|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
10-311 |
1.09e-139 |
|
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: 397.70 E-value: 1.09e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 10 VALAGGTHTW--VPTPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGNKNLGA-EFSVWTKAPTGLGGGaGKRE 86
Cdd:cd19075 1 PKIILGTMTFgsQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGErGFKIDTKANPGVGGG-LSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 87 NILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQ 166
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 167 ASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVEQIENGNGTERWDPNSPYGMVNRQLYFKPSYMKMLTEYGK 246
Cdd:cd19075 160 GMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGRFDPNNALGKLYRDRYWKPSYFEALEKVEE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 995934143 247 LSEQSGVSKVGLAYRWVRYHSALKGELGDAMIIGANSATQFREAVKEIENGPLEEWIVERIDELW 311
Cdd:cd19075 240 AAEKEGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
15-312 |
3.66e-45 |
|
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: 156.49 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWvPTPKSEATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN---KNLGAEFSVWTKAPTGLGGGA----GK 84
Cdd:COG0667 19 GTMTF-GGPWGGVDEAEAIAILDaalDAGINFFDTADVYGPGRSEELLGEalkGRPRDDVVIATKVGRRMGPGPngrgLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqNFILPTV 164
Cdd:COG0667 98 REHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVeqiengNGTERWDPNSPYGMVNRQLYFKPSYMKMLTEY 244
Cdd:COG0667 176 VQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKY------RRGATFPEGDRAATNFVQGYLTERNLALVDAL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995934143 245 GKLSEQSGVSKVGLAYRWVRYHSALkgelgDAMIIGANSATQFREAVKEIENgPLEEWIVERIDELWE 312
Cdd:COG0667 250 RAIAAEHGVTPAQLALAWLLAQPGV-----TSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAALA 311
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-311 |
1.03e-40 |
|
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: 143.99 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 19 WVPTPKSEATQDEVVAImqEHGITNLDTARSYGMGASEETIGNknLGAEFSVW-------TKAPTGLGG--GAGKRENIL 89
Cdd:pfam00248 12 WGPISKEEALEALRAAL--EAGINFIDTAEVYGDGKSEELLGE--ALKDYPVKrdkvviaTKVPDGDGPwpSGGSKENIR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 90 EQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSrdqvLEHYNYAKSQNFILPTVYQASY 169
Cdd:pfam00248 88 KSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFD----AEQIEKALTKGKIPIVAVQVEY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 170 SIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVEQIEN-GNGTERWDPNSPYgmvnrqlyfkPSYMKMLTEYGKLS 248
Cdd:pfam00248 164 NLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDkGPGERRRLLKKGT----------PLNLEALEALEEIA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995934143 249 EQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFrEAVKEIENGPLEEWIVERIDELW 311
Cdd:pfam00248 234 KEHGVSPAQVALRW-----ALSKPGVTIPIPGASNPEQL-EDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
15-308 |
3.88e-36 |
|
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: 132.26 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVPTPKSEATqdEVVAIMQEHGITNLDTARSYGMGASEETIGnKNLGAE----------FSVWTKAPTGLGGGagK 84
Cdd:cd19084 15 GGTWWGEVDDQESI--EAIKAAIDLGINFFDTAPVYGFGHSEEILG-KALKGRrddvviatkcGLRWDGGKGVTKDL--S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfilPTV 164
Cdd:cd19084 90 PESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP------IVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVeqiengNGTERWDPNspyGMVNRQLYFKPS----YMKM 240
Cdd:cd19084 164 LQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKY------KKEPTFPPD---DRRSRFPFFRGEnfekNLEI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 241 LTEYGKLSEQSGVSKVGLAYRWVRYHSALkgelgDAMIIGANSATQFREAVK--EIEngpLEEWIVERID 308
Cdd:cd19084 235 VDKLKEIAEKYGKSLAQLAIAWTLAQPGV-----TSAIVGAKNPEQLEENAGalDWE---LTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-309 |
1.36e-33 |
|
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: 125.39 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 14 GGTHTWvptpkSEATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGnKNLGA---EFSVWTKAptglGGGAGKREN 87
Cdd:cd19085 12 GGGYWW-----GDQDDEESIATIHaalDAGINFFDTAEAYGDGHSEEVLG-KALKGrrdDVVIATKV----SPDNLTPED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 88 I---LEQGRKSnvvLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfilPTV 164
Cdd:cd19085 82 VrksCERSLKR---LGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSK---TVEQIENGNGTERwdpnspygmvnRQLYFKPSYMKML 241
Cdd:cd19085 153 NQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGkfsSAEDFPPGDARTR-----------LFRHFEPGAEEET 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 995934143 242 TEY----GKLSEQSGVSKVGLAYRWVRYHSALkgelgDAMIIGANSATQFREAVKEIEnGPLEEWIVERIDE 309
Cdd:cd19085 222 FEAleklKEIADELGVTMAQLALAWVLQQPGV-----TSVIVGARNPEQLEENAAAVD-LELSPSVLERLDE 287
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-200 |
2.93e-33 |
|
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: 122.63 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWvPTPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN----KNLGAEFSVWTKA----PTGLGGGAGKRE 86
Cdd:cd06660 6 GTMTF-GGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRwlkgRGNRDDVVIATKGghppGGDPSRSRLSPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 87 NILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQ 166
Cdd:cd06660 85 HIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQ 164
|
170 180 190
....*....|....*....|....*....|....*
gi 995934143 167 ASYSIVVRG-IETNLLSTLRELGISIQAYSPLAAG 200
Cdd:cd06660 165 PQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARG 199
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-292 |
2.33e-29 |
|
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: 114.23 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 18 TWVpTPKSEATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGNKNLG---AEFSVWTKAPTGLGGGAGK----REN 87
Cdd:cd19074 11 TWL-TFGGQVDDEDAKACVRkayDLGINFFDTADVYAAGQAEEVLGKALKGwprESYVISTKVFWPTGPGPNDrglsRKH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 88 ILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQA 167
Cdd:cd19074 90 IFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 168 SYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLS-KTVEQIENGNGTERWDPNSPYgMVNRqlYFKPSYMKMLTEYGK 246
Cdd:cd19074 170 QYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTgKYRDGIPPPSRSRATDEDNRD-KKRR--LLTDENLEKVKKLKP 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 995934143 247 LSEQSGVSKVGLAYRWVryhsaLKGELGDAMIIGANSATQFREAVK 292
Cdd:cd19074 247 IADELGLTLAQLALAWC-----LRNPAVSSAIIGASRPEQLEENVK 287
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
38-295 |
4.30e-29 |
|
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: 113.83 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGMGASEETIGN--KNLGA--EFSVWTK--APTGLGGGAG--KRENILEQGRKSNVVLRLSKIPVYLL 109
Cdd:cd19079 46 DLGINFFDTANVYSGGASEEILGRalKEFAPrdEVVIATKvyFPMGDGPNGRglSRKHIMAEVDASLKRLGTDYIDLYQI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 110 HAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVRGIETNLLSTLRELGI 189
Cdd:cd19079 126 HRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 190 SIQAYSPLAAGFLSKtveqieNGNGTERWDPNSPYGMVNRQLYFKPSYMKMLTEYGKLSEQSGVSKVGLAYRWVryhsaL 269
Cdd:cd19079 206 GVIPWSPLARGRLAR------PWGDTTERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWL-----L 274
|
250 260
....*....|....*....|....*.
gi 995934143 270 KGELGDAMIIGANSATQFREAVKEIE 295
Cdd:cd19079 275 SKPGVTAPIVGATKLEHLEDAVAALD 300
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
25-311 |
5.29e-29 |
|
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: 113.44 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 25 SEATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKA--PTGLG---GGAGKReNILEQGRK 94
Cdd:cd19087 25 GRTDEETSFAIMDralDAGINFFDTADVYGGGRSEEIIGRwiAGRRDDIVLATKVfgPMGDDpndRGLSRR-HIRRAVEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 95 SNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVR 174
Cdd:cd19087 104 SLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 175 GIETNLLSTLRELGISIQAYSPLAAGFLS-KTveQIENGNGTERWDPNSPYgmvnRQLYFKPSYMKMLTEYGKLSEQSGV 253
Cdd:cd19087 184 QAELEILPAARAYGLGVIPYSPLAGGLLTgKY--GKGKRPESGRLVERARY----QARYGLEEYRDIAERFEALAAEAGL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 995934143 254 SKVGLAYRWVRYHSALKgelgdAMIIGANSATQFREAVKEIENgPLEEWIVERIDELW 311
Cdd:cd19087 258 TPASLALAWVLSHPAVT-----SPIIGPRTLEQLEDSLAALEI-TLTPELLAEIDELF 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
14-291 |
2.23e-28 |
|
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: 111.17 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 14 GGTHTWVPTPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIG----NKNLGAEFSVWTK-APTGLGGGagkRENI 88
Cdd:cd19093 13 GDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGrflkELGDRDEVVIATKfAPLPWRLT---RRSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 89 LEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETL-GAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVyQA 167
Cdd:cd19093 90 VKALKASLERLGLDSIDLYQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGVPLASN-QV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 168 SYSIVVRGIETN-LLSTLRELGISIQAYSPLAAGFLsktveqiengngTERWDPNSPYGMVNRQLYFKPSYMKM---LTE 243
Cdd:cd19093 169 EYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLL------------TGKYSPENPPPGGRRRLFGRKNLEKVqplLDA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 995934143 244 YGKLSEQSGVSKVGLAYRWVRYHSALKgelgdamIIGANSATQFREAV 291
Cdd:cd19093 237 LEEIAEKYGKTPAQVALNWLIAKGVVP-------IPGAKNAEQAEENA 277
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
28-292 |
3.40e-27 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 108.51 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 28 TQDEVVAIMQ--EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAptGL----GGGAG-------------KRE 86
Cdd:cd19149 32 DNESIRTIHAalDLGINLIDTAPAYGFGHSEEIVGKaiKGRRDKVVLATKC--GLrwdrEGGSFffvrdgvtvyknlSPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 87 NILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfilPTVYQ 166
Cdd:cd19149 110 SIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ------LDIIQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 167 ASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTV--EQIENGNGTERWDPnspygmvnrqlYFKPSYMK----M 240
Cdd:cd19149 184 EKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKItpDREFDAGDARSGIP-----------WFSPENREkvlaL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 995934143 241 LTEYGKLSEQSGVSKVGLAYRWVRYHSALkgelgDAMIIGANSATQFREAVK 292
Cdd:cd19149 253 LEKWKPLCEKYGCTLAQLVIAWTLAQPGI-----TSALCGARKPEQAEENAK 299
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
38-263 |
8.24e-27 |
|
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: 107.30 E-value: 8.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGA------GKRENILEQGRKSNVVLRLSKIPVYLL 109
Cdd:cd19076 43 ELGVTFLDTADMYGPGTNEELLGKalKDRRDEVVIATKFGIVRDPGSgfrgvdGRPEYVRAACEASLKRLGTDVIDLYYQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 110 HAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVlehynyaKSQNFILP-TVYQASYSIVVRGIETNLLSTLRELG 188
Cdd:cd19076 123 HRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTI-------RRAHAVHPiTAVQSEYSLWTRDIEDEVLPTCRELG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 189 ISIQAYSPLAAGFLS---KTVEQIENGNGtERWDPNspygmvnrqlyFKPSYM----KMLTEYGKLSEQSGVSKVGLAYR 261
Cdd:cd19076 196 IGFVAYSPLGRGFLTgaiKSPEDLPEDDF-RRNNPR-----------FQGENFdknlKLVEKLEAIAAEKGCTPAQLALA 263
|
..
gi 995934143 262 WV 263
Cdd:cd19076 264 WV 265
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
44-308 |
2.47e-26 |
|
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: 106.14 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 44 LDTARSYG-------MGASEETIGN--KNLGA--EFSVWTK--APTGLGGGAGKRENILEQGRKSNVVLRLSKIPVYLLH 110
Cdd:cd19081 43 IDTADVYSawvpgnaGGESETIIGRwlKSRGKrdRVVIATKvgFPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 111 APDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVRG-IETNLLSTLRELGI 189
Cdd:cd19081 123 WDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 190 SIQAYSPLAAGFLSktveqiengnGTERWD---PNSPYGMVNRQLYFKPSYMKMLTEYGKLSEQSGVSKVGLAYRWVRYH 266
Cdd:cd19081 203 GVIPYSPLAGGFLT----------GKYRSEadlPGSTRRGEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLAR 272
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 995934143 267 SALkgelgDAMIIGANSATQFREAVKEIEnGPLEEWIVERID 308
Cdd:cd19081 273 PGV-----TAPIAGARTVEQLEDLLAAAG-LRLTDEEVARLD 308
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-310 |
3.78e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 102.75 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 13 AGGTHTWVPT-PKSEatqDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTK---APTGLGGGAG 83
Cdd:cd19102 11 IGGGGWGGGWgPQDD---RDSIAAIRaalDLGINWIDTAAVYGLGHSEEVVGRalKGLRDRPIVATKcglLWDEEGRIRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 84 --KRENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVlehynyaKSQNFIL 161
Cdd:cd19102 88 slKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM-------KRCQAIH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 162 P-TVYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVEQiengngtERWDPNSPYGMVNRQLYFKPSYM-- 238
Cdd:cd19102 161 PiASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTP-------ERVASLPADDWRRRSPFFQEPNLar 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 995934143 239 --KMLTEYGKLSEQSGVSKVGLAYRWVRYHSALKGelgdaMIIGANSATQFREAVK--EIENGPlEEWivERIDEL 310
Cdd:cd19102 234 nlALVDALRPIAERHGRTVAQLAIAWVLRRPEVTS-----AIVGARRPDQIDETVGaaDLRLTP-EEL--AEIEAL 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
15-310 |
4.10e-25 |
|
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: 103.03 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVptpkSEATQDEVVAIMQ---EHGITNLDTARSYGM-------GASEETIGN----KNLGAEFSVWTKAPTG--- 77
Cdd:cd19094 7 GTMTWG----EQNTEAEAHEQLDyafDEGVNFIDTAEMYPVppspetqGRTEEIIGSwlkkKGNRDKVVLATKVAGPgeg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 78 ---LGGGAGK--RENILEQGRKSnvVLRLSK--IPVYLLHAPD------------------ESVPVAETLGAIQTLYEEG 132
Cdd:cd19094 83 itwPRGGGTRldRENIREAVEGS--LKRLGTdyIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 133 RFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVEQIENG 212
Cdd:cd19094 161 KIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 213 NGTERWDPNSPYGmvnrQLYFKPSYMKMLTEYGKLSEQSGVSKVGLAYRWVRYHSALKgelgdAMIIGANSATQFREAVK 292
Cdd:cd19094 241 PEGGRLNLFPGYM----ARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVT-----STIIGATTLEQLKENID 311
|
330
....*....|....*...
gi 995934143 293 EIeNGPLEEWIVERIDEL 310
Cdd:cd19094 312 AF-DVPLSDELLAEIDAV 328
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
13-310 |
2.30e-24 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 100.57 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 13 AGGTHTWVPTPKsEATQDEVVAIMQEHGITNLDTARSYGMGASEETIG------NKNlgaEFSVWTKAPTGLGGGAGKRE 86
Cdd:cd19083 20 AVGGHNLYPNLD-EEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGevlkeyNRN---EVVIATKGAHKFGGDGSVLN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 87 N----ILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQvLEHYNYAKSQNfilp 162
Cdd:cd19083 96 NspefLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQ-LKEANKDGYVD---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 163 tVYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLsktveqiengngTERWDPN---SPYGMVNRQLYFK-PSYM 238
Cdd:cd19083 171 -VLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLL------------AGKYTKDtkfPDNDLRNDKPLFKgERFS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 995934143 239 KMLTEYGKL---SEQSGVSKVGLAYRWVryhsaLKGELGDAMIIGANSATQFREAVKEIeNGPLEEWIVERIDEL 310
Cdd:cd19083 238 ENLDKVDKLksiADEKGVTVAHLALAWY-----LTRPAIDVVIPGAKRAEQVIDNLKAL-DVTLTEEEIAFIDAL 306
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
38-205 |
4.17e-24 |
|
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: 99.23 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGMGASEETIGN--KNLGAE--FSVwTKA-PTGLgggagKRENILEQGRKSNVVLRLSKIPVYLLHAP 112
Cdd:cd19072 37 ELGINLIDTAEMYGGGHAEELVGKaiKGFDREdlFIT-TKVsPDHL-----KYDDVIKAAKESLKRLGTDYIDLYLIHWP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 113 DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSqnfILPTVYQASYSIVVRGIETNLLSTLRELGISIQ 192
Cdd:cd19072 111 NPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDREEESGLLPYCQKNGIAII 187
|
170
....*....|...
gi 995934143 193 AYSPLAAGFLSKT 205
Cdd:cd19072 188 AYSPLEKGKLSNA 200
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
30-310 |
1.45e-22 |
|
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: 96.14 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 30 DEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKA--PTGLG---GGAGKReNILEQGRKSNVVLRLS 102
Cdd:cd19091 42 DRLVDIALDAGINFFDTADVYSEGESEEILGKalKGRRDDVLIATKVrgRMGEGpndVGLSRH-HIIRAVEASLKRLGTD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 103 KIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVRGIETNLLS 182
Cdd:cd19091 121 YIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 183 TLRELGISIQAYSPLAAGFLSKTV---EQIENGNGTERWDPNSPYgmVNR-QLYFkpsymkMLTEYGKLSEQSGVSKVGL 258
Cdd:cd19091 201 LALDQGVGLLVWSPLAGGLLSGKYrrgQPAPEGSRLRRTGFDFPP--VDReRGYD------VVDALREIAKETGATPAQV 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 995934143 259 AYRWVryhsaLKGELGDAMIIGANSATQFREAVKEIE-NGPLEEwiVERIDEL 310
Cdd:cd19091 273 ALAWL-----LSRPTVSSVIIGARNEEQLEDNLGAAGlSLTPEE--IARLDKV 318
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
38-263 |
2.31e-22 |
|
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: 95.07 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGMGASEETIGN--KNLGA--EFSVWTKAptGLGGGAGK-------RENILEQGRKSNVVLRLSKIPV 106
Cdd:cd19148 36 DLGINLIDTAPVYGFGLSEEIVGKalKEYGKrdRVVIATKV--GLEWDEGGevvrnssPARIRKEVEDSLRRLQTDYIDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 107 YLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfiLPTVyQASYSIVVRGIETNLLSTLRE 186
Cdd:cd19148 114 YQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAP-----LHTV-QPPYNLFEREIEKDVLPYARK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 187 LGISIQAYSPLAAGFLSK--TVEQIENGNGTERWDPNspygmvnrqlYFKPSYMKMLTEYGKLS----EQSGVSKVGLAY 260
Cdd:cd19148 188 HNIVTLAYGALCRGLLSGkmTKDTKFEGDDLRRTDPK----------FQEPRFSQYLAAVEELDklaqERYGKSVIHLAV 257
|
...
gi 995934143 261 RWV 263
Cdd:cd19148 258 RWL 260
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
38-292 |
1.01e-20 |
|
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: 90.30 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYG----MGASEETIGN--KNLGAEFSVW--TK-APTGLGGGAGKR---ENILEQGRKSNVVLRLSKIP 105
Cdd:cd19082 28 ELGGNFIDTARVYGdwveRGASERVIGEwlKSRGNRDKVViaTKgGHPDLEDMSRSRlspEDIRADLEESLERLGTDYID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 106 VYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSI--VVRGIETNLLST 183
Cdd:cd19082 108 LYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQWSLarPNEPPWPGPTLV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 184 ---------LRELGISIQAYSPLAAGFLSKtveqiengngteRWDPNSPYGMVNRQLYFKPSYMKMLTEYGKLSEQSGVS 254
Cdd:cd19082 188 amdeemrawHEENQLPVFAYSSQARGFFSK------------RAAGGAEDDSELRRVYYSEENFERLERAKELAEEKGVS 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 995934143 255 KVGLAYRWVrYHSALKGelgdAMIIGANSATQFREAVK 292
Cdd:cd19082 256 PTQIALAYV-LNQPFPT----VPIIGPRTPEQLRDSLA 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
38-301 |
2.56e-20 |
|
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: 89.62 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGM--GASEETIGN------KNLGAEFSVWTKA----PTGLGGGAGKRENILEQGRKSNVVLRLSKIP 105
Cdd:cd19089 40 DLGITHFDLANNYGPppGSAEENFGRilkrdlRPYRDELVISTKAgygmWPGPYGDGGSRKYLLASLDQSLKRMGLDYVD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 106 VYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNfILPTVYQASYSIVVRGIETNLLSTLR 185
Cdd:cd19089 120 IFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDRWAEDGLLEVLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 186 ELGISIQAYSPLAAGFLS-KTVEQIENGNGTERWDPNSPYGMVNrqlyfkPSYMKMLTEYGKLSEQSGVSKVGLAYRWVR 264
Cdd:cd19089 199 EAGIGFIAFSPLAQGLLTdKYLNGIPPDSRRAAESKFLTEEALT------PEKLEQLRKLNKIAAKRGQSLAQLALSWVL 272
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 995934143 265 YH----SALkgelgdamiIGANSATQFREAVKEIENGPLEE 301
Cdd:cd19089 273 RDprvtSVL---------IGASSPSQLEDNVAALKNLDFSE 304
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
11-204 |
3.06e-20 |
|
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: 88.43 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 11 ALAGGTHTWVPTPKSEAtqdevVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAptGL---GGG- 81
Cdd:cd19088 10 RLTGPGIWGPPADREEA-----IAVLRralELGVNFIDTADSYGPDVNERLIAEalHPYPDDVVIATKG--GLvrtGPGw 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 82 ---AGKRENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqn 158
Cdd:cd19088 83 wgpDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR--- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 995934143 159 fiLPTVyQASYSIVVRGIEtNLLSTLRELGISIQAYSPLAAGFLSK 204
Cdd:cd19088 160 --IVSV-QNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQ 201
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
19-309 |
8.53e-20 |
|
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: 88.04 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 19 WVpTPKSEATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLG---AEFSVWTKAPTGLGGGAGK-----R 85
Cdd:cd19143 21 WV-TFGNQVDVDEAKECMKaayDAGVNFFDNAEVYANGQSEEIMGQaiKELGwprSDYVVSTKIFWGGGGPPPNdrglsR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 86 ENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVY 165
Cdd:cd19143 100 KHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVME 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 166 QASYSIVVRG-IETNLLSTLRELGISIQAYSPLAAGFLS-KTVEQIENGNgteRWDPNSPYGMVNRQLYFKPSYMKMLTE 243
Cdd:cd19143 180 QPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTgKYNNGIPEGS---RLALPGYEWLKDRKEELGQEKIEKVRK 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 995934143 244 YGKLSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIENGP-LEEWIVERIDE 309
Cdd:cd19143 257 LKPIAEELGCSLAQLAIAW-----CLKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEKIEA 318
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-299 |
2.08e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 86.04 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 29 QDEVVAIMQ---EHGITNLDTARSYgmGASEETIGNKNLGA-EFSVWTKAPTGLGGGAGKRENILEQGRKSNVVLRLSKI 104
Cdd:cd19097 25 EKEAKKILEyalKAGINTLDTAPAY--GDSEKVLGKFLKRLdKFKIITKLPPLKEDKKEDEAAIEASVEASLKRLKVDSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 105 PVYLLHAP-DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQ---VLEHYNyaksqnfilPTVYQASYSIV-VRGIETN 179
Cdd:cd19097 103 DGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEElekALESFK---------IDIIQLPFNILdQRFLKSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 180 LLSTLRELGISIQAYSPLAAGFLSKTVEQIengngterwdpnspygmvnrQLYFKPsYMKMLTEYGKLSEQSGVSKVGLA 259
Cdd:cd19097 174 LLAKLKKKGIEIHARSVFLQGLLLMEPDKL--------------------PAKFAP-AKPLLKKLHELAKKLGLSPLELA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 995934143 260 YRWVRYHsalkgELGDAMIIGANSATQFREAVKEIENGPL 299
Cdd:cd19097 233 LGFVLSL-----PEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
15-200 |
3.69e-19 |
|
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: 85.38 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVPTPKSEATQDEVVAIMQ--EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTK-APTGLGggagkRENIL 89
Cdd:cd19138 15 GQGTWYMGEDPAKRAQEIEALRAgiDLGMTLIDTAEMYGDGGSEELVGEaiRGRRDKVFLVSKvLPSNAS-----RQGTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 90 EQGRKSNVVLRLSKIPVYLLHAPdESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNfilPTVYQASY 169
Cdd:cd19138 90 RACERSLRRLGTDYLDLYLLHWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGN---CAANQVLY 165
|
170 180 190
....*....|....*....|....*....|.
gi 995934143 170 SIVVRGIETNLLSTLRELGISIQAYSPLAAG 200
Cdd:cd19138 166 NLGSRGIEYDLLPWCREHGVPVMAYSPLAQG 196
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
40-316 |
1.31e-18 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 85.43 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 40 GITNLDTARSYG--MGASEETIGnKNLGAEFSVW-------TKA-----PTGLGGGaGKRENILEQGRKSNVVLRLSKIP 105
Cdd:PRK09912 56 GITHFDLANNYGppPGSAEENFG-RLLREDFAAYrdeliisTKAgydmwPGPYGSG-GSRKYLLASLDQSLKRMGLEYVD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 106 VYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILpTVYQASYSIVVRGIE-TNLLSTL 184
Cdd:PRK09912 134 IFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPL-LIHQPSYNLLNRWVDkSGLLDTL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 185 RELGISIQAYSPLAAGFLS-KTVEQIENGNGTERwDPNSPYGMVNRQLyfKPSYMKMLTEYGKLSEQSGVSKVGLAYRWV 263
Cdd:PRK09912 213 QNNGVGCIAFTPLAQGLLTgKYLNGIPQDSRMHR-EGNKVRGLTPKML--TEANLNSLRLLNEMAQQRGQSMAQMALSWL 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 995934143 264 ryhsaLKGELGDAMIIGANSATQFREAVKEIENGPLEEWIVERIDE--------LWELVKD 316
Cdd:PRK09912 290 -----LKDERVTSVLIGASRAEQLEENVQALNNLTFSTEELAQIDQhiadgelnLWQASSD 345
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
15-310 |
2.25e-18 |
|
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: 84.27 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVP--TPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGAGK------ 84
Cdd:cd19160 19 GLGTWVTfgSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNilKSKGWRRSSYVVTTKIYWGGQAEtergls 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTV 164
Cdd:cd19160 99 RKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVR-GIETNLLSTLRELGISIQAYSPLAAGFL-SKTVEQIengngterwdPNSPYGMVNRQLYFKPsymKMLT 242
Cdd:cd19160 179 EQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLItGKYDGRV----------PDTCRAAVKGYQWLKE---KVQS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 243 EYGK-----------LSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIEN-GPLEEWIVERIDEL 310
Cdd:cd19160 246 EEGKkqqakvkelhpIADRLGCTVAQLAIAW-----CLRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDAL 320
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
15-265 |
2.66e-18 |
|
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: 83.64 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVPTPKSEAtqdEVVAIMQ---EHGITNLDTARSYGMGASEETIGNKN---------LGAEFSVWTKAPTGLGGgA 82
Cdd:cd19145 21 GLSGDYGAPKPEE---EGIALIHhafNSGVTFLDTSDIYGPNTNEVLLGKALkdgprekvqLATKFGIHEIGGSGVEV-R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 83 GKRENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVlehynyaKSQNFILP 162
Cdd:cd19145 97 GDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTI-------RRAHAVHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 163 -TVYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSK--TVEQIENGNGTERWDPNSPYGMV--NRQLYFKPSy 237
Cdd:cd19145 170 iTAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGkaKLEELLENSDVRKSHPRFQGENLekNKVLYERVE- 248
|
250 260
....*....|....*....|....*...
gi 995934143 238 mkmlteygKLSEQSGVSKVGLAYRWVRY 265
Cdd:cd19145 249 --------ALAKKKGCTPAQLALAWVLH 268
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
44-289 |
4.29e-18 |
|
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: 83.04 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 44 LDTARSYGMGASEETIGN--KNLGAEFSVWTK-----APTGLGGGAGKRENILEQGRKSNVVLRLSKIPVYLLHAPDESV 116
Cdd:cd19080 48 IDTANNYTNGTSERLLGEfiAGNRDRIVLATKytmnrRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 117 PVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVRGIETNLLSTLRELGISIQAYSP 196
Cdd:cd19080 128 PVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 197 LAAGFLS-KtvEQIENGnGTERWDPNSPYGMVnrqlYFKPSYMKMLTEYGKLSEQSGVSKVGLAYRWVRYHSAlkgelGD 275
Cdd:cd19080 208 LGGGLLTgK--YQRGEE-GRAGEAKGVTVGFG----KLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPG-----VV 275
|
250
....*....|....
gi 995934143 276 AMIIGANSATQFRE 289
Cdd:cd19080 276 IPIIGARTLEQLKD 289
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
27-208 |
7.16e-18 |
|
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: 82.67 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 27 ATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGAGK-------RENILEQGRK 94
Cdd:cd19078 22 PDKEEMIELIRkavELGITFFDTAEVYGPYTNEELVGEalKPFRDQVVIATKFGFKIDGGKPGplgldsrPEHIRKAVEG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 95 SNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVlehynyaKSQNFILP-TVYQASYSIVV 173
Cdd:cd19078 102 SLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI-------RRAHAVCPvTAVQSEYSMMW 174
|
170 180 190
....*....|....*....|....*....|....*
gi 995934143 174 RGIETNLLSTLRELGISIQAYSPLAAGFLSKTVEQ 208
Cdd:cd19078 175 REPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDE 209
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
9-307 |
1.06e-17 |
|
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: 82.51 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 9 LVALAggthTWV--PTPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLG---AEFSVWTKA--PTGLG 79
Cdd:cd19142 15 NVGLG----TWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRilKKKGwkrSSYIVSTKIywSYGSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 80 GGAGKRENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNF 159
Cdd:cd19142 91 ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 160 ILPTVYQASYSIVVR-GIETNLLSTLRELGISIQAYSPLAAGFLSKTVE---QIENGNGTERWDPNSPYGMVNRQLYFKP 235
Cdd:cd19142 171 PTPICEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSLGLDPGISEetrRLVTKLSFKSSKYKVGSDGNGIHEETRR 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995934143 236 SYMKmLTEYGKLSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIENGP------LEEwiVERI 307
Cdd:cd19142 251 ASHK-LRELSLIAERLGCDLTQLLIAW-----SLKNENVQCVLIGASSLEQLYSQLNSLQLLPklnsavMEE--LERI 320
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
30-209 |
1.45e-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: 81.08 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 30 DEVVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLGAE--FSVWTKAPTGLgggagKRENILEQGRKSNVVLRLS 102
Cdd:cd19137 26 EEMVELLKtaiELGYTHIDTAEMYGGGHTEELVGKaiKDFPREdlFIVTKVWPTNL-----RYDDLLRSLQNSLRRLDTD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 103 KIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSqnfilPTVY-QASYSIVVRGIETN-L 180
Cdd:cd19137 101 YIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-----PIVCnQVKYNLEDRDPERDgL 175
|
170 180 190
....*....|....*....|....*....|.
gi 995934143 181 LSTLRELGISIQAYSPLAAGFLSK--TVEQI 209
Cdd:cd19137 176 LEYCQKNGITVVAYSPLRRGLEKTnrTLEEI 206
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-203 |
2.63e-17 |
|
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: 79.83 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVPTPKSEATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGAGKR---- 85
Cdd:cd19086 9 GTWGLGGDWWGDVDDAEAIRALRaalDLGINFFDTADVYGDGHSERLLGKalKGRRDKVVIATKFGNRFDGGPERPqdfs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 86 -ENILEQGRKSNVVLRLSKIPVYLLH-APDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQnfilpt 163
Cdd:cd19086 89 pEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGID------ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 995934143 164 VYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLS 203
Cdd:cd19086 163 VVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLT 202
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
38-296 |
3.91e-17 |
|
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: 80.52 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYG--MGASEETIGnKNLGAEFSVW-------TKAP----TGLGGGAGKRENI---LEQGRKSnvvLRL 101
Cdd:cd19151 41 DLGITHFDLANNYGppPGSAEENFG-RILKEDLKPYrdeliisTKAGytmwPGPYGDWGSKKYLiasLDQSLKR---MGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 102 SKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSqnfiLPT---VYQASYSIVVRGIET 178
Cdd:cd19151 117 DYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKD----LGTpclIHQPKYSMFNRWVEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 179 NLLSTLRELGISIQAYSPLAAGFLS-KTVEQI-ENGNGTERWDPNSPYGMVnrqlyfkPSYMKMLTEYGKLSEQSGVSKV 256
Cdd:cd19151 193 GLLDVLEEEGIGCIAFSPLAQGLLTdRYLNGIpEDSRAAKGSSFLKPEQIT-------EEKLAKVRRLNEIAQARGQKLA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 995934143 257 GLAYRWVryhsaLKGELGDAMIIGANSATQFREAVKEIEN 296
Cdd:cd19151 266 QMALAWV-----LRNKRVTSVLIGASKPSQIEDAVGALDN 300
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-311 |
2.37e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 78.46 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 10 VALAGGT--HTWVPTpkSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTK---APTGLGGGA 82
Cdd:cd19104 15 LTFGGGGigGLMGRT--TREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRalKGLPAGPYITTKvrlDPDDLGDIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 83 GKRENILEqgrKSNVVLRLSKIPVYLLH---APDESVPVAETLG------------AIQTLYEEGRFEKFGLSNMSRD-- 145
Cdd:cd19104 93 GQIERSVE---KSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSttdvlglggvadAFERLRSEGKIRFIGITGLGNPpa 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 146 --QVLEHYNYAKSQ---NFILPTVYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKTVEQIENGNGTErwdp 220
Cdd:cd19104 170 irELLDSGKFDAVQvyyNLLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTS---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 221 NSPYG-MVNRQLYFKPsymkmlteygkLSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIENGPL 299
Cdd:cd19104 246 DSDVAiDFRRAAAFRA-----------LAREWGETLAQLAHRF-----ALSNPGVSTVLVGVKNREELEEAVAAEAAGPL 309
|
330
....*....|..
gi 995934143 300 EEWIVERIDELW 311
Cdd:cd19104 310 PAENLARLEALW 321
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
27-296 |
3.75e-16 |
|
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: 77.88 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 27 ATQDEVVAIMQEHGITNLDTARSYG--MGASEETIGnKNLGAEFS-------VWTKAP----TGLGGGAGKRENILEQGR 93
Cdd:cd19150 30 ETQRAILRTAFDLGITHFDLANNYGppPGSAEENFG-RILREDFAgyrdeliISTKAGydmwPGPYGEWGSRKYLLASLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 94 KSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILpTVYQASYSIVV 173
Cdd:cd19150 109 QSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELGTPL-LIHQPSYNMLN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 174 RGIE-TNLLSTLRELGISIQAYSPLAAGFL-SKTVEQIENGNGTERWDPNSPYGMVNRQLyfkpSYMKMLTEygkLSEQS 251
Cdd:cd19150 188 RWVEeSGLLDTLQELGVGCIAFTPLAQGLLtDKYLNGIPEGSRASKERSLSPKMLTEANL----NSIRALNE---IAQKR 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 995934143 252 GVSKVGLAYRWVryhsaLKGELGDAMIIGANSATQFREAVKEIEN 296
Cdd:cd19150 261 GQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEENVGALDN 300
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
15-310 |
3.76e-16 |
|
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: 77.77 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVP--TPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN---KNLGAEFSVWTKAPTGLGGGAG-----K 84
Cdd:cd19159 17 GLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSiikKKGWRRSSLVITTKLYWGGKAEterglS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTV 164
Cdd:cd19159 97 RKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVR-GIETNLLSTLRELGISIQAYSPLAAGFLSKTVEqiengNGTerwdPNSPYGMVNRQLYFKPsymKMLTE 243
Cdd:cd19159 177 EQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG-----NGV----PESSRASLKCYQWLKE---RIVSE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 995934143 244 YGK-----------LSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIENGP-LEEWIVERIDEL 310
Cdd:cd19159 245 EGRkqqnklkdlspIAERLGCTLPQLAVAW-----CLRNEGVSSVLLGSSTPEQLIENLGAIQVLPkMTSHVVNEIDNI 318
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-263 |
4.65e-16 |
|
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: 77.48 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 13 AGGTHTWVPTPKSEATQDEVVAIMQEHGITNLDTARSYGmgASEETIGN---KNLG--------AEFSVWTKAPTGLGGG 81
Cdd:cd19144 20 AMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYG--DSEELIGRwfkQNPGkrekiflaTKFGIEKNVETGEYSV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 82 AGKRENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNyaksqnfIL 161
Cdd:cd19144 98 DGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-------VH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 162 P-TVYQASYSIVVRGIETN---LLSTLRELGISIQAYSPLAAGFLSKTVEQiengngTERWDPNSPYGMVNRqlyFK--- 234
Cdd:cd19144 171 PiAAVQIEYSPFSLDIERPeigVLDTCRELGVAIVAYSPLGRGFLTGAIRS------PDDFEEGDFRRMAPR---FQaen 241
|
250 260 270
....*....|....*....|....*....|
gi 995934143 235 -PSYMKMLTEYGKLSEQSGVSKVGLAYRWV 263
Cdd:cd19144 242 fPKNLELVDKIKAIAKKKNVTAGQLTLAWL 271
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-295 |
1.75e-15 |
|
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: 75.95 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVP--TPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGAGK------ 84
Cdd:cd19141 16 GLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKilKKKGWRRSSYVITTKIFWGGKAEtergls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTV 164
Cdd:cd19141 96 RKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVR-GIETNLLSTLRELGISIQAYSPLAAGFLSktveqienGNGTERWDPNSPYGMVNRQLYFKpsymKMLTE 243
Cdd:cd19141 176 EQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILS--------GKYDDGVPEYSRASLKGYQWLKE----KILSE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995934143 244 YGK-----------LSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIE 295
Cdd:cd19141 244 EGRrqqaklkelqiIADRLGCTLPQLAIAW-----CLKNEGVSSVLLGASSTEQLYENLQAIQ 301
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
15-310 |
3.63e-15 |
|
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: 75.12 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVP--TPKSEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGAGK------ 84
Cdd:cd19158 17 GLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNiiKKKGWRRSSLVITTKIFWGGKAEtergls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTV 164
Cdd:cd19158 97 RKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPIC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 165 YQASYSIVVR-GIETNLLSTLRELGISIQAYSPLAAGFLSktveqienGNGTERWDPNSPYGMVNRQlYFKPsymKMLTE 243
Cdd:cd19158 177 EQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVS--------GKYDSGIPPYSRASLKGYQ-WLKD---KILSE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 995934143 244 YGK-----------LSEQSGVSKVGLAYRWvryhsALKGELGDAMIIGANSATQFREAVKEIENGP-LEEWIVERIDEL 310
Cdd:cd19158 245 EGRrqqaklkelqaIAERLGCTLPQLAIAW-----CLRNEGVSSVLLGASNAEQLMENIGAIQVLPkLSSSIVHEIDSI 318
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
38-268 |
3.64e-15 |
|
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: 74.51 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGMGASEETIG-----NKNLGAEFSVWTKA----PTGLGGGAGKR-----ENILEQGRKSNVVLRLSK 103
Cdd:cd19092 35 ELGITTFDHADIYGGGKCEELFGealalNPGLREKIEIQTKCgirlGDDPRPGRIKHydtskEHILASVEGSLKRLGTDY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 104 IPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQV--LEHYnyaksqnfiLP---TVYQASYSIVVRG-IE 177
Cdd:cd19092 115 LDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIelLQSY---------LDqplVTNQIELSLLHTEaID 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 178 TNLLSTLRELGISIQAYSPLAAGFLSKTveqiengngterwdpnspygmvnrqlyFKPSYMKMLTEYGKLSEQSGVSKVG 257
Cdd:cd19092 186 DGTLDYCQLLDITPMAWSPLGGGRLFGG---------------------------FDERFQRLRAALEELAEEYGVTIEA 238
|
250
....*....|.
gi 995934143 258 LAYRWVRYHSA 268
Cdd:cd19092 239 IALAWLLRHPA 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-204 |
3.06e-14 |
|
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: 71.50 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 14 GGTHTW-VPTPKSEATQDEVVAIMQEHGITNLDTARSYgmGASEETIGN---KNLGAEFSVWTKAPTGLGGGAGKR---- 85
Cdd:cd19095 6 GTSGIGrVWGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRalaGLRRDDLFIATKVGTHGEGGRDRKdfsp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 86 ENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSnmSRDQVLEHynYAKSQNFilpTVY 165
Cdd:cd19095 84 AAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS--GDGEELEA--AIASGVF---DVV 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 995934143 166 QASYSIVVRGIEtNLLSTLRELGISIQAYSPLAAGFLSK 204
Cdd:cd19095 157 QLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLRR 194
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
18-293 |
1.01e-13 |
|
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: 70.73 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 18 TWVPTPkseATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIgnKNLGAEF------------SVWTKAPTGLGGGA 82
Cdd:cd19077 16 TWRPNP---TPDEEAFETMKaalDAGSNLWNGGEFYGPPDPHANL--KLLARFFrkypeyadkvvlSVKGGLDPDTLRPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 83 GKRENILEQGRKSNVVLRLSK-IPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfil 161
Cdd:cd19077 91 GSPEAVRKSIENILRALGGTKkIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVHP------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 162 PTVYQASYSIVVRGIETN-LLSTLRELGISIQAYSPLAAGFLSktveqienGNGTERWD-PNSPY-GMVNRqlyFKPSY- 237
Cdd:cd19077 165 IAAVEVEYSLFSREIEENgVLETCAELGIPIIAYSPLGRGLLT--------GRIKSLADiPEGDFrRHLDR---FNGENf 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 995934143 238 ---MKMLTEYGKLSEQSGVSKVGLAYRWVRYhsalkgeLGDAMII---GANSATQFREAVKE 293
Cdd:cd19077 234 eknLKLVDALQELAEKKGCTPAQLALAWILA-------QSGPKIIpipGSTTLERVEENLKA 288
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-200 |
2.20e-13 |
|
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: 68.84 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWvptpksEATQDEVVAIMQ---EHGITNLDTARSYGmgaSEETIGNKNLGA-----EFSVWTKAPT-GLgggagKR 85
Cdd:cd19073 5 GLGTW------QLRGDDCANAVKealELGYRHIDTAEIYN---NEAEVGEAIAESgvpreDLFITTKVWRdHL-----RP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 86 ENILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRdqvlEHYNYAKSQNFILPTVY 165
Cdd:cd19073 71 EDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTI----ELLEEALDISPLPIAVN 146
|
170 180 190
....*....|....*....|....*....|....*
gi 995934143 166 QASYSIVVRGIEtnLLSTLRELGISIQAYSPLAAG 200
Cdd:cd19073 147 QVEFHPFLYQAE--LLEYCRENDIVITAYSPLARG 179
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
44-200 |
5.85e-12 |
|
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: 64.59 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 44 LDTARSYGmgaSEETIGN--KNLG---AEFSVWTK-APTGLgggagKRENILEQGRKSNVVLRLSKIPVYLLHAPDESVP 117
Cdd:cd19140 38 IDTAQMYG---NEAQVGEaiAASGvprDELFLTTKvWPDNY-----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 118 VAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFilptVYQASYSIVVRgiETNLLSTLRELGISIQAYSPL 197
Cdd:cd19140 110 LAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLF----TNQVEYHPYLD--QRKLLDAAREHGIALTAYSPL 183
|
...
gi 995934143 198 AAG 200
Cdd:cd19140 184 ARG 186
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
18-200 |
1.13e-11 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 63.92 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 18 TWvptpksEATQDEVVAIMQ---EHGITNLDTARSYGmgaSEETIGN--KNLG---AEFSVWTK-APTGLGggagkRENI 88
Cdd:COG0656 12 TW------QLPGEEAAAAVRtalEAGYRHIDTAAMYG---NEEGVGEaiAASGvprEELFVTTKvWNDNHG-----YDDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 89 LEQGRKSNVVLRLSKIPVYLLHAPDeSVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEhynyAKSQNFILPTVYQAS 168
Cdd:COG0656 78 LAAFEESLERLGLDYLDLYLIHWPG-PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEE----LLAETGVKPAVNQVE 152
|
170 180 190
....*....|....*....|....*....|..
gi 995934143 169 YSIVVRgiETNLLSTLRELGISIQAYSPLAAG 200
Cdd:COG0656 153 LHPYLQ--QRELLAFCREHGIVVEAYSPLGRG 182
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
28-301 |
2.92e-11 |
|
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: 62.96 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 28 TQDEVVAIMQ---EHGITNLDTARSYgmGASEETIG---NKNLGAEFSVWTKA---PTGLGGGAGKR-----ENILEqgr 93
Cdd:cd19090 18 DDDEAVATIRaalDLGINYIDTAPAY--GDSEERLGlalAELPREPLVLSTKVgrlPEDTADYSADRvrrsvEESLE--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 94 ksnvVLRLSKIPVYLLHAPDESVPVAET-----LGAIQTLYEEGRFEKFGLSNMSRDqvlEHYNYAKSQNF--ILptVYQ 166
Cdd:cd19090 93 ----RLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGLGGGPPD---LLRRAIETGDFdvVL--TAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 167 AsYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLsktveqienGNGTERWDPNSPYGMVNRQLyfkPSYMKMLteygK 246
Cdd:cd19090 164 R-YTLLDQSAADELLPAAARHGVGVINASPLGMGLL---------AGRPPERVRYTYRWLSPELL---DRAKRLY----E 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 995934143 247 LSEQSGVSKVGLAYRWVryhsaLKGELGDAMIIGANSATQFREAVKEIeNGPLEE 301
Cdd:cd19090 227 LCDEHGVPLPALALRFL-----LRDPRISTVLVGASSPEELEQNVAAA-EGPLPE 275
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
29-200 |
3.26e-11 |
|
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: 62.73 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 29 QDEVVAIMQEHGITNLDTARSYGmgaSEETIGN--KNLG---AEFSVWTKA-PTGLGGGAGKR--ENILEQgrksnvvLR 100
Cdd:cd19135 28 HEAVVYALKECGYRHIDTAKRYG---CEELLGKaiKESGvprEDLFLTTKLwPSDYGYESTKQafEASLKR-------LG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 101 LSKIPVYLLHAPDESVPV-------AETLGAIQTLYEEGRFEKFGLSNMSrdqvLEHYNYAKSQNFILPTVYQASYSIVV 173
Cdd:cd19135 98 VDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFL----IEHLEQLLEDCSVVPHVNQVEFHPFQ 173
|
170 180
....*....|....*....|....*..
gi 995934143 174 RGIEtnLLSTLRELGISIQAYSPLAAG 200
Cdd:cd19135 174 NPVE--LIEYCRDNNIVFEGYCPLAKG 198
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
24-209 |
4.13e-10 |
|
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: 59.42 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 24 KSEATQDEVV-AImqEHGITNLDTARSYGmgaSEETIGN--KNLG---AEFSVWTK-APTGLGggagkRENILEQGRKSN 96
Cdd:cd19071 12 KPEETAEAVLaAL--EAGYRHIDTAAAYG---NEAEVGEaiRESGvprEELFITTKlWPTDHG-----YERVREALEESL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 97 VVLRLSKIPVYLLHAP------DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfILPTVYQasys 170
Cdd:cd19071 82 KDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQ---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 995934143 171 ivvrgIETN-------LLSTLRELGISIQAYSPLAAGFL---------------SKTVEQI 209
Cdd:cd19071 154 -----IELHpylqqkeLVEFCKEHGIVVQAYSPLGRGRRpllddpvlkeiakkyGKTPAQV 209
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-204 |
6.33e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 59.27 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 25 SEATQDEVVAIMQEHGITNLDTARSYGMGASEETIGN--KNLGAE-FSVWTK-APTGLGGGAGKRENILEQGRKSnvvLR 100
Cdd:cd19103 30 DEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEflKRYPREdYIISTKfTPQIAGQSADPVADMLEGSLAR---LG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 101 LSKIPVYLLHAPDEsVPvAETLGAIqTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVyQASYSIVVRGIETN- 179
Cdd:cd19103 107 TDYIDIYWIHNPAD-VE-RWTPELI-PLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAV-QNHYSLLYRSSEEAg 182
|
170 180
....*....|....*....|....*
gi 995934143 180 LLSTLRELGISIQAYSPLAAGFLSK 204
Cdd:cd19103 183 ILDYCKENGITFFAYMVLEQGALSG 207
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-200 |
2.23e-09 |
|
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: 57.73 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGM-------GASEETIGN--------------KNLGA---EFSVWTKAPTGLGggagkRENILEQGR 93
Cdd:cd19752 28 AAGGNFLDTANNYAFwteggvgGESERLIGRwlkdrgnrddvviaTKVGAgprDPDGGPESPEGLS-----AETIEQEID 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 94 KSNVVLRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSI-- 171
Cdd:cd19752 103 KSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYlr 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 995934143 172 --------VVRGIETNLLSTLRELG-ISIQAYSPLAAG 200
Cdd:cd19752 183 prpgadfgVQRIVTDELLDYASSRPdLTLLAYSPLLSG 220
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-209 |
2.55e-08 |
|
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: 54.16 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 11 ALAGGTHT-WVPTPKSEATQDEVVAIMQ--EHGITNLDTARSYGmgaSEETIGN--KNLGA---EFSVWTKAPTGLGGGA 82
Cdd:cd19120 6 AIAFGTGTaWYKSGDDDIQRDLVDSVKLalKAGFRHIDTAEMYG---NEKEVGEalKESGVpreDLFITTKVSPGIKDPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 83 GKRENILEQgrksnvvLRLSKIPVYLLHAP----DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqn 158
Cdd:cd19120 83 EALRKSLAK-------LGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK--- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 995934143 159 fILPTVYQASYSIVVRGIETNLLSTLRELGISIQAYSPLAA------GFLSKTVEQI 209
Cdd:cd19120 153 -IKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLSPltrdagGPLDPVLEKI 208
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
26-312 |
3.07e-08 |
|
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: 54.29 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 26 EATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIG---NKNLGAEFSVWTKA-------PTGLGGGAGKRENILEQG 92
Cdd:cd19162 15 RAGEDEAAATLDaawDAGIRYFDTAPLYGLGLSERRLGaalARHPRAEYVVSTKVgrllepgAAGRPAGADRRFDFSADG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 93 RKSNVV-----LRLSKIPVYLLHAPDE--SVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILptvy 165
Cdd:cd19162 95 IRRSIEaslerLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVDVVMV---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 166 QASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLSKtveqieNGNGTERWDpnspYGMVNRQLyfkpsyMKMLTEYG 245
Cdd:cd19162 171 AGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT------DDPAGDRYD----YRPATPEV------LARARRLA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995934143 246 KLSEQSGVSKVGLAYRWVRYHSALKgelgdAMIIGANSATQFREAVkeiengpleEWIVERI-DELWE 312
Cdd:cd19162 235 AVCRRYGVPLPAAALQFPLRHPAVA-----SVVVGAASPAELRDNL---------ALLRTPIpAEFWA 288
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-199 |
3.72e-08 |
|
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: 54.04 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWvptpksEATQDEVVAIMQ---EHGITNLDTARSYGmgaSEETIGN---------KNLGAEFSVWTKAPTgLGGGA 82
Cdd:cd19111 8 GLGTY------QSPPEEVRAAVDyalFVGYRHIDTALSYQ---NEKAIGEalkwwlkngKLKREEVFITTKLPP-VYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 83 GKRENILEQGRKSnvvLRLSKIPVYLLHAP-------------DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLE 149
Cdd:cd19111 78 KDTEKSLEKSLEN---LKLPYVDLYLIHHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 995934143 150 HYNYAKsqnfILPTVYQASYSIVVRgiETNLLSTLRELGISIQAYSPLAA 199
Cdd:cd19111 155 ILAYAK----VKPSNLQLECHAYLQ--QRELRKFCNKKNIVVTAYAPLGS 198
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
26-260 |
7.53e-08 |
|
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: 53.20 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 26 EATQDEVVAIMQ---EHGITNLDTARSYGMGASEETIG-------NKNlgaEFSVWTKAPTGLGGGAGKRENILEQG--R 93
Cdd:cd19146 31 ECDKETAFKLLDafyEQGGNFIDTANNYQGEESERWVGewmasrgNRD---EMVLATKYTTGYRRGGPIKIKSNYQGnhA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 94 KSNVV--------LRLSKIPVYLLHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVY 165
Cdd:cd19146 108 KSLRLsveaslkkLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 166 QASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLsKTVEQIENGNGTER--WDPNSPYGMVNRQLyfkpsyMKMLTE 243
Cdd:cd19146 188 QGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQF-RTEEEFKRRGRSGRkgGPQTEKERKVSEKL------EKVAEE 260
|
250
....*....|....*..
gi 995934143 244 YGKLseqsgVSKVGLAY 260
Cdd:cd19146 261 KGTA-----ITSVALAY 272
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
44-200 |
1.60e-07 |
|
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: 51.81 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 44 LDTARSYGmgaSEETIGN--KNLG---AEFSVWTKAPTGLGGGAGKRENILEQGRKsnvvLRLSKIPVYLLHAPDESVPv 118
Cdd:cd19133 40 IDTAAAYG---NEEAVGRaiKKSGiprEELFITTKLWIQDAGYEKAKKAFERSLKR----LGLDYLDLYLIHQPFGDVY- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 119 aETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfILPTVYQasysivvrgIETN-------LLSTLRELGISI 191
Cdd:cd19133 112 -GAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE----VKPAVNQ---------IETHpfnqqieAVEFLKKYGVQI 177
|
....*....
gi 995934143 192 QAYSPLAAG 200
Cdd:cd19133 178 EAWGPFAEG 186
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-221 |
1.86e-07 |
|
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: 52.03 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWvptpksEATQDEVVAIMQ---EHGITNLDTARSYgmgASEETIGN--KNLGAEFS-------VWTKAPTGlgggA 82
Cdd:cd19154 16 GLGTW------QSKGAEGITAVRtalKAGYRLIDTAFLY---QNEEAIGEalAELLEEGVvkredlfITTKLWTH----E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 83 GKRENILEQGRKSNVVLRLSKIPVYLLHAP-------------------DESVPVAETLGAIQTLYEEGRFEKFGLSNMS 143
Cdd:cd19154 83 HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 995934143 144 RDQVLEHYNYAKsqnfILPTVYQASYSIVVRGIEtnLLSTLRELGISIQAYSPLAA-GFLSKTVEQIENGNGTERWDPN 221
Cdd:cd19154 163 NDQIQRILDNAR----VKPHNNQVECHLYFPQKE--LVEFCKKHNISVTSYATLGSpGRANFTKSTGVSPAPNLLQDPI 235
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-204 |
2.82e-07 |
|
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: 51.05 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 38 EHGITNLDTARSYGMGASEETIGN--KNLGAEfSVW--TKAPtgLGGGAGKRENILEQGRKSNVVLRLSKIPVYLLHA-- 111
Cdd:cd19105 36 DLGINYFDTAEGYGNGNSEEIIGEalKGLRRD-KVFlaTKAS--PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGvd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 112 -PDESVPVAETLGAIQTLYEEGRFEKFGLSnmsrdqvlEHYNYAKSQNFILPT----VYQASYSIVVRGIETN-LLSTLR 185
Cdd:cd19105 113 tPEERLLNEELLEALEKLKKEGKVRFIGFS--------THDNMAEVLQAAIESgwfdVIMVAYNFLNQPAELEeALAAAA 184
|
170
....*....|....*....
gi 995934143 186 ELGISIQAYSPLAAGFLSK 204
Cdd:cd19105 185 EKGIGVVAMKTLAGGYLQP 203
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
29-153 |
3.42e-07 |
|
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: 50.64 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 29 QDEVVAIMQ---EHGITNLDTARSYGMGASEETIGN---KNLGAEFSVWTKAPTGLGGGAGKRENILEQGRKsnvVLRLS 102
Cdd:cd19096 20 EEKAIEMIRyaiDAGINYFDTAYGYGGGKSEEILGEalkEGPREKFYLATKLPPWSVKSAEDFRRILEESLK---RLGVD 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 995934143 103 KIPVYLLHAP--DESVPVAETLGAIQTL---YEEGRFEKFGLS-NMSRDQVLE------------HYNY 153
Cdd:cd19096 97 YIDFYLLHGLnsPEWLEKARKGGLLEFLekaKKEGLIRHIGFSfHDSPELLKEildsydfdfvqlQYNY 165
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-202 |
4.67e-07 |
|
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: 50.17 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 8 TLVALAGGTHTWVPtpkseatQDEVVAIMQ---EHGITNLDTARSYgmGASEETIGNknlgaefsvwtkaptGLgggAGK 84
Cdd:cd19100 12 SRLGFGGGPLGRLS-------QEEAAAIIRralDLGINYFDTAPSY--GDSEEKIGK---------------AL---KGR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENI-----------------LEQGRKSnvvLRLSKIPVYLLHAPDESVPVAETL---GAIQTLYE---EGRFEKFGLSN 141
Cdd:cd19100 65 RDKVflatktgardyegakrdLERSLKR---LGTDYIDLYQLHAVDTEEDLDQVFgpgGALEALLEakeEGKIRFIGISG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 995934143 142 MSRD---QVLEHYNYAksqnfilpTVyQASYSIVVRGI---ETNLLSTLRELGISIQAYSPLAAGFL 202
Cdd:cd19100 142 HSPEvllRALETGEFD--------VV-LFPINPAGDHIdsfREELLPLAREKGVGVIAMKVLAGGRL 199
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
29-200 |
1.40e-06 |
|
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: 48.78 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 29 QDEVVAIMQ---EHGITNLDTARSYGmgaSEETIGN--KNLGAEFS-------VWTK-APTGLGGGAGkRENILeqgrKS 95
Cdd:cd19136 14 EEEVRQAVDaalKAGYRLIDTASVYR---NEADIGKalRDLLPKYGlsredifITSKlAPKDQGYEKA-RAACL----GS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 96 NVVLRLSKIPVYLLHAP-----DESVPV-----AETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfILPTVY 165
Cdd:cd19136 86 LERLGTDYLDLYLIHWPgvqglKPSDPRnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE----VPPAVN 161
|
170 180 190
....*....|....*....|....*....|....*
gi 995934143 166 QASYSivVRGIETNLLSTLRELGISIQAYSPLAAG 200
Cdd:cd19136 162 QVEFH--PHLVQKELLKFCKDHGIHLQAYSSLGSG 194
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
9-202 |
1.66e-06 |
|
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: 48.76 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 9 LVALAGGthtWVPTPKSEATQDEVVAImqEHGITNLDTARSYGMGASEETIGN--KNLGAE-FSVWTKA----------- 74
Cdd:cd19152 7 TAPLGNL---YEAVSDEEAKATLVAAW--DLGIRYFDTAPWYGAGLSEERLGAalRELGREdYVISTKVgrllvplqeve 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 75 PTGLGGGAGKREN----------ILEQGRKSNVVLRLSKIPVYLLHAPDESVPVAETL-----------GAIQTLYEEGR 133
Cdd:cd19152 82 PTFEPGFWNPLPFdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafRALEELREEGV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995934143 134 FEKFGL-SNMSR--DQVLEHynyAKSQNFILptvyqA-SYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFL 202
Cdd:cd19152 162 IKAIGLgVNDWEviLRILEE---ADLDWVML-----AgRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFL 226
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
15-199 |
2.57e-06 |
|
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: 48.29 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVpTPKSEATQDEVVAImqEHGITNLDTARSYGmgaSEETIGN---------KNLGAEFSVWTKAPTGlgggAGKR 85
Cdd:cd19155 16 GLGTWQ-SSPEEIETAVDTAL--EAGYRHIDTAYVYR---NEAAIGNvlkkwidsgKVKREELFIVTKLPPG----GNRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 86 ENILEQGRKSNVVLRLSKIPVYLLHAP---------------------DESVPVAETLGAIQTLYEEGRFEKFGLSNMSR 144
Cdd:cd19155 86 EKVEKFLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 995934143 145 DQVLEHYNYAKsqnfILPTVYQASYSIVVRgiETNLLSTLRELGISIQAYSPLAA 199
Cdd:cd19155 166 EQMARILKNAR----IKPANLQVELHVYLQ--QKDLVDFCSTHSITVTAYAPLGS 214
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
99-207 |
6.95e-06 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 47.07 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 99 LRLSKIPVYLLHAP--------------------DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqn 158
Cdd:cd19129 93 LQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR--- 169
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 995934143 159 fILPTVYQASYSIVVRgiETNLLSTLRELGISIQAYSPLAAGFLSKTVE 207
Cdd:cd19129 170 -IKPAVVQVESHPYLP--EWELLDFCKNHGIVLQAFAPLGHGMEPKLLE 215
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
44-217 |
1.36e-05 |
|
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: 46.36 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 44 LDTARSYGMGASEETIG-------NKNLGAEFSVWTKAPTGLGGGAGKRENILEQGRKSNVV--------LRLSKIPVYL 108
Cdd:cd19147 51 IDTANNYQDEQSETWIGewmksrkNRDQIVIATKFTTDYKAYEVGKGKAVNYCGNHKRSLHVsvrdslrkLQTDWIDILY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 109 LHAPDESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKSQNFILPTVYQASYSIVVRGIETNLLSTLRELG 188
Cdd:cd19147 131 VHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFG 210
|
170 180 190
....*....|....*....|....*....|..
gi 995934143 189 ISIQAYSPLAAG-FLSKTV--EQIENGNGTER 217
Cdd:cd19147 211 MALAPWDVLGGGkFQSKKAveERKKNGEGLRS 242
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
28-310 |
1.44e-05 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 46.35 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 28 TQDEVVAIMQ---EHGITNLDTARSYGMgaSEETIGN--KNLGAEFSVWTKAPTGLGGGAGKRENILEQGRKsnvvLRLS 102
Cdd:COG1453 27 DEEEAEALIRraiDNGINYIDTARGYGD--SEEFLGKalKGPRDKVILATKLPPWVRDPEDMRKDLEESLKR----LQTD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 103 KIPVYLLHAPDESV----PVAET--LGAIQTLYEEGRFEKFGLSNMSRDQVLE-------------HYNYaksqnfilpt 163
Cdd:COG1453 101 YIDLYLIHGLNTEEdlekVLKPGgaLEALEKAKAEGKIRHIGFSTHGSLEVIKeaidtgdfdfvqlQYNY---------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 164 VYQaSYSIVVRGIEtnllsTLRELGISIQAYSPLAAGFLSKTVEQIEngngtERWDPnspygmvnrqlyfkpsymkmlte 243
Cdd:COG1453 171 LDQ-DNQAGEEALE-----AAAEKGIGVIIMKPLKGGRLANPPEKLV-----ELLCP----------------------- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995934143 244 ygklseqsGVSKVGLAYRWVRYHSALkgelgDAMIIGANSATQFREAVKEIENG-PLEEWIVERIDEL 310
Cdd:COG1453 217 --------PLSPAEWALRFLLSHPEV-----TTVLSGMSTPEQLDENLKTADNLePLTEEELAILERL 271
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
93-197 |
2.24e-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: 45.45 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 93 RKSNVVLRLSKIPVYLLHAP------DE-------------SVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNY 153
Cdd:cd19106 89 RKTLKDLQLDYLDLYLIHWPyafergDNpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSV 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 995934143 154 AKsqnfILPTVYQasysivvrgIE-------TNLLSTLRELGISIQAYSPL 197
Cdd:cd19106 169 AR----IKPAVLQ---------VEchpylaqNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
29-296 |
2.41e-05 |
|
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: 45.22 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 29 QDEVVAIMQE---HGITNLDTARSYGMGASEETIGN--KNLGAEFSVWTKAPTGLGGGAGKRENILEQGRKS--NVVLRL 101
Cdd:cd19153 32 QDEAVAIVAEafaAGINHFDTSPYYGAESSEAVLGKalAALQVPRSSYTVATKVGRYRDSEFDYSAERVRASvaTSLERL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 102 SKIPVYLLHAPD-ESVP----VAETLGAIQTLYEEGRFEKFGLSNMSRDQVlehynyAKSQNFILPTVYQASYSIVVRGI 176
Cdd:cd19153 112 HTTYLDVVYLHDiEFVDydtlVDEALPALRTLKDEGVIKRIGIAGYPLDTL------TRATRRCSPGSLDAVLSYCHLTL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 177 ETNLLSTL-----RELGISIQAYSPLAAGFLSktvEQiengnGTERWDPNSPygmvnrqlyfkpsymkMLTEYGKLS--- 248
Cdd:cd19153 186 QDARLESDapglvRGAGPHVINASPLSMGLLT---SQ-----GPPPWHPASG----------------ELRHYAAAAdav 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 995934143 249 -EQSGVSKVGLAyrwVRYHSALKGELGdAMIIGANSATQFREAVKEIEN 296
Cdd:cd19153 242 cASVEASLPDLA---LQYSLAAHAGVG-TVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
99-219 |
2.77e-05 |
|
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: 45.07 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 99 LRLSKIPVYLLHAPDESVPVaETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAKsqnfILPTVYQASYSivVRGIET 178
Cdd:cd19157 94 LGLDYLDLYLIHWPVKGKYK-ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFH--PRLTQK 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 995934143 179 NLLSTLRELGISIQAYSPLAAGFL-------------SKTVEQIengngTERWD 219
Cdd:cd19157 167 ELRDYCKKQGIQLEAWSPLMQGQLldnpvlkeiaekyNKSVAQV-----ILRWD 215
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
26-209 |
4.07e-05 |
|
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: 44.29 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 26 EATQDEVVAIMQ---EHGITNLDTARSYGmgaSEETIGN--KNLG---AEFSVWTKaptgLGGGAGKRENILEQGRKSNV 97
Cdd:cd19131 19 QVSNDEAASAVRealEVGYRSIDTAAIYG---NEEGVGKaiRASGvprEELFITTK----LWNSDQGYDSTLRAFDESLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 98 VLRLSKIPVYLLHAPdesVPVA----ETLGAIQTLYEEGRFEKFGLSNMSrdqvLEHYNYAKSQNFILPTVYQasysivv 173
Cdd:cd19131 92 KLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFT----IEHLQRLIDETGVVPVVNQ------- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 995934143 174 rgIETNLLSTLREL-------GISIQAYSPLAAGFL--SKTVEQI 209
Cdd:cd19131 158 --IELHPRFQQRELrafhakhGIQTESWSPLGQGGLlsDPVIGEI 200
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-292 |
8.19e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 43.74 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 30 DEVVAIMQEH---GITNLDTARSYGmgASEETIG--NKNLGAEFSVW------TK-APTGLGGGAGKR--ENILEQGRKS 95
Cdd:cd19101 23 DAAVRAMAAYvdaGLTTFDCADIYG--PAEELIGefRKRLRRERDAAddvqihTKwVPDPGELTMTRAyvEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 96 nvvLRLSKIPVYLLHAPDESVP-VAETLGAIQTLYEEGRFEKFGLSNMSrdqvLEHYNYAKSQNFilPTVY-QASYSIVV 173
Cdd:cd19101 101 ---LGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFD----TERLREILDAGV--PIVSnQVQYSLLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 174 RGIETNLLSTLRELGISIQAYSPLAAGFLSktveqiengngtERW-DPNSPYGMV--NRQLYfkpSYMKMLTEYG----- 245
Cdd:cd19101 172 RRPENGMAALCEDHGIKLLAYGTLAGGLLS------------EKYlGVPEPTGPAleTRSLQ---KYKLMIDEWGgwdlf 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 995934143 246 --------KLSEQSGVSKVGLAYRWVRYHSALKGelgdaMIIGANSATQFREAVK 292
Cdd:cd19101 237 qellrtlkAIADKHGVSIANVAVRWVLDQPGVAG-----VIVGARNSEHIDDNVR 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
93-200 |
8.96e-05 |
|
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: 43.11 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 93 RKSNVVLRLSKIPVYLLH--APDESVPVAETLGAIQTLYEEGRFEKFGLSnmsrdqvlehynyaksqNFILPTVYQASYS 170
Cdd:cd19139 78 EESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVS-----------------NFTIALLDEAIAV 140
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 995934143 171 IVVRGIETN------------LLSTLRELGISIQAYSPLAAG 200
Cdd:cd19139 141 VGAGAIATNqielspylqnrkLVAHCKQHGIHVTSYMTLAYG 182
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
29-316 |
2.58e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 42.07 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 29 QDEVVAIMQEH---GITNLDTARSYGMGASEETIGN--KNLGA---EFSVWTKAPTGLGGGAGKRENILEQGRKSNVVLR 100
Cdd:PLN02587 30 EEDAIASVREAfrlGINFFDTSPYYGGTLSEKVLGKalKALGIpreKYVVSTKCGRYGEGFDFSAERVTKSVDESLARLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 101 LSKIPVYLLH-----APDESVpvAETLGAIQTLYEEGRFEKFGLSNMSrdqvLEHYNYA------KSQNFILPtvyQASY 169
Cdd:PLN02587 110 LDYVDILHCHdiefgSLDQIV--NETIPALQKLKESGKVRFIGITGLP----LAIFTYVldrvppGTVDVILS---YCHY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 170 SIVVRGIEtNLLSTLRELGISIQAYSPLAAGFLSktveqienGNGTERWDPNSPygmvnrQLyfkPSYMKMLTEYGKLSE 249
Cdd:PLN02587 181 SLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLT--------ENGPPEWHPAPP------EL---KSACAAAATHCKEKG 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 250 QSgVSKVGLAYrwvryhsALKGELGDAMIIGANSATQFREAVK---EIENGPLEEWIVERIDELWELVKD 316
Cdd:PLN02587 243 KN-ISKLALQY-------SLSNKDISTTLVGMNSVQQVEENVAaatELETSGIDEELLSEVEAILAPVKN 304
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
25-202 |
3.23e-04 |
|
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: 41.77 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 25 SEATQDEVVAImqEHGITNLDTARSYGmgaSEETIGNKNLG-----AEFSVWTKAPTGLGGGAGKRENIleqgRKSNVVL 99
Cdd:cd19134 24 DEAERSVSAAL--EAGYRLIDTAAAYG---NEAAVGRAIAAsgiprGELFVTTKLATPDQGFTASQAAC----RASLERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 100 RLSKIPVYLLH--APDESVPVaETLGAIQTLYEEGRFEKFGLSNMSRdqvlEHYNYAKSQNFILPTVYQasysivvrgIE 177
Cdd:cd19134 95 GLDYVDLYLIHwpAGREGKYV-DSWGGLMKLREEGLARSIGVSNFTA----EHLENLIDLTFFTPAVNQ---------IE 160
|
170 180 190
....*....|....*....|....*....|..
gi 995934143 178 TNLLSTLREL-------GISIQAYSPLAAGFL 202
Cdd:cd19134 161 LHPLLNQAELrkvnaqhGIVTQAYSPLGVGRL 192
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-288 |
3.41e-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: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVPTPkSEATQDEVVAIMQehGITNLDTARSYGmgaSEETIGN------KNLGA---EFSVWTKA-PTGLgggagK 84
Cdd:cd19128 5 GFGTYKITE-SESKEAVKNAIKA--GYRHIDCAYYYG---NEAFIGIafseifKDGGVkreDLFITSKLwPTMH-----Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAP-------------------DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRD 145
Cdd:cd19128 74 PENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 146 QVLEHYNYAKsqnfILPTVYQASYSIVVRgiETNLLSTLRELGISIQAYSPLAagflsktveqiengnGTERWDPNSPYG 225
Cdd:cd19128 154 LLTDLLNYCK----IKPFMNQIECHPYFQ--NDKLIKFCIENNIHVTAYRPLG---------------GSYGDGNLTFLN 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995934143 226 MvnrqlyfkPSYMKMLTEYGKlseqsGVSKVGLAYRWVRYhsalkgeLGDAMIIgANSATQFR 288
Cdd:cd19128 213 D--------SELKALATKYNT-----TPPQVIIAWHLQKW-------PKNYSVI-PKSANKSR 254
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
85-319 |
5.72e-04 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 41.38 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 85 RENILEQGRKSNVVLRLSKIPVYLLHAPD--------------ESVPVA---ETLGAIQTLYEEGRFEKFGLSNMSRDQV 147
Cdd:PRK10625 107 RKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtDSAPAVsllETLDALAEQQRAGKIRYIGVSNETAFGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 148 LEHYNYAKSQNfiLPTVY--QASYSIVVRGIETNLLSTLRELGISIQAYSPLAAGFLS-KTVeqiengNGTERWDP-NSP 223
Cdd:PRK10625 187 MRYLHLAEKHD--LPRIVtiQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTgKYL------NGAKPAGArNTL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 224 YGMVNRqlYFKPSYMKMLTEYGKLSEQSGVSKVGLAYRWVRYHSALKGELgdamiIGANSATQFREAVkEIENGPLEEWI 303
Cdd:PRK10625 259 FSRFTR--YSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTL-----LGATTMEQLKTNI-ESLHLTLSEEV 330
|
250
....*....|....*.
gi 995934143 304 VERIDELWELVKDDAP 319
Cdd:PRK10625 331 LAEIEAVHQVYTYPAP 346
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
18-202 |
6.24e-04 |
|
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: 41.11 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 18 TWVPTPKSEATQDEVVAImqEHGITNLDTARSYG----MG-ASEETIGNKNLG-AEFSVWTKaptgLGGGAGKRENILEQ 91
Cdd:cd19116 18 TWKLKDDEGVRQAVKHAI--EAGYRHIDTAYLYGneaeVGeAIREKIAEGVVKrEDLFITTK----LWNSYHEREQVEPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 92 GRKSNVVLRLSKIPVYLLHAP----------------DESVPVAETLGAIQTLYEEGRFEKFGLSNMSRDQVLEHYNYAK 155
Cdd:cd19116 92 LRESLKRLGLDYVDLYLIHWPvafkenndsesngdgsLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 995934143 156 sqnfILPTVYQasysivvrgIETN-------LLSTLRELGISIQAYSPLaaGFL 202
Cdd:cd19116 172 ----IKPAVNQ---------IEVHptltqekLVAYCQSNGIVVMAYSPF--GRL 210
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
15-197 |
1.08e-03 |
|
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: 40.02 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 15 GTHTWVPTPKSeaTQDEVVAIMQEhGITNLDTARSYGmgaSEETIGnKNLGAEFsvwtkaptglGGGAGKRENI------ 88
Cdd:cd19125 15 GLGTWQADPGV--VGNAVKTAIKE-GYRHIDCAAIYG---NEKEIG-KALKKLF----------EDGVVKREDLfitskl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 89 -------------LEQGRKSnvvLRLSKIPVYLLHAP--------------DESVPVAETLGAIQTLYEEGRFEKFGLSN 141
Cdd:cd19125 78 wctdhapedvppaLEKTLKD---LQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 995934143 142 MSRDQVLEHYNYAKsqnfILPTVYQASYSIVVRgiETNLLSTLRELGISIQAYSPL 197
Cdd:cd19125 155 FSVKKLEDLLAVAR----VPPAVNQVECHPGWQ--QDKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-220 |
1.95e-03 |
|
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: 39.61 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 25 SEATQDEVVAIMQE---HGITNLDTARSYGMGASEETIGN--KNLGA-------EFSVWTKA---PTGLGGGAGKRENIL 89
Cdd:cd19099 16 DDETDEEYREALKAaldSGINVIDTAINYRGGRSERLIGKalRELIEkggikrdEVVIVTKAgyiPGDGDEPLRPLKYLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 90 EQGRKSNVV--------------------------LRLSKIPVYLLHAPDESVPVA------ETLGAIQTLYE----EGR 133
Cdd:cd19099 96 EKLGRGLIDvadsaglrhcispayledqierslkrLGLDTIDLYLLHNPEEQLLELgeeefyDRLEEAFEALEeavaEGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 134 FEKFGLS--NMSR-----DQVL---------------EH--------YNYAKSQNFILPTVYQASYsivvrgieTNLLST 183
Cdd:cd19099 176 IRYYGIStwDGFRappalPGHLsleklvaaaeevggdNHhfkviqlpLNLLEPEALTEKNTVKGEA--------LSLLEA 247
|
250 260 270
....*....|....*....|....*....|....*..
gi 995934143 184 LRELGISIQAYSPLAAGFLSKTVEQIENGNGTERWDP 220
Cdd:cd19099 248 AKELGLGVIASRPLNQGQLLGELRLADLLALPGGATL 284
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
3-170 |
2.84e-03 |
|
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: 38.80 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 3 APSFKTLVALAGGTHT----WVPTPKSEATQDeVVAIMQEHGITNLDTARSYgmGASEETIGN--KNLGAEFS-----VW 71
Cdd:cd19164 7 ALSLAGLPPLIFGAATfsyqYTTDPESIPPVD-IVRRALELGIRAFDTSPYY--GPSEIILGRalKALRDEFPrdtyfII 83
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995934143 72 TKAptglGGGAGK-----RENILEQGRKSNVVLRLSKIPVYLLHapD-ESVPVAETLGAIQTLYE---EGRFEKFGLSNM 142
Cdd:cd19164 84 TKV----GRYGPDdfdysPEWIRASVERSLRRLHTDYLDLVYLH--DvEFVADEEVLEALKELFKlkdEGKIRNVGISGY 157
|
170 180
....*....|....*....|....*...
gi 995934143 143 SRDQVLEHYNYAKSQnFILPTVYQASYS 170
Cdd:cd19164 158 PLPVLLRLAELARTT-AGRPLDAVLSYC 184
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