEGLIKSIGVCN---FQIHHLQRLIDETG- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 187 IAPVADQPQynyltrdhfekdLLPL---QQIYGYGAT------VWSPLKSGiltgkyndgipegsrlsttftslagqlqt 257
Cdd:PRK11565 154 VTPVINQIE------------LHPLmqqRQLHAWNAThkiqteSWSPLAQG----------------------------- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 258 peGKTQLDQvRQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEF 317
Cdd:PRK11565 193 --GKGVFDQ-KVIRDLADKYGKTPAQIVIRWHLDSGLV--VIPKSVTPSRIAENFDVFDF 247
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
21-332 |
2.36e-15 |
|
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: 75.07 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELG----WDRSEYVITTKV 96
Cdd:cd19125 7 TGAKIPAVGLGTWQADPGV------VGNAVKTAIKEGYRHIDCAAIYGN---EKEIGKALKKLFedgvVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 FfgagtklpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRP--------------DPSVPMEEVVRAFTQLIQDGKAF 162
Cdd:cd19125 78 W---------CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAMEKLVDSGKVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 163 YWGTSEWSAFEIEHAHHIAtkynLIAPVADQPQYNYLTRDHfekDLLPLQQIYGYGATVWSPLKSgiltgkyndgipegs 242
Cdd:cd19125 149 AIGVSNFSVKKLEDLLAVA----RVPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPLGS--------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 243 rlSTTFTSLAGQLQTPegktqldqvrQISKIAEQIGATPSQLALAWTLKNpyvSTTILGAS-KPEQIVENVKAVEFidKL 321
Cdd:cd19125 207 --PGTTWVKKNVLKDP----------IVTKVAEKLGKTPAQVALRWGLQR---GTSVLPKStNEERIKENIDVFDW--SI 269
|
330
....*....|.
gi 19076016 322 TPEILKKIDEI 332
Cdd:cd19125 270 PEEDFAKFSSI 280
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
44-330 |
2.63e-15 |
|
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: 74.89 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 44 EHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFfgagtklpnTTGLSRKHIIEGLNASL 123
Cdd:cd19134 24 DEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKLA---------TPDQGFTASQAACRASL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 124 KRLGLPYVDVIMAHRPDPSVpmEEVVRAFTQLIQ---DGKAFYWGTSEWsafeieHAHHIATKYNL--IAPVADQPQYNY 198
Cdd:cd19134 92 ERLGLDYVDLYLIHWPAGRE--GKYVDSWGGLMKlreEGLARSIGVSNF------TAEHLENLIDLtfFTPAVNQIELHP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 199 LTRdhfEKDLLPLQQIYGYGATVWSPLKSGILtgkyndgipegsrlsttftslagqLQTPEgktqldqvrqISKIAEQIG 278
Cdd:cd19134 164 LLN---QAELRKVNAQHGIVTQAYSPLGVGRL------------------------LDNPA----------VTAIAAAHG 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19076016 279 ATPSQLALAWTLKNPyvSTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19134 207 RTPAQVLLRWSLQLG--NVVISRSSNPERIASNLDVFDF--ELTADHMDALD 254
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
50-155 |
4.04e-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: 71.92 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 50 LKQAWDLGINTFDTAEIYsnGNSETVMGKAIKEL--GWDRSEYVITTKVffgaGTKLPNTTGLSRKHIIEGLNASLKRLG 127
Cdd:cd19164 40 VRRALELGIRAFDTSPYY--GPSEIILGRALKALrdEFPRDTYFIITKV----GRYGPDDFDYSPEWIRASVERSLRRLH 113
|
90 100
....*....|....*....|....*....
gi 19076016 128 LPYVDVIMAHrpDPS-VPMEEVVRAFTQL 155
Cdd:cd19164 114 TDYLDLVYLH--DVEfVADEEVLEALKEL 140
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
42-330 |
1.01e-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: 69.91 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 42 DVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWDRSEYVITTKVFFgagtklpntTGLSRKHIIEGLNA 121
Cdd:cd19133 21 DPEECERAVLEAIKAGYRLIDTAAAYGN---EEAVGRAIKKSGIPREELFITTKLWI---------QDAGYEKAKKAFER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 122 SLKRLGLPYVDVIMAHRPDPSVPMeeVVRAFTQLIQDGKAFYWGTSEWSAFEI-EHAHHiatkyNLIAPVADQPQYNYLt 200
Cdd:cd19133 89 SLKRLGLDYLDLYLIHQPFGDVYG--AWRAMEELYKEGKIRAIGVSNFYPDRLvDLILH-----NEVKPAVNQIETHPF- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 201 rdHFEKDLLPLQQIYGYGATVWSPLKsgiltgkyndgipegsrlsttftslagqlqtpEGKTQLDQVRQISKIAEQIGAT 280
Cdd:cd19133 161 --NQQIEAVEFLKKYGVQIEAWGPFA--------------------------------EGRNNLFENPVLTEIAEKYGKS 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19076016 281 PSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19133 207 VAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFDF--ELSDEDMEAIA 252
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
44-332 |
1.19e-12 |
|
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: 67.29 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 44 EHTKNCLKQAWDLGINTFDTAEIYsngNSETVMGKAIKE-----LGWDRSEYVITTKVFfgagtklpnTTGLSRKHIIEG 118
Cdd:cd19124 20 EDIKAAVLEAIEVGYRHFDTAAAY---GTEEALGEALAEalrlgLVKSRDELFVTSKLW---------CSDAHPDLVLPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 119 LNASLKRLGLPYVDVIMAHRPDPSVP----------------MEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIAT 182
Cdd:cd19124 88 LKKSLRNLQLEYVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 183 kynlIAPVADQPQYNYLTRdhfEKDLLPLQQIYGYGATVWSPLksgiltgkyndgipegsrlsttftslaGQLQTPEGKT 262
Cdd:cd19124 168 ----IPPAVNQVEMNPAWQ---QKKLREFCKANGIHVTAYSPL---------------------------GAPGTKWGSN 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076016 263 QLDQVRQISKIAEQIGATPSQLALAWTLKNpyvsttilGAS------KPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19124 214 AVMESDVLKEIAAAKGKTVAQVSLRWVYEQ--------GVSlvvksfNKERMKQNLDIFDW--ELTEEDLEKISEI 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
21-332 |
1.26e-12 |
|
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: 67.51 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKElGWD-----RSEYVITTK 95
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGE------IKELILNAIKIGYRHFDCAADYKN---EKEVGEALAE-AFKtglvkREDLFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 VFfgagtklpNTtglSRKHIIEGLNASLKRLGLPYVDVIMAHRP-----------------------DPSVPMEEVVRAF 152
Cdd:cd19112 77 LW--------NS---DHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 153 TQLIQDGKAFYWGTSEWSAFEIehahHIATKYNLIAPVADQPQ-YNYLTRDhfekDLLPLQQIYGYGATVWSPLKSGILT 231
Cdd:cd19112 146 EKLVSAGLVRSIGISNYDIFLT----RDCLAYSKIKPAVNQIEtHPYFQRD----SLVKFCQKHGISVTAHTPLGGAAAN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 GKYndgipegsrlsttFTSLAgQLQTPegktqldqvrQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVEN 311
Cdd:cd19112 218 AEW-------------FGSVS-PLDDP----------VLKDLAKKYGKSAAQIVLRWGIQRNTA--VIPKSSKPERLKEN 271
|
330 340
....*....|....*....|.
gi 19076016 312 VKAVEFidKLTPEILKKIDEI 332
Cdd:cd19112 272 IDVFDF--QLSKEDMKLIKSL 290
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
20-332 |
3.58e-12 |
|
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: 65.90 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 20 RSGLKVSAFSLGGWLTYGNEGYDVehtkncLKQAWDLGINTFDTAEIYSNgnsETVMGKAI----KELGWDRSEYVITTK 95
Cdd:cd19123 7 SNGDLIPALGLGTWKSKPGEVGQA------VKQALEAGYRHIDCAAIYGN---EAEIGAALaevfKEGKVKREDLWITSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 VFfgagtklpnttglSRKH----IIEGLNASLKRLGLPYVDVIMAHRP------------------DPSVPMEEVVRAFT 153
Cdd:cd19123 78 LW-------------NNSHapedVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAME 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 154 QLIQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQPQYN-YLTrdhfEKDLLPLQQIYGYGATVWSPLKSGiltg 232
Cdd:cd19123 145 ELVDKGLCRHIGVSNFSVKKLEDLLATAR----IKPAVNQVELHpYLQ----QPELLAFCRDNGIHLTAYSPLGSG---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 233 kyndgipegsrlsttftslagqlQTPEGKTQLDQVRQ-----ISKIAEQIGATPSQLALAWTLKNPyvSTTILGASKPEQ 307
Cdd:cd19123 213 -----------------------DRPAAMKAEGEPVLledpvINKIAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPER 267
|
330 340
....*....|....*....|....*
gi 19076016 308 IVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19123 268 IQQNLEAAEV--ELDASDMATIAAL 290
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
34-333 |
6.15e-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: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 34 LTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL---GWDRSEYVITTkvffgagTKLPNTTgl 110
Cdd:cd19129 9 LGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRN---EAEVGEAMQEVfkaGKIRREDLFVT-------TKLWNTN-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 111 SRKHIIE-GLNASLKRLGLPYVDVIMAHRP--------------------DPSVPMEEVVRAFTQLIQDGKAFYWGTSEW 169
Cdd:cd19129 77 HRPERVKpAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 170 SAFEIEHAHHIATkynlIAPVADQPQ-YNYLTrdhfEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIpegsrlsttf 248
Cdd:cd19129 157 SLEKLREIFEAAR----IKPAVVQVEsHPYLP----EWELLDFCKNHGIVLQAFAPLGHGMEPKLLEDPV---------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 249 tslagqlqtpegktqldqvrqISKIAEQIGATPSQLALAWTLKNpyvSTTILGASK-PEQIVENVKavefIDKLTPEILK 327
Cdd:cd19129 219 ---------------------ITAIARRVNKTPAQVLLAWAIQR---GTALLTTSKtPSRIRENFD----ISTLPEDAMR 270
|
....*.
gi 19076016 328 KIDEIL 333
Cdd:cd19129 271 EINEGI 276
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
21-332 |
8.97e-12 |
|
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: 64.74 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL-----GWDRSEYVITTK 95
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGE------VGAAVKIALKAGYRHLDLAKVYQN---QHEVGQALKELlkeepGVKREDLFITSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 VFfgagtklpNTTGlSRKHIIEGLNASLKRLGLPYVDVIMAHRP------------------------DPSVPMEEVVRA 151
Cdd:cd19118 74 LW--------NNSH-RPEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltavptnggevdlDLSVSLVDTWKA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 152 FTQLIQDGKAFYWGTSEwsaFEIEHAHHIaTKYNLIAPVADQPQYNyltrdhfekDLLPLQQIYGYGAtvwsplKSGILT 231
Cdd:cd19118 145 MVELKKTGKVKSIGVSN---FSIDHLQAI-IEETGVVPAVNQIEAH---------PLLLQDELVDYCK------SKNIHI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 gkyndgipegsrlsTTFTSLAGQLQtpeGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYvsTTILGASKPEQIVEN 311
Cdd:cd19118 206 --------------TAYSPLGNNLA---GLPLLVQHPEVKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIRSN 266
|
330 340
....*....|....*....|.
gi 19076016 312 VKAVEfidkLTPEILKKIDEI 332
Cdd:cd19118 267 FEQVE----LSDDEFNAVTAL 283
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
42-330 |
2.27e-11 |
|
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: 63.42 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 42 DVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL----GWDRSEYVITTKVFfgagtklPNTTGLSRKhiIE 117
Cdd:cd19136 13 GEEEVRQAVDAALKAGYRLIDTASVYRN---EADIGKALRDLlpkyGLSREDIFITSKLA-------PKDQGYEKA--RA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 118 GLNASLKRLGLPYVDVIMAHRP-----DPSVPME-----EVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHIaTKYNLI 187
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSN---YTVRHLEEL-LKYCEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 188 APVADQ----PQYnyltrdhFEKDLLPLQQIYGYGATVWSPLKSGILTgkyndgipegsrlsttftslagQLQTPEgktq 263
Cdd:cd19136 157 PPAVNQvefhPHL-------VQKELLKFCKDHGIHLQAYSSLGSGDLR----------------------LLEDPT---- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076016 264 ldqvrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEFIdkLTPEILKKID 330
Cdd:cd19136 204 ------VLAIAKKYGRTPAQVLLRWALQQGIG--VIPKSTNPERIAENIKVFDFE--LSEEDMAELN 260
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
21-337 |
2.36e-11 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 63.67 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWltygNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSngnSETVMGKAIKELGWD----RSEYVITTKV 96
Cdd:cd19119 8 TGASIPALGLGTA----SPHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAIDDgsikREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 FfgagtklPNTtglsRKHIIEGLNASLKRLGLPYVDVIMAHRPdpsVPM----EEVVRAFTQLIQDGKAFYWGTSEW--- 169
Cdd:cd19119 81 W-------PTF----YDEVERSLDESLKALGLDYVDLLLVHWP---VCFekdsDDSGKPFTPVNDDGKTRYAASGDHitt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 170 ------------------SAFEIEHAHHIATKYNLIAPVADQPQYNYLTRdhfeKDLLPLQQIYGYGATVWSPLKSGilt 231
Cdd:cd19119 147 ykqlekiyldgrakaigvSNYSIVYLERLIKECKVVPAVNQVELHPHLPQ----MDLRDFCFKHGILVTAYSPLGSH--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 gkyndgipegsrlsttftsLAGQLQTPEgktqldqvrqISKIAEQIGATPSQLALAWTLKNpyvSTTILGAS-KPEQIVE 310
Cdd:cd19119 220 -------------------GAPNLKNPL----------VKKIAEKYNVSTGDILISYHVRQ---GVIVLPKSlKPVRIVS 267
|
330 340
....*....|....*....|....*..
gi 19076016 311 NVKAVefidKLTPEILKKIDEILNFTP 337
Cdd:cd19119 268 NGKIV----SLTKEDLQKLDDIGEKYP 290
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
21-332 |
5.46e-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: 62.30 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEGydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL----GWDRSEYVITTKV 96
Cdd:cd19116 7 DGNEIPAIALGTWKLKDDEG-----VRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREKiaegVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 97 FfgagtklpnTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRP-------DPSVPME---------EVVRAFTQLIQDGK 160
Cdd:cd19116 79 W---------NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 161 AFYWGTSEwsaFEIEHAHHIATKYNlIAPVADQ----PQYNyltrdhfEKDLLPLQQIYGYGATVWSPLksgiltGKYNd 236
Cdd:cd19116 150 TRSIGVSN---FNSEQINRLLSNCN-IKPAVNQievhPTLT-------QEKLVAYCQSNGIVVMAYSPF------GRLV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 237 giPEGSRLSTTFtslagqLQTPEgktqldqvrqISKIAEQIGATPSQLALAWTLKNPYVSttILGASKPEQIVENVKAVE 316
Cdd:cd19116 212 --PRGQTNPPPR------LDDPT----------LVAIAKKYGKTTAQIVLRYLIDRGVVP--IPKSSNKKRIKENIDIFD 271
|
330
....*....|....*.
gi 19076016 317 FidKLTPEILKKIDEI 332
Cdd:cd19116 272 F--QLTPEEVAALNSF 285
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
21-319 |
5.72e-11 |
|
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: 62.25 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGgwlTYGNEGYDVEhTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL-----GWDRSEYVITTK 95
Cdd:cd19122 5 NGVKIPAVGFG---TFANEGAKGE-TYAAVTKALDVGYRHLDCAWFYLN---EDEVGDAVRDFlkenpSVKREDLFICTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 VFfgagtklpntTGLSR-KHIIEGLNASLKRLGLPYVDVIMAHRP------DPSVPM-----------------EEVVRA 151
Cdd:cd19122 78 VW----------NHLHEpEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 152 FTQLIQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQPQYNyltrdhfekDLLPLQQIYGYGatvwspLKSGILT 231
Cdd:cd19122 148 MEEIYESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIH---------PFLPNEELVDYC------FSNDILP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 GKYNdgiPEGSrlsttftslagQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVEN 311
Cdd:cd19122 209 EAYS---PLGS-----------QNQVPSTGERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESN 272
|
....*...
gi 19076016 312 VKAVEFID 319
Cdd:cd19122 273 FKSIELSD 280
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
50-332 |
8.68e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 61.91 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 50 LKQAWDLGINTFDTAEIYSNGnsetVMGKAIKE-LGWDRSEYVITTKVFFGAGTKLPNTTGLSRKHIIEGLNASLKRLGL 128
Cdd:PRK10376 46 LREAVALGVNHIDTSDFYGPH----VTNQLIREaLHPYPDDLTIVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 129 PYVDV----IM--AHRPDPSvPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVadQPQYNYLTRD 202
Cdd:PRK10376 122 DVLDVvnlrLMgdGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE----IVCV--QNHYNLAHRA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 203 hfeKDLLplqqIYGYGAtvwsplksgiltgkynDGI------PEGSrlsttFTSLagqlqtpegktqldQVRQISKIAEQ 276
Cdd:PRK10376 195 ---DDAL----IDALAR----------------DGIayvpffPLGG-----FTPL--------------QSSTLSDVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19076016 277 IGATPSQLALAWTLKNpyvSTTIL---GASKPEQIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:PRK10376 233 LGATPMQVALAWLLQR---SPNILlipGTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
46-330 |
4.08e-10 |
|
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: 59.54 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 46 TKNCLKQAWDLGINTFDTAEIYsnGNSETVmGKAIKELGWDRSEYVITTKVffGAGTKLPNTTGLSrkhiiegLNASLKR 125
Cdd:cd19130 25 TQRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL--WNDRHDGDEPAAA-------FAESLAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 126 LGLPYVDVIMAHRPDPSVPME-EVVRAFTQLIQDGKAFYWGTSEwsaFEIEHAHHIAtKYNLIAPVADQPQYNYLTRDHF 204
Cdd:cd19130 93 LGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSN---FLPPHLERIV-AATGVVPAVNQIELHPAYQQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 205 EKDllpLQQIYGYGATVWSPLksgiltgkyndgipegsrlsttftslaGQlqtpeGKTQLDQVrqISKIAEQIGATPSQL 284
Cdd:cd19130 169 IRD---WAQAHDVKIEAWSPL---------------------------GQ-----GKLLGDPP--VGAIAAAHGKTPAQI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19076016 285 ALAWTLKNPYvsTTILGASKPEQIVENVKAVEFidKLTPEILKKID 330
Cdd:cd19130 212 VLRWHLQKGH--VVFPKSVRRERMEDNLDVFDF--DLTDTEIAAID 253
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
34-324 |
5.59e-10 |
|
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: 59.46 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 34 LTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL----GWDRSEYVITTKVFfgagtklpnTTG 109
Cdd:cd19128 4 LGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGN---EAFIGIAFSEIfkdgGVKREDLFITSKLW---------PTM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 110 LSRKHIIEGLNASLKRLGLPYVDVIMAHRP-------------------DPSVPMEEVVRAFTQLIQDGKAFYWGTSEWS 170
Cdd:cd19128 72 HQPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 171 -AFEIEhahhiATKYNLIAPVADQPQYN-YLTRDHFEKdlLPLQQiyGYGATVWSPlksgiLTGKYNDgipegsrlsttf 248
Cdd:cd19128 152 tKLLTD-----LLNYCKIKPFMNQIECHpYFQNDKLIK--FCIEN--NIHVTAYRP-----LGGSYGD------------ 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076016 249 tslagqlqtpeGKTQLDQVRQISKIAEQIGATPSQLALAWTLKN-PYVSTTILGASKPEQIVENVKAVEFidKLTPE 324
Cdd:cd19128 206 -----------GNLTFLNDSELKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDL--ALTKE 269
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
21-332 |
6.19e-10 |
|
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: 59.08 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKEL---GWDRSEYVITTKVF 97
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGE------VKAAVAHALKIGYRHIDGALCYQN---EDEVGEGIKEAiagGVKREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 98 FGAGTKlpnttglsrkhIIEGLNASLKRLGLPYVDVIMAHRPDPSVP---------MEEVVRAFTQ-------------L 155
Cdd:cd19121 79 STYHRR-----------VELCLDRSLKSLGLDYVDLYLVHWPVLLNPngnhdlfptLPDGSRDLDWdwnhvdtwkqmekV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 156 IQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQ----PQynyltrdhfekdlLPLQQIYGYGatvwspLKSGILT 231
Cdd:cd19121 148 LKTGKTKAIGVSNYSIPYLEELLKHAT----VVPAVNQvenhPY-------------LPQQELVDFC------KEKGILI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 GKYNdgiPEGSRlsttftslAGQLQTPEGktqldqvrqISKIAEQIGATPSQLALAWTLKNPyvSTTILGASKPEQIVEN 311
Cdd:cd19121 205 EAYS---PLGST--------GSPLISDEP---------VVEIAKKHNVGPGTVLISYQVARG--AVVLPKSVTPDRIKSN 262
|
330 340
....*....|....*....|.
gi 19076016 312 VKAVefidKLTPEILKKIDEI 332
Cdd:cd19121 263 LEII----DLDDEDMNKLNDI 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
21-330 |
1.26e-09 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 58.55 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWLTYGNEgydvehTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKE-----LGWDRSEYVITTK 95
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQ------VKAAVKYALDAGYRHIDCAAVYGN---EQEVGEALKEkvgpgKAVPREDLFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 96 vffgagtkLPNTtglsrKH----IIEGLNASLKRLGLPYVDVIMAHRP------------DP-------SVPMEEVVRAF 152
Cdd:cd19106 74 --------LWNT-----KHhpedVEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpkNPdgtirydSTHYKETWKAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 153 TQLIQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQPQ-YNYLTrdhfEKDLLPLQQIYGYGATVWSPLKSgilt 231
Cdd:cd19106 141 EKLVDKGLVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVEcHPYLA----QNELIAHCKARGLVVTAYSPLGS---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 gkyndgiPEGSrlsttftslagqLQTPEGKTQLDQVRqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVEN 311
Cdd:cd19106 209 -------PDRP------------WAKPDEPVLLEEPK-VKALAKKYNKSPAQILLRWQVQRGVV--VIPKSVTPSRIKQN 266
|
330
....*....|....*....
gi 19076016 312 VKAVEFidKLTPEILKKID 330
Cdd:cd19106 267 IQVFDF--TLSPEEMKQLD 283
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
21-332 |
1.38e-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: 52.45 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 21 SGLKVSAFSLGGWltygneGYDVEHTKNCLKQAWDLGINTFDTAEIYsnGNSETV---MGKAIKELGWDRSEYVITTKVF 97
Cdd:cd19113 7 SGYKMPSVGFGCW------KLDNATAADQIYQAIKAGYRLFDGAEDY--GNEKEVgegVNRAIDEGLVKREELFLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 98 FGAGTKlpnttglsrKHIIEGLNASLKRLGLPYVDVIMAHRP-------------------------DPSVPMEEVVRAF 152
Cdd:cd19113 79 NNFHDP---------KNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 153 TQLIQDGKAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQPQYN-YLTRDHfekdLLPLQQIYGYGATVWSplksgilt 231
Cdd:cd19113 150 EKLVDAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHHpYLQQPK----LIEYAQKAGITITAYS-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 232 gkyndgipegSRLSTTFTSLAGQ--LQTP---EGKTqldqvrqISKIAEQIGATPSQLALAWTLKNPYvsTTILGASKPE 306
Cdd:cd19113 214 ----------SFGPQSFVELNQGraLNTPtlfEHDT-------IKSIAAKHNKTPAQVLLRWATQRGI--AVIPKSNLPE 274
|
330 340
....*....|....*....|....*.
gi 19076016 307 QIVENVKAVEFidKLTPEILKKIDEI 332
Cdd:cd19113 275 RLLQNLSVNDF--DLTKEDFEEIAKL 298
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
22-332 |
5.61e-07 |
|
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: 50.60 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTygnegyDVEHTKNCLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKElgWDRSEYVITTKVFFGag 101
Cdd:cd19155 9 GEKMPVVGLGTWQS------SPEEIETAVDTALEAGYRHIDTAYVYRN---EAAIGNVLKK--WIDSGKVKREELFIV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 102 TKLPNTTglSRKHIIEG-LNASLKRLGLPYVDVIMAHRP---------------------DPSVPMEEVVRAFTQLIQDG 159
Cdd:cd19155 76 TKLPPGG--NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 160 KAFYWGTSEWSAFEIEHAHHIATkynlIAPVADQPQYN-YLTrdhfEKDLLPLQQIYGYGATVWSPLKS-GILTGKYNDG 237
Cdd:cd19155 154 LTRSIGLSNFNREQMARILKNAR----IKPANLQVELHvYLQ----QKDLVDFCSTHSITVTAYAPLGSpGAAHFSPGTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 238 IPEGsrlsttftSLAGQLQTPEgktqldqvrqISKIAEQIGATPSQLALAWTLKNPYVstTILGASKPEQIVENVKAVEF 317
Cdd:cd19155 226 SPSG--------SSPDLLQDPV----------VKAIAERHGKSPAQVLLRWLMQRGVV--VIPKSTNAARIKENFQVFDF 285
|
330
....*....|....*
gi 19076016 318 idKLTPEILKKIDEI 332
Cdd:cd19155 286 --ELTEADMAKLSSL 298
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
270-322 |
4.47e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 44.64 E-value: 4.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 19076016 270 ISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLT 322
Cdd:cd19098 241 LKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLE 293
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
22-141 |
2.70e-03 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 39.08 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 22 GLKVSAFSLGGWLTYGNEGYDVehtkncLKQAWDLGINTFDTAEIYSNgnsETVMGKAIKELgwdRSEYVITTKVFFGAg 101
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEV------IYNAIKVGYRLIDGALLYGN---EAEVGRGIRKA---IQEGLVKREDLFIV- 67
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19076016 102 TKLPNTTGlSRKHIIEGLNASLKRLGLPYVDVIMAHRPDP 141
Cdd:cd19114 68 TKLWNNFH-GKDHVREAFDRQLKDYGLDYIDLYLIHFPIP 106
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
51-147 |
7.71e-03 |
|
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: 37.59 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076016 51 KQAWDLGINTFDTAEIYSNgnsETVMGKAIKELGWD----RSEYVITTKVFfgagtklpnTTGLSRKHIIEGLNASLKRL 126
Cdd:cd19108 34 KLAIDAGFRHIDSAYLYQN---EEEVGQAIRSKIADgtvkREDIFYTSKLW---------CTFHRPELVRPALEKSLKKL 101
|
90 100
....*....|....*....|.
gi 19076016 127 GLPYVDVIMAHRPDPSVPMEE 147
Cdd:cd19108 102 QLDYVDLYLIHFPVALKPGEE 122
|
|
| |
