|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
20-338 |
0e+00 |
|
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: 688.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 20 VLSKTAGIRVSPLILGGASIGDAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLRDQIV 99
Cdd:cd19147 1 VLSKTAGIRVSPLILGAMSIGDAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 100 IATKFTGDYKKYEVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLG 179
Cdd:cd19147 81 IATKFTTDYKAYEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 180 VSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGL 259
Cdd:cd19147 161 VSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 260 RTFVGGPEQTELEVKISEALTKIAEEHGTESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19147 241 RSFVGGTEQTPEEVKISEALEKVAEEHGTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
19-352 |
0e+00 |
|
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: 510.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTAGIRVSPLILGGASIGDAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLRDQI 98
Cdd:cd19146 1 RQLSPTAGVRVSPLCLGAMSFGEAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKFTGDYKKYEVGGGKSaNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYL 178
Cdd:cd19146 81 VLATKYTTGYRRGGPIKIKS-NYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 179 GVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKkamEERKKNGEG 258
Cdd:cd19146 160 GVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFRTE---EEFKRRGRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 259 LRTfvGGPeQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19146 237 GRK--GGP-QTEKERKVSEKLEKVAEEKGT-AITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIE 312
|
330
....*....|....
gi 2360743992 339 GIVPFDVGFPKSLI 352
Cdd:cd19146 313 DAYPFDVGFPMNFL 326
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
21-338 |
2.07e-160 |
|
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: 452.06 E-value: 2.07e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 21 LSKTAGIRVSPLILGGASIGDAWSGfmgSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRklRDQIVI 100
Cdd:cd19080 2 LLGRSGLRVSPLALGTMTFGTEWGW---GADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN--RDRIVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 101 ATKFTGDYKKyevgggKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGV 180
Cdd:cd19080 77 ATKYTMNRRP------GDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 181 SDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLR 260
Cdd:cd19080 151 SDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2360743992 261 TFVGGPEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19080 231 VTVGFGKLTERNWAIVDVVAAVAEELGR-SAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
19-342 |
6.80e-94 |
|
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: 283.22 E-value: 6.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGDAWsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQI 98
Cdd:COG0667 4 RRLGRS-GLKVSRLGLGTMTFGGPW----GGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRP-RDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKFTGDYkkyevggGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYL 178
Cdd:COG0667 78 VIATKVGRRM-------GPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 179 GVSDTPAWVVSAANyyATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEG 258
Cdd:COG0667 151 GVSNYSAEQLRRAL--AIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 259 LRTFVGGPEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:COG0667 229 AATNFVQGYLTERNLALVDALRAIAAEHGV-TPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALD 307
|
....
gi 2360743992 339 GIVP 342
Cdd:COG0667 308 AALA 311
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
32-341 |
8.24e-87 |
|
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: 264.17 E-value: 8.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 32 LILGGASIGDAWsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKL-RDQIVIATKftgdykk 110
Cdd:pfam00248 1 IGLGTWQLGGGW----GPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVkRDKVVIATK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 111 yeVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSa 190
Cdd:pfam00248 70 --VPDGDGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIE- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 191 anyYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFvggPEQTE 270
Cdd:pfam00248 147 ---KALTKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLL---KKGTP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2360743992 271 LEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLEGIV 341
Cdd:pfam00248 221 LNLEALEALEEIAKEHG-VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
21-338 |
2.46e-84 |
|
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: 258.67 E-value: 2.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 21 LSKTaGIRVSPLILGGASIGD-AWSGFMgsMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLRDQIV 99
Cdd:cd19079 5 LGNS-GLKVSRLCLGCMSFGDpKWRPWV--LDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 100 IATKFTGDykkyevgGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLG 179
Cdd:cd19079 82 IATKVYFP-------MGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 180 VSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGL 259
Cdd:cd19079 155 ASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTD 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 260 RTFVGGPEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19079 235 TAKLKYDYFTEADKEIVDRVEEVAKERGV-SMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
30-323 |
7.02e-81 |
|
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: 247.05 E-value: 7.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGdawsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLRDQIVIATKFTGDYk 109
Cdd:cd06660 1 SRLGLGTMTFG-------GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDDVVIATKGGHPP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 110 kyevggGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVS 189
Cdd:cd06660 73 ------GGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 190 AANYYATSHGKTPFSVYQGKWNVLNRDF-ERDIIPMARHFGMALAPWDVMGGGrfqskkameerkkngeglrtfvggpeq 268
Cdd:cd06660 147 EALAYAKAHGLPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG--------------------------- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2360743992 269 televkisealtkiaeehgtesVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIE 323
Cdd:cd06660 200 ----------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
23-337 |
4.73e-78 |
|
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: 242.51 E-value: 4.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 23 KTAGIRVSPLILGGasigdawSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSY-------QNEESEIWIGEWMASRKLR 95
Cdd:cd19081 3 GRTGLSVSPLCLGT-------MVFGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLKSRGKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 96 DQIVIATKftgdykkyeVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKV 175
Cdd:cd19081 76 DRVVIATK---------VGFPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 176 LYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGG----GRFQSKKAME 250
Cdd:cd19081 147 RYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGgfltGKYRSEADLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 251 ERKKNGEGLRTFVggpeqTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLT 330
Cdd:cd19081 227 GSTRRGEAAKRYL-----NERGLRILDALDEVAAEHGA-TPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLT 300
|
....*..
gi 2360743992 331 PEQIEYL 337
Cdd:cd19081 301 DEEVARL 307
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
17-338 |
1.51e-77 |
|
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: 241.75 E-value: 1.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 17 RLRVLSKTaGIRVSPLILGGASIG--DAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKL 94
Cdd:cd19091 2 EYRTLGRS-GLKVSELALGTMTFGggGGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGK--ALKGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 95 RDQIVIATKFTGdykkyEVGGGksANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGK 174
Cdd:cd19091 79 RDDVLIATKVRG-----RMGEG--PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 175 VLYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKK 254
Cdd:cd19091 152 VRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 255 NGEGLRTFVGGPEQTELE--VKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPE 332
Cdd:cd19091 232 EGSRLRRTGFDFPPVDRErgYDVVDALREIAKETGA-TPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPE 310
|
....*.
gi 2360743992 333 QIEYLE 338
Cdd:cd19091 311 EIARLD 316
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
19-342 |
3.80e-72 |
|
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: 227.46 E-value: 3.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGdawsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRklRDQI 98
Cdd:cd19087 4 RTLGRT-GLKVSRLCLGTMNFG-------GRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR--RDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKFTGDYkkyevggGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYL 178
Cdd:cd19087 74 VLATKVFGPM-------GDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 179 GVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEG 258
Cdd:cd19087 147 GVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 259 L-RTFVGGPEQTELEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYL 337
Cdd:cd19087 227 VeRARYQARYGLEEYRDIAERFEALAAEAG-LTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEI 305
|
....*
gi 2360743992 338 EGIVP 342
Cdd:cd19087 306 DELFP 310
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
30-326 |
5.92e-64 |
|
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: 205.86 E-value: 5.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGDAWSgfmgsmnKEQAFELLDAFYEAGGNCIDTANSYQNEE----SEIWIGEWMASRKLRDQIVIATKft 105
Cdd:cd19082 1 SRIVLGTADFGTRID-------EEEAFALLDAFVELGGNFIDTARVYGDWVergaSERVIGEWLKSRGNRDKVVIATK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 gdykkyevGG-----GKSANYCgnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGV 180
Cdd:cd19082 72 --------GGhpdleDMSRSRL--SPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 181 SDtpaWV---VSAANYYATSHGKTPFSVYQGKWN--VLNRDFERD--IIPM---ARHF----GMALAPWDVMGGGRFqSK 246
Cdd:cd19082 142 SN---WSterIAEANAYAKAHGLPGFAASSPQWSlaRPNEPPWPGptLVAMdeeMRAWheenQLPVFAYSSQARGFF-SK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 247 KAMEERKKNGEGLRTFvggpeQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALS 326
Cdd:cd19082 218 RAAGGAEDDSELRRVY-----YSEENFERLERAKELAEEKGV-SPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
26-338 |
1.01e-60 |
|
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: 197.36 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGDAWSGfmgSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKLRDQIVIATKFt 105
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWWG---EVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGK--ALKGRRDDVVIATKC- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 gdykkYEVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPA 185
Cdd:cd19084 75 -----GLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 186 WVVSAANYYAtshgktPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGG----RFQSK---KAMEERKKNgeg 258
Cdd:cd19084 150 EQLEEARKYG------PIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGlltgKYKKEptfPPDDRRSRF--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 259 lRTFVGgpEQTELEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19084 221 -PFFRG--ENFEKNLEIVDKLKEIAEKYG-KSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
29-332 |
1.00e-56 |
|
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: 188.16 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 29 VSPLILGGASIGdawsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSY---QNEE----SEIWIGEWMASRKLRDQIVIA 101
Cdd:cd19094 1 VSEICLGTMTWG-------EQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvpPSPEtqgrTEEIIGSWLKKKGNRDKVVLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 102 TKFTGDYKKYEVGGGKSANYCGNHKRSlhvSVRDSLRKLQTDWIDILYVHWWD-----------------YMS-SIEEVM 163
Cdd:cd19094 74 TKVAGPGEGITWPRGGGTRLDRENIRE---AVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeEDSvSFEEQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 164 DSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrF 243
Cdd:cd19094 151 EALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGG-V 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 244 QSKKAMEERKKNGEGLRTFVGGPEQ---TELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQ 320
Cdd:cd19094 230 LTGKYLDGAARPEGGRLNLFPGYMAryrSPQALEAVAEYVKLARKHGL-SPAQLALAWVRSRPFVTSTIIGATTLEQLKE 308
|
330
....*....|..
gi 2360743992 321 NIEALSIKLTPE 332
Cdd:cd19094 309 NIDAFDVPLSDE 320
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
26-332 |
3.43e-48 |
|
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: 165.07 E-value: 3.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQIVIATKFT 105
Cdd:cd19074 1 GLKVSELSLG------TWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWP-RESYVISTKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 GdykkyevGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPA 185
Cdd:cd19074 74 W-------PTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 186 WVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGG----RFQSKKAMEER-KKNGEGLR 260
Cdd:cd19074 147 EQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGlltgKYRDGIPPPSRsRATDEDNR 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2360743992 261 TFVGGPEQTELEVKIsEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPE 332
Cdd:cd19074 227 DKKRRLLTDENLEKV-KKLKPIADELGL-TLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
29-340 |
3.07e-47 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 162.37 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 29 VSPLILGGASIGDAWSGfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKLRDQIVIATKFTGDY 108
Cdd:cd19085 1 VSRLGLGCWQFGGGYWW--GDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGK--ALKGRRDDVVIATKVSPDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 109 KKYEvgggksanycgnhkrSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWvv 188
Cdd:cd19085 77 LTPE---------------DVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPA-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 189 saanYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMG----GGRFQSKKAMEE---RKKNgegLRT 261
Cdd:cd19085 140 ----QLEEALDAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAqgllTGKFSSAEDFPPgdaRTRL---FRH 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 262 FVGGPEQTELEVkiSEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLEGI 340
Cdd:cd19085 213 FEPGAEEETFEA--LEKLKEIADELGV-TMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-337 |
4.07e-46 |
|
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: 159.69 E-value: 4.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 17 RLRVLSKTaGIRVSPLILGGASIgdawSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRklRD 96
Cdd:cd19076 1 PTRKLGTQ-GLEVSALGLGCMGM----SAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDR--RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 97 QIVIATKFTgdykkYEVGGGKSANycGNHKRSLHV--SVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGK 174
Cdd:cd19076 74 EVVIATKFG-----IVRDPGSGFR--GVDGRPEYVraACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 175 VLYLGVSDtpawvvSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKK 254
Cdd:cd19076 147 VRYIGLSE------ASADTIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 255 NGEGLRT---FVGgpEQTELEVKISEALTKIAEEHGtesVTA--IAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKL 329
Cdd:cd19076 221 EDDFRRNnprFQG--ENFDKNLKLVEKLEAIAAEKG---CTPaqLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVL 295
|
....*...
gi 2360743992 330 TPEQIEYL 337
Cdd:cd19076 296 TPEELAEI 303
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
47-326 |
1.36e-44 |
|
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: 155.57 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 47 MGS-MNKEQAFELLDAFYEAGGNCIDTANSY-------QNEESEIWIGEWMASRKLRDQIVIATKFTGDYKKYevgGGKS 118
Cdd:cd19752 10 FGTrTDEETSFAILDRYVAAGGNFLDTANNYafwteggVGGESERLIGRWLKDRGNRDDVVIATKVGAGPRDP---DGGP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 119 ANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSH 198
Cdd:cd19752 87 ESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 199 GKTPFSVYQGKWNVL----NRDF------ERDIIPMAR-HFGMALAPWDVMGGGRFqSKKAMEERKkngeglrtfvggPE 267
Cdd:cd19752 167 GWAEFSAIQQRHSYLrprpGADFgvqrivTDELLDYASsRPDLTLLAYSPLLSGAY-TRPDRPLPE------------QY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2360743992 268 QTELEVKISEALTKIAEEHGtesVTA--IAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALS 326
Cdd:cd19752 234 DGPDSDARLAVLEEVAGELG---ATPnqVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
19-338 |
1.33e-43 |
|
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: 153.58 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGdAWSgFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKLRDQI 98
Cdd:cd19149 2 RKLGKS-GIEASVIGLGTWAIG-GGP-WWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGK--AIKGRRDKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKF-----TGDYKKYEVGGGKSANYCGNhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQG 173
Cdd:cd19149 77 VLATKCglrwdREGGSFFFVRDGVTVYKNLS-PESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 174 KVLYLGVSDTPAWVVSAANYYAtshgktPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERK 253
Cdd:cd19149 156 KIRAIGASNVSVEQIKEYVKAG------QLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQG-LLTGKITPDRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 254 KNGEGLRTFVG--GPEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTP 331
Cdd:cd19149 229 FDAGDARSGIPwfSPENREKVLALLEKWKPLCEKYGC-TLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSA 307
|
....*..
gi 2360743992 332 EQIEYLE 338
Cdd:cd19149 308 EDIATMR 314
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
28-338 |
1.10e-41 |
|
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: 147.76 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 28 RVSPLILGGASIGDAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLRDQIVIATKFTGD 107
Cdd:cd19093 1 EVSPLGLGTWQWGDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 108 YKKyevgggksanycgNHKRSLHVSVRDSLRKLQTDWIDILYVHW-WDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAW 186
Cdd:cd19093 81 PWR-------------LTRRSVVKALKASLERLGLDSIDLYQLHWpGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 187 VVSAANYYATSHGkTPFSVYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGG 265
Cdd:cd19093 148 QLRRAHKALKERG-VPLASNQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2360743992 266 PEQTElevKISEALTKIAEEHGtESVTAIAIAYVRskAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19093 227 LEKVQ---PLLDALEEIAEKYG-KTPAQVALNWLI--AKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-337 |
2.10e-41 |
|
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: 147.58 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTAGIRVSPLILGGASIgdawSGFMGSMNKEQ-AFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASrKLRDQ 97
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGL----SGDYGAPKPEEeGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKD-GPREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 98 IVIATKF---TGDYKKYEVGGgkSANYcgnhkrslhvsVR----DSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILV 170
Cdd:cd19145 77 VQLATKFgihEIGGSGVEVRG--DPAY-----------VRaaceASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 171 QQGKVLYLGVSDTPAWVVSAAnyyatsHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAME 250
Cdd:cd19145 144 EEGKIKYIGLSEASADTIRRA------HAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 251 ERKKNGEGLRT---FVGgpEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSI 327
Cdd:cd19145 218 ELLENSDVRKShprFQG--ENLEKNKVLYERVEALAKKKGC-TPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSV 294
|
330
....*....|
gi 2360743992 328 KLTPEQIEYL 337
Cdd:cd19145 295 KLTKEDLKEI 304
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
26-333 |
5.24e-40 |
|
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: 143.08 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGDAWsgfmgsMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRK-LRDQIVIATKf 104
Cdd:cd19092 3 GLEVSRLVLGCMRLADWG------ESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPgLREKIEIQTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 105 TGDYKKYEVGGGKSANYCGNHKRSLHvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTP 184
Cdd:cd19092 76 CGIRLGDDPRPGRIKHYDTSKEHILA-SVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 185 AWVVSAANyyatSHGKTPFSVYQGKWNVLNRDF----------ERDIIPMArhfgmalapWDVMGGGRFQSkkameerkk 254
Cdd:cd19092 155 PSQIELLQ----SYLDQPLVTNQIELSLLHTEAiddgtldycqLLDITPMA---------WSPLGGGRLFG--------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 255 ngeglrtfvggpEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQ 333
Cdd:cd19092 213 ------------GFDERFQRLRAALEELAEEYGV-TIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
26-338 |
2.19e-39 |
|
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: 141.99 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGDAWSGFMgsmNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKLRDQIVIATKF- 104
Cdd:cd19078 1 GLEVSAIGLGCMGMSHGYGPPP---DKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGE--ALKPFRDQVVIATKFg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 105 -TGDYKKYEVGGGKSANycgNHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDT 183
Cdd:cd19078 76 fKIDGGKPGPLGLDSRP---EHIRK---AVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 184 pawvvsAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEGLRTFV 263
Cdd:cd19078 150 ------GVETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKG-FLTGKIDENTKFDEGDDRASL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2360743992 264 G--GPEQTELEVKISEALTKIAEEHGTESVtAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19078 223 PrfTPEALEANQALVDLLKEFAEEKGATPA-QIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
19-340 |
2.63e-39 |
|
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: 142.35 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKL---R 95
Cdd:cd19143 4 RRLGRS-GLKVSALSFG------SWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQ--AIKELgwpR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 96 DQIVIATK-FTGdykkyevGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGK 174
Cdd:cd19143 75 SDYVVSTKiFWG-------GGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 175 VLYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRD-FERDIIPMARHFGMALAPW--------------DVMG 239
Cdd:cd19143 148 AFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWsplasglltgkynnGIPE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 240 GGRFqskkAMEerkkNGEGLRTFVGGPEQTELEVkiSEALTKIAEEHGTeSVTAIAIAYVrSKAKNVFPLI-GGRKIEHL 318
Cdd:cd19143 228 GSRL----ALP----GYEWLKDRKEELGQEKIEK--VRKLKPIAEELGC-SLAQLAIAWC-LKNPNVSTVItGATKVEQL 295
|
330 340
....*....|....*....|....
gi 2360743992 319 KQNIEALSI--KLTPEQIEYLEGI 340
Cdd:cd19143 296 EENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
26-338 |
7.58e-39 |
|
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: 139.29 E-value: 7.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGDAWSGFMGsmNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQIVIATKFT 105
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYS--DDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFD-REDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 GDYKKYEvgggksanycgnhkrSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPA 185
Cdd:cd19072 78 PDHLKYD---------------DVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 186 WVVSAANYYAtshGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAmeerkkngeglrtfvgg 265
Cdd:cd19072 143 EELEEAQSYL---KKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG----------------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2360743992 266 peqtelevkiSEALTKIAEEHGtESVTAIAIAYVRSKaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19072 203 ----------SPLLDEIAKKYG-KTPAQIALNWLISK-PNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
19-333 |
1.35e-38 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 139.90 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTAGIRVSPLILGGASIGDAwsgfmgSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRK-LRDQ 97
Cdd:COG4989 3 RIKLGASGLSVSRIVLGCMRLGEW------DLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPsLREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 98 IVIATK----FTGDYKKYEVgggKSANYCGNHkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQG 173
Cdd:COG4989 77 IELQTKcgirLPSEARDNRV---KHYDTSKEH---IIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 174 KVLYLGVSDTPAWVVSAANyyatSHGKTPFSVYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGGGRFQSkkameer 252
Cdd:COG4989 151 KVRHFGVSNFTPSQFELLQ----SALDQPLVTNQIELSLLHTDaFDDGTLDYCQLNGITPMAWSPLAGGRLFG------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 253 kkngeglrtfvggpEQTELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPE 332
Cdd:COG4989 220 --------------GFDEQFPRLRAALDELAEKYGV-SPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTRE 284
|
.
gi 2360743992 333 Q 333
Cdd:COG4989 285 E 285
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
32-326 |
2.09e-37 |
|
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: 136.92 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 32 LILGGASIGdaWSGfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlrdQIVIATKFTGDYKky 111
Cdd:cd19075 3 IILGTMTFG--SQG--RFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGER---GFKIDTKANPGVG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 112 evgggksanycGNHKR-SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSA 190
Cdd:cd19075 74 -----------GGLSPeNVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 191 ANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEG-----------L 259
Cdd:cd19075 143 IVEICKENGWVLPTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGG-FLTGKYKYSEDKAGGGrfdpnnalgklY 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2360743992 260 RTFVGGPEQTELevkiSEALTKIAEEHGtESVTAIAIAYVR-----SKAKNVFPLIGGRKIEHLKQNIEALS 326
Cdd:cd19075 222 RDRYWKPSYFEA----LEKVEEAAEKEG-ISLAEAALRWLYhhsalDGEKGDGVILGASSLEQLEENLAALE 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
19-334 |
2.89e-34 |
|
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: 128.53 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEE--SEIWIGEWMAS--RKL 94
Cdd:cd19089 2 RRCGRS-GLHLPAISLG------LWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPgsAEENFGRILKRdlRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 95 RDQIVIATKfTGdykkYEVGGGKSANYcGNHKRsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGK 174
Cdd:cd19089 75 RDELVISTK-AG----YGMWPGPYGDG-GSRKY-LLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 175 VLYLGVSDTPAWVVSAANYYATSHGkTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK-----KAM 249
Cdd:cd19089 148 ALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKylngiPPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 250 EERKKNGEGLRTfvggPEQTELEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEAL-SIK 328
Cdd:cd19089 227 SRRAAESKFLTE----EALTPEKLEQLRKLNKIAAKRG-QSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkNLD 301
|
....*.
gi 2360743992 329 LTPEQI 334
Cdd:cd19089 302 FSEEEL 307
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
27-232 |
2.87e-33 |
|
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: 123.74 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 27 IRVSPLILGGASIGdawSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRklRDQIVIATKFtG 106
Cdd:cd19086 1 LEVSEIGFGTWGLG---GDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGR--RDKVVIATKF-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 107 dYKKYEvGGGKSANYCGNHKRSlhvSVRDSLRKLQTDWIDILYVH-WWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPA 185
Cdd:cd19086 75 -NRFDG-GPERPQDFSPEYIRE---AVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2360743992 186 WVVSAANyyatSHGKtpFSVYQGKWNVLNRDFERDIIPMARHFGMAL 232
Cdd:cd19086 150 EEALAAL----RRGG--IDVVQVIYNLLDQRPEEELFPLAEEHGVGV 190
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-341 |
4.58e-33 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 125.09 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 29 VSPLILGGASIGDA-WSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKLRDQIVIATK--FT 105
Cdd:cd19102 1 LTTIGLGTWAIGGGgWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGR--ALKGLRDRPIVATKcgLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 GDYKKYEVGGGKSAnycgnhkrSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPA 185
Cdd:cd19102 79 WDEEGRIRRSLKPA--------SIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 186 WVVSAAnyyATSHgktPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFqSKKAMEERKKNGEGLRTFVGG 265
Cdd:cd19102 151 DQMKRC---QAIH---PIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLL-TGKMTPERVASLPADDWRRRS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 266 PEQTELE----VKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLEGIV 341
Cdd:cd19102 224 PFFQEPNlarnLALVDALRPIAERHGR-TVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
26-341 |
1.09e-32 |
|
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: 123.96 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGdawsGFM-GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLRDQIVIATKF 104
Cdd:cd19148 1 DLPVSRIALGTWAIG----GWMwGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDRVVIATKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 105 TGDYKKyevGGGKSANycgNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSdtp 184
Cdd:cd19148 77 GLEWDE---GGEVVRN---SSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVS--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 185 awvvsaaNY----YATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEGLR 260
Cdd:cd19148 148 -------NFspeqMETFRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRG-LLSGKMTKDTKFEGDDLR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 261 TFVGGPEQTELEVKIS--EALTKIAEEHGTESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19148 220 RTDPKFQEPRFSQYLAavEELDKLAQERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
...
gi 2360743992 339 GIV 341
Cdd:cd19148 300 AIL 302
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-341 |
4.12e-32 |
|
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: 122.53 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGDawSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQI 98
Cdd:cd19083 2 VKLGKS-DIDVNPIGLGTNAVGG--HNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYN-RNEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKftGDYKkyEVGGGKSANycgNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYL 178
Cdd:cd19083 78 VIATK--GAHK--FGGDGSVLN---NSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 179 GVSDTPAWVVSAANyyatshGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEG 258
Cdd:cd19083 151 GVSNFSLEQLKEAN------KDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASG-LLAGKYTKDTKFPDND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 259 LRT----FVGgpEQTELEVKISEALTKIAEEHGTEsVTAIAIAYVRSKaknvfPLI-----GGRKIEHLKQNIEALSIKL 329
Cdd:cd19083 224 LRNdkplFKG--ERFSENLDKVDKLKSIADEKGVT-VAHLALAWYLTR-----PAIdvvipGAKRAEQVIDNLKALDVTL 295
|
330
....*....|..
gi 2360743992 330 TPEQIEYLEGIV 341
Cdd:cd19083 296 TEEEIAFIDALF 307
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-341 |
1.26e-31 |
|
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: 121.78 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 11 PPTELGRlrvlsktAGIRVSPLILGGASIGdawSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIwiGEWMA 90
Cdd:cd19144 2 PTRTLGR-------NGPSVPALGFGAMGLS---AFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGDSEELI--GRWFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 91 -SRKLRDQIVIATKFTgdYKKYEVGGGKSAN----YCGNhkrslhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDS 165
Cdd:cd19144 70 qNPGKREKIFLATKFG--IEKNVETGEYSVDgspeYVKK-------ACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 166 LHILVQQGKVLYLGVSDTPAWVVSAAnyyatsHGKTPFSVYQGKWNVLNRDFER---DIIPMARHFGMALAPWDVMG--- 239
Cdd:cd19144 141 MAELVQEGKIKHIGLSECSAETLRRA------HAVHPIAAVQIEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGrgf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 240 -GGRFQSKKAMEERKkngegLRTFVG--GPEQTELEVKISEALTKIAEEHGtesVTA--IAIAYVRSKAKNVFPLIGGRK 314
Cdd:cd19144 215 lTGAIRSPDDFEEGD-----FRRMAPrfQAENFPKNLELVDKIKAIAKKKN---VTAgqLTLAWLLAQGDDIIPIPGTTK 286
|
330 340
....*....|....*....|....*..
gi 2360743992 315 IEHLKQNIEALSIKLTPEQIEYLEGIV 341
Cdd:cd19144 287 LKRLEENLGALKVKLTEEEEKEIREIA 313
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
30-324 |
2.33e-31 |
|
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: 119.26 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGDAWsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGEWMASRkLRDQIVIATKF-TGDy 108
Cdd:cd19095 1 SVLGLGTSGIGRVW----GVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALAGL-RRDDLFIATKVgTHG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 109 kkyeVGGGKSANYCGNHKRSlhvSVRDSLRKLQTDWIDILYVH----WWDYmssiEEVMDSLHILVQQGKVLYLGVS-DT 183
Cdd:cd19095 73 ----EGGRDRKDFSPAAIRA---SIERSLRRLGTDYIDLLQLHgpsdDELT----GEVLETLEDLKAAGKVRYIGVSgDG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 184 PawvvsAANYYATSHgktPFSVYQGKWNVLNRDfERDIIPMARHFGMAlapwdVMGGGRFqskkameerkKNGEGLRTFV 263
Cdd:cd19095 142 E-----ELEAAIASG---VFDVVQLPYNVLDRE-EEELLPLAAEAGLG-----VIVNRPL----------ANGRLRRRVR 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2360743992 264 GGPEQTELevkisEALTKIAEEHGTESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEA 324
Cdd:cd19095 198 RRPLYADY-----ARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-323 |
1.06e-30 |
|
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: 117.20 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGDawsgfmgsMNKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGEWMASRklRDQI 98
Cdd:cd19100 2 RRLGRT-GLKVSRLGFGGGPLGR--------LSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKGR--RDKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKfTGDYKKYEVgggksanycgnhKRSLHvsvrDSLRKLQTDWIDILYVH------WWDYMSSIEEVMDSLHILVQQ 172
Cdd:cd19100 69 FLATK-TGARDYEGA------------KRDLE----RSLKRLGTDYIDLYQLHavdteeDLDQVFGPGGALEALLEAKEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 173 GKVLYLGVSD-TPAWVVSAANYYatshgktPFSVYQGKWNVL---NRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKA 248
Cdd:cd19100 132 GKIRFIGISGhSPEVLLRALETG-------EFDVVLFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDP 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2360743992 249 MEerkkngeglrtfvggPEQtelevkisealtkiaeehgtesvtaiAIAYVRSKAKNVFPLIGGRKIEHLKQNIE 323
Cdd:cd19100 205 LD---------------PEQ--------------------------ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
29-330 |
2.87e-29 |
|
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: 113.85 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 29 VSPLILGGASIgdAWSGFMG-SMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRklRDQIVIATKftgd 107
Cdd:cd19088 1 VSRLGYGAMRL--TGPGIWGpPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPY--PDDVVIATK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 108 ykkyeVG----GGKSANYCGnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDt 183
Cdd:cd19088 73 -----GGlvrtGPGWWGPDG-SPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSN- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 184 pawvVSAANyYATSHGKTPFSVYQGKWNVLNRDFErDIIPMARHFGMALAPWDVMGGGRfqskKAMEERKkngeglrtfv 263
Cdd:cd19088 146 ----VTVAQ-IEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGD----LAQPGGL---------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2360743992 264 ggpeqtelevkiseaLTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLT 330
Cdd:cd19088 206 ---------------LAEVAARLGA-TPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
30-332 |
5.90e-29 |
|
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: 113.42 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGDAWSGFMgsmnKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGEWMASRKlRDQIVIATKftgdyk 109
Cdd:cd19090 1 SALGLGTAGLGGVFGGVD----DDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAELP-REPLVLSTK------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 110 kyeVGGGKSANYCGNHKRsLHVSVRDSLRKLQTDWIDILYVH------WWDYMsSIEEVMDSLHILVQQGKVLYLGVSDT 183
Cdd:cd19090 68 ---VGRLPEDTADYSADR-VRRSVEESLERLGRDRIDLLMIHdpervpWVDIL-APGGALEALLELKEEGLIKHIGLGGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 184 PAwvvsAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMAlapwdVMGGGRFQ----SKKAMEERKKNGEGL 259
Cdd:cd19090 143 PP----DLLRRAIETGDFDVVLTANRYTLLDQSAADELLPAAARHGVG-----VINASPLGmgllAGRPPERVRYTYRWL 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2360743992 260 rtfvggpeqTELEVKISEALTKIAEEHGtESVTAIAIAYV-RSKAKNVFpLIGGRKIEHLKQNIEALSIKLTPE 332
Cdd:cd19090 214 ---------SPELLDRAKRLYELCDEHG-VPLPALALRFLlRDPRISTV-LVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-254 |
5.69e-28 |
|
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: 109.98 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGDAwsgfmgsmnkeqAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQI 98
Cdd:cd19105 4 RTLGKT-GLKVSRLGFGGGGLPRE------------SPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLR-RDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKFtgDYKKYEVGggksanycgnhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSI---EEVMDSLHILVQQGKV 175
Cdd:cd19105 70 FLATKA--SPRLDKKD-----------KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 176 LYLGVS--DTPAWVVSAAnyyatSHGKtPFSVYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSKKAMEER 252
Cdd:cd19105 137 RFIGFSthDNMAEVLQAA-----IESG-WFDVIMVAYNFLNQPAELEeALAAAAEKGIGVVAMKTLAGGYLQPALLSVLK 210
|
..
gi 2360743992 253 KK 254
Cdd:cd19105 211 AK 212
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
27-340 |
6.65e-28 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 112.25 E-value: 6.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 27 IRVSPLILGGASIGDawsgfmgsMNKE-QAFELLDAFYEAGGNCIDTANSY----QNEE---SEIWIGEWMASRKLRDQI 98
Cdd:PRK10625 11 LEVSTLGLGTMTFGE--------QNSEaDAHAQLDYAVAQGINLIDVAEMYpvppRPETqglTETYIGNWLAKRGSREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 99 VIATKFTGDYKkyevggGKSANYCGNH---KRSLHVSVRDSLRKLQTDWIDILYVHW------------WDYMSS----- 158
Cdd:PRK10625 83 IIASKVSGPSR------NNDKGIRPNQaldRKNIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgYSWTDSapavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 159 IEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVM 238
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 239 GGGRFQSK---KAMEERKKNGEGLRTFVGGPEQTELEVKiseALTKIAEEHGTESvTAIAIAYVRSKAKNVFPLIGGRKI 315
Cdd:PRK10625 237 AFGTLTGKylnGAKPAGARNTLFSRFTRYSGEQTQKAVA---AYVDIAKRHGLDP-AQMALAFVRRQPFVASTLLGATTM 312
|
330 340
....*....|....*....|....*
gi 2360743992 316 EHLKQNIEALSIKLTPEQIEYLEGI 340
Cdd:PRK10625 313 EQLKTNIESLHLTLSEEVLAEIEAV 337
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
19-338 |
3.94e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.29 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSplILGgasigdawsgfMGSM-----NKEQAFELLDAFYEAGGNCIDTANSYqnEESEIWIGEWMASRk 93
Cdd:COG1453 4 RRLGKT-GLEVS--VLG-----------FGGMrlprkDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGP- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 94 lRDQIVIATKFTGDYKKYEvgggksanycgNHKRSLHvsvrDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHIL---- 169
Cdd:COG1453 67 -RDKVILATKLPPWVRDPE-----------DMRKDLE----ESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPGGALeale 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 170 --VQQGKVLYLGVS--DTPAWVVSAANYYatshgktPFSVYQGKWNVLNRDF--ERDIIPMARHFGMALApwdVM---GG 240
Cdd:COG1453 131 kaKAEGKIRHIGFSthGSLEVIKEAIDTG-------DFDFVQLQYNYLDQDNqaGEEALEAAAEKGIGVI---IMkplKG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 241 GRFqskkameerkkngeglrtfvggpeqteleVKISEALTKIAEEhgTESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQ 320
Cdd:COG1453 201 GRL-----------------------------ANPPEKLVELLCP--PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDE 249
|
330 340
....*....|....*....|
gi 2360743992 321 NIEALS--IKLTPEQIEYLE 338
Cdd:COG1453 250 NLKTADnlEPLTEEELAILE 269
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-340 |
2.47e-24 |
|
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: 101.77 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 17 RLRVLSKTaGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKL-R 95
Cdd:cd19142 2 KYRNLGKS-GLRVSNVGLG------TWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWkR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 96 DQIVIATKFTGDYKKYEvgggksanyCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKV 175
Cdd:cd19142 75 SSYIVSTKIYWSYGSEE---------RGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 176 LYLGVSD-TPAWVVSAANYYATSHGKTPFsVYQGKWNVLNRD-FERDIIPMARHFGMALAPW--------DVMGGGRFQS 245
Cdd:cd19142 146 MYWGTSRwSPVEIMEAFSIARQFNCPTPI-CEQSEYHMFCREkMELYMPELYNKVGVGLITWsplslgldPGISEETRRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 246 KKAMEERKKNGEGLRTFVGGPEQTELEVKISEALTKIAEEHGTeSVTAIAIAY-VRSKAKNVFpLIGGRKIEHLKQNIEA 324
Cdd:cd19142 225 VTKLSFKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGC-DLTQLLIAWsLKNENVQCV-LIGASSLEQLYSQLNS 302
|
330
....*....|....*...
gi 2360743992 325 LSI--KLTPEQIEYLEGI 340
Cdd:cd19142 303 LQLlpKLNSAVMEELERI 320
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
26-338 |
3.06e-22 |
|
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: 94.56 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGdawsGFMGS--MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQIVIATK 103
Cdd:cd19137 1 GEKIPALGLGTWGIG----GFLTPdySRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP-REDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 104 FTGDYKKYEvgggksanycgnhkrSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDT 183
Cdd:cd19137 76 VWPTNLRYD---------------DLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 184 PAWVVSAANYYAtshgKTPFSVYQGKWNVLNRDFERD-IIPMARHFG---MALAPWDvmgggrfqskkameerkkngegl 259
Cdd:cd19137 141 NRRLLEEAISKS----QTPIVCNQVKYNLEDRDPERDgLLEYCQKNGitvVAYSPLR----------------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 260 RTFvggpeqteleVKISEALTKIAEEHGtESVTAIAIAYVRSKaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19137 194 RGL----------EKTNRTLEEIAKNYG-KTIAQIALAWLIQK-PNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
19-341 |
3.39e-21 |
|
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: 93.13 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLR-DQ 97
Cdd:cd19160 6 RNLGKS-GLRVSCLGLG------TWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRrSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 98 IVIATKFtgdykkyeVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLY 177
Cdd:cd19160 79 YVVTTKI--------YWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 178 LGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMGGGRFQSK------KAME 250
Cdd:cd19160 151 WGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHkIGVGSVTWSPLACGLITGKydgrvpDTCR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 251 ERKKNGEGLRTFVGGPEQTELEVKISEaLTKIAEEHGTeSVTAIAIAY-VRSKAKNVFpLIGGRKIEHLKQNIEALSI-- 327
Cdd:cd19160 231 AAVKGYQWLKEKVQSEEGKKQQAKVKE-LHPIADRLGC-TVAQLAIAWcLRSEGVSSV-LLGVSSAEQLIENLGSIQVls 307
|
330
....*....|....
gi 2360743992 328 KLTPEQIEYLEGIV 341
Cdd:cd19160 308 QLTPQTVMEIDALL 321
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
26-338 |
5.08e-21 |
|
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: 91.16 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 26 GIRVSPLILGGASIGDAwsgfMGSMNKEQafELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRklRDQIVIATKFt 105
Cdd:cd19138 8 GTKVPALGQGTWYMGED----PAKRAQEI--EALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGR--RDKVFLVSKV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 gdykkyevgggksanYCGNHKR-SLHVSVRDSLRKLQTDWIDILYVHWwdyMSSI--EEVMDSLHILVQQGKVLYLGVS- 181
Cdd:cd19138 79 ---------------LPSNASRqGTVRACERSLRRLGTDYLDLYLLHW---RGGVplAETVAAMEELKKEGKIRAWGVSn 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 182 -DTP----AWVVSAANYYATShgktpfsvyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEerkkng 256
Cdd:cd19138 141 fDTDdmeeLWAVPGGGNCAAN---------QVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLE------ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 257 eglrtfvggpeqtelevkiSEALTKIAEEHGTeSVTAIAIAYV-RSkaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIE 335
Cdd:cd19138 206 -------------------NPTLKEIAARHGA-TPAQVALAWVlRD--GNVIAIPKSGSPEHARENAAAADLELTEEDLA 263
|
...
gi 2360743992 336 YLE 338
Cdd:cd19138 264 ELD 266
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
30-326 |
5.35e-21 |
|
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: 92.08 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNE--ESEIWIGEWMAS--RKLRDQIVIATK-- 103
Cdd:cd19151 8 SGLKLPAISLG-LWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPpgSAEENFGRILKEdlKPYRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 104 FT------GDY--KKYevgggksanycgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKV 175
Cdd:cd19151 87 YTmwpgpyGDWgsKKY-----------------LIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 176 LYLGVSDTPAWVVSAANYYATSHGkTPFSVYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK--KAMEERK 253
Cdd:cd19151 150 LYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylNGIPEDS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2360743992 254 KNGEGlRTFVGGPEQTELEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALS 326
Cdd:cd19151 229 RAAKG-SSFLKPEQITEEKLAKVRRLNEIAQARG-QKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
17-331 |
1.20e-20 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 91.35 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 17 RLRVLSKTaGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKL-R 95
Cdd:cd19141 1 PYRNLGKS-GLRVSCLGLG------TWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWrR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 96 DQIVIATKFtgdykkyeVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKV 175
Cdd:cd19141 74 SSYVITTKI--------FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 176 LYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARH-FGMALAPWD-VMGG---GRFQSKKAME 250
Cdd:cd19141 146 MYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHkIGVGAMTWSpLACGilsGKYDDGVPEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 251 ERK--KNGEGLRTFVGGPEQTELEVKISEaLTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSI- 327
Cdd:cd19141 226 SRAslKGYQWLKEKILSEEGRRQQAKLKE-LQIIADRLGC-TLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVl 303
|
....*
gi 2360743992 328 -KLTP 331
Cdd:cd19141 304 pKLTP 308
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
63-335 |
1.62e-20 |
|
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: 89.25 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 63 YEAGGNCIDTANSYQNEESeiwIGEWMA-SRKLRDQIVIATKFTGDYKKYEvgggksanycgnhkrSLHVSVRDSLRKLQ 141
Cdd:cd19073 24 LELGYRHIDTAEIYNNEAE---VGEAIAeSGVPREDLFITTKVWRDHLRPE---------------DLKKSVDRSLEKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 142 TDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYyatshGKTPFSVYQ-------GKWNVL 213
Cdd:cd19073 86 TDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNfTIELLEEALDI-----SPLPIAVNQvefhpflYQAELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 214 NRDFERDIIPMARhfgMALApwdvmgggrfqskkameerkkNGEGLRtfvggpeqtelevkiSEALTKIAEEHGTESVTa 293
Cdd:cd19073 161 EYCRENDIVITAY---SPLA---------------------RGEVLR---------------DPVIQEIAEKYDKTPAQ- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2360743992 294 IAIAYVRSkaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIE 335
Cdd:cd19073 201 VALRWLVQ--KGIVVIPKASSEDHLKENLAIFDWELTSEDVA 240
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-328 |
1.74e-20 |
|
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: 89.89 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGDA--WSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYqnEESEIWIGEWMASrklRDQIVIATKFTgd 107
Cdd:cd19097 1 SKLALGTAQFGLDygIANKSGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKR---LDKFKIITKLP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 108 ykkyevgggKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSI-EEVMDSLHILVQQGKVLYLGVS-DTPA 185
Cdd:cd19097 74 ---------PLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHgGKLVEALLELKKEGLIRKIGVSvYSPE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 186 WVVSAANYYatshgktPFSVYQGKWNVLNRDFER-DIIPMAR------H----F--GMALAPwdvmgggrfqskkaMEER 252
Cdd:cd19097 145 ELEKALESF-------KIDIIQLPFNILDQRFLKsGLLAKLKkkgieiHarsvFlqGLLLME--------------PDKL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2360743992 253 KKNGEGLRTFVggpeqtelevkisEALTKIAEEHGTeSVTAIAIAYVRSKaKNVFP-LIGGRKIEHLKQNIEALSIK 328
Cdd:cd19097 204 PAKFAPAKPLL-------------KKLHELAKKLGL-SPLELALGFVLSL-PEIDKiVVGVDSLEQLKEIIAAFKKP 265
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
19-181 |
2.06e-20 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 90.30 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGGASIGdawsGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKL-RDQ 97
Cdd:cd19163 4 RKLGKT-GLKVSKLGFGASPLG----GVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGK--ALKGIpRDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 98 IVIATKfTGdykKYEVGGGKSANYcgNHKRSLHvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMD----SLHILVQQG 173
Cdd:cd19163 77 YYLATK-VG---RYGLDPDKMFDF--SAERITK-SVEESLKRLGLDYIDIIQVHDIEFAPSLDQILNetlpALQKLKEEG 149
|
....*...
gi 2360743992 174 KVLYLGVS 181
Cdd:cd19163 150 KVRFIGIT 157
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-341 |
2.12e-20 |
|
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: 90.35 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 28 RVSPLILGGASIGDAWSGfmgSMNKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGE----WMASRKLRDQIVIATK 103
Cdd:cd19101 1 TISRVINGMWQLSGGHGG---IRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEfrkrLRRERDAADDVQIHTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 104 FTGDYKKYEVgggksanycgnhKRSlHV--SVRDSLRKLQTDWIDILYVHWWDY-MSSIEEVMDSLHILVQQGKVLYLGV 180
Cdd:cd19101 76 WVPDPGELTM------------TRA-YVeaAIDRSLKRLGVDRLDLVQFHWWDYsDPGYLDAAKHLAELQEEGKIRHLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 181 S--DTPAWvvsaanYYATSHGKTPFSVyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEG 258
Cdd:cd19101 143 TnfDTERL------REILDAGVPIVSN-QVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGG-LLSEKYLGVPEPTGPA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 259 LRTF-----------VGGPeqtELEVKISEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSI 327
Cdd:cd19101 215 LETRslqkyklmideWGGW---DLFQELLRTLKAIADKHGV-SIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF 290
|
330
....*....|....
gi 2360743992 328 KLTPEQIEYLEGIV 341
Cdd:cd19101 291 RLDDEDRAAIDAVL 304
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
50-340 |
2.78e-20 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 88.96 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 50 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGE-WMASRKLRDQIVIATKFTGDYKKYEvgggksanycgnhkrS 128
Cdd:COG0656 15 LPGEEAAAAVRTALEAGYRHIDTAAMYGNEEG---VGEaIAASGVPREELFVTTKVWNDNHGYD---------------D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 129 LHVSVRDSLRKLQTDWIDILYVHW---WDYMSSIEEvMDSlhiLVQQGKVLYLGVSdtpawvvsaaNYY------ATSHG 199
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWpgpGPYVETWRA-LEE---LYEEGLIRAIGVS----------NFDpehleeLLAET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 200 KTPFSVYQGKWNVLNRdfERDIIPMARHFGMALAPWDVMGGGrfqskKAMEErkkngeglrtfvggpeqtelevkisEAL 279
Cdd:COG0656 143 GVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRG-----KLLDD-------------------------PVL 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2360743992 280 TKIAEEHGTeSVTAIAIAYVRskAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLEGI 340
Cdd:COG0656 191 AEIAEKHGK-TPAQVVLRWHL--QRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
50-338 |
4.30e-20 |
|
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: 88.31 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 50 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkrS 128
Cdd:cd19071 11 LKPEETAEAVLAALEAGYRHIDTAAAYGNEAE---VGEAIRESGVpREELFITTKLWPTDHGYE---------------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 129 LHVSVRDSLRKLQTDWIDILYVHW---WDYMSSIEEVMDS---LHILVQQGKVLYLGVSdtpawvvsaaNYYAT------ 196
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHWpvpGKEGGSKEARLETwraLEELVDEGLVRSIGVS----------NFNVEhleell 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 197 SHGKTPFSVYQGKWNVLN-----RDF--ERDIIPMArhfgmalapWDVMGGGRFQSKKameerkkngeglrtfvggpeqt 269
Cdd:cd19071 143 AAARIKPAVNQIELHPYLqqkelVEFckEHGIVVQA---------YSPLGRGRRPLLD---------------------- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 270 elevkiSEALTKIAEEHGTeSVTAIAIAYVRSkaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19071 192 ------DPVLKEIAKKYGK-TPAQVLLRWALQ--RGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-338 |
2.50e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 87.39 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 27 IRVSPLILGGASIGDAWSG----FMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQIVIAT 102
Cdd:cd19103 2 KKLPKIALGTWSWGSGGAGgdqvFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYP-REDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 103 KFTgdykkyEVGGGKSANycgnhkrslhvSVRD----SLRKLQTDWIDILYVHwwdYMSSIEEVMDSLHILVQQGKVLYL 178
Cdd:cd19103 81 KFT------PQIAGQSAD-----------PVADmlegSLARLGTDYIDIYWIH---NPADVERWTPELIPLLKSGKVKHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 179 GVSDTPAWVVSAANYYAtshGKTPFSVY--QGKWNVLNRDFERD-IIPMARHFGMALAPWDV----MGGGRFQSKKAMEE 251
Cdd:cd19103 141 GVSNHNLAEIKRANEIL---AKAGVSLSavQNHYSLLYRSSEEAgILDYCKENGITFFAYMVleqgALSGKYDTKHPLPE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 252 RKKNGEGLRtfvggPEQTELEvKISEALTKIAEEHGTeSVTAIAIAYVRskAKNVFPLIGGRKIEHLKQNIEALSIKLTP 331
Cdd:cd19103 218 GSGRAETYN-----PLLPQLE-ELTAVMAEIGAKHGA-SIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARAASITLTD 288
|
....*..
gi 2360743992 332 EQIEYLE 338
Cdd:cd19103 289 DEIKELE 295
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-340 |
8.84e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 86.17 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 13 TELGRLrvlsktaGIRVSPLILGGASIGdawsGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASR 92
Cdd:cd19104 3 RRFGRT-------GLKVSELTFGGGGIG----GLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGR--ALK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 93 KLRDQIVIATKftgdykkYEVGGGKSANYCGNHKRSLHvsvrDSLRKLQTDWIDILYVH------------------WWD 154
Cdd:cd19104 70 GLPAGPYITTK-------VRLDPDDLGDIGGQIERSVE----KSLKRLKRDSVDLLQLHnrigderdkpvggtlsttDVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 155 YMssiEEVMDSLHILVQQGKVLYLGVSdtpAWVVSAANYYATSHGKtpFSVYQGKWNVLN-----------RDFE-RDII 222
Cdd:cd19104 139 GL---GGVADAFERLRSEGKIRFIGIT---GLGNPPAIRELLDSGK--FDAVQVYYNLLNpsaaearprgwSAQDyGGII 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 223 PMARHFGMALAPWDVMGGGrfqskkAMEERKKNGEGLRTFVGGPEQTELEVkiSEALTKIAEEHGtESVTAIAIAYVRSK 302
Cdd:cd19104 211 DAAAEHGVGVMGIRVLAAG------ALTTSLDRGREAPPTSDSDVAIDFRR--AAAFRALAREWG-ETLAQLAHRFALSN 281
|
330 340 350
....*....|....*....|....*....|....*....
gi 2360743992 303 AKNVFPLIGGRKIEHLKQNIEALSI-KLTPEQIEYLEGI 340
Cdd:cd19104 282 PGVSTVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-323 |
2.60e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 84.68 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 28 RVSPLILGGASIGDAWSGFmgsmnkEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIG----EWMASRKL-RDQIVIAT 102
Cdd:cd19099 2 TLSSLGLGTYRGDSDDETD------EEYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIkRDEVVIVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 103 K---FTGD---------YKKYEVGGGKSANYCGN------HKRSLHVSVRDSLRKLQTDWIDILYVH----------WWD 154
Cdd:cd19099 76 KagyIPGDgdeplrplkYLEEKLGRGLIDVADSAglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllelgEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 155 YMSSIEEVMDSLHILVQQGKVLYLGVS-DTPAWVVSAANYYATS--------------HG----KTPFSVYQ-----GKW 210
Cdd:cd19099 156 FYDRLEEAFEALEEAVAEGKIRYYGIStWDGFRAPPALPGHLSLeklvaaaeevggdnHHfkviQLPLNLLEpealtEKN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 211 NVLNRDFErdIIPMARHFGMAlapwdVMGGgrfqskkameerkkngeglRTFVGGPEQTELevkiseALTKIAEEHGTES 290
Cdd:cd19099 236 TVKGEALS--LLEAAKELGLG-----VIAS-------------------RPLNQGQLLGEL------RLADLLALPGGAT 283
|
330 340 350
....*....|....*....|....*....|....
gi 2360743992 291 VTAIAIAYVRSkAKNVF-PLIGGRKIEHLKQNIE 323
Cdd:cd19099 284 LAQRALQFARS-TPGVDsALVGMRRPEHVDENLA 316
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-341 |
9.43e-18 |
|
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: 83.17 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 19 RVLSKTaGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLR-DQ 97
Cdd:cd19159 4 RNLGKS-GLRVSCLGLG------TWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRrSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 98 IVIATKFtgdykkyeVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLY 177
Cdd:cd19159 77 LVITTKL--------YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 178 LGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMGGGRFQSK------KAME 250
Cdd:cd19159 149 WGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLACGIISGKygngvpESSR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 251 ERKKNGEGLRTFVGGPEQTELEVKISEaLTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSI--K 328
Cdd:cd19159 229 ASLKCYQWLKERIVSEEGRKQQNKLKD-LSPIAERLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpK 306
|
330
....*....|...
gi 2360743992 329 LTPEQIEYLEGIV 341
Cdd:cd19159 307 MTSHVVNEIDNIL 319
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
53-335 |
1.58e-17 |
|
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: 81.15 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 53 EQAFELLDAFYEAGGNCIDTANSYQNEEseiWIGEWMASRKL-RDQIVIATKFTGDykkyevgggksaNYcgnHKRSLHV 131
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMYGNEA---QVGEAIAASGVpRDELFLTTKVWPD------------NY---SPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 132 SVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAanyyATSHGKTPFSVYQGKWN 211
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE----AVELSEAPLFTNQVEYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 212 VLNRdfERDIIPMARHFGMALAPWDVMGGGrfqskkameerkkngeglrtfvggpeqtelEVKISEALTKIAEEHGtESV 291
Cdd:cd19140 159 PYLD--QRKLLDAAREHGIALTAYSPLARG------------------------------EVLKDPVLQEIGRKHG-KTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2360743992 292 TAIAIAYVRSKaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIE 335
Cdd:cd19140 206 AQVALRWLLQQ-EGVAAIPKATNPERLEENLDIFDFTLSDEEMA 248
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
53-338 |
1.41e-16 |
|
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: 79.21 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 53 EQAFELLDAFYEAGGNCIDTANSYQNEESEI---WIGEWMASR-KLRDQIVIATKFTGDYKKYEVGGGKSAnycgnhkrs 128
Cdd:cd19077 25 EEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYpEYADKVVLSVKGGLDPDTLRPDGSPEA--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 129 LHVSVRDSLRKL-QTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyyatsHGKTPFSVYQ 207
Cdd:cd19077 96 VRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRA------HAVHPIAAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 208 GKWNVLNRD-FERDIIPMARHFGMALAPWDVMG----GGRFQSKKAMEERKKNGeGLRTFvgGPEQTELEVKISEALTKI 282
Cdd:cd19077 170 VEYSLFSREiEENGVLETCAELGIPIIAYSPLGrgllTGRIKSLADIPEGDFRR-HLDRF--NGENFEKNLKLVDALQEL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2360743992 283 AEEHGTeSVTAIAIAYVRSKAKNVF-PLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19077 247 AEKKGC-TPAQLALAWILAQSGPKIiPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
25-341 |
1.80e-16 |
|
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: 79.36 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 25 AGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKLR-DQIVIATK 103
Cdd:cd19158 9 SGLRVSCLGLG------TWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRrSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 104 FtgdykkyeVGGGKSANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDT 183
Cdd:cd19158 83 I--------FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 184 PAWVVSAANYYATSHGKTPFSVYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMG----GGRFQSKKAMEERK--KNG 256
Cdd:cd19158 155 SSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKYDSGIPPYSRAslKGY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 257 EGLRTFVGGPEQTELEVKISEaLTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSI--KLTPEQI 334
Cdd:cd19158 235 QWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIV 312
|
....*..
gi 2360743992 335 EYLEGIV 341
Cdd:cd19158 313 HEIDSIL 319
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
30-335 |
4.20e-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: 78.26 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNE--ESEIWIGEWMAS--RKLRDQIVIATKFT 105
Cdd:cd19150 8 SGLKLPALSLG-LWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPpgSAEENFGRILREdfAGYRDELIISTKAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 106 GDYKKYEVGGGKSANYcgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TP 184
Cdd:cd19150 87 YDMWPGPYGEWGSRKY-------LLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSySP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 185 AWVVSAANYYATShgKTPFSVYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSK--KAMEE--RKKNGEGL 259
Cdd:cd19150 160 ERTREAAAILREL--GTPLLIHQPSYNMLNRWVEESgLLDTLQELGVGCIAFTPLAQGLLTDKylNGIPEgsRASKERSL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2360743992 260 RTfvggPEQTELEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEAL-SIKLTPEQIE 335
Cdd:cd19150 238 SP----KMLTEANLNSIRALNEIAQKRG-QSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALdNLTFSADELA 309
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
25-326 |
1.36e-15 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 76.95 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 25 AGIRVSPLILGgasigdAWSGFMGSMNKEQAFELLDAFYEAGGNCIDTANSY-----QNEESeiwIGEWMAS--RKLRDQ 97
Cdd:PRK09912 21 SGLRLPALSLG------LWHNFGHVNALESQRAILRKAFDLGITHFDLANNYgpppgSAEEN---FGRLLREdfAAYRDE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 98 IVIATKFTGDYKKYEVGGGKSANYcgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLY 177
Cdd:PRK09912 92 LIISTKAGYDMWPGPYGSGGSRKY-------LLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 178 LGVSD-TPAWVVSAANYYatSHGKTPFSVYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSK--------K 247
Cdd:PRK09912 165 VGISSySPERTQKMVELL--REWKIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 248 AMEERKKNGEGLRTFVggpeQTELEVKISEALTKIAEEHGtESVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALS 326
Cdd:PRK09912 243 RMHREGNKVRGLTPKM----LTEANLNSLRLLNEMAQQRG-QSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALN 316
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
34-332 |
8.71e-15 |
|
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: 73.93 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 34 LGGASIGDAwsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMAsRKLRDQIVIATKFTgdykKYEV 113
Cdd:cd19162 5 LGAASLGNL-----ARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA-RHPRAEYVVSTKVG----RLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 114 GGGksANYCGNHKRSLHV-------SVRDSLRKLQTDWIDILYVHWWD--YMSSIEEVMDSLHILVQQGKVLYLGVSDTp 184
Cdd:cd19162 75 PGA--AGRPAGADRRFDFsadgirrSIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVVGAIGVGVT- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 185 awVVSAANYYATSHGKTPFSVyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFqskkAMEERkkngEGLRTFVG 264
Cdd:cd19162 152 --DWAALLRAARRADVDVVMV-AGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL----ATDDP----AGDRYDYR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2360743992 265 GPEQTELEVkiSEALTKIAEEHGTESVTAiAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPE 332
Cdd:cd19162 221 PATPEVLAR--ARRLAAVCRRYGVPLPAA-ALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
25-188 |
2.15e-14 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 72.95 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 25 AGIRVSPLILGGASIGDAWSGFMGSMNKEQAFEllDAFyEAGGNCIDTANSYQNEESEIWIGEWMASRKL-RDQIVIATK 103
Cdd:cd19153 8 ALGNVSPVGLGTAALGGVYGDGLEQDEAVAIVA--EAF-AAGINHFDTSPYYGAESSEAVLGKALAALQVpRSSYTVATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 104 ftgdykkyeVGGGKSANYcgNHKRS-LHVSVRDSLRKLQTDWIDILYVH---WWDYMSSIEEVMDSLHILVQQGKVLYLG 179
Cdd:cd19153 85 ---------VGRYRDSEF--DYSAErVRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIG 153
|
170
....*....|...
gi 2360743992 180 VS----DTPAWVV 188
Cdd:cd19153 154 IAgyplDTLTRAT 166
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
30-332 |
3.33e-14 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 72.36 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGdawsGFMGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMAsRKLRDQIVIATKftgdyk 109
Cdd:cd19161 1 SELGLGTAGLG----NLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLR-EKPRDEFVLSTK------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 110 kyeVG-------GGKSANYCGNHK----------------RslhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEE----- 161
Cdd:cd19161 70 ---VGrllkparEGSVPDPNGFVDplpfeivydysydgimR----SFEDSLQRLGLNRIDILYVHDIGVYTHGDRkerhh 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 162 ---VMDS----LHILVQQG--KVLYLGVSDTPAwVVSAANYYatshgktPF--SVYQGKWNVLNRDFERDIIPMARHFGM 230
Cdd:cd19161 143 faqLMSGgfkaLEELKKAGviKAFGLGVNEVQI-CLEALDEA-------DLdcFLLAGRYSLLDQSAEEEFLPRCEQRGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 231 ALAPwdvmgGGRFQSKKAmeerKKNGEGLRTFVGGPEQTELEVKISEaLTKIAEEHGTESVTAiAIAYV-RSKA-KNVfp 308
Cdd:cd19161 215 SLVI-----GGVFNSGIL----ATGTKSGAKFNYGDAPAEIISRVME-IEKICDAYNVPLAAA-ALQFPlRHPAvASV-- 281
|
330 340
....*....|....*....|....
gi 2360743992 309 LIGGRKIEHLKQNIEALSIKLtPE 332
Cdd:cd19161 282 LTGARNPAQLRQNVEAFQTDI-PE 304
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
29-184 |
1.88e-13 |
|
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: 70.00 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 29 VSPLILGGASIGDAWSGFMGSMNKEqafELLDAFYEAGGNCIDTANSYQneESEIWIGEwmASRKL-----RDQIVIATK 103
Cdd:cd19164 13 LPPLIFGAATFSYQYTTDPESIPPV---DIVRRALELGIRAFDTSPYYG--PSEIILGR--ALKALrdefpRDTYFIITK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 104 fTGDYkkyevgGGKSANYCGNHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYMSSiEEVMDSLHILVQ---QGKVLYLGV 180
Cdd:cd19164 86 -VGRY------GPDDFDYSPEWIRA---SVERSLRRLHTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGI 154
|
....
gi 2360743992 181 SDTP 184
Cdd:cd19164 155 SGYP 158
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
51-340 |
7.91e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 68.07 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 51 NKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwmASRKLRDQIVIATKftgdykkyeVGGGKSANYCGNHKRS-- 128
Cdd:PRK10376 38 DRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIRE--ALHPYPDDLTIVTK---------VGARRGEDGSWLPAFSpa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 129 -LHVSVRDSLRKLQTDWIDILYVH-WWDYMS----SIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAanyyatsHGKT 201
Cdd:PRK10376 107 eLRRAVHDNLRNLGLDVLDVVNLRlMGDGHGpaegSIEEPLTVLAELQRQGLVRHIGLSNvTPTQVAEA-------RKIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 202 PFSVYQGKWNVLNRDFERDIIPMARHfGMALAPWDVMGGgrFQskkameerkkngeglrtfvggPEQtelevkiSEALTK 281
Cdd:PRK10376 180 EIVCVQNHYNLAHRADDALIDALARD-GIAYVPFFPLGG--FT---------------------PLQ-------SSTLSD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2360743992 282 IAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLEGI 340
Cdd:PRK10376 229 VAASLGA-TPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
64-335 |
1.03e-12 |
|
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: 67.38 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEWMA-SRKLRDQIVIATKFTGDykkyevgggksaNYcgnHKRSLHVSVRDSLRKLQT 142
Cdd:cd19139 25 ELGYRHIDTAQIYDNEAA---VGQAIAeSGVPRDELFITTKIWID------------NL---SKDKLLPSLEESLEKLRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 143 DWIDILYVHW--WDYMSSIEEVMDSLHILVQQGKVLYLGVSDtpawvvsaanyYATSHGKTPFSVYqGKWNVLNRDFE-- 218
Cdd:cd19139 87 DYVDLTLIHWpsPNDEVPVEEYIGALAEAKEQGLTRHIGVSN-----------FTIALLDEAIAVV-GAGAIATNQIEls 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 219 -----RDIIPMARHFGMALAPWDVMGGGrfqskKAMEErkkngeglrtfvggpeqtelevkisEALTKIAEEHGTeSVTA 293
Cdd:cd19139 155 pylqnRKLVAHCKQHGIHVTSYMTLAYG-----KVLDD-------------------------PVLAAIAERHGA-TPAQ 203
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2360743992 294 IAIAYVRSKAKNVFPliGGRKIEHLKQNIEALSIKLTPEQIE 335
Cdd:cd19139 204 IALAWAMARGYAVIP--SSTKREHLRSNLLALDLTLDADDMA 243
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-341 |
7.55e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 65.44 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 34 LG-GASIGDAWSgfMGSMnKEQAFELLDAFYEAGGNCIDTANSYQneESEIWIGEWMASRKL-RDQIVIATK----FTGD 107
Cdd:cd19098 18 LGhAADLGSGRS--VEAM-RAHTHAVLDAAWAAGVRYFDAARSYG--RAEEFLGSWLRSRNIaPDAVFVGSKwgytYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 108 YKkyeVGGGKsanycgnHKRSLHvsvrdSLRKLQTDW----------IDILYVHWWDYMSSI---EEVMDSLHILVQQGK 174
Cdd:cd19098 93 WQ---VDAAV-------HEVKDH-----SLARLLKQWeetrsllgkhLDLYQIHSATLESGVledADVLAALAELKAEGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 175 VLYLGVSDTPAWVVSAANYYATSHGKTPFSVYQGKWNVlnrdFERDIIP---MARHFGMALAPWDVMGGGRFqskkamee 251
Cdd:cd19098 158 KIGLSLSGPQQAETLRRALEIEIDGARLFDSVQATWNL----LEQSAGEaleEAHEAGMGVIVKEALANGRL-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 252 rkkngeglrtfVGGPEQTELEVKiSEALTKIAEEHGTeSVTAIAIAYVRSKAKNVFPLIGGRKIEHLKQNIEALSIKLTP 331
Cdd:cd19098 226 -----------TDRNPSPELAPL-MAVLKAVADRLGV-TPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDL 292
|
330
....*....|
gi 2360743992 332 EQIEYLEGIV 341
Cdd:cd19098 293 ELLAALADLA 302
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
48-254 |
9.29e-12 |
|
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: 64.50 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 48 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKlRDQIVIATKF-TGDYKKYEvgggksanycgNHK 126
Cdd:cd19096 16 DSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGP-REKFYLATKLpPWSVKSAE-----------DFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 127 RSLHvsvrDSLRKLQTDWIDILYVHWWDyMSSIEEVMDSLHIL------VQQGKVLYLGVS--DTPAWVVSAANYYatsh 198
Cdd:cd19096 84 RILE----ESLKRLGVDYIDFYLLHGLN-SPEWLEKARKGGLLeflekaKKEGLIRHIGFSfhDSPELLKEILDSY---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2360743992 199 gktPFSVYQGKWNVLNRDFERDI--IPMARHFGMALApwdVM---GGGRF--QSKKAMEERKK 254
Cdd:cd19096 155 ---DFDFVQLQYNYLDQENQAGRpgIEYAAKKGMGVI---IMeplKGGGLanNPPEALAILCG 211
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
70-335 |
2.54e-10 |
|
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: 60.32 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 70 IDTANSYQNEESeiwIGE-WMASRKLRDQIVIATKFtgdykkyevgggksanycgnHKRSLHV--SVRDSLRKLQTDWID 146
Cdd:cd19120 42 IDTAEMYGNEKE---VGEaLKESGVPREDLFITTKV--------------------SPGIKDPreALRKSLAKLGVDYVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 147 ILYVH--WWDYMS--SIEEVMDSLHILVQQGKVLYLGVSdtpawvvsaaNYYAT------SHGKTPFSVYQGKWNVLNRD 216
Cdd:cd19120 99 LYLIHspFFAKEGgpTLAEAWAELEALKDAGLVRSIGVS----------NFRIEdleellDTAKIKPAVNQIEFHPYLYP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 217 FERDIIPMARHFGMA------LAPwdvmgggrfqskkameerkkngegLRTFVGGPeqtelevkISEALTKIAEEHGtES 290
Cdd:cd19120 169 QQPALLEYCREHGIVvsayspLSP------------------------LTRDAGGP--------LDPVLEKIAEKYG-VT 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2360743992 291 VTAIAIAYVRskAKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIE 335
Cdd:cd19120 216 PAQVLLRWAL--QKGIVVVTTSSKEERMKEYLEAFDFELTEEEVE 258
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-184 |
1.72e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 58.25 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 18 LRVLSKTaGIRVSPLILGGASIGDAWsgfmGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMASRKL-RD 96
Cdd:PLN02587 1 LRELGST-GLKVSSVGFGASPLGSVF----GPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIpRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 97 QIVIATKfTGDYKKyevGGGKSAnycgnhKRSLHvSVRDSLRKLQTDWIDILYVHWWDYMS---SIEEVMDSLHILVQQG 173
Cdd:PLN02587 76 KYVVSTK-CGRYGE---GFDFSA------ERVTK-SVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESG 144
|
170
....*....|.
gi 2360743992 174 KVLYLGVSDTP 184
Cdd:PLN02587 145 KVRFIGITGLP 155
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
30-332 |
5.77e-09 |
|
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: 56.85 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 30 SPLILGGASIGDAWSgfmgSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwMASRKLRDQIVIATKftgdyk 109
Cdd:cd19152 1 PKLGFGTAPLGNLYE----AVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGA-ALRELGREDYVISTK------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 110 kyeVG-------GGKSANYCGNHKRSLHV------------SVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILV 170
Cdd:cd19152 70 ---VGrllvplqEVEPTFEPGFWNPLPFDavfdysydgilrSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 171 Q-----------QGKVLYLGV-------------SDTPAWVVSAanyyatshgktpfsvyqGKWNVLNRDFERDIIPMAR 226
Cdd:cd19152 147 KgafraleelreEGVIKAIGLgvndwevilrileEADLDWVMLA-----------------GRYTLLDHSAARELLPECE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 227 HFGMAlapwdVMGGGRFQSKKAMeerkkNGEGLRTFVGGPEQTELEVKiSEALTKIAEEHGTeSVTAIAIAYVRSKAKNV 306
Cdd:cd19152 210 KRGVK-----VVNAGPFNSGFLA-----GGDNFDYYEYGPAPPELIAR-RDRIEALCEQHGV-SLAAAALQFALAPPAVA 277
|
330 340
....*....|....*....|....*.
gi 2360743992 307 FPLIGGRKIEHLKQNIEALSIKLTPE 332
Cdd:cd19152 278 SVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
59-335 |
4.23e-08 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 53.73 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 59 LDAFyEAGGNCIDTANSYQNEESeiwIGEWM-ASRKLRDQIVIATKFTGDYKKYEvgggksanycgNHKRSLHvsvrDSL 137
Cdd:cd19133 30 LEAI-KAGYRLIDTAAAYGNEEA---VGRAIkKSGIPREELFITTKLWIQDAGYE-----------KAKKAFE----RSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 138 RKLQTDWIDILYVHW--------WDYMssiEEvmdslhiLVQQGKVLYLGVSdtpawvvsaaNYYA------TSHGKTPF 203
Cdd:cd19133 91 KRLGLDYLDLYLIHQpfgdvygaWRAM---EE-------LYKEGKIRAIGVS----------NFYPdrlvdlILHNEVKP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 204 SVYQGKWNVLNRdfERDIIPMARHFGMALAPWDVMGGGRFQskkAMEErkkngeglrtfvggpeqtelevkisEALTKIA 283
Cdd:cd19133 151 AVNQIETHPFNQ--QIEAVEFLKKYGVQIEAWGPFAEGRNN---LFEN-------------------------PVLTEIA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2360743992 284 EEHGtESVTAIAIAYVRSKAKNVFPliGGRKIEHLKQNIEALSIKLTPEQIE 335
Cdd:cd19133 201 EKYG-KSVAQVILRWLIQRGIVVIP--KSVRPERIAENFDIFDFELSDEDME 249
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
53-182 |
9.60e-08 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 52.76 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 53 EQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkRSLHv 131
Cdd:cd19131 23 DEAASAVREALEVGYRSIDTAAIYGNEEG---VGKAIRASGVpREELFITTKLWNSDQGYD--------------STLR- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2360743992 132 SVRDSLRKLQTDWIDILYVHWwdYMSSIEEVMDSLHILVQ---QGKVLYLGVSD 182
Cdd:cd19131 85 AFDESLRKLGLDYVDLYLIHW--PVPAQDKYVETWKALIElkkEGRVKSIGVSN 136
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
64-182 |
2.52e-07 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 51.56 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEWMA-SRKLRDQIVIATKFTGDykkyevgggksaNYCgnhKRSLHVSVRDSLRKLQT 142
Cdd:PRK11172 27 ELGYRAIDTAQIYDNEAA---VGQAIAeSGVPRDELFITTKIWID------------NLA---KDKLIPSLKESLQKLRT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2360743992 143 DWIDILYVHW--WDYMSSIEEVMDSLHILVQQGKVLYLGVSD 182
Cdd:PRK11172 89 DYVDLTLIHWpsPNDEVSVEEFMQALLEAKKQGLTREIGISN 130
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
50-181 |
3.32e-07 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 51.12 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 50 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDYKKYEvgggksanycgNHKRS 128
Cdd:cd19132 17 LKGDEGVEAVVAALQAGYRLLDTAFNYENEGA---VGEAVRRSGVpREELFVTTKLPGRHHGYE-----------EALRT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2360743992 129 LhvsvRDSLRKLQTDWIDILYVHWWD-----YMSSIEEVMDslhiLVQQGKVLYLGVS 181
Cdd:cd19132 83 I----EESLYRLGLDYVDLYLIHWPNpsrdlYVEAWQALIE----AREEGLVRSIGVS 132
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
53-181 |
9.53e-07 |
|
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: 49.55 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 53 EQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEwmASRKL-------RDQIVIATKFTgdykKYEVGGGKSANYCGNh 125
Cdd:cd19136 15 EEVRQAVDAALKAGYRLIDTASVYRNEAD---IGK--ALRDLlpkyglsREDIFITSKLA----PKDQGYEKARAACLG- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2360743992 126 krslhvsvrdSLRKLQTDWIDILYVHW--------------------WdymssieEVMDSLHilvQQGKVLYLGVS 181
Cdd:cd19136 85 ----------SLERLGTDYLDLYLIHWpgvqglkpsdprnaelrresW-------RALEDLY---KEGKLRAIGVS 140
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
50-338 |
1.36e-06 |
|
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: 49.42 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 50 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGE----WMASRKL-RDQIVIATKftgdykkyevgggksANYCGN 124
Cdd:cd19111 14 SPPEEVRAAVDYALFVGYRHIDTALSYQNEKA---IGEalkwWLKNGKLkREEVFITTK---------------LPPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 125 HKRSLHVSVRDSLRKLQTDWIDILYVHW-W------------DYMSSIEEVMDSLHILVQQGKVLYLGVSDtpaWVVSAA 191
Cdd:cd19111 76 EFKDTEKSLEKSLENLKLPYVDLYLIHHpCgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSN---FNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 192 NyYATSHGKTPFSVYQGKWNVLNRdfERDIIPMARHFGMALAPWDVMGggrfqskkameerkknGEGLRTFVGGPEQ-TE 270
Cdd:cd19111 153 N-KILAYAKVKPSNLQLECHAYLQ--QRELRKFCNKKNIVVTAYAPLG----------------SPGRANQSLWPDQpDL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2360743992 271 LEvkiSEALTKIAEEHGtESVTAIAIAYVRSkaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLE 338
Cdd:cd19111 214 LE---DPTVLAIAKELD-KTPAQVLLRFVLQ--RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
64-151 |
2.92e-06 |
|
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: 48.56 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEEsEIW--IGEWMASRKL-RDQIVIATKFtgdykkyevgggksanYCGNHKRS-LHVSVRDSLRK 139
Cdd:cd19154 36 KAGYRLIDTAFLYQNEE-AIGeaLAELLEEGVVkREDLFITTKL----------------WTHEHAPEdVEEALRESLKK 98
|
90
....*....|..
gi 2360743992 140 LQTDWIDILYVH 151
Cdd:cd19154 99 LQLEYVDLYLIH 110
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
64-182 |
4.41e-06 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 47.43 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDYKKYEvgGGKSAnycgnhkrslhvsVRDSLRKLQT 142
Cdd:cd19126 34 ENGYRSIDTAAIYKNEEG---VGEAIRESGVpREELFVTTKLWNDDQRAR--RTEDA-------------FQESLDRLGL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2360743992 143 DWIDILYVHW---------WDYMssiEEVMDSlhilvqqGKVLYLGVSD 182
Cdd:cd19126 96 DYVDLYLIHWpgkdkfidtWKAL---EKLYAS-------GKVKAIGVSN 134
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
64-340 |
4.91e-06 |
|
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: 47.66 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEwmASRKL-------RDQIVIATKFTGDYkkyevgggksanycgnHKRSLHV-SVRD 135
Cdd:cd19116 36 EAGYRHIDTAYLYGNEAE---VGE--AIREKiaegvvkREDLFITTKLWNSY----------------HEREQVEpALRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 136 SLRKLQTDWIDILYVHWwdYMSSIEEVMDSLHILVQQGKVLYLgvsDTpaW-----VVSaaNYYATSHGKTPFSVYQgkw 210
Cdd:cd19116 95 SLKRLGLDYVDLYLIHW--PVAFKENNDSESNGDGSLSDIDYL---ET--WrgmedLVK--LGLTRSIGVSNFNSEQ--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 211 nvLNRDFER-DIIPMARHfgMALAPwdvmgggRFQSKKAMEERKKNGEGLRTF--VGGPE---QTELEVKI-SEALTKIA 283
Cdd:cd19116 163 --INRLLSNcNIKPAVNQ--IEVHP-------TLTQEKLVAYCQSNGIVVMAYspFGRLVprgQTNPPPRLdDPTLVAIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2360743992 284 EEHGtESVTAIAIAYVRSkaKNVFPLIGGRKIEHLKQNIEALSIKLTPEQIEYLEGI 340
Cdd:cd19116 232 KKYG-KTTAQIVLRYLID--RGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSF 285
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
70-181 |
5.86e-06 |
|
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: 47.32 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 70 IDTANSYQNEESeiwIGEWMASRKL-RDQIVIATK-FTGDYkkyevgGGKSAnycgnhKRSLHvsvrDSLRKLQTDWIDI 147
Cdd:cd19135 43 IDTAKRYGCEEL---LGKAIKESGVpREDLFLTTKlWPSDY------GYEST------KQAFE----ASLKRLGVDYLDL 103
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2360743992 148 LYVHWWDYMSS-------IEEVMDSLHILVQQGKVLYLGVS 181
Cdd:cd19135 104 YLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVS 144
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
64-182 |
7.54e-06 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDykkyevgggksanycgNHKRSlHVSVRDSLRKLQT 142
Cdd:PRK11565 39 EVGYRSIDTAAIYKNEEG---VGKALKEASVaREELFITTKLWND----------------DHKRP-REALEESLKKLQL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2360743992 143 DWIDILYVHWWD-----YMSSIEEVMDslhiLVQQGKVLYLGVSD 182
Cdd:PRK11565 99 DYVDLYLMHWPVpaidhYVEAWKGMIE----LQKEGLIKSIGVCN 139
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
59-151 |
4.43e-05 |
|
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: 44.82 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 59 LDAFYEAGGNCIDTANSYQNEESeiwIG----EWMASRKL-RDQIVIATKFTgdykkyevgggksanYCGNHKRSLHVSV 133
Cdd:cd19155 31 VDTALEAGYRHIDTAYVYRNEAA---IGnvlkKWIDSGKVkREELFIVTKLP---------------PGGNRREKVEKFL 92
|
90
....*....|....*...
gi 2360743992 134 RDSLRKLQTDWIDILYVH 151
Cdd:cd19155 93 LKSLEKLQLDYVDLYLIH 110
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
43-182 |
1.03e-04 |
|
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: 43.53 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 43 WSGFmGSMNKEQAFELLDAFYEA---GGNCIDTANSYQNEESeiwIGEWM-ASRKLRDQIVIATKFTGDYKKYEvgggks 118
Cdd:cd19157 12 WLGL-GVFKVEEGSEVVNAVKTAlknGYRSIDTAAIYGNEEG---VGKGIkESGIPREELFITSKVWNADQGYD------ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2360743992 119 anycgnhkrSLHVSVRDSLRKLQTDWIDILYVHwWDYMSSIEEVMDSLHILVQQGKVLYLGVSD 182
Cdd:cd19157 82 ---------STLKAFEASLERLGLDYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVSN 135
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
54-182 |
1.53e-04 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 43.26 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 54 QAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWM-ASRKLRDQIVIATKFTGDYkkyevgggksanycgnHKRsLHVS 132
Cdd:cd19117 28 EVAKAVEAALKAGYRHIDTAAIYGNEEE---VGQGIkDSGVPREEIFITTKLWCTW----------------HRR-VEEA 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2360743992 133 VRDSLRKLQTDWIDILYVHW-------------------------WDYMSSIEEVMDslhiLVQQGKVLYLGVSD 182
Cdd:cd19117 88 LDQSLKKLGLDYVDLYLMHWpvpldpdgndflfkkddgtkdhepdWDFIKTWELMQK----LPATGKVKAIGVSN 158
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
64-182 |
2.46e-04 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 42.50 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkrSLHVSVRDSLRKLQT 142
Cdd:cd19156 34 EAGYRHIDTAAIYKNEEG---VGQGIRESGVpREEVFVTTKLWNSDQGYE---------------STLAAFEESLEKLGL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2360743992 143 DWIDILYVHW------WDYMSSIEEvmdslhiLVQQGKVLYLGVSD 182
Cdd:cd19156 96 DYVDLYLIHWpvkgkfKDTWKAFEK-------LYKEKKVRAIGVSN 134
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
64-340 |
3.35e-04 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 41.82 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 64 EAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDYKKyevgggksanycgnHKRSLhVSVRDSLRKLQT 142
Cdd:cd19130 34 EVGYRHIDTAAIYGNEEG---VGAAIAASGIpRDELFVTTKLWNDRHD--------------GDEPA-AAFAESLAKLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 143 DWIDILYVHW-----------WDYMSSieevmdslhiLVQQGKVLYLGVSDtpaWVVSAANYYATSHGKTPfSVYQgkWN 211
Cdd:cd19130 96 DQVDLYLVHWptpaagnyvhtWEAMIE----------LRAAGRTRSIGVSN---FLPPHLERIVAATGVVP-AVNQ--IE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 212 VLNRDFERDIIPMARHFGMALAPWDVMGGGrfqskkameerkkngeglrTFVGGPeqtelevkiseALTKIAEEHGtESV 291
Cdd:cd19130 160 LHPAYQQRTIRDWAQAHDVKIEAWSPLGQG-------------------KLLGDP-----------PVGAIAAAHG-KTP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2360743992 292 TAIAIAYVRSKAKNVFPliGGRKIEHLKQNIEALSIKLTPEQIEYLEGI 340
Cdd:cd19130 209 AQIVLRWHLQKGHVVFP--KSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
70-182 |
5.51e-04 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 41.24 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 70 IDTANSYQNEESeiwIGEWM-ASRKLRDQIVIATK-FTGDYKkYEvgggksanycgnhkRSLHvSVRDSLRKLQTDWIDI 147
Cdd:cd19127 39 IDTAAAYGNERE---VGEGIrRSGVDRSDIFVTTKlWISDYG-YD--------------KALR-GFDASLRRLGLDYVDL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2360743992 148 LYVHW-----WDymSSIEEVMDSLHILVqQGKVLYLGVSD 182
Cdd:cd19127 100 YLLHWpvpndFD--RTIQAYKALEKLLA-EGRVRAIGVSN 136
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
47-152 |
2.91e-03 |
|
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: 39.07 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360743992 47 MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMASRKL-RDQIVIATKFTGDykkyEVGGGKSANYCgnh 125
Cdd:cd19134 18 VGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAA---VGRAIAASGIpRGELFVTTKLATP----DQGFTASQAAC--- 87
|
90 100
....*....|....*....|....*..
gi 2360743992 126 krslhvsvRDSLRKLQTDWIDILYVHW 152
Cdd:cd19134 88 --------RASLERLGLDYVDLYLIHW 106
|
|
| |
