|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-296 |
1.33e-93 |
|
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: 277.82 E-value: 1.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 12 MVSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCGRALNPHT 91
Cdd:cd19086 2 EVSEIGFGTWGLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNRFDGGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 --AEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGKLIDYGVSIETAEEGLLAMEY-DI 168
Cdd:cd19086 82 erPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRgGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 169 AAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRynactqfgkddhrtfnrngeafdkgetfsgvdyqlgl 248
Cdd:cd19086 162 DVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK------------------------------------- 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 493290592 249 qaveelkalfgtedLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAV 296
Cdd:cd19086 205 --------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-320 |
2.51e-93 |
|
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: 280.14 E-value: 2.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTKWGEPfNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYV 79
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPWGGV-DEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPrDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 80 VTKCGRALNP-HTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRnDEIFTKLEQLKAGGKLIDYGVSIETAE 158
Cdd:COG0667 80 ATKVGRRMGPgPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPI-EETLGALDELVREGKIRYIGVSNYSAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 159 EGLLAMEY-----DIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFNRngeaf 233
Cdd:COG0667 159 QLRRALAIaeglpPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAATNF----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 234 dkgetFSGVDYQLGLQAVEELKAL---FGTeDLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKV 310
Cdd:COG0667 234 -----VQGYLTERNLALVDALRAIaaeHGV-TPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL-ELSAEDLAAL 306
|
330
....*....|
gi 493290592 311 EDIYNRLIRP 320
Cdd:COG0667 307 DAALAAVPAP 316
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-311 |
7.65e-67 |
|
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: 211.62 E-value: 7.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCG--RALNPH 90
Cdd:cd19084 4 VSRIGLGTWAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGlrWDGGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 91 TAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCP--PTLVyrnDEIFTKLEQLKAGGKLIDYGVSIETAEEGLLAMEY-D 167
Cdd:cd19084 84 VTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPdpNTPI---EETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYgP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 168 IAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFNRNgeafdkgetFSGVDYQLG 247
Cdd:cd19084 161 IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPF---------FRGENFEKN 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493290592 248 LQAVEELKALFGTEDLIPY--ALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVE 311
Cdd:cd19084 232 LEIVDKLKEIAEKYGKSLAqlAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW-ELTEEELKEID 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-314 |
4.71e-66 |
|
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: 209.48 E-value: 4.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTKWGePFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDF---FYVVTKCGRALNPHTA 92
Cdd:pfam00248 1 IGLGTWQLGGGWG-PISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKrdkVVIATKVPDGDGPWPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 EMyTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRnDEIFTKLEQLKAGGKLIDYGVS---IETAEEGLLAMEYDIA 169
Cdd:pfam00248 80 GG-SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPI-EETWDALEELKKEGKIRAIGVSnfdAEQIEKALTKGKIPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 170 AMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFNRNGeafdkgetfsGVDYQLGLQ 249
Cdd:pfam00248 158 AVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKG----------TPLNLEALE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493290592 250 AVEELKALFGtEDLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVEDIY 314
Cdd:pfam00248 228 ALEEIAKEHG-VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEF-PLSDEEVARIDELL 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-313 |
8.05e-54 |
|
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: 177.78 E-value: 8.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQL-GTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCGralnpht 91
Cdd:cd19085 1 VSRLGLGCWQFgGGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVS------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 AEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVyRNDEIFTKLEQLKAGGKLIDYGVS---IETAEEgllAMEYD- 167
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDV-PLEETMEALEKLKEEGKIRAIGVSnfgPAQLEE---ALDAGr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 168 IAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTfnRNGEAFDKGEtfsgvdYQLG 247
Cdd:cd19085 150 IDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDART--RLFRHFEPGA------EEET 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290592 248 LQAVEELKALFGTEDLIPY--ALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVEDI 313
Cdd:cd19085 222 FEALEKLKEIADELGVTMAqlALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-319 |
2.13e-47 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 163.45 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTKwgepfNHQEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYPDFFYVV 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRK-----DEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGPRDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 81 TKCgralnphTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTL-----VYRNDEIFTKLEQLKAGGKlIDY-GVS- 153
Cdd:COG1453 74 TKL-------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEedlekVLKPGGALEALEKAKAEGK-IRHiGFSt 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 154 ---IETAEEglLAMEYDIAAMEVIFNMF--RLKPLEQLFPTAQQKNVGIIARVLLASGLLTgrynactqfgkddhrtfnr 228
Cdd:COG1453 146 hgsLEVIKE--AIDTGDFDFVQLQYNYLdqDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 229 ngeafdkgetfsgvdyqlglQAVEELKALFGTEDLIP-YALRWVLMNEAVSTVIPGASKVSQVITNAAV-DNFPPLTENE 306
Cdd:COG1453 205 --------------------NPPEKLVELLCPPLSPAeWALRFLLSHPEVTTVLSGMSTPEQLDENLKTaDNLEPLTEEE 264
|
330
....*....|...
gi 493290592 307 MQKVEDIYNRLIR 319
Cdd:COG1453 265 LAILERLAEELGE 277
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-301 |
3.13e-44 |
|
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: 153.13 E-value: 3.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVV-TKCGRALNPHT 91
Cdd:cd19074 4 VSELSLGTW---LTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVIsTKVFWPTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 AE--MYTPQAIEKfVDGSLSHLGTEKLDMILLH-----CPPtlvyrnDEIFTKLEQLKAGGKLIDYGVSIETAEEglLAM 164
Cdd:cd19074 81 NDrgLSRKHIFES-IHASLKRLQLDYVDIYYCHrydpeTPL------EETVRAMDDLIRQGKILYWGTSEWSAEQ--IAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 165 EYDIA---------AMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFNRNGEAFDK 235
Cdd:cd19074 152 AHDLArqfglippvVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEDNRDKKRR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 236 GETfsgvDYQlgLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITN--AAVDNFPP 301
Cdd:cd19074 232 LLT----DEN--LEKVKKLKPIADELGLTLaqLALAWCLRNPAVSSAIIGASRPEQLEENvkASGVKLSP 295
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-296 |
6.08e-44 |
|
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: 151.23 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWGePFNHQEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYP-DFFYVVTKCG---RALNP 89
Cdd:cd19095 1 SVLGLGTSGIGRVWG-VPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRrDDLFIATKVGthgEGGRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 90 HTAemYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPtLVYRNDEIFTKLEQLKAGGKlIDY-GVSIETAE-EGLLAMEyD 167
Cdd:cd19095 78 RKD--FSPAAIRASIERSLRRLGTDYIDLLQLHGPS-DDELTGEVLETLEDLKAAGK-VRYiGVSGDGEElEAAIASG-V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 168 IAAMEVIFNMFRLKpLEQLFPTAQQKNVGIIARVLLASGLLTGRynactqfgkddhrtfnrngeafdkgetFSGVDYQLG 247
Cdd:cd19095 153 FDVVQLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRLRRR---------------------------VRRRPLYAD 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493290592 248 LQAVEELKALFGTEDLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAV 296
Cdd:cd19095 205 YARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-311 |
1.17e-42 |
|
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: 148.92 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKW---GEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDF--FYVVTKCgrAL 87
Cdd:cd19093 2 VSPLGLGTWQWGDRLwwgYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRdeVVIATKF--AP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 NPHTAemyTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGkLIDY-GVS------IETAEEG 160
Cdd:cd19093 80 LPWRL---TRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMDGLADAVEEG-LVRAvGVSnysadqLRRAHKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 161 LLAMEYDIAAMEVIFNMFRLKPLEQ-LFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFNRngEAFDKgetf 239
Cdd:cd19093 156 LKERGVPLASNQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGR--KNLEK---- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 240 sgvDYQLgLQAVEEL-KALFGTedLIPYALRWVLMNEAVstVIPGASKVSQVITNAAVDNFpPLTENEMQKVE 311
Cdd:cd19093 230 ---VQPL-LDALEEIaEKYGKT--PAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW-RLSEEEVAELD 293
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
4-294 |
2.96e-42 |
|
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: 148.57 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWQLGT-KWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTK 82
Cdd:cd19149 2 RKLGKSGIEASVIGLGTWAIGGgPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLATK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 83 CG------RALNPHTAEMYT------PQAIEKFVDGSLSHLGTEKLDMILLH--CPPTLVyrnDEIFTKLEQLKAGGKLI 148
Cdd:cd19149 82 CGlrwdreGGSFFFVRDGVTvyknlsPESIREEVEQSLKRLGTDYIDLYQTHwqDVETPI---EETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 149 DYGVSIETAEEGLLAMEY-DIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHrtfn 227
Cdd:cd19149 159 AIGASNVSVEQIKEYVKAgQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDA---- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493290592 228 RNGEAFDKGETFSGVdyqlgLQAVEELKALFGTED--LIPYALRWVLMNEAVSTVIPGASKVSQVITNA 294
Cdd:cd19149 235 RSGIPWFSPENREKV-----LALLEKWKPLCEKYGctLAQLVIAWTLAQPGITSALCGARKPEQAEENA 298
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-295 |
3.12e-42 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 146.12 E-value: 3.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWGEpfnhQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP--DFFYVVTKCG-RALNPH 90
Cdd:cd06660 1 SRLGLGTMTFGGDGDE----EEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGnrDDVVIATKGGhPPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 91 TAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRnDEIFTKLEQLKAGGKLIDYGVSIETAEEGLLAMEY---- 166
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPV-EETLEALNELVREGKIRYIGVSNWSAERLAEALAYakah 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 167 ---DIAAMEVIFNMFRLKPLEQ-LFPTAQQKNVGIIARVLLASGLltgrynacTQFgkddhrtfnrngeafdkgetfsgv 242
Cdd:cd06660 156 glpGFAAVQPQYSLLDRSPMEEeLLDWAEENGLPLLAYSPLARGP--------AQL------------------------ 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 493290592 243 dyqlglqaveelkalfgtedlipyALRWVLMNEAVSTVIPGASKVSQVITNAA 295
Cdd:cd06660 204 ------------------------ALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-313 |
5.03e-41 |
|
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: 144.76 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 11 KMVSEIGLGTWQL-GTKWGEPfNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKY--PDFFYVVTKCGraL 87
Cdd:cd19148 2 LPVSRIALGTWAIgGWMWGGT-DEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgkRDRVVIATKVG--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 NPHTAEMY----TPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVyRNDEIFTKLEQLKAGGKLIDYGVSIETAEEglla 163
Cdd:cd19148 79 EWDEGGEVvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLV-PIEETAEALKELLDEGKIRAIGVSNFSPEQ---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 164 MEY-----DIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRtfnRNGEAFdKGET 238
Cdd:cd19148 154 METfrkvaPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLR---RTDPKF-QEPR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493290592 239 FSGvdYqlgLQAVEELKAL----FGTeDLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVEDI 313
Cdd:cd19148 230 FSQ--Y---LAAVEELDKLaqerYGK-SVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGW-SLNDEDMKEIDAI 301
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-296 |
3.42e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 141.18 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTkwgepfnhqEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYV 79
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPR---------ESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRrDKVFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 80 VTKCgralnPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLH--CPPTLVYRNDEIFTKLEQLKAGGKlIDY-GVSIET 156
Cdd:cd19105 72 ATKA-----SPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHgvDTPEERLLNEELLEALEKLKKEGK-VRFiGFSTHD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 157 AEEGLL--AME---YDIaAMeVIFN-MFRLKPLEQLFPTAQQKNVGIIARVLLASGlltgrynactqfgkddhrTFNRNG 230
Cdd:cd19105 146 NMAEVLqaAIEsgwFDV-IM-VAYNfLNQPAELEEALAAAAEKGIGVVAMKTLAGG------------------YLQPAL 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493290592 231 EAFDKGETFSGVdyqlglQAveelkalfgtedlipyALRWVLMNEAVSTVIPGASKVSQVITNAAV 296
Cdd:cd19105 206 LSVLKAKGFSLP------QA----------------ALKWVLSNPRVDTVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-314 |
3.82e-37 |
|
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: 134.85 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWQLGTKWGEP-FNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVT 81
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNLYPnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNrNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 82 KCGRALNPHTAEM-YTPQAIEKFVDGSLSHLGTEKLDMILLHCP----PTlvyrnDEIFTKLEQLKAGGKLIDYGVSIET 156
Cdd:cd19083 82 KGAHKFGGDGSVLnNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPdgetPK-----AEAVGALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 157 AEEgLLAMEYD--IAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTfnrngeafD 234
Cdd:cd19083 157 LEQ-LKEANKDgyVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRN--------D 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 235 KGEtFSGVDYQLGLQAVEELKALFGTE--DLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVED 312
Cdd:cd19083 228 KPL-FKGERFSENLDKVDKLKSIADEKgvTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV-TLTEEEIAFIDA 305
|
..
gi 493290592 313 IY 314
Cdd:cd19083 306 LF 307
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-309 |
1.08e-36 |
|
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: 133.50 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 2 KQRRFGKTNKMVSEIGLGTWQLGTKWGePFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVT 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYG-PADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 82 KCGRALNPHTAEMY---TPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTkLEQLKAGGKLIDYGVSIETAE 158
Cdd:cd19076 80 KFGIVRDPGSGFRGvdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGA-MAELVEEGKVRYIGLSEASAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 159 EGLLAME-YDIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFN-R-NGEAFDK 235
Cdd:cd19076 159 TIRRAHAvHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNpRfQGENFDK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493290592 236 getfsgvdyqlGLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITN-AAVDnfPPLTENEMQK 309
Cdd:cd19076 239 -----------NLKLVEKLEAIAAEKGCTPaqLALAWVLAQGDDIVPIPGTKRIKYLEENvGALD--VVLTPEELAE 302
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-295 |
1.08e-36 |
|
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: 132.65 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWG------EPfNHQEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYPDFFyVVTKCgRAL 87
Cdd:cd19097 1 SKLALGTAQFGLDYGianksgKP-SEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFK-IITKL-PPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 NPHTAEmyTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGKLIDYGVSIETAEEGLLAME-Y 166
Cdd:cd19097 76 KEDKKE--DEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALEsF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 167 DIAAMEVIFNMF--RLKpLEQLFPTAQQKNVGIIAR-VLLaSGLLTGRYNACTQFgkddhrtFNRNGEAFDKGETFSGvd 243
Cdd:cd19097 154 KIDIIQLPFNILdqRFL-KSGLLAKLKKKGIEIHARsVFL-QGLLLMEPDKLPAK-------FAPAKPLLKKLHELAK-- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 493290592 244 yQLGLqaveelkalfgteDLIPYALRWVLMNEAVSTVIPGASKVSQVITNAA 295
Cdd:cd19097 223 -KLGL-------------SPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIA 260
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-295 |
4.14e-35 |
|
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: 127.60 E-value: 4.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 3 QRRFGKTNKMVSEIGLGTWQLGTKWGEpfnhqEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYPDFFYVVTK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQE-----EAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKGRRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 83 CGRalnphtaemYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTL-----VYRNDEIFTKLEQLKAGGKlIDY-GVSIET 156
Cdd:cd19100 74 TGA---------RDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEedldqVFGPGGALEALLEAKEEGK-IRFiGISGHS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 157 AEEGLLAME-YDIAAMEVIFN---MFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTgrynactqfgkddhrtfnrNGEA 232
Cdd:cd19100 144 PEVLLRALEtGEFDVVLFPINpagDHIDSFREELLPLAREKGVGVIAMKVLAGGRLL-------------------SGDP 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 233 FDKGEtfsgvdyqlglqaveelkalfgtedlipyALRWVLMNEAVSTVIPGASKVSQVITNAA 295
Cdd:cd19100 205 LDPEQ-----------------------------ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-300 |
1.14e-34 |
|
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: 127.67 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWGePFNHQEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYP-DFFYVVTKCGRALNPHTA 92
Cdd:cd19090 1 SALGLGTAGLGGVFG-GVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPrEPLVLSTKVGRLPEDTAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 emYTPQAIEKFVDGSLSHLGTEKLDMILLH----CPPTLVYRNDEIFTKLEQLKAGGkLIDYgvsIetaeeGLLAMEYDI 168
Cdd:cd19090 78 --YSADRVRRSVEESLERLGRDRIDLLMIHdperVPWVDILAPGGALEALLELKEEG-LIKH---I-----GLGGGPPDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 169 AA-------MEVI-----FNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRynactqfgkDDHRTFNRNGEAFDKG 236
Cdd:cd19090 147 LRraietgdFDVVltanrYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGR---------PPERVRYTYRWLSPEL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493290592 237 etfsgvdyqlgLQAVEELKALFGTE--DLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFP 300
Cdd:cd19090 218 -----------LDRAKRLYELCDEHgvPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGP 272
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-314 |
1.24e-34 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 128.17 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQL-GTKWGEPFNHQ---EAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCGRAL- 87
Cdd:cd19102 1 LTTIGLGTWAIgGGGWGGGWGPQddrDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLLWd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 -NPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLH--CPPTLVyrnDEIFTKLEQLKAGGKLIDYGVSietaeegllam 164
Cdd:cd19102 81 eEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHwpDPDEPI---EEAWGALAELKEEGKVRAIGVS----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 165 EYDIAAMEVI------------FNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACT--QFGKDDHRTFNRNg 230
Cdd:cd19102 147 NFSVDQMKRCqaihpiaslqppYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvaSLPADDWRRRSPF- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 231 eafdkgetFSGVDYQLGLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQ 308
Cdd:cd19102 226 --------FQEPNLARNLALVDALRPIAERHGRTVaqLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL-RLTPEELA 296
|
....*.
gi 493290592 309 KVEDIY 314
Cdd:cd19102 297 EIEALL 302
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-313 |
3.38e-34 |
|
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: 126.92 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTKWGEpfnhQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVV 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDE----ETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 81 TKC----GRALNPHTAEMYTpqaIEKFVDGSLSHLGTEKLDMILLHCPPTLVyRNDEIFTKLEQLKAGGKlIDY-GVS-- 153
Cdd:cd19087 77 TKVfgpmGDDPNDRGLSRRH---IRRAVEASLRRLQTDYIDLYQMHHFDRDT-PLEETLRALDDLVRQGK-IRYiGVSnf 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 154 ----IETAEEglLAMEYDIAAMEVI---FNM-FRLKPLEQLfPTAQQKNVGIIARVLLASGLLTGRYnactqfGKDDHRT 225
Cdd:cd19087 152 aawqIAKAQG--IAARRGLLRFVSEqpmYNLlKRQAELEIL-PAARAYGLGVIPYSPLAGGLLTGKY------GKGKRPE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 226 FNRNGEAFDKGETFSGVDYQLGLQAVEELKALFGtEDLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDnfPPLTE 304
Cdd:cd19087 223 SGRLVERARYQARYGLEEYRDIAERFEALAAEAG-LTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSlAALE--ITLTP 299
|
....*....
gi 493290592 305 NEMQKVEDI 313
Cdd:cd19087 300 ELLAEIDEL 308
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-314 |
3.82e-34 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 127.38 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 2 KQRRFGKTNKMVSEIGLGTWQLGTKWGEPfNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVT 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGLMGRT-TREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 82 KCGRALNPhTAEMYtpQAIEKFVDGSLSHLGTEKLDMILLH--------------CPPTLVYRNDEIFTKLEQLKAGGKL 147
Cdd:cd19104 80 KVRLDPDD-LGDIG--GQIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvggtLSTTDVLGLGGVADAFERLRSEGKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 148 IDYGVS----IETAEEGLLAMEYDI-----------AAMEVIfNMFRLKPLEQLFPTAQQKNVGIIA-RVlLASGLLTGr 211
Cdd:cd19104 157 RFIGITglgnPPAIRELLDSGKFDAvqvyynllnpsAAEARP-RGWSAQDYGGIIDAAAEHGVGVMGiRV-LAAGALTT- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 212 ynactqfgkddhrTFNRNGEAFDkgetFSGVDYQLGLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQ 289
Cdd:cd19104 234 -------------SLDRGREAPP----TSDSDVAIDFRRAAAFRALAREWGETLaqLAHRFALSNPGVSTVLVGVKNREE 296
|
330 340
....*....|....*....|....*
gi 493290592 290 VITNAAVDNFPPLTENEMQKVEDIY 314
Cdd:cd19104 297 LEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
12-312 |
1.40e-33 |
|
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: 125.42 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 12 MVSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCGRALNPHT 91
Cdd:cd19078 3 EVSAIGLGCMGMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKIDGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 AEMYT----PQAIEKFVDGSLSHLGTEKLDMILLHcpptlvyRND------EIFTKLEQLKAGGKLIDYGVSiETAEEGL 161
Cdd:cd19078 83 PGPLGldsrPEHIRKAVEGSLKRLQTDYIDLYYQH-------RVDpnvpieEVAGTMKELIKEGKIRHWGLS-EAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 162 -LAME-YDIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRT--FNRNGEAFDKGE 237
Cdd:cd19078 155 rRAHAvCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRAslPRFTPEALEANQ 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493290592 238 TFsgvdyqlglqaVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVED 312
Cdd:cd19078 235 AL-----------VDLLKEFAEEKGATPaqIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI-ELTPEELREIED 299
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-313 |
1.24e-32 |
|
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: 123.09 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKK--YPDFFY 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSW---VTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKElgWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 79 VV-TKC--GRALNPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHcpptlvyRND------EIFTKLEQLKAGGKLID 149
Cdd:cd19143 78 VVsTKIfwGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCH-------RPDpatpieETVRAMNDLIDQGKAFY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 150 YGVSIETAEEgllAME-YDIA--------AMEVI-FNMFRLKPLEQLF-PTAQQKNVGIIARVLLASGLLTGRYNActqf 218
Cdd:cd19143 151 WGTSEWSAQQ---IEEaHEIAdrlglippVMEQPqYNLFHRERVEVEYaPLYEKYGLGTTTWSPLASGLLTGKYNN---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 219 GKDDHRTFNRNGEAFDKGETFSGVDYQlgLQAVEELKALfgTEDL----IPYALRWVLMNEAVSTVIPGASKVSQVITN- 293
Cdd:cd19143 224 GIPEGSRLALPGYEWLKDRKEELGQEK--IEKVRKLKPI--AEELgcslAQLAIAWCLKNPNVSTVITGATKVEQLEENl 299
|
330 340
....*....|....*....|
gi 493290592 294 AAVDNFPPLTENEMQKVEDI 313
Cdd:cd19143 300 KALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-313 |
3.08e-32 |
|
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: 122.17 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYP---DFF 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPgkrEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 78 YVVTKCGRALNPHTAEMYT---PQAIEKFVDGSLSHLGTEKLDMILLH--CPPTLVyrnDEIFTKLEQLKAGGKLIDYGV 152
Cdd:cd19144 79 FLATKFGIEKNVETGEYSVdgsPEYVKKACETSLKRLGVDYIDLYYQHrvDGKTPI---EKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 153 SIETAEEGLLAME-YDIAAMEVIFNMFRL---KPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHRTFNR 228
Cdd:cd19144 156 SECSAETLRRAHAvHPIAAVQIEYSPFSLdieRPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRRMAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 229 --NGEAFDKgetfsgvdyqlGLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTE 304
Cdd:cd19144 236 rfQAENFPK-----------NLELVDKIKAIAKKKNVTAgqLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV-KLTE 303
|
....*....
gi 493290592 305 NEMQKVEDI 313
Cdd:cd19144 304 EEEKEIREI 312
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-290 |
3.39e-32 |
|
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: 121.55 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 5 RFGKTNKMVSEIGLGTWQLGTKWGEpfnhQEAMAILETAYEQGINFIDTADVYN-------NGQSEKAIGDILKKYP--D 75
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTADE----ETSFALLDAFVDAGGNFIDTADVYSawvpgnaGGESETIIGRWLKSRGkrD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 76 FFYVVTKCGRALNPHtAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRnDEIFTKLEQLKAGGKLIDYGVS-- 153
Cdd:cd19081 77 RVVIATKVGFPMGPN-GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPL-EETLGALNDLIRQGKVRYIGASny 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 154 --------IETAEEGLLAMeydIAAMEVIFNMFRLKPLEQ-LFPTAQQKNVGIIARVLLASGLLTGRYNActqfgKDDHR 224
Cdd:cd19081 155 sawrlqeaLELSRQHGLPR---YVSLQPEYNLVDRESFEGeLLPLCREEGIGVIPYSPLAGGFLTGKYRS-----EADLP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290592 225 TFNRNGEAFDKGETFSGVDYqlgLQAVEELKALFGTEdliP--YALRWVLMNEAVSTVIPGASKVSQV 290
Cdd:cd19081 227 GSTRRGEAAKRYLNERGLRI---LDALDEVAAEHGAT---PaqVALAWLLARPGVTAPIAGARTVEQL 288
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-313 |
8.67e-32 |
|
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: 121.13 E-value: 8.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTwqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVY-------NNGQSEKAIGDILKKYP--DFFYVVTK- 82
Cdd:cd19094 1 VSEICLGT----MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKKKGnrDKVVLATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 83 CGRALN----PHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLV----------YRNDEIFTKL-EQLKAGGKL 147
Cdd:cd19094 77 AGPGEGitwpRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTplfgggyytePSEEEDSVSFeEQLEALGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 148 ID------YGVSIETAeEGLlaMEY----------DIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGR 211
Cdd:cd19094 157 VKagkirhIGLSNETP-WGV--MKFlelaeqlglpRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 212 YNAcTQFGKDDHR--TFNRNGEAFDKgetfsgvdyQLGLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKV 287
Cdd:cd19094 234 YLD-GAARPEGGRlnLFPGYMARYRS---------PQALEAVAEYVKLARKHGLSPaqLALAWVRSRPFVTSTIIGATTL 303
|
330 340
....*....|....*....|....*..
gi 493290592 288 SQVITN-AAVDnfPPLTENEMQKVEDI 313
Cdd:cd19094 304 EQLKENiDAFD--VPLSDELLAEIDAV 328
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-304 |
2.32e-31 |
|
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: 119.19 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTKWGePFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYV 79
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFG-PVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPrDSYYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 80 VTKCGR-ALNPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLH---CPPTLvyrnDEIFTK----LEQLKAGGKLIDYG 151
Cdd:cd19163 80 ATKVGRyGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdieFAPSL----DQILNEtlpaLQKLKEEGKVRFIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 152 VS---IETAEEgllAMEYDIAAMEVIFNMFRL----KPLEQLFPTAQQKNVGIIARVLLASGLLTGRynactqfGKDD-H 223
Cdd:cd19163 156 ITgypLDVLKE---VLERSPVKIDTVLSYCHYtlndTSLLELLPFFKEKGVGVINASPLSMGLLTER-------GPPDwH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 224 RTFNRNGEAFDKGETFS---GVDyqlglqaVEELkalfgtedlipyALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFP 300
Cdd:cd19163 226 PASPEIKEACAKAAAYCksrGVD-------ISKL------------ALQFALSNPDIATTLVGTASPENLRKNLEAAEEP 286
|
....
gi 493290592 301 PLTE 304
Cdd:cd19163 287 LDAH 290
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-311 |
2.67e-31 |
|
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: 118.10 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 10 NKMVSEIGLGTWQLGTKWGEPFNH-QEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVTKcgraL 87
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDdKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDrEDLFITTK----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 NPHTAemyTPQAIEKFVDGSLSHLGTEKLDMILLHCPptlvyrND-----EIFTKLEQLKAGGKlIDY-GVS---IETAE 158
Cdd:cd19072 77 SPDHL---KYDDVIKAAKESLKRLGTDYIDLYLIHWP------NPsipieETLRAMEELVEEGK-IRYiGVSnfsLEELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 159 EGLLAME-YDIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTgrynactqfGKDDHRTFNRNGEAFDKge 237
Cdd:cd19072 147 EAQSYLKkGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLS---------NAKGSPLLDEIAKKYGK-- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493290592 238 TFSGVdyqlglqaveelkalfgtedlipyALRWvLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQKVE 311
Cdd:cd19072 216 TPAQI------------------------ALNW-LISKPNVIAIPKASNIEHLEENAGALGW-ELSEEDLQRLD 263
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-311 |
8.65e-31 |
|
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: 118.07 E-value: 8.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 2 KQRRFGKTNKMVSEIGLGTWQLG-TKWGE-PFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYV 79
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGdPKWRPwVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 80 V--TKCGRALNPHT-AEMYTPQAIEKFVDGSLSHLGTEKLDMILLHcpptlvyRND------EIFTKLEQLKAGGKLIDY 150
Cdd:cd19079 81 ViaTKVYFPMGDGPnGRGLSRKHIMAEVDASLKRLGTDYIDLYQIH-------RWDyetpieETLEALHDVVKSGKVRYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 151 GVS----------IETAE-EGLLAMeydiAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYnactqfG 219
Cdd:cd19079 154 GASsmyawqfakaLHLAEkNGWTKF----VSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPW------G 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 220 KDDHRTFNRNGEAFDKGETFSGVDYQLgLQAVEELKALFGTEdLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDn 298
Cdd:cd19079 224 DTTERRRSTTDTAKLKYDYFTEADKEI-VDRVEEVAKERGVS-MAQVALAWLLSKPGVTAPIVGATKLEHLEDAvAALD- 300
|
330
....*....|...
gi 493290592 299 fPPLTENEMQKVE 311
Cdd:cd19079 301 -IKLSEEEIKYLE 312
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-308 |
1.14e-30 |
|
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: 117.71 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKC 83
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 84 GRALNP--------HTAEMYtpQAiekfVDGSLSHLGTEKLDMILLHCP----PTlvyrnDEIFTKLEQLKAGGKLIDYG 151
Cdd:cd19080 81 TMNRRPgdpnaggnHRKNLR--RS----VEASLRRLQTDYIDLLYVHAWdfttPV-----EEVMRALDDLVRAGKVLYVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 152 VS------IETAEEglLAMEYD---IAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNactqfgKDD 222
Cdd:cd19080 150 ISdtpawvVARANT--LAELRGwspFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQ------RGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 223 HRTFNRNGEAFDKGETFSGVDYQLglqaVEELKALfGTEDLIP---YALRWVLMNEAVSTVIPGASKVSQVITNAAVDNF 299
Cdd:cd19080 222 EGRAGEAKGVTVGFGKLTERNWAI----VDVVAAV-AEELGRSaaqVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
....*....
gi 493290592 300 pPLTENEMQ 308
Cdd:cd19080 297 -TLSPEQLA 304
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-313 |
1.30e-29 |
|
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: 115.02 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQLGTKWGePFNH------QEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP 74
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGG-FFGAwggvdqEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 75 DFFYVVTKC----GRALNPHTAEMYtpqAIEKFVDGSLSHLGTEKLDMILLHC--PPTLVyrnDEIFTKLEQLKAGGKLI 148
Cdd:cd19091 80 DDVLIATKVrgrmGEGPNDVGLSRH---HIIRAVEASLKRLGTDYIDLYQLHGfdALTPL---EETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 149 DYGVS------IETA-----EEGL-----LAMEYDIAAMEVIFnmfrlkpleQLFPTAQQKNVGIIARVLLASGLLTGRY 212
Cdd:cd19091 154 YIGVSnfsawqIMKAlgiseRRGLarfvaLQAYYSLLGRDLEH---------ELMPLALDQGVGLLVWSPLAGGLLSGKY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 213 NAcTQFGKDDHRTFNRNGEafdkgetFSGVDYQLGLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQV 290
Cdd:cd19091 225 RR-GQPAPEGSRLRRTGFD-------FPPVDRERGYDVVDALREIAKETGATPaqVALAWLLSRPTVSSVIIGARNEEQL 296
|
330 340
....*....|....*....|....
gi 493290592 291 ITN-AAVDnfPPLTENEMQKVEDI 313
Cdd:cd19091 297 EDNlGAAG--LSLTPEEIARLDKV 318
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-301 |
3.87e-29 |
|
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: 112.27 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVTKCgralnpHTA 92
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPrEKFYLATKL------PPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 EMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTL----VYRNDEIFTKLEQLKAGGKLIDYGVSIETAEEGLLAM--EY 166
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPewleKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPELLKEIldSY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 167 DIAAMEVIFNMF--RLKPLEQLFPTAQQKNVGIIARVLLASGLLtgrynactqfgkddhrtfnrngeafdkgetfsgvdy 244
Cdd:cd19096 155 DFDFVQLQYNYLdqENQAGRPGIEYAAKKGMGVIIMEPLKGGGL------------------------------------ 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 245 qlgLQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITN-AAVDNFPP 301
Cdd:cd19096 199 ---ANNPPEALAILCGAPLSPaeWALRFLLSHPEVTTVLSGMSTPEQLDENiAAADEFEP 255
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-293 |
3.99e-29 |
|
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: 113.57 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWgEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVTKCGRALNPHTA 92
Cdd:cd19161 1 SELGLGTAGLGNLY-TAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPrDEFVLSTKVGRLLKPARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 EM------------------YTPQAIEKFVDGSLSHLGTEKLDMILLH--CPPTLVYRNDEI---------FTKLEQLKA 143
Cdd:cd19161 80 GSvpdpngfvdplpfeivydYSYDGIMRSFEDSLQRLGLNRIDILYVHdiGVYTHGDRKERHhfaqlmsggFKALEELKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 144 GGKLIDYGVSIETAEEGLLAMEY---DIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGrynactqfGK 220
Cdd:cd19161 160 AGVIKAFGLGVNEVQICLEALDEadlDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILAT--------GT 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493290592 221 DDHRTFNRNG---EAFDKGEtfsgvdyqlglqAVEELKALFGTEdLIPYALRWVLMNEAVSTVIPGASKVSQVITN 293
Cdd:cd19161 232 KSGAKFNYGDapaEIISRVM------------EIEKICDAYNVP-LAAAALQFPLRHPAVASVLTGARNPAQLRQN 294
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
13-153 |
8.09e-29 |
|
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: 112.26 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGEPfnhQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDF---FYVVTKCG----R 85
Cdd:cd19092 6 VSRLVLGCMRLADWGESA---EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLrekIEIQTKCGirlgD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 86 ALNPHTAEMY--TPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVyRNDEIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19092 83 DPRPGRIKHYdtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLM-DPEEVAEAFDELVKSGKVRYFGVS 151
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-295 |
1.42e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 109.33 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTkwgEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDF-------FYVVTKCG- 84
Cdd:cd19099 3 LSSLGLGTYRGDS---DDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKggikrdeVVIVTKAGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 85 ---RALNPHTAEMY----------------------TPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLV---------YR 130
Cdd:cd19099 80 ipgDGDEPLRPLKYleeklgrglidvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLlelgeeefyDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 131 NDEIFTKLEQLKAGGKLIDYGVSIETA------------EEGLLAMEYDIA-------AMEVIFNMFRLKPLEQ------ 185
Cdd:cd19099 160 LEEAFEALEEAVAEGKIRYYGISTWDGfrappalpghlsLEKLVAAAEEVGgdnhhfkVIQLPLNLLEPEALTEkntvkg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 186 ----LFPTAQQKNVGIIARVLLASGLLtgrynactqfgkddhrtfnrngeafdkgetfsgvdyqLGLQAVEELKALFGTE 261
Cdd:cd19099 240 ealsLLEAAKELGLGVIASRPLNQGQL-------------------------------------LGELRLADLLALPGGA 282
|
330 340 350
....*....|....*....|....*....|....
gi 493290592 262 DLIPYALRWVLMNEAVSTVIPGASKVSQVITNAA 295
Cdd:cd19099 283 TLAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-296 |
3.86e-27 |
|
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: 106.92 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTK--WGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCG------ 84
Cdd:cd19088 1 VSRLGYGAMRLTGPgiWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGlvrtgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 85 RALNPHTAEMYTPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRnDEIFTKLEQLKAGGKLIDYGVS------IETAE 158
Cdd:cd19088 81 GWWGPDGSPEYLRQAVEA----SLRRLGLDRIDLYQLHRIDPKVPF-EEQLGALAELQDEGLIRHIGLSnvtvaqIEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 159 EgllamEYDIAAMEVIFNMFRLKPlEQLFPTAQQKNVGIIARVLLASGLLTGRynactqfgkddhrtfnrngeafdkGET 238
Cdd:cd19088 156 A-----IVRIVSVQNRYNLANRDD-EGVLDYCEAAGIAFIPWFPLGGGDLAQP------------------------GGL 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 493290592 239 FSGVDYQLGLQAVEelkalfgtedlipYALRWVLMNEAVSTVIPGASKVSQVITNAAV 296
Cdd:cd19088 206 LAEVAARLGATPAQ-------------VALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-295 |
2.08e-26 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 105.90 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLG--TKWGEpfnhQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVTKCGRALNPH 90
Cdd:cd19162 1 PRLGLGAASLGnlARAGE----DEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPrAEYVVSTKVGRLLEPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 91 TAEM---------YTPQAIEKFVDGSLSHLGTEKLDMILLHCP-PTLVYRNDEIFTKLEQLKAGGKLIDYGVSIETAEEG 160
Cdd:cd19162 77 AAGRpagadrrfdFSADGIRRSIEASLERLGLDRLDLVFLHDPdRHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 161 LLAMEydIAAMEVI-----FNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGrynactqfgkdDHRTfnrnGEAFDK 235
Cdd:cd19162 157 LRAAR--RADVDVVmvagrYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT-----------DDPA----GDRYDY 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493290592 236 GETFSGVdyqlgLQAVEELKALFGTED--LIPYALRWVLMNEAVSTVIPGASKVSQVITNAA 295
Cdd:cd19162 220 RPATPEV-----LARARRLAAVCRRYGvpLPAAALQFPLRHPAVASVVVGAASPAELRDNLA 276
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-306 |
2.79e-25 |
|
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: 103.11 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWQLgtkWGEPFNHQEAMAILETAYEQGINFIDTAdvyNN-----GQSEKAIGDILKK----YP 74
Cdd:cd19089 2 RRCGRSGLHLPAISLGLWHN---FGDYTSPEEARELLRTAFDLGITHFDLA---NNygpppGSAEENFGRILKRdlrpYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 75 DFFYVVTKCGRALNPHTaemYTPQAIEKFV----DGSLSHLGTEKLDMILLHC--PPTLVyrnDEIFTKLEQLKAGGKLI 148
Cdd:cd19089 76 DELVISTKAGYGMWPGP---YGDGGSRKYLlaslDQSLKRMGLDYVDIFYHHRydPDTPL---EETMTALADAVRSGKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 149 DYGVS------IETAEEGLLAMEYDIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYnacTQFGKDD 222
Cdd:cd19089 150 YVGISnypgakARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY---LNGIPPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 223 HRTFnrNGEAFDKGETFSGvDYQLGLQAVEELKALFG--TEDLipyALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFP 300
Cdd:cd19089 227 SRRA--AESKFLTEEALTP-EKLEQLRKLNKIAAKRGqsLAQL---ALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNL 300
|
....*.
gi 493290592 301 PLTENE 306
Cdd:cd19089 301 DFSEEE 306
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-311 |
1.49e-23 |
|
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: 98.08 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 9 TNKMVSEIGLGTWQLgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQ---SEKAIGDILKKYPDFF-YVVTKCG 84
Cdd:cd19077 1 NGKLVGPIGLGLMGL-TWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDphaNLKLLARFFRKYPEYAdKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 85 RALNPHTAEMY-TPQAIEKFVDGSLSHLG-TEKLDmiLLHCPptlvyRNDEIFTKLEQLKAGGKLIDYG---------VS 153
Cdd:cd19077 80 GGLDPDTLRPDgSPEAVRKSIENILRALGgTKKID--IFEPA-----RVDPNVPIEETIKALKELVKEGkirgiglseVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 154 IETAEEGllAMEYDIAAMEVIFNMFRLKPLEQ-LFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDD-HRTFNR-NG 230
Cdd:cd19077 153 AETIRRA--HAVHPIAAVEVEYSLFSREIEENgVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDfRRHLDRfNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 231 EAFDKgetfsgvdyqlGLQAVEELKALFGTEDLIP--YALRWVLM-NEAVSTVIPGASKVSQVITNAAVDNFpPLTENEM 307
Cdd:cd19077 231 ENFEK-----------NLKLVDALQELAEKKGCTPaqLALAWILAqSGPKIIPIPGSTTLERVEENLKAANV-ELTDEEL 298
|
....
gi 493290592 308 QKVE 311
Cdd:cd19077 299 KEIN 302
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-311 |
6.98e-23 |
|
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: 95.78 E-value: 6.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 2 KQRRFGKTNKmVSEIGLGTWQLGTKwgePFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVT 81
Cdd:cd19138 1 RTVTLPDGTK-VPALGQGTWYMGED---PAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 82 KcgraLNPHTAemyTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTlvYRNDEIFTKLEQLKAGGKLIDYGVS-IETAE-E 159
Cdd:cd19138 77 K----VLPSNA---SRQGTVRACERSLRRLGTDYLDLYLLHWRGG--VPLAETVAAMEELKKEGKIRAWGVSnFDTDDmE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 160 GLLAMEY--DIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASG--LLTGRYNactqfgkddHRTFNRNGEAfdk 235
Cdd:cd19138 148 ELWAVPGggNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGglLRRGLLE---------NPTLKEIAAR--- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493290592 236 getfsgvdYQLGLQAVeelkalfgtedlipyALRWVLMNEAVsTVIPGASKVSQVITNAAVDNFpPLTENEMQKVE 311
Cdd:cd19138 216 --------HGATPAQV---------------ALAWVLRDGNV-IAIPKSGSPEHARENAAAADL-ELTEEDLAELD 266
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-313 |
1.70e-22 |
|
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: 95.82 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP---DFF 77
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTW---VTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwrrSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 78 YVVTKCGRALNPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHcpptlvyRNDEIFTKLEQLKAGGKLIDYGVSIETA 157
Cdd:cd19160 80 VVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFAN-------RSDPNSPMEEIVRAMTYVINQGMAMYWG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 158 EEGLLAME----YDIAAM---------EVIFNMFRLKPLEQLFPTAQQK-NVGIIARVLLASGLLTGRYnaCTQFGKDDH 223
Cdd:cd19160 153 TSRWSAMEimeaYSVARQfnlippvceQAEYHLFQREKVEMQLPELYHKiGVGSVTWSPLACGLITGKY--DGRVPDTCR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 224 RTFNRNGEAFDKGETFSGVDYQLGLQAVEELKALFGTEdLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDNFPPL 302
Cdd:cd19160 231 AAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCT-VAQLAIAWCLRSEGVSSVLLGVSSAEQLIENlGSIQVLSQL 309
|
330
....*....|.
gi 493290592 303 TENEMQKVEDI 313
Cdd:cd19160 310 TPQTVMEIDAL 320
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-153 |
1.27e-21 |
|
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: 92.62 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWGEpfnhQEAMAILETAYEQGINFIDTADVYNN----GQSEKAIGDILKKYP--DFFYVVTKCG--R 85
Cdd:cd19082 1 SRIVLGTADFGTRIDE----EEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGnrDKVVIATKGGhpD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493290592 86 ALNPHTAEMyTPQAIEKFVDGSLSHLGTEKLDMILLHcpptlvyRND------EIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19082 77 LEDMSRSRL-SPEDIRADLEESLERLGTDYIDLYFLH-------RDDpsvpvgEIVDTLNELVRAGKIRAFGAS 142
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
4-306 |
5.50e-21 |
|
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: 91.35 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKK--YPDFFYVV- 80
Cdd:cd19141 3 RNLGKSGLRVSCLGLGTW---VTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKkgWRRSSYVIt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 81 TKC---GRAlnpHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILL-----HCPptlvyrNDEIFTKLEQLKAGGKLIDYGV 152
Cdd:cd19141 80 TKIfwgGKA---ETERGLSRKHIIEGLKASLERLQLEYVDIVFAnrpdpNTP------MEEIVRAFTHVINQGMAMYWGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 153 SIETAEEgllAME-YDIA---------AMEVIFNMFRLKPLEQLFPTAQQK-NVGIIARVLLASGLLTGRY-NACTQFGK 220
Cdd:cd19141 151 SRWSAME---IMEaYSVArqfnlippiVEQAEYHLFQREKVEMQLPELFHKiGVGAMTWSPLACGILSGKYdDGVPEYSR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 221 DDHRTFNRNGEAFDKGEtfsGVDYQLGLQAVEELKALFGTEdLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDNF 299
Cdd:cd19141 228 ASLKGYQWLKEKILSEE---GRRQQAKLKELQIIADRLGCT-LPQLAIAWCLKNEGVSSVLLGASSTEQLYENlQAIQVL 303
|
....*..
gi 493290592 300 PPLTENE 306
Cdd:cd19141 304 PKLTPNI 310
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-313 |
8.90e-21 |
|
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: 90.87 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP---DFF 77
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrrSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 78 YVVTKCGRALNPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTlvyrndeiFTKLEQL-KAGGKLIDYGVSIET 156
Cdd:cd19159 78 VITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS--------NTPMEEIvRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 157 AEEGLLAME----YDIAAM---------EVIFNMFRLKPLEQLFPTAQQK-NVGIIARVLLASGLLTGRY-NACTQFGKD 221
Cdd:cd19159 150 GTSRWSAMEimeaYSVARQfnmippvceQAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYgNGVPESSRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 222 DHRTFNRNGEAFDKGEtfsGVDYQLGLQAVEELKALFGTEdLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDNFP 300
Cdd:cd19159 230 SLKCYQWLKERIVSEE---GRKQQNKLKDLSPIAERLGCT-LPQLAVAWCLRNEGVSSVLLGSSTPEQLIENlGAIQVLP 305
|
330
....*....|...
gi 493290592 301 PLTENEMQKVEDI 313
Cdd:cd19159 306 KMTSHVVNEIDNI 318
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-295 |
1.84e-20 |
|
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: 89.59 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKWgEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVV-TKCGRALNP--- 89
Cdd:cd19152 1 PKLGFGTAPLGNLY-EAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVIsTKVGRLLVPlqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 90 ----------HTAEM-----YTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRND----------EIFTKLEQLKAG 144
Cdd:cd19152 80 veptfepgfwNPLPFdavfdYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAEsdehfaqaikGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 145 GKLIDYGVSIETAEEGLLAMEydiaamEVIFNMF----RLKPLEQ-----LFPTAQQKNVGIIARVLLASGLLTGRynac 215
Cdd:cd19152 160 GVIKAIGLGVNDWEVILRILE------EADLDWVmlagRYTLLDHsaareLLPECEKRGVKVVNAGPFNSGFLAGG---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 216 TQFGKDDHRTFNRngEAFDKGETFSGV--DYQLGLQAVeelkalfgtedlipyALRWVLMNEAVSTVIPGASKVSQVITN 293
Cdd:cd19152 230 DNFDYYEYGPAPP--ELIARRDRIEALceQHGVSLAAA---------------ALQFALAPPAVASVAPGASSPERVEEN 292
|
..
gi 493290592 294 AA 295
Cdd:cd19152 293 VA 294
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-313 |
4.59e-20 |
|
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: 88.99 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKK---YPDFF 77
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 78 YVVTKCGRALNPHTAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPptlvyrnDEIFTKLEQLKAGGKLIDYGVSIETA 157
Cdd:cd19158 78 VITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPMEETVRAMTHVINQGMAMYWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 158 EEGLLAME----YDIAAM---------EVIFNMFRLKPLEQLFPTAQQK-NVGIIARVLLASGLLTGRYNActqfGKDDH 223
Cdd:cd19158 151 TSRWSSMEimeaYSVARQfnlippiceQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVSGKYDS----GIPPY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 224 RTFNRNGEAFDKGETFS--GVDYQLGLQAVEELKALFGTEdLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDNFP 300
Cdd:cd19158 227 SRASLKGYQWLKDKILSeeGRRQQAKLKELQAIAERLGCT-LPQLAIAWCLRNEGVSSVLLGASNAEQLMENiGAIQVLP 305
|
330
....*....|...
gi 493290592 301 PLTENEMQKVEDI 313
Cdd:cd19158 306 KLSSSIVHEIDSI 318
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-313 |
1.04e-19 |
|
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: 87.90 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQlgtKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKK--YPDFFY 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWS---TFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKkgWKRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 79 VV-TKCGRALNPHTAEMYTPQAIEKfVDGSLSHLGTEKLDMILLHcpptlvyRNDEIFTKLEQLKAGGKLIDYGV----- 152
Cdd:cd19142 78 IVsTKIYWSYGSEERGLSRKHIIES-VRASLRRLQLDYIDIVIIH-------KADPMCPMEEVVRAMSYLIDNGLimywg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 153 -----SIETAEEGLLAMEYD-----IAAMEviFNMFRLKPLEQLFPTAQQK-NVGIIARVLLASGLLTGRYNACTQFGKD 221
Cdd:cd19142 150 tsrwsPVEIMEAFSIARQFNcptpiCEQSE--YHMFCREKMELYMPELYNKvGVGLITWSPLSLGLDPGISEETRRLVTK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 222 DHRTFNRNGEAFDKGETFSGV-DYQLGLQAVEELKALFGTeDLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVDNF 299
Cdd:cd19142 228 LSFKSSKYKVGSDGNGIHEETrRASHKLRELSLIAERLGC-DLTQLLIAWSLKNENVQCVLIGASSLEQLYSQlNSLQLL 306
|
330
....*....|....
gi 493290592 300 PPLTENEMQKVEDI 313
Cdd:cd19142 307 PKLNSAVMEELERI 320
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-314 |
3.00e-19 |
|
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: 86.46 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 18 LGTWQLGtKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDfFYVVTKcgraLNPHTAEMYTP 97
Cdd:cd19075 5 LGTMTFG-SQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERG-FKIDTK----ANPGVGGGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 98 QAIEKFVDGSLSHLGTEKLDMILLHCPptlvyrnDEIfTKL-EQLKA------GGKLIDYGVSIETAEEglLAMEYDIAA 170
Cdd:cd19075 79 ENVRKQLETSLKRLKVDKVDVFYLHAP-------DRS-TPLeETLAAidelykEGKFKEFGLSNYSAWE--VAEIVEICK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 171 ME------V---IFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYnacTQFgkDDHRTFNRngeaFDkGETFSG 241
Cdd:cd19075 149 ENgwvlptVyqgMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKY---KYS--EDKAGGGR----FD-PNNALG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 242 VDYQ------LGLQAVEELKALFGTEDLIPY--ALRWVLMNEAVS-----TVIPGASKVSQVITN-AAVDNfPPLTENEM 307
Cdd:cd19075 219 KLYRdrywkpSYFEALEKVEEAAEKEGISLAeaALRWLYHHSALDgekgdGVILGASSLEQLEENlAALEK-GPLPEEVV 297
|
....*..
gi 493290592 308 QKVEDIY 314
Cdd:cd19075 298 KAIDEAW 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
16-311 |
9.00e-19 |
|
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: 83.85 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP---DFFYVVTKCgraLNPHta 92
Cdd:cd19140 11 LGLGTYPL--------TGEECTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAASGvprDELFLTTKV---WPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 emYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIfTKLEQLKAGGKLIDYGVS---IETAEEGLLAMEYDIA 169
Cdd:cd19140 75 --YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETL-GALNEAQEAGLARHIGVSnftVALLREAVELSEAPLF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 170 AMEVIFN-MFRLKPLEQlfpTAQQKNVGIIARVLLASGLLTgrynactqfgkdDHRTFNRNGEAFDKgeTFSGVdyqlgl 248
Cdd:cd19140 152 TNQVEYHpYLDQRKLLD---AAREHGIALTAYSPLARGEVL------------KDPVLQEIGRKHGK--TPAQV------ 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 249 qaveelkalfgtedlipyALRWVLMNEAVStVIPGASKVSQVITNAAVDNFpPLTENEMQKVE 311
Cdd:cd19140 209 ------------------ALRWLLQQEGVA-AIPKATNPERLEENLDIFDF-TLSDEEMARIA 251
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
13-298 |
1.95e-18 |
|
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: 83.74 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILK--KYP-DFFYVVTKCGRaLNP 89
Cdd:cd19153 12 VSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAalQVPrSSYTVATKVGR-YRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 90 HTAEmYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRN--DEIFTKLEQLKAGGKLIDYGVS---IETAEEglLAM 164
Cdd:cd19153 91 SEFD-YSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTlvDEALPALRTLKDEGVIKRIGIAgypLDTLTR--ATR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 165 EYDIAAMEVIFNMFRL----KPLEQLFPTAQQKN-VGIIARVLLASGLLTGRynACTQFGKDDH--RTFNRNGEAFdkge 237
Cdd:cd19153 168 RCSPGSLDAVLSYCHLtlqdARLESDAPGLVRGAgPHVINASPLSMGLLTSQ--GPPPWHPASGelRHYAAAADAV---- 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 238 tfsgvdyqlgLQAVEelkalFGTEDLipyALRWVLMNEA-VSTVIPGASKVSQVITN-AAVDN 298
Cdd:cd19153 242 ----------CASVE-----ASLPDL---ALQYSLAAHAgVGTVLLGPSSLAQLRSMlAAVDA 286
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
4-313 |
2.31e-18 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 84.06 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWQLGTKWGePFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP---DFFYVV 80
Cdd:PLN02587 2 RELGSTGLKVSSVGFGASPLGSVFG-PVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGiprEKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 81 TKCGRALNPHTaemYTPQAIEKFVDGSLSHLGTEKLDMILLHcpptlvyrnDEIFTKLEQ-----------LKAGGKLID 149
Cdd:PLN02587 81 TKCGRYGEGFD---FSAERVTKSVDESLARLQLDYVDILHCH---------DIEFGSLDQivnetipalqkLKESGKVRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 150 YGVS----------IETAEEGllameydiaAMEVIFNMFRL----KPLEQLFPTAQQKNVGIIARVLLASGLLTGR---- 211
Cdd:PLN02587 149 IGITglplaiftyvLDRVPPG---------TVDVILSYCHYslndSSLEDLLPYLKSKGVGVISASPLAMGLLTENgppe 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 212 --------YNACTQFGKddhrtfnrngEAFDKGETFSGVdyqlglqaveelkalfgtedlipyALRWVLMNEAVSTVIPG 283
Cdd:PLN02587 220 whpappelKSACAAAAT----------HCKEKGKNISKL------------------------ALQYSLSNKDISTTLVG 265
|
330 340 350
....*....|....*....|....*....|...
gi 493290592 284 ASKVSQVITN-AAVDNFPPLT--ENEMQKVEDI 313
Cdd:PLN02587 266 MNSVQQVEENvAAATELETSGidEELLSEVEAI 298
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-206 |
4.36e-17 |
|
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: 79.24 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 15 EIGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP----DFFyVVTKCGRalnph 90
Cdd:cd19073 3 ALGLGTWQL--------RGDDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGvpreDLF-ITTKVWR----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 91 taEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCP-PTlvYRNDEIFTKLEQLKAGGKLIDYGVS---IETAEEGLLAMEY 166
Cdd:cd19073 66 --DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPnPT--VPLEETLGALKELKEAGKVKSIGVSnftIELLEEALDISPL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493290592 167 DIAAMEVIFNMFrlkpLEQ--LFPTAQQKNVGIIARVLLASG 206
Cdd:cd19073 142 PIAVNQVEFHPF----LYQaeLLEYCRENDIVITAYSPLARG 179
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-208 |
6.09e-17 |
|
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: 79.15 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGEPFNH-QEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVTKCGralnpH 90
Cdd:cd19137 4 IPALGLGTWGIGGFLTPDYSRdEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPrEDLFIVTKVW-----P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 91 TAEMYtpQAIEKFVDGSLSHLGTEKLDMILLHCP-PTLVYrnDEIFTKLEQLKAGGKLIDYGVS---IETAEEGLLAMEY 166
Cdd:cd19137 79 TNLRY--DDLLRSLQNSLRRLDTDYIDLYLIHWPnPNIPL--EETLSAMAEGVRQGLIRYIGVSnfnRRLLEEAISKSQT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493290592 167 DIAAMEVIFNMFRLKPLEQ-LFPTAQQKNVGIIARVLLASGLL 208
Cdd:cd19137 155 PIVCNQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLE 197
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-321 |
1.69e-16 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 79.13 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTwqlgTKWGEPFNHQEAMAILETAYEQGINFIDTADVY-------NNGQSEKAIGDILKKY 73
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT----MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 74 P--DFFYVVTKCGRALNPHTAEMYTPQA-----IEKFVDGSLSHLGTEKLDMILLHCP--PT-----LVYRNDE---IFT 136
Cdd:PRK10625 77 GsrEKLIIASKVSGPSRNNDKGIRPNQAldrknIREALHDSLKRLQTDYLDLYQVHWPqrPTncfgkLGYSWTDsapAVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 137 KLEQLKA------GGKLIDYGVSIETAEEGL----LAMEYDIAAMEVIFNMFRL--KPLE-QLFPTAQQKNVGIIARVLL 203
Cdd:PRK10625 157 LLETLDAlaeqqrAGKIRYIGVSNETAFGVMrylhLAEKHDLPRIVTIQNPYSLlnRSFEvGLAEVSQYEGVELLAYSCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 204 ASGLLTGRY-NACTQFGKddhrtfnRNgEAFDKGETFSGVDYQlglQAVEELKALFGTEDLIP--YALRWVLMNEAVSTV 280
Cdd:PRK10625 237 AFGTLTGKYlNGAKPAGA-------RN-TLFSRFTRYSGEQTQ---KAVAAYVDIAKRHGLDPaqMALAFVRRQPFVAST 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 493290592 281 IPGASKVSQVITNaaVDNFP-PLTENEMQKVEDIYNRLIRPS 321
Cdd:PRK10625 306 LLGATTMEQLKTN--IESLHlTLSEEVLAEIEAVHQVYTYPA 345
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
16-313 |
9.73e-16 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 75.48 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGtkwgepfnHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP----DFFyVVTKcgraLNPHt 91
Cdd:COG0656 8 LGLGTWQLP--------GEEAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAASGvpreELF-VTTK----VWND- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 aeMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTlvYRNDEIFTKLEQLKAGGKLIDYGVS---IETAEEGLLAMEYDI 168
Cdd:COG0656 71 --NHGYDDTLAAFEESLERLGLDYLDLYLIHWPGP--GPYVETWRALEELYEEGLIRAIGVSnfdPEHLEELLAETGVKP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 169 AAMEVIFNMFRlkPLEQLFPTAQQKNVGIIARVLLASG-LLtgrynactqfgkdDHRTFNRNGEAFDKGETfsgvdyQLg 247
Cdd:COG0656 147 AVNQVELHPYL--QQRELLAFCREHGIVVEAYSPLGRGkLL-------------DDPVLAEIAEKHGKTPA------QV- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493290592 248 lqaveelkalfgtedlipyALRWVLMNEAVstVIPGASKVSQVITNAAVDNFpPLTENEMQKVEDI 313
Cdd:COG0656 205 -------------------VLRWHLQRGVV--VIPKSVTPERIRENLDAFDF-ELSDEDMAAIDAL 248
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-313 |
2.19e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 75.32 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKKYPDFFYVVTKcgraLNPHT- 91
Cdd:cd19101 2 ISRVINGMWQLSGGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRERDAADD----VQIHTk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 ------AEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGKLIDYGVS----IETAEegL 161
Cdd:cd19101 76 wvpdpgELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGLTnfdtERLRE--I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 162 LAMEYDIAAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYnactqFGKDDHRTFNrngeafdkGETFSG 241
Cdd:cd19101 154 LDAGVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-----LGVPEPTGPA--------LETRSL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 242 VDYQL------GLQAVEE-LKALFGTEDL----IP-YALRWVLMNEAVSTVIPGASKVSQVITNAAVDNFpPLTENEMQK 309
Cdd:cd19101 221 QKYKLmidewgGWDLFQElLRTLKAIADKhgvsIAnVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF-RLDDEDRAA 299
|
....
gi 493290592 310 VEDI 313
Cdd:cd19101 300 IDAV 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-153 |
2.85e-15 |
|
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: 74.06 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGtkwgepfnHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKY----PDFFyVVTKCGralNPHT 91
Cdd:cd19071 4 IGLGTYKLK--------PEETAEAVLAALEAGYRHIDTAAAYGN---EAEVGEAIRESgvprEELF-ITTKLW---PTDH 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493290592 92 AEMYTPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRNDEIFTK-----LEQLKAGGKLIDYGVS 153
Cdd:cd19071 69 GYERVREALEE----SLKDLGLDYLDLYLIHWPVPGKEGGSKEARLetwraLEELVDEGLVRSIGVS 131
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-311 |
3.05e-15 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 75.41 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFGKTNKMVSEIGLGTWQlgtkwgePFNHQEAM----AILETAYEQGINFIDTADVYN--NGQSEKAIGDILKK-- 72
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWH-------NFGHVNALesqrAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 73 --YPDFFYVVTKCGRALNPHTaemYTPQAIEKFV----DGSLSHLGTEKLDMILLHcpptLVYRN---DEIFTKLEQLKA 143
Cdd:PRK09912 86 aaYRDELIISTKAGYDMWPGP---YGSGGSRKYLlaslDQSLKRMGLEYVDIFYSH----RVDENtpmEETASALAHAVQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 144 GGKLIDYGVSI----ETAEEGLLAMEYDIAAM--EVIFNMF-RLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACT 216
Cdd:PRK09912 159 SGKALYVGISSyspeRTQKMVELLREWKIPLLihQPSYNLLnRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 217 QFGKDDHRTFNRNGEAFDKGETFSGVDyqlGLQAVEELKALFGtEDLIPYALRWVLMNEAVSTVIPGASKVSQVITNAAV 296
Cdd:PRK09912 239 PQDSRMHREGNKVRGLTPKMLTEANLN---SLRLLNEMAQQRG-QSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
330
....*....|....*
gi 493290592 297 DNFPPLTENEMQKVE 311
Cdd:PRK09912 315 LNNLTFSTEELAQID 329
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-307 |
5.72e-15 |
|
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: 74.36 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 2 KQRRFGKTNKMVSEIGLGTWQlgtKWGEPFNHQEAMAILETAYEQGINFIDTADVYN--NGQSEKAIGDILKK----YPD 75
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWH---NFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlkpYRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 76 FFYVVTKCGRALNPHTaemYTPQAIEKFV----DGSLSHLGTEKLDMILLHCP----PTlvyrnDEIFTKLEQLKAGGKL 147
Cdd:cd19151 78 ELIISTKAGYTMWPGP---YGDWGSKKYLiaslDQSLKRMGLDYVDIFYHHRPdpetPL-----EETMGALDQIVRQGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 148 IDYGVSIETAEEG--LLAMEYDIAAMEVI----FNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYnacTQFGKD 221
Cdd:cd19151 150 LYVGISNYPPEEAreAAAILKDLGTPCLIhqpkYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRY---LNGIPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 222 DHRTfnRNGEAFDKGETFSgvdyQLGLQAVEELKALFGTED--LIPYALRWVLMNEAVSTVIPGASKVSQVITNAAVDNF 299
Cdd:cd19151 227 DSRA--AKGSSFLKPEQIT----EEKLAKVRRLNEIAQARGqkLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDN 300
|
....*...
gi 493290592 300 PPLTENEM 307
Cdd:cd19151 301 REFSEEEL 308
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-312 |
8.21e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 73.52 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 10 NKMVSEIGLGTWQlgtkWGEPF--------NH---QEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFY 78
Cdd:cd19103 1 DKKLPKIALGTWS----WGSGGaggdqvfgNHldeDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 79 VV-TKcgralnphtaemYTPQA-------IEKFVDGSLSHLGTEKLDMILLHcPPTLVYRNDEiftKLEQLKAGGKLIDY 150
Cdd:cd19103 77 IIsTK------------FTPQIagqsadpVADMLEGSLARLGTDYIDIYWIH-NPADVERWTP---ELIPLLKSGKVKHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 151 GVS------IETAEEGLLAMEYDIAAMEvifNMFRL--KPLEQ--LFPTAQQKNVGIIARVLLASGLLTGRYNactqfgk 220
Cdd:cd19103 141 GVSnhnlaeIKRANEILAKAGVSLSAVQ---NHYSLlyRSSEEagILDYCKENGITFFAYMVLEQGALSGKYD------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 221 ddhrTFNRNGEAFDKGETFSGVDYQLG--LQAVEELKALFGTeDLIPYALRWVLmneAVSTV-IPGASKVSQViTNAAVD 297
Cdd:cd19103 211 ----TKHPLPEGSGRAETYNPLLPQLEelTAVMAEIGAKHGA-SIAQVAIAWAI---AKGTTpIIGVTKPHHV-EDAARA 281
|
330
....*....|....*
gi 493290592 298 NFPPLTENEMQKVED 312
Cdd:cd19103 282 ASITLTDDEIKELEQ 296
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
4-298 |
2.49e-14 |
|
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: 72.49 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 4 RRFGKTNKMVSEIGLGTWQlgtKWGEPFNHQEAMAILETAYEQGINFIDTADVYN--NGQSEKAIGDILKK----YPDFF 77
Cdd:cd19150 3 RRCGKSGLKLPALSLGLWH---NFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdfagYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 78 YVVTKCGRALNPHTaemYTPQAIEKFV----DGSLSHLGTEKLDMILLHC--PPTLVyrnDEIFTKLEQLKAGGKLIDYG 151
Cdd:cd19150 80 IISTKAGYDMWPGP---YGEWGSRKYLlaslDQSLKRMGLDYVDIFYSHRfdPDTPL---EETMGALDHAVRSGKALYVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 152 VSI----ETAEEGLLAMEYDIAAM--EVIFNMF-RLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRY-NACTQfgkddh 223
Cdd:cd19150 154 ISSyspeRTREAAAILRELGTPLLihQPSYNMLnRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYlNGIPE------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 224 rtfnrnGEAFDKGETFSGVDyqLGLQAVEELKALFGT-----EDLIPYALRWVLMNEAVSTVIPGASKVSQVITN-AAVD 297
Cdd:cd19150 228 ------GSRASKERSLSPKM--LTEANLNSIRALNEIaqkrgQSLAQMALAWVLRDGRVTSALIGASRPEQLEENvGALD 299
|
.
gi 493290592 298 N 298
Cdd:cd19150 300 N 300
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-152 |
4.25e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 71.59 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 14 SEIGLGTWQLGTKwgepFNHQEAMAILETAYEQGINFIDTADVYN-------NGQSEKAIGDILK--KYPDFFYVVTKCG 84
Cdd:cd19752 1 SELCLGTMYFGTR----TDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKdrGNRDDVVIATKVG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493290592 85 -RALNPH----TAEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCpptlvyrnDEIFTKLEQ-LKAGGKLIDYGV 152
Cdd:cd19752 77 aGPRDPDggpeSPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHV--------DDRDTPLEEtLEAFNELVKAGK 142
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
16-195 |
2.09e-13 |
|
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: 69.18 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTwqlGTKWGEPFNH---QEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP---DFFYVVTKCGRALNp 89
Cdd:cd19120 7 IAFGT---GTAWYKSGDDdiqRDLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALKESGvprEDLFITTKVSPGIK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 90 htaemytpqAIEKFVDGSLSHLGTEKLDMILLHCPPT---LVYRNDEIFTKLEQLKAGGKLIDYGVS---IETAEEGLLA 163
Cdd:cd19120 80 ---------DPREALRKSLAKLGVDYVDLYLIHSPFFakeGGPTLAEAWAELEALKDAGLVRSIGVSnfrIEDLEELLDT 150
|
170 180 190
....*....|....*....|....*....|..
gi 493290592 164 MEYDIAAMEVIFNMFRLKPLEQLFPTAQQKNV 195
Cdd:cd19120 151 AKIKPAVNQIEFHPYLYPQQPALLEYCREHGI 182
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
13-287 |
1.71e-12 |
|
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: 67.07 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP-DFFYVVTKCG-RALNPH 90
Cdd:cd19145 12 VSAQGLGCMGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPrEKVQLATKFGiHEIGGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 91 TAEMY-TPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIfTKLEQLKAGGKLIDYGVSIETAEEGLLAME-YDI 168
Cdd:cd19145 92 GVEVRgDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITM-GELKKLVEEGKIKYIGLSEASADTIRRAHAvHPI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 169 AAMEVIFNMFRLKPLEQLFPTAQQKNVGIIARVLLASGLLTGRYNACTQFGKDDHR-TFNR-NGEAFDKGEtfsgvdyql 246
Cdd:cd19145 171 TAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRkSHPRfQGENLEKNK--------- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 493290592 247 glQAVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKV 287
Cdd:cd19145 242 --VLYERVEALAKKKGCTPaqLALAWVLHQGEDVVPIPGTTKI 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
16-150 |
2.72e-12 |
|
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: 66.40 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQlgtkwGEPfnhQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYPDF-------FYVVTKCGRALN 88
Cdd:cd19155 15 VGLGTWQ-----SSP---EEIETAVDTALEAGYRHIDTAYVYRN---EAAIGNVLKKWIDSgkvkreeLFIVTKLPPGGN 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493290592 89 phtaemyTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEiftKLEQLKAGGKLIDY 150
Cdd:cd19155 84 -------RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDD---SGKLDPTGEHKQDY 135
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-153 |
7.73e-12 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 64.83 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTkwgepfnhQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYPDF-------FYVVTKcgraLN 88
Cdd:cd19111 7 IGLGTYQSPP--------EEVRAAVDYALFVGYRHIDTALSYQN---EKAIGEALKWWLKNgklkreeVFITTK----LP 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493290592 89 PHTAEmytPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRND------------EIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19111 72 PVYLE---FKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDkgerelassdvtSVWRAMEALVSEGKVKSIGLS 145
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-153 |
1.14e-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: 63.80 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP--------DFFyVVTKcgraL 87
Cdd:cd19136 4 LGLGTFRLR-------GEEEVRQAVDAALKAGYRLIDTASVYRN---EADIGKALRDLLpkyglsreDIF-ITSK----L 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493290592 88 NPHtaEMYTPQAiEKFVDGSLSHLGTEKLDMILLHCPPTLVYRND---------EIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19136 69 APK--DQGYEKA-RAACLGSLERLGTDYLDLYLIHWPGVQGLKPSdprnaelrrESWRALEDLYKEGKLRAIGVS 140
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
30-153 |
2.51e-11 |
|
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: 63.45 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 30 PFNHQ--------EAMAILETAYEQGINFIDTADVYnnGQSEKAIGDILKK----YP-DFFYVVTKCGR-ALNPHTaemY 95
Cdd:cd19164 22 TFSYQyttdpesiPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrdeFPrDTYFIITKVGRyGPDDFD---Y 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 96 TPQAIEKFVDGSLSHLGTEKLDMILLH-----CPPTLVyrndEIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19164 97 SPEWIRASVERSLRRLHTDYLDLVYLHdvefvADEEVL----EALKELFKLKDEGKIRNVGIS 155
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
13-119 |
3.46e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 62.68 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTK--WGEPFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYPDFFYVVTKCGR----- 85
Cdd:PRK10376 17 VNRLGYGAMQLAGPgvFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTKVGArrged 96
|
90 100 110
....*....|....*....|....*....|....*
gi 493290592 86 -ALNPhtaeMYTPQAIEKFVDGSLSHLGTEKLDMI 119
Cdd:PRK10376 97 gSWLP----AFSPAELRRAVHDNLRNLGLDVLDVV 127
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
16-317 |
5.22e-11 |
|
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: 62.43 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKY--------PDFFyVVTKcgraL 87
Cdd:cd19154 15 IGLGTWQS--------KGAEGITAVRTALKAGYRLIDTAFLYQN---EEAIGEALAELleegvvkrEDLF-ITTK----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 NPHtaeMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGG--KLIDYGVSIETA-EEGLL-- 162
Cdd:cd19154 79 WTH---EHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDavDVEDVWRGMEKVyDEGLTka 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 163 --AMEYDIAAMEVIFNMFRLKPLEQ---LFPTAQQK---------NVGIIARVLLASgllTGRYNactqfgkddhrtfnr 228
Cdd:cd19154 156 igVSNFNNDQIQRILDNARVKPHNNqveCHLYFPQKelvefckkhNISVTSYATLGS---PGRAN--------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 229 ngeaFDKGETFSGVDYQLGLQAVEELKALFG-TEDLIpyALRWVLMNEAVstVIPGASKVSQVITNAAVDNFpPLTENEM 307
Cdd:cd19154 218 ----FTKSTGVSPAPNLLQDPIVKAIAEKHGkTPAQV--LLRYLLQRGIA--VIPKSATPSRIKENFNIFDF-SLSEEDM 288
|
330
....*....|
gi 493290592 308 QKVEDIYNRL 317
Cdd:cd19154 289 ATLEEIEKSL 298
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
13-153 |
5.95e-11 |
|
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: 62.44 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGE---PFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILKKYP--DFFYVVTKCGRAL 87
Cdd:cd19146 11 VSPLCLGAMSFGEAWKSmmgECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGnrDEMVLATKYTTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 88 NPHtaemyTPQAIEKF------------VDGSLSHLGTEKLDMILLH-----CPPtlvyrnDEIFTKLEQLKAGGKLIDY 150
Cdd:cd19146 91 RRG-----GPIKIKSNyqgnhakslrlsVEASLKKLQTSYIDILYVHwwdytTSI------PELMQSLNHLVAAGKVLYL 159
|
...
gi 493290592 151 GVS 153
Cdd:cd19146 160 GVS 162
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
16-139 |
1.78e-08 |
|
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: 54.84 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTKwgepfnhqEAMAILETAYEQGINFIDTADVYNN----GQSEKAIGDILKKYPDFFyVVTKCGRALNpht 91
Cdd:cd19121 15 VGLGTWQAKAG--------EVKAAVAHALKIGYRHIDGALCYQNedevGEGIKEAIAGGVKREDLF-VTTKLWSTYH--- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493290592 92 aemytpQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYR-NDEIFTKLE 139
Cdd:cd19121 83 ------RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNgNHDLFPTLP 125
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
15-153 |
2.22e-08 |
|
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: 54.30 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 15 EIGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKY---PDFFYVVTKCgraLNPHT 91
Cdd:cd19131 12 QLGLGVWQV--------SNDEAASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRASgvpREELFITTKL---WNSDQ 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493290592 92 AEMYTPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19131 78 GYDSTLRAFDE----SLRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVS 135
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
13-153 |
3.72e-08 |
|
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: 54.06 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLGTKWGE---PFNHQEAMAILETAYEQGINFIDTADVYNNGQSEKAIGDILK--KYPDFFYVVTK----- 82
Cdd:cd19147 10 VSPLILGAMSIGDAWSGfmgSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKsrKNRDQIVIATKfttdy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 83 ------CGRALN---PHTAEMYTPqaiekfVDGSLSHLGTEKLDMILLHcppTLVYRN--DEIFTKLEQLKAGGKLIDYG 151
Cdd:cd19147 90 kayevgKGKAVNycgNHKRSLHVS------VRDSLRKLQTDWIDILYVH---WWDYTTsiEEVMDSLHILVQQGKVLYLG 160
|
..
gi 493290592 152 VS 153
Cdd:cd19147 161 VS 162
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
16-153 |
6.10e-08 |
|
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: 52.96 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKY----PDFFyVVTKcgraLNPHT 91
Cdd:cd19133 12 LGFGVFQIP-------DPEECERAVLEAIKAGYRLIDTAAAYGN---EEAVGRAIKKSgiprEELF-ITTK----LWIQD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 92 AEMY-TPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYrndEIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19133 77 AGYEkAKKAFER----SLKRLGLDYLDLYLIHQPFGDVY---GAWRAMEELYKEGKIRAIGVS 132
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
16-313 |
6.93e-08 |
|
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: 52.71 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTkwgepFNHQeamAILETAYEQGINFIDTADVYNNgqsEKAIGDILK----KYPDFFyVVTKcgraLNPht 91
Cdd:cd19135 16 LGLGTSHSGG-----YSHE---AVVYALKECGYRHIDTAKRYGC---EELLGKAIKesgvPREDLF-LTTK----LWP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 92 AEMYTPQAIEKFVDgSLSHLGTEKLDMILLHCPPTLVYRND------EIFTKLEQLKAGGKLIDYGVS---IETAEEglL 162
Cdd:cd19135 78 SDYGYESTKQAFEA-SLKRLGVDYLDLYLLHWPDCPSSGKNvketraETWRALEELYDEGLCRAIGVSnflIEHLEQ--L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 163 AMEYDIAAM--EVIFNMFrlKPLEQLFPTAQQKNVGIIARVLLASGLLtgrynactqfgkddhrtfnrngeafdkgetfs 240
Cdd:cd19135 155 LEDCSVVPHvnQVEFHPF--QNPVELIEYCRDNNIVFEGYCPLAKGKA-------------------------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493290592 241 gvdyqLGLQAVEELKALFG-TEDLIpyALRWVLMNEAVstVIPGASKVSQVITNAAVDNFpPLTENEMQKVEDI 313
Cdd:cd19135 201 -----LEEPTVTELAKKYQkTPAQI--LIRWSIQNGVV--TIPKSTKEERIKENCQVFDF-SLSEEDMATLDSL 264
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
12-313 |
9.65e-08 |
|
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: 52.44 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 12 MVSEIGLGTWQLGtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKK--YP-DFFYVVTKcgrALN 88
Cdd:cd19126 8 RMPWLGLGVFQTP-------DGDETERAVQTALENGYRSIDTAAIYKN---EEGVGEAIREsgVPrEELFVTTK---LWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 89 PHTAEMYTPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRndEIFTKLEQLKAGGKLIDYGVS--IETAEEGLLAMEy 166
Cdd:cd19126 75 DDQRARRTEDAFQE----SLDRLGLDYVDLYLIHWPGKDKFI--DTWKALEKLYASGKVKAIGVSnfQEHHLEELLAHA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 167 DIAAMeviFNMFRLKPLEQlfptaQQKNVGIIArvllASGLLTGRYNACTQFGKDDHRTFNRNGEAFDKGETfsgvdyql 246
Cdd:cd19126 148 DVVPA---VNQVEFHPYLT-----QKELRGYCK----SKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAA-------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493290592 247 glQAVeelkalfgtedlipyaLRWVLMNEAVstVIPGASKVSQVITNAAVDNFpPLTENEMQKVEDI 313
Cdd:cd19126 208 --QVV----------------LRWDIQHGVV--TIPKSVHASRIKENADIFDF-ELSEDDMTAIDAL 253
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
16-124 |
1.13e-07 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 52.41 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQlgtkwGEPfnhQEAMAILETAYEQGINFIDTADVYNNgQSE--KAIGDILKKYP-----DFFyvVTkcGRALN 88
Cdd:cd19118 10 IGLGTWQ-----AEP---GEVGAAVKIALKAGYRHLDLAKVYQN-QHEvgQALKELLKEEPgvkreDLF--IT--SKLWN 76
|
90 100 110
....*....|....*....|....*....|....*.
gi 493290592 89 PHTAemytPQAIEKFVDGSLSHLGTEKLDMILLHCP 124
Cdd:cd19118 77 NSHR----PEYVEPALDDTLKELGLDYLDLYLIHWP 108
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-206 |
3.47e-07 |
|
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: 50.43 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP---DFFYVVTKCgralnphTA 92
Cdd:cd19139 4 FGLGTFRL--------KDDVVIDSVRTALELGYRHIDTAQIYDN---EAAVGQAIAESGvprDELFITTKI-------WI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 EMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTlvyrNDEI-----FTKLEQLKAGGKLIDYGVS---IETAEEGLLAm 164
Cdd:cd19139 66 DNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPSP----NDEVpveeyIGALAEAKEQGLTRHIGVSnftIALLDEAIAV- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493290592 165 eydIAAMEVIFNMFRLKPLEQ---LFPTAQQKNVGIIARVLLASG 206
Cdd:cd19139 141 ---VGAGAIATNQIELSPYLQnrkLVAHCKQHGIHVTSYMTLAYG 182
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-295 |
1.14e-06 |
|
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: 49.27 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 35 EAM-----AILETAYEQGINFIDTADVYnnGQSEKAIGDILKK---YPDFFYVVTKCGRAlnpHTAEMYTPQAIEKFVDG 106
Cdd:cd19098 31 EAMrahthAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSrniAPDAVFVGSKWGYT---YTADWQVDAAVHEVKDH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 107 SLSHLGTE----------KLDMILLHcPPTL---VYRNDEIFTKLEQLKAGGKLIDYGVS-IETAEEGLLAMEYDIA--- 169
Cdd:cd19098 106 SLARLLKQweetrsllgkHLDLYQIH-SATLesgVLEDADVLAALAELKAEGVKIGLSLSgPQQAETLRRALEIEIDgar 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 170 ---AMEVIFNMFRLKPLEQLfPTAQQKNVGIIARVLLASGLLTGrynactqfgkddhrtfnRNGEAFDKGEtfsgvdyql 246
Cdd:cd19098 185 lfdSVQATWNLLEQSAGEAL-EEAHEAGMGVIVKEALANGRLTD-----------------RNPSPELAPL--------- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 493290592 247 glqaVEELKALFGTEDLIP--YALRWVLMNEAVSTVIPGASKVSQVITNAA 295
Cdd:cd19098 238 ----MAVLKAVADRLGVTPdaLALAAVLAQPFVDVVLSGAATPEQLRSNLR 284
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
13-153 |
1.84e-06 |
|
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: 48.37 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 13 VSEIGLGTWQLgtkwgEPFNHQEAMAileTAYEQGINFIDTADVYNNGQS-EKAIG--DILKkypDFFYVVTKCGRalnp 89
Cdd:cd19130 10 IPQLGYGVFKV-----PPADTQRAVA---TALEVGYRHIDTAAIYGNEEGvGAAIAasGIPR---DELFVTTKLWN---- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493290592 90 htaEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19130 75 ---DRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVS 135
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
16-153 |
1.85e-06 |
|
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: 48.56 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTkwgepfnhQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILK----KYPDFFyVVTKCgralnphT 91
Cdd:cd19127 12 LGLGVFQTPP--------EETADAVATALADGYRLIDTAAAYGN---EREVGEGIRrsgvDRSDIF-VTTKL-------W 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 92 AEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCP-PTLVYRNDEIFTKLEQLKAGGKLIDYGVS 153
Cdd:cd19127 73 ISDYGYDKALRGFDASLRRLGLDYVDLYLLHWPvPNDFDRTIQAYKALEKLLAEGRVRAIGVS 135
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
16-311 |
2.03e-06 |
|
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: 48.54 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNGQS-EKAIGDILKKYPDFFyVVTKcgrALNPHTAEM 94
Cdd:cd19157 13 LGLGVFKVE-------EGSEVVNAVKTALKNGYRSIDTAAIYGNEEGvGKGIKESGIPREELF-ITSK---VWNADQGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 95 YTPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRndEIFTKLEQLKAGGKLIDYGVSietaeegllamEYDIAAMEVI 174
Cdd:cd19157 82 STLKAFEA----SLERLGLDYLDLYLIHWPVKGKYK--ETWKALEKLYKDGRVRAIGVS-----------NFQVHHLEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 175 FNMFRLKPL---EQLFPTAQQKNVgiiARVLLASGLLTGRYNACTQFGKDDHRTFNRNGEAFDKgeTFSGVdyqlglqav 251
Cdd:cd19157 145 LADAEIVPMvnqVEFHPRLTQKEL---RDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNK--SVAQV--------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 252 eelkalfgtedlipyALRWVLMNEAVstVIPGASKVSQVITNAAVDNFpPLTENEMQKVE 311
Cdd:cd19157 211 ---------------ILRWDLQNGVV--TIPKSIKEHRIIENADVFDF-ELSQEDMDKID 252
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
16-183 |
3.18e-06 |
|
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: 47.93 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKKYP---DFFYVVTKCGRALNPHTA 92
Cdd:cd19134 14 IGLGVGEL--------SDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGiprGELFVTTKLATPDQGFTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 93 EMYTPQAiekfvdgSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAGGKLIDYGVSIETAE--EGLLAMEYDIAA 170
Cdd:cd19134 83 SQAACRA-------SLERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEhlENLIDLTFFTPA 155
|
170
....*....|...
gi 493290592 171 MevifNMFRLKPL 183
Cdd:cd19134 156 V----NQIELHPL 164
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
16-153 |
3.66e-06 |
|
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: 47.73 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTKwgepfnhQEAMAIlETAYEQGINFIDTADVYNNgqsEKAIGDILK--------KYPDFFyVVTK--Cgr 85
Cdd:cd19125 14 VGLGTWQADPG-------VVGNAV-KTAIKEGYRHIDCAAIYGN---EKEIGKALKklfedgvvKREDLF-ITSKlwC-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 86 alnphtaEMYTPQAIEKFVDGSLSHLGTEKLDMILLHCP-----------PTLVYRND--EIFTKLEQLKAGGKLIDYGV 152
Cdd:cd19125 80 -------TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpePEEVLPPDipSTWKAMEKLVDSGKVRAIGV 152
|
.
gi 493290592 153 S 153
Cdd:cd19125 153 S 153
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
16-124 |
1.89e-05 |
|
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: 45.34 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLgtkwgepfNHQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILK--KYP-DFFYVVTKC-GRAlnpHT 91
Cdd:cd19132 10 IGFGTYPL--------KGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRrsGVPrEELFVTTKLpGRH---HG 75
|
90 100 110
....*....|....*....|....*....|...
gi 493290592 92 AEmytpQAIEKFvDGSLSHLGTEKLDMILLHCP 124
Cdd:cd19132 76 YE----EALRTI-EESLYRLGLDYVDLYLIHWP 103
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
16-150 |
2.13e-05 |
|
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: 45.35 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTKwgepfnhQEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILK--------KYPDFFyVVTKCGRal 87
Cdd:cd19116 14 IALGTWKLKDD-------EGVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIRekiaegvvKREDLF-ITTKLWN-- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493290592 88 NPHTAEMYTPqAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRNDEIFTKLEQLKAggklIDY 150
Cdd:cd19116 81 SYHEREQVEP-ALRE----SLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLSD----IDY 134
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
12-124 |
3.34e-05 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 12 MVSEIGLGTWQLGtkwgepfNHQEAMAILEtAYEQGINFIDTADVYNNgqsEKAIGDILKKYP---DFFYVVTKC--GRA 86
Cdd:PRK11565 14 VMPQLGLGVWQAS-------NEEVITAIHK-ALEVGYRSIDTAAIYKN---EEGVGKALKEASvarEELFITTKLwnDDH 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 493290592 87 LNPHtaemytpQAIEKfvdgSLSHLGTEKLDMILLHCP 124
Cdd:PRK11565 83 KRPR-------EALEE----SLKKLQLDYVDLYLMHWP 109
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
16-151 |
3.34e-05 |
|
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: 44.68 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQlgtkwGEPFNHQEAmaiLETAYEQGINFIDTADVYNNgqsEKAIGDILK---------KYPDFFyVVTKCGRa 86
Cdd:cd19106 10 IGLGTWK-----SKPGQVKAA---VKYALDAGYRHIDCAAVYGN---EQEVGEALKekvgpgkavPREDLF-VTSKLWN- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290592 87 lNPHTAEMYTPqAIEKfvdgSLSHLGTEKLDMILLHCPPTLVyRNDEIFTK-------------LEQLKAGGKLIDYG 151
Cdd:cd19106 77 -TKHHPEDVEP-ALRK----TLKDLQLDYLDLYLIHWPYAFE-RGDNPFPKnpdgtirydsthyKETWKAMEKLVDKG 147
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-150 |
3.56e-05 |
|
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: 44.80 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 8 KTNKM-----VSEIGLGTWQlgTKWGEpfnhqeAMAILETAYEQGINFIDTADVYNN----GQSEKAIGDILKKypdfFY 78
Cdd:cd19117 4 KTFKLntgaeIPAVGLGTWQ--SKPNE------VAKAVEAALKAGYRHIDTAAIYGNeeevGQGIKDSGVPREE----IF 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493290592 79 VVTKCGRALNPHTAEMytpqaiekfVDGSLSHLGTEKLDMILLHCPPTLVYRNDEiftkLEQLKAGGKLIDY 150
Cdd:cd19117 72 ITTKLWCTWHRRVEEA---------LDQSLKKLGLDYVDLYLMHWPVPLDPDGND----FLFKKDDGTKDHE 130
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-133 |
2.95e-04 |
|
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: 41.74 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLgtkwgEPFNHQEAmaiLETAYEQGINFIDTADVYNNGQS-EKAIGDILK----KYPDFFyVVTKcgraLNPH 90
Cdd:cd19128 4 LGFGTYKI-----TESESKEA---VKNAIKAGYRHIDCAYYYGNEAFiGIAFSEIFKdggvKREDLF-ITSK----LWPT 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 493290592 91 taeMYTPQAIEKFVDGSLSHLGTEKLDMILLHCPptLVYRNDE 133
Cdd:cd19128 71 ---MHQPENVKEQLLITLQDLQLEYLDLFLIHWP--LAFDMDT 108
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-124 |
5.20e-04 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 41.24 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 1 MKQRRFgKTNKMVSEIGLGTWQlgtkwgepFNHQEAMAILETAYEQGINFIDTADVYNNgQSE--KAIGDILK----KYP 74
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTWK--------SKPGEVGQAVKQALEAGYRHIDCAAIYGN-EAEigAALAEVFKegkvKRE 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 493290592 75 DFFyVVTKCGRalNPHTAEMYTPqAIEKfvdgSLSHLGTEKLDMILLHCP 124
Cdd:cd19123 71 DLW-ITSKLWN--NSHAPEDVLP-ALEK----TLADLQLDYLDLYLMHWP 112
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-208 |
5.64e-04 |
|
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: 40.96 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 12 MVSEIGLGTWQLgtKWGEpfnhqEAMAILETAYEQGINFIDTADVYNNgqsEKAIGDILKK--YP-DFFYVVTKcgrALN 88
Cdd:cd19156 8 EMPRLGLGVWRV--QDGA-----EAENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIREsgVPrEEVFVTTK---LWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 89 PHTAEMYTPQAIEKfvdgSLSHLGTEKLDMILLHCPPTLVYRndEIFTKLEQLKAGGKLIDYGVS--IETAEEGLLAMEy 166
Cdd:cd19156 75 SDQGYESTLAAFEE----SLEKLGLDYVDLYLIHWPVKGKFK--DTWKAFEKLYKEKKVRAIGVSnfHEHHLEELLKSC- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493290592 167 DIAAMeviFNMFRLKPL---EQLFPTAQQKNVGIIARVLLASGLL 208
Cdd:cd19156 148 KVAPM---VNQIELHPLltqEPLRKFCKEKNIAVEAWSPLGQGKL 189
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
16-131 |
6.82e-04 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 41.00 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTKWGEPFNHQeamailetAYEQGINFIDTADVYNNGQS-----EKAIGDILKKYPDFFyVVTKCGRALnpH 90
Cdd:cd19114 7 VGFGTAKIKANETEEVIYN--------AIKVGYRLIDGALLYGNEAEvgrgiRKAIQEGLVKREDLF-IVTKLWNNF--H 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 493290592 91 TAEMYTPqaiekFVDGSLSHLGTEKLDMILLHCPPTLVYRN 131
Cdd:cd19114 76 GKDHVRE-----AFDRQLKDYGLDYIDLYLIHFPIPAAYVD 111
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
16-124 |
5.43e-03 |
|
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: 37.99 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290592 16 IGLGTWQLGTKWGEPFNhqEAMAILETAYEQginfIDTADVY-NNGQSEKAIGDILKKYPDF----FYVVTKCGRALnph 90
Cdd:cd19122 12 VGFGTFANEGAKGETYA--AVTKALDVGYRH----LDCAWFYlNEDEVGDAVRDFLKENPSVkredLFICTKVWNHL--- 82
|
90 100 110
....*....|....*....|....*....|....
gi 493290592 91 taemYTPQAIEKFVDGSLSHLGTEKLDMILLHCP 124
Cdd:cd19122 83 ----HEPEDVKWSIDNSLKNLKLDYIDLFLVHWP 112
|
|
| |
