|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
1-292 |
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: 624.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKYEVGGGKSANYCGNHK 80
Cdd:cd19147 28 MGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIVIATKFTTDYKAYEVGKGKAVNYCGNHK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIY 160
Cdd:cd19147 108 RSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTELEVKISEALNKIAEEH 240
Cdd:cd19147 188 QGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGLRSFVGGTEQTPEEVKISEALEKVAEEH 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 241 GTESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19147 268 GTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
1-306 |
5.15e-164 |
|
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: 459.97 E-value: 5.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKYEVGGGKSaNYCGNHK 80
Cdd:cd19146 29 MGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMVLATKYTTGYRRGGPIKIKS-NYQGNHA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIY 160
Cdd:cd19146 108 KSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKkamEERKKNGEGLRTfvGGPeQTELEVKISEALNKIAEEH 240
Cdd:cd19146 188 QGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFRTE---EEFKRRGRSGRK--GGP-QTEKERKVSEKLEKVAEEK 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190409293 241 GTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIVTFDVGFPKSLI 306
Cdd:cd19146 262 GT-AITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAYPFDVGFPMNFL 326
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-292 |
5.33e-151 |
|
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: 426.25 E-value: 5.33e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTGDYKKyevgggKSANYCGNHKHSL 83
Cdd:cd19080 28 ADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN--RDRIVLATKYTMNRRP------GDPNAGGNHRKNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 HVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQGK 163
Cdd:cd19080 100 RRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTELEVKISEALNKIAEEHGTe 243
Cdd:cd19080 180 YSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTVGFGKLTERNWAIVDVVAAVAEELGR- 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190409293 244 SVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19080 259 SAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
2-295 |
4.20e-87 |
|
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: 264.35 E-value: 4.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKFTGDYkkyevggGKSANYCGNHKH 81
Cdd:COG0667 28 GGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRP-RDDVVIATKVGRRM-------GPGPNGRGLSRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANyyATSHGKTPFSIYQ 161
Cdd:COG0667 100 HIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRAL--AIAEGLPPIVAVQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTELEVKISEALNKIAEEHG 241
Cdd:COG0667 178 NEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAATNFVQGYLTERNLALVDALRAIAAEHG 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 190409293 242 TeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:COG0667 258 V-TPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAAL 310
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
2-295 |
4.80e-85 |
|
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: 258.01 E-value: 4.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKL-RDQIVIATKftgdykkyeVGGGKSANYCGNHK 80
Cdd:pfam00248 13 GPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVkRDKVVIATK---------VPDGDGPWPSGGSK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSaanyYATSHGKTPFSIY 160
Cdd:pfam00248 84 ENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIE----KALTKGKIPIVAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFvggPEQTELEVKISEALNKIAEEH 240
Cdd:pfam00248 160 QVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLL---KKGTPLNLEALEALEEIAKEH 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 241 GtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:pfam00248 237 G-VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
5-292 |
5.21e-79 |
|
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: 243.26 E-value: 5.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 5 NKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKYEVGGGKSAnycgnhKHsLH 84
Cdd:cd19079 33 DEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRDEVVIATKVYFPMGDGPNGRGLSR------KH-IM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 85 VSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQGKW 164
Cdd:cd19079 106 AEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 165 NVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTELEVKISEALNKIAEEHGTeS 244
Cdd:cd19079 186 NLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGV-S 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 190409293 245 VTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19079 265 MAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
2-277 |
1.13e-78 |
|
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: 239.73 E-value: 1.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYkkyevggGKSANYCGNHKH 81
Cdd:cd06660 12 GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDDVVIATKGGHPP-------GGDPSRSRLSPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQ 161
Cdd:cd06660 85 HIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDF-ERDIIPMARHFGMALAPWDVMGGGrfqskkameerkkngeglrtfvggpeqtelevkisealnkiaeeh 240
Cdd:cd06660 165 PQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG--------------------------------------------- 199
|
250 260 270
....*....|....*....|....*....|....*..
gi 190409293 241 gtesVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIE 277
Cdd:cd06660 200 ----PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-291 |
2.73e-75 |
|
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: 233.65 E-value: 2.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 5 NKEQAFELLDAFYEAGGNCIDTANSY-------QNEESEIWIGEWMKSRKLRDQIVIATKftgdykkyeVGGGKSANYCG 77
Cdd:cd19081 24 DEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLKSRGKRDRVVIATK---------VGFPMGPNGPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 78 NHKHSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPF 157
Cdd:cd19081 95 LSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 158 SIYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGG----GRFQSKKAMEERKKNGEGLRTFVggpeqTELEVKISEA 232
Cdd:cd19081 175 VSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGgfltGKYRSEADLPGSTRRGEAAKRYL-----NERGLRILDA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 190409293 233 LNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYL 291
Cdd:cd19081 250 LDEVAAEHGA-TPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
2-294 |
6.08e-75 |
|
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: 233.27 E-value: 6.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTGdykkyEVGGGksANYCGNHKH 81
Cdd:cd19091 34 GGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR--RDDVLIATKVRG-----RMGEG--PNDVGLSRH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQ 161
Cdd:cd19091 105 HIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTELE--VKISEALNKIAEE 239
Cdd:cd19091 185 AYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGSRLRRTGFDFPPVDRErgYDVVDALREIAKE 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 240 HGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:cd19091 265 TGA-TPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
2-295 |
2.39e-65 |
|
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: 208.20 E-value: 2.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMN------KEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTGdykkyEVGGGKsany 75
Cdd:cd19087 19 GTMNfggrtdEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR--RDDIVLATKVFG-----PMGDDP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 76 cgNHKHS--LHV--SVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATS 151
Cdd:cd19087 88 --NDRGLsrRHIrrAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 152 HGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGL-RTFVGGPEQTELEVKIS 230
Cdd:cd19087 166 RGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVeRARYQARYGLEEYRDIA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 231 EALNKIAEEHGtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19087 246 ERFEALAAEAG-LTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDELF 309
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
3-280 |
7.38e-62 |
|
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: 198.93 E-value: 7.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 3 SMNKEQAFELLDAFYEAGGNCIDTANSYQNEE----SEIWIGEWMKSRKLRDQIVIATKftgdykkyevGG-----GKSA 73
Cdd:cd19082 13 RIDEEEAFALLDAFVELGGNFIDTARVYGDWVergaSERVIGEWLKSRGNRDKVVIATK----------GGhpdleDMSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 74 NYCgnHKHSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDtpaWV---VSAANYYAT 150
Cdd:cd19082 83 SRL--SPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSterIAEANAYAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 151 SHGKTPFSIYQGKWN--VLNRDFERD--IIPM---ARHF----GMALAPWDVMGGGRFqSKKAMEERKKNGEGLRTFvgg 219
Cdd:cd19082 158 AHGLPGFAASSPQWSlaRPNEPPWPGptLVAMdeeMRAWheenQLPVFAYSSQARGFF-SKRAAGGAEDDSELRRVY--- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190409293 220 peQTELEVKISEALNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALS 280
Cdd:cd19082 234 --YSEENFERLERAKELAEEKGV-SPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
1-286 |
3.77e-57 |
|
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: 187.77 E-value: 3.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSM------NKEQAFELLDAFYEAGGNCIDTANSY---QNEE----SEIWIGEWMKSRKLRDQIVIATKFTGDYKKYEV 67
Cdd:cd19094 6 LGTMtwgeqnTEAEAHEQLDYAFDEGVNFIDTAEMYpvpPSPEtqgrTEEIIGSWLKKKGNRDKVVLATKVAGPGEGITW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 68 GGGKSANYcgNHKHsLHVSVRDSLRKLQTDWIDILYVHWWD-----------------YMS-SIEEVMDSLHILVQQGKV 129
Cdd:cd19094 86 PRGGGTRL--DREN-IREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeEDSvSFEEQLEALGELVKAGKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 130 LYLGVSDTPAWVVSAANYYATSHGKTPF-SIyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKK 208
Cdd:cd19094 163 RHIGLSNETPWGVMKFLELAEQLGLPRIvSI-QNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGG-VLTGKYLDGAAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 209 NGEGLRTFVGGPEQ---TELEVKISEALNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTP 285
Cdd:cd19094 241 PEGGRLNLFPGYMAryrSPQALEAVAEYVKLARKHGL-SPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVPLSD 319
|
.
gi 190409293 286 E 286
Cdd:cd19094 320 E 320
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
2-292 |
1.30e-56 |
|
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: 185.42 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTGDYkkyevGGGKSANYCGNHKH 81
Cdd:cd19084 20 GEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR--RDDVVIATKCGLRW-----DGGKGVTKDLSPES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 sLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAtshgktPFSIYQ 161
Cdd:cd19084 93 -IRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYG------PIVSLQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDFERDIIPMARHFGMALAPWDVMGGG----RFQSK---KAMEERKKNgeglRTFVGgpEQTELEVKISEALN 234
Cdd:cd19084 166 PPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGlltgKYKKEptfPPDDRRSRF----PFFRG--ENFEKNLEIVDKLK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 190409293 235 KIAEEHGtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19084 240 EIAEKYG-KSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-294 |
2.21e-45 |
|
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: 156.21 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 13 LDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTGDYKKYEvgggksanycgnhkhSLHVSVRDSLR 92
Cdd:cd19085 29 IHAALDAGINFFDTAEAYGDGHSEEVLGKALKGR--RDDVVIATKVSPDNLTPE---------------DVRKSCERSLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 93 KLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWvvsaanYYATSHGKTPFSIYQGKWNVLNRDFE 172
Cdd:cd19085 92 RLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPA------QLEEALDAGRIDSNQLPYNLLWRAIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 173 RDIIPMARHFGMALAPWDVMG----GGRFQSKKAMEE---RKKNgegLRTFVGGPEQTELEVkiSEALNKIAEEHGTeSV 245
Cdd:cd19085 166 YEILPFCREHGIGVLAYSPLAqgllTGKFSSAEDFPPgdaRTRL---FRHFEPGAEEETFEA--LEKLKEIADELGV-TM 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190409293 246 TAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:cd19085 240 AQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-280 |
5.34e-45 |
|
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: 155.18 E-value: 5.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGS-MNKEQAFELLDAFYEAGGNCIDTANSY-------QNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKYevgGGKS 72
Cdd:cd19752 10 FGTrTDEETSFAILDRYVAAGGNFLDTANNYafwteggVGGESERLIGRWLKDRGNRDDVVIATKVGAGPRDP---DGGP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 73 ANYCGNHKHSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSH 152
Cdd:cd19752 87 ESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 153 GKTPFSIYQGKWNVL----NRDF------ERDIIPMAR-HFGMALAPWDVMGGGRFqSKKAMEERKkngeglrtfvggPE 221
Cdd:cd19752 167 GWAEFSAIQQRHSYLrprpGADFgvqrivTDELLDYASsRPDLTLLAYSPLLSGAY-TRPDRPLPE------------QY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190409293 222 QTELEVKISEALNKIAEEHGtesVTA--IAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALS 280
Cdd:cd19752 234 DGPDSDARLAVLEEVAGELG---ATPnqVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
2-286 |
4.17e-44 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 153.13 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKFTGdykkyevGGGKSANYCG-NHK 80
Cdd:cd19074 17 GQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWP-RESYVISTKVFW-------PTGPGPNDRGlSRK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIY 160
Cdd:cd19074 89 H-IFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGG----RFQSKKAMEER-KKNGEGLRTFVGGPEQTELEVKIsEALNK 235
Cdd:cd19074 168 QPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGlltgKYRDGIPPPSRsRATDEDNRDKKRRLLTDENLEKV-KKLKP 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 190409293 236 IAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPE 286
Cdd:cd19074 247 IADELGL-TLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-291 |
8.78e-43 |
|
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: 149.67 E-value: 8.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTgdykkYEVGGGKSANYCGNHKH 81
Cdd:cd19076 27 GPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDR--RDEVVIATKFG-----IVRDPGSGFRGVDGRPE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDtpawvvSAANYYATSHGKTPFSIYQ 161
Cdd:cd19076 100 YVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE------ASADTIRRAHAVHPITAVQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRT---FVGgpEQTELEVKISEALNKIAE 238
Cdd:cd19076 174 SEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNnprFQG--ENFDKNLKLVEKLEAIAA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 239 EHGtesVTA--IAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYL 291
Cdd:cd19076 252 EKG---CTPaqLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
7-291 |
8.63e-42 |
|
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: 147.19 E-value: 8.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSrKLRDQIVIATKF---TGDYKKYEVGGgkSANYcgnhkhsl 83
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKD-GPREKVQLATKFgihEIGGSGVEVRG--DPAY-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 hvsVR----DSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyyatsHGKTPFSI 159
Cdd:cd19145 102 ---VRaaceASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRA------HAVHPITA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 160 YQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRT---FVGgpEQTELEVKISEALNKI 236
Cdd:cd19145 173 VQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKShprFQG--ENLEKNKVLYERVEAL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 237 AEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYL 291
Cdd:cd19145 251 AKKKGC-TPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
4-293 |
3.56e-40 |
|
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: 142.76 E-value: 3.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFTGDYkkyeVGGGKSANYCGNHKHSL 83
Cdd:cd19078 22 PDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF--RDQVVIATKFGFKI----DGGKPGPLGLDSRPEHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 HVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTpawvvsAANYYATSHGKTPFSIYQGK 163
Cdd:cd19078 96 RKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEA------GVETIRRAHAVCPVTAVQSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEGLRTFVG--GPEQTELEVKISEALNKIAEEHG 241
Cdd:cd19078 170 YSMMWREPEKEVLPTLEELGIGFVPFSPLGKG-FLTGKIDENTKFDEGDDRASLPrfTPEALEANQALVDLLKEFAEEKG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 242 TESVtAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLES 293
Cdd:cd19078 249 ATPA-QIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
2-293 |
3.82e-40 |
|
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: 143.18 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKF-----TGDYKKYEVGGGKSANYC 76
Cdd:cd19149 28 GGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR--RDKVVLATKCglrwdREGGSFFFVRDGVTVYKN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 77 GNhKHSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAtshgktP 156
Cdd:cd19149 106 LS-PESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAG------Q 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 157 FSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEerkkngeglRTFVGGPE-------QTELEVKI 229
Cdd:cd19149 179 LDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPD---------REFDAGDArsgipwfSPENREKV 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190409293 230 SEALNK---IAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLES 293
Cdd:cd19149 250 LALLEKwkpLCEKYGC-TLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
5-292 |
4.20e-39 |
|
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: 139.67 E-value: 4.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 5 NKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKyevgggksanycgNHKHSLH 84
Cdd:cd19093 24 GDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDEVVIATKFAPLPWR-------------LTRRSVV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 85 VSVRDSLRKLQTDWIDILYVHW-WDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIyQGK 163
Cdd:cd19093 91 KALKASLERLGLDSIDLYQLHWpGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGVPLASN-QVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTElevKISEALNKIAEEHGt 242
Cdd:cd19093 170 YSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQ---PLLDALEEIAEKYG- 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 190409293 243 ESVTAIAIAYVRskAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19093 246 KTPAQVALNWLI--AKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
7-287 |
2.32e-37 |
|
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: 134.99 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRK-LRDQIVIATKfTGDYKKYEVGGGKSANYCGNHKHSLHv 85
Cdd:cd19092 24 EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPgLREKIEIQTK-CGIRLGDDPRPGRIKHYDTSKEHILA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 86 SVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANyyatSHGKTPFSIYQGKWN 165
Cdd:cd19092 102 SVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQ----SYLDQPLVTNQIELS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 166 VLNRDF----------ERDIIPMArhfgmalapWDVMGGGRFQSkkameerkkngeglrtfvggpEQTELEVKISEALNK 235
Cdd:cd19092 178 LLHTEAiddgtldycqLLDITPMA---------WSPLGGGRLFG---------------------GFDERFQRLRAALEE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 236 IAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQ 287
Cdd:cd19092 228 LAEEYGV-TIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
5-292 |
3.68e-37 |
|
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: 133.89 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 5 NKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKFTGDYKKYevgggksanycgnhkHSLH 84
Cdd:cd19072 24 DDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFD-REDLFITTKVSPDHLKY---------------DDVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 85 VSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAtshGKTPFSIYQGKW 164
Cdd:cd19072 88 KAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYL---KKGPIVANQVEY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 165 NVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAmeerkkngeglrtfvggpeqtelevkiSEALNKIAEEHGtES 244
Cdd:cd19072 165 NLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG---------------------------SPLLDEIAKKYG-KT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 190409293 245 VTAIAIAYVRSKaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19072 217 PAQIALNWLISK-PNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
4-287 |
7.65e-36 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 131.43 E-value: 7.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRK-LRDQIVIATK----FTGDYKKYEVgggKSANYCGN 78
Cdd:COG4989 28 LSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPsLREKIELQTKcgirLPSEARDNRV---KHYDTSKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 79 HkhsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANyyatSHGKTPFS 158
Cdd:COG4989 105 H---IIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPSQFELLQ----SALDQPLV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 159 IYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGGGRFQSkkameerkkngeglrtfvggpEQTELEVKISEALNKIA 237
Cdd:COG4989 178 TNQIELSLLHTDaFDDGTLDYCQLNGITPMAWSPLAGGRLFG---------------------GFDEQFPRLRAALDELA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 190409293 238 EEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQ 287
Cdd:COG4989 237 EKYGV-SPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
4-280 |
1.24e-34 |
|
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: 128.06 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEwMKSRKLRdqIVIATKFTGDYKKyevgggksanycGNHKHSL 83
Cdd:cd19075 17 TTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGE-LGLGERG--FKIDTKANPGVGG------------GLSPENV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 HVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQGK 163
Cdd:cd19075 82 RKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEG-----------LRTFVGGPEQTELevkiSEA 232
Cdd:cd19075 162 YNAITRQVETELFPCLRKLGIRFYAYSPLAGG-FLTGKYKYSEDKAGGGrfdpnnalgklYRDRYWKPSYFEA----LEK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 190409293 233 LNKIAEEHGtESVTAIAIAYVR-----SKAKNVFPLVGGRKIEHLKQNIEALS 280
Cdd:cd19075 237 VEEAAEKEG-ISLAEAALRWLYhhsalDGEKGDGVILGASSLEQLEENLAALE 288
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
7-294 |
1.88e-34 |
|
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: 128.10 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKL-RDQIVIATK-FTGdykkyevGGGKSANYCG-NHKHSL 83
Cdd:cd19143 31 DEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWpRSDYVVSTKiFWG-------GGGPPPNDRGlSRKHIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 HvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQGK 163
Cdd:cd19143 104 E-GTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRD-FERDIIPMARHFGMALAPW--------------DVMGGGRFqskkAMEerkkNGEGLRTFVGGPEQTELEVk 228
Cdd:cd19143 183 YNLFHRErVEVEYAPLYEKYGLGTTTWsplasglltgkynnGIPEGSRL----ALP----GYEWLKDRKEELGQEKIEK- 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190409293 229 iSEALNKIAEEHGTeSVTAIAIAYVrskAKNvfPLV-----GGRKIEHLKQNIEALSI--KLTPEQIEYLESI 294
Cdd:cd19143 254 -VRKLKPIAEELGC-SLAQLAIAWC---LKN--PNVstvitGATKVEQLEENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
7-288 |
2.05e-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: 127.76 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEE--SEIWIGEWMKS--RKLRDQIVIATKfTGdykkYEVGGGKSANYcGNHKHs 82
Cdd:cd19089 29 EEARELLRTAFDLGITHFDLANNYGPPPgsAEENFGRILKRdlRPYRDELVISTK-AG----YGMWPGPYGDG-GSRKY- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 83 LHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGkTPFSIYQG 162
Cdd:cd19089 102 LLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 163 KWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK-----KAMEERKKNGEGLRTfvggPEQTELEVKISEALNKIA 237
Cdd:cd19089 181 RYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKylngiPPDSRRAAESKFLTE----EALTPEKLEQLRKLNKIA 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 238 EEHGtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEAL-SIKLTPEQI 288
Cdd:cd19089 257 AKRG-QSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkNLDFSEEEL 307
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-295 |
1.83e-32 |
|
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: 122.40 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 17 YEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATK--FTGDYKKYEVGGGKSAnycgnhkhSLHVSVRDSLRKL 94
Cdd:cd19102 36 LDLGINWIDTAAVYGLGHSEEVVGRALKGL--RDRPIVATKcgLLWDEEGRIRRSLKPA--------SIRAECEASLRRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 95 QTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyyATSHgktPFSIYQGKWNVLNRDFERD 174
Cdd:cd19102 106 GVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRC---QAIH---PIASLQPPYSLLRRGIEAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 175 IIPMARHFGMALAPWDVMGGGRFqSKKAMEERKKNGEGLRTFVGGPEQTELE----VKISEALNKIAEEHGTeSVTAIAI 250
Cdd:cd19102 180 ILPFCAEHGIGVIVYSPMQSGLL-TGKMTPERVASLPADDWRRRSPFFQEPNlarnLALVDALRPIAERHGR-TVAQLAI 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 190409293 251 AYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19102 258 AWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
2-295 |
4.19e-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: 121.26 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKyevGGGKSANycgNHKH 81
Cdd:cd19148 20 GGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDRVVIATKVGLEWDE---GGEVVRN---SSPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSdtpawvvsaaNY----YATSHGKTPF 157
Cdd:cd19148 94 RIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVS----------NFspeqMETFRKVAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 158 SIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEGLRTFVGGPEQTELEVKIS--EALNK 235
Cdd:cd19148 164 HTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRG-LLSGKMTKDTKFEGDDLRRTDPKFQEPRFSQYLAavEELDK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 236 IAEEHGTESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19148 243 LAQERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAIL 302
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
7-295 |
6.14e-32 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 121.40 E-value: 6.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIwiGEWMK-SRKLRDQIVIATKFTgdYKKYEVGGGKSAN----YCGNhkh 81
Cdd:cd19144 34 EERFAVLDAAFELGCTFWDTADIYGDSEELI--GRWFKqNPGKREKIFLATKFG--IEKNVETGEYSVDgspeYVKK--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 slhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyyatsHGKTPFSIYQ 161
Cdd:cd19144 107 ----ACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRA------HAVHPIAAVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDFER---DIIPMARHFGMALAPWDVMG----GGRFQSKKAMEERKkngegLRTFVG--GPEQTELEVKISEA 232
Cdd:cd19144 177 IEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGrgflTGAIRSPDDFEEGD-----FRRMAPrfQAENFPKNLELVDK 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 233 LNKIAEEHGtesVTA--IAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19144 252 IKAIAKKKN---VTAgqLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIA 313
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-295 |
6.89e-31 |
|
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: 118.29 E-value: 6.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKftGDYKkyEVGGGKSANycgNHKHSL 83
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYN-RNEVVIATK--GAHK--FGGDGSVLN---NSPEFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 HVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANyyatshGKTPFSIYQGK 163
Cdd:cd19083 102 RSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEAN------KDGYVDVLQGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEGLRT----FVGgpEQTELEVKISEALNKIAEE 239
Cdd:cd19083 176 YNLLQREAEEDILPYCVENNISFIPYFPLASG-LLAGKYTKDTKFPDNDLRNdkplFKG--ERFSENLDKVDKLKSIADE 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190409293 240 HGTEsVTAIAIAYVRSKaknvfPLV-----GGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19083 253 KGVT-VAHLALAWYLTR-----PAIdvvipGAKRAEQVIDNLKALDVTLTEEEIAFIDALF 307
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
2-186 |
5.18e-30 |
|
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: 114.11 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFtGdYKKYEvGGGKSANYCGNHkh 81
Cdd:cd19086 19 GDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGR--RDKVVIATKF-G-NRFDG-GPERPQDFSPEY-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 sLHVSVRDSLRKLQTDWIDILYVH-WWDYMSSIEEVMDSLHILVQQGKVLYLGVSdtpawVVSAANYYATSHGKTPFSIy 160
Cdd:cd19086 92 -IREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVS-----VGDPEEALAALRRGGIDVV- 164
|
170 180
....*....|....*....|....*.
gi 190409293 161 QGKWNVLNRDFERDIIPMARHFGMAL 186
Cdd:cd19086 165 QVIYNLLDQRPEEELFPLAEEHGVGV 190
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
2-278 |
3.23e-28 |
|
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: 109.63 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGEWMKSRkLRDQIVIATKfTGdykkyEVGGGKSANYCGNHKH 81
Cdd:cd19095 15 GVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALAGL-RRDDLFIATK-VG-----THGEGGRDRKDFSPAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHvSVRDSLRKLQTDWIDILYVH----WWDYmssiEEVMDSLHILVQQGKVLYLGVS-DTPawvvsAANYYATSHgktP 156
Cdd:cd19095 86 IRA-SIERSLRRLGTDYIDLLQLHgpsdDELT----GEVLETLEDLKAAGKVRYIGVSgDGE-----ELEAAIASG---V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 157 FSIYQGKWNVLNRDfERDIIPMARHFGMAlapwdVMGGGRFqskkameerkKNGEGLRTFVGGPEQTELevkisEALNKI 236
Cdd:cd19095 153 FDVVQLPYNVLDRE-EEELLPLAAEAGLG-----VIVNRPL----------ANGRLRRRVRRRPLYADY-----ARRPEF 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 190409293 237 AEEHGTESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEA 278
Cdd:cd19095 212 AAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
4-284 |
3.46e-28 |
|
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: 110.00 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKftgdykkyeVG----GGKSANYCGNH 79
Cdd:cd19088 21 ADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPY--PDDVVIATK---------GGlvrtGPGWWGPDGSP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 80 KHsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDtpawvVSAANyYATSHGKTPFSI 159
Cdd:cd19088 90 EY-LRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSN-----VTVAQ-IEEARAIVRIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 160 YQGKWNVLNRDFErDIIPMARHFGMALAPWDVMGGGRfqskKAMEERKkngeglrtfvggpeqtelevkiseaLNKIAEE 239
Cdd:cd19088 163 VQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGD----LAQPGGL-------------------------LAEVAAR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 190409293 240 HGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLT 284
Cdd:cd19088 213 LGA-TPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
2-294 |
1.48e-27 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 110.33 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKE-QAFELLDAFYEAGGNCIDTANSY----QNEE---SEIWIGEWMKSRKLRDQIVIATKFTGDYKKYEvgGGKSA 73
Cdd:PRK10625 24 GEQNSEaDAHAQLDYAVAQGINLIDVAEMYpvppRPETqglTETYIGNWLAKRGSREKLIIASKVSGPSRNND--KGIRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 74 NYCGNHKhSLHVSVRDSLRKLQTDWIDILYVHW------------WDYMSS-----IEEVMDSLHILVQQGKVLYLGVSD 136
Cdd:PRK10625 102 NQALDRK-NIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgYSWTDSapavsLLETLDALAEQQRAGKIRYIGVSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 137 TPAWVVSAANYYATSHGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK---KAMEERKKNGEGL 213
Cdd:PRK10625 181 ETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKylnGAKPAGARNTLFS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 214 RTFVGGPEQTELEVKiseALNKIAEEHGTESvTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLES 293
Cdd:PRK10625 261 RFTRYSGEQTQKAVA---AYVDIAKRHGLDP-AQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHLTLSEEVLAEIEA 336
|
.
gi 190409293 294 I 294
Cdd:PRK10625 337 V 337
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-294 |
9.37e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 105.29 E-value: 9.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSM-----NKEQAFELLDAFYEAGGNCIDTANSYqnEESEIWIGEWMKSRklRDQIVIATKFTGDYKKYEvgggksany 75
Cdd:COG1453 18 FGGMrlprkDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGP--RDKVILATKLPPWVRDPE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 76 cgNHKHSLHvsvrDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHIL------VQQGKVLYLGVS--DTPAWVVSAANY 147
Cdd:COG1453 85 --DMRKDLE----ESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPGGALealekaKAEGKIRHIGFSthGSLEVIKEAIDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 148 YatshgktPFSIYQGKWNVLNRDF--ERDIIPMARHFGMALApwdVM---GGGRFqskkameerkkngeglrtfvggpeq 222
Cdd:COG1453 159 G-------DFDFVQLQYNYLDQDNqaGEEALEAAAEKGIGVI---IMkplKGGRL------------------------- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190409293 223 teleVKISEALNKIAEEhgTESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALS--IKLTPEQIEYLESI 294
Cdd:COG1453 204 ----ANPPEKLVELLCP--PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
7-286 |
4.20e-25 |
|
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: 101.86 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGEWMKSRKlRDQIVIATKFtgDYKKyEVGGGKSANYcgnhkhsLHVS 86
Cdd:cd19090 20 DEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAELP-REPLVLSTKV--GRLP-EDTADYSADR-------VRRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 87 VRDSLRKLQTDWIDILYVH------WWDYMsSIEEVMDSLHILVQQGKVLYLGVSDTPAwvvsAANYYATSHGKTPFSIY 160
Cdd:cd19090 87 VEESLERLGRDRIDLLMIHdpervpWVDIL-APGGALEALLELKEEGLIKHIGLGGGPP----DLLRRAIETGDFDVVLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARHFGMAlapwdVMGGGRFQ----SKKAMEERKKNGEGLrtfvggpeqTELEVKISEALNKI 236
Cdd:cd19090 162 ANRYTLLDQSAADELLPAAARHGVG-----VINASPLGmgllAGRPPERVRYTYRWL---------SPELLDRAKRLYEL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 190409293 237 AEEHGtESVTAIAIAYV-RSKAKNVFpLVGGRKIEHLKQNIEALSIKLTPE 286
Cdd:cd19090 228 CDEHG-VPLPALALRFLlRDPRISTV-LVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-279 |
4.23e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 98.81 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSMN-KEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKFtgDYKKYEVGggksanycgnh 79
Cdd:cd19105 18 FGGGGlPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLR-RDKVFLATKA--SPRLDKKD----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 80 KHSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSI---EEVMDSLHILVQQGKVLYLGVS--DTPAWVVSAAnyyatSHGK 154
Cdd:cd19105 84 KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSthDNMAEVLQAA-----IESG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 155 tPFSIYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKngeglrtfvggpeqtelevkiseal 233
Cdd:cd19105 159 -WFDVIMVAYNFLNQPAELEeALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAK------------------------- 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 190409293 234 nkiaeehgTESVTAIAIAYVRSKaKNV-FPLVGGRKIEHLKQNIEAL 279
Cdd:cd19105 213 --------GFSLPQAALKWVLSN-PRVdTVVPGMRNFAELEENLAAA 250
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-277 |
8.71e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 97.55 E-value: 8.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGEWMKSRklRDQIVIATKfTGDYKKYEVgggksanycgnhK 80
Cdd:cd19100 21 LGRLSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKGR--RDKVFLATK-TGARDYEGA------------K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHvsvrDSLRKLQTDWIDILYVH------WWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYatshg 153
Cdd:cd19100 84 RDLE----RSLKRLGTDYIDLYQLHavdteeDLDQVFGPGGALEALLEAKEEGKIRFIGISGhSPEVLLRALETG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 154 ktPFSIYQGKWNVL---NRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEerkkngeglrtfvggPEQtelevkis 230
Cdd:cd19100 155 --EFDVVLFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLD---------------PEQ-------- 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 190409293 231 ealnkiaeehgtesvtaiAIAYVRSKAKNVFPLVGGRKIEHLKQNIE 277
Cdd:cd19100 210 ------------------ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
7-292 |
5.67e-23 |
|
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: 95.72 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKFTGDYKKYEvgggksanycgnhkhSLHVS 86
Cdd:cd19137 26 EEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP-REDLFIVTKVWPTNLRYD---------------DLLRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 87 VRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAtshgKTPFSIYQGKWNV 166
Cdd:cd19137 90 LQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKS----QTPIVCNQVKYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 167 LNRDFERD-IIPMARHFG---MALAPWDvmgggrfqskkameerkkngeglRTFvggpeqteleVKISEALNKIAEEHGt 242
Cdd:cd19137 166 EDRDPERDgLLEYCQKNGitvVAYSPLR-----------------------RGL----------EKTNRTLEEIAKNYG- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 190409293 243 ESVTAIAIAYVRSKaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19137 212 KTIAQIALAWLIQK-PNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
5-294 |
2.14e-21 |
|
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: 92.91 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 5 NKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKL-RDQIVIATKFTGDYKkyEVGGGKSanycgnHKHSL 83
Cdd:cd19142 29 SEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWkRSSYIVSTKIYWSYG--SEERGLS------RKHII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 84 HvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYATSHGKTPFsIYQG 162
Cdd:cd19142 101 E-SVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRwSPVEIMEAFSIARQFNCPTPI-CEQS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 163 KWNVLNRD-FERDIIPMARHFGMALAPW--------DVMGGGRFQSKKAMEERKKNGEGLRTFVGGPEQTELEVKISEAL 233
Cdd:cd19142 179 EYHMFCREkMELYMPELYNKVGVGLITWsplslgldPGISEETRRLVTKLSFKSSKYKVGSDGNGIHEETRRASHKLREL 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190409293 234 NKIAEEHGTeSVTAIAIAY-VRSKAKNVFpLVGGRKIEHLKQNIEALSI--KLTPEQIEYLESI 294
Cdd:cd19142 259 SLIAERLGC-DLTQLLIAWsLKNENVQCV-LIGASSLEQLYSQLNSLQLlpKLNSAVMEELERI 320
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-280 |
3.03e-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: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNK-EQAFELLDAFYEAGGNCIDTANSYQNE--ESEIWIGEWMKS--RKLRDQIVIATK-----FTGDYKKYevgggk 71
Cdd:cd19151 24 GDVDRyENSRAMLRRAFDLGITHFDLANNYGPPpgSAEENFGRILKEdlKPYRDELIISTKagytmWPGPYGDW------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 72 sanycGNHKHsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATS 151
Cdd:cd19151 98 -----GSKKY-LIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 152 HGkTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK--KAMEERKKNGEGlRTFVGGPEQTELEVKI 229
Cdd:cd19151 172 LG-TPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylNGIPEDSRAAKG-SSFLKPEQITEEKLAK 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 190409293 230 SEALNKIAEEHGtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALS 280
Cdd:cd19151 250 VRRLNEIAQARG-QKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-292 |
3.36e-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: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRklRDQIVIATKFtgdykkyevgggksanYCGN-HKHSLHV 85
Cdd:cd19138 29 AQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGR--RDKVFLVSKV----------------LPSNaSRQGTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 86 SVRDSLRKLQTDWIDILYVHWwdyMSSI--EEVMDSLHILVQQGKVLYLGVS--DTP----AWVVSAANYYATShgktpf 157
Cdd:cd19138 91 ACERSLRRLGTDYLDLYLLHW---RGGVplAETVAAMEELKKEGKIRAWGVSnfDTDdmeeLWAVPGGGNCAAN------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 158 siyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEerkkngeglrtfvggpeqtelevkiSEALNKIA 237
Cdd:cd19138 162 ---QVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLE-------------------------NPTLKEIA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 190409293 238 EEHGTeSVTAIAIAYV-RSkaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19138 214 ARHGA-TPAQVALAWVlRD--GNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-282 |
2.35e-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: 88.74 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYqnEESEIWIGEWMKSrklRDQIVIATKFTgdykkyevgggKSANYCGNHKH 81
Cdd:cd19097 21 GKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKR---LDKFKIITKLP-----------PLKEDKKEDEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSI-EEVMDSLHILVQQGKVLYLGVS-DTPAWVVSAANYYatshgktPFSI 159
Cdd:cd19097 85 AIEASVEASLKRLKVDSLDGLLLHNPDDLLKHgGKLVEALLELKKEGLIRKIGVSvYSPEELEKALESF-------KIDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 160 YQGKWNVLNRDFER-DIIPMAR------H----F--GMALAPwdvmgggrfqskkaMEERKKNGEGLRTFVggpeqtele 226
Cdd:cd19097 158 IQLPFNILDQRFLKsGLLAKLKkkgieiHarsvFlqGLLLME--------------PDKLPAKFAPAKPLL--------- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 190409293 227 vkisEALNKIAEEHGTeSVTAIAIAYVRSKaKNVFP-LVGGRKIEHLKQNIEALSIK 282
Cdd:cd19097 215 ----KKLHELAKKLGL-SPLELALGFVLSL-PEIDKiVVGVDSLEQLKEIIAAFKKP 265
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
4-292 |
2.64e-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: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkhS 82
Cdd:cd19071 11 LKPEETAEAVLAALEAGYRHIDTAAAYGNEAE---VGEAIRESGVpREELFITTKLWPTDHGYE---------------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 83 LHVSVRDSLRKLQTDWIDILYVHW---WDYMSSIEEVMDS---LHILVQQGKVLYLGVSdtpawvvsaaNYYAT------ 150
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHWpvpGKEGGSKEARLETwraLEELVDEGLVRSIGVS----------NFNVEhleell 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 151 SHGKTPFSIYQGKWNVLN-----RDF--ERDIIPMArhfgmalapWDVMGGGRFQSKKameerkkngeglrtfvggpeqt 223
Cdd:cd19071 143 AAARIKPAVNQIELHPYLqqkelVEFckEHGIVVQA---------YSPLGRGRRPLLD---------------------- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190409293 224 elevkiSEALNKIAEEHGTeSVTAIAIAYVRSkaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19071 192 ------DPVLKEIAKKYGK-TPAQVLLRWALQ--RGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
4-302 |
4.98e-20 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 87.80 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkhS 82
Cdd:COG0656 15 LPGEEAAAAVRTALEAGYRHIDTAAMYGNEEG---VGEAIAASGVpREELFVTTKVWNDNHGYD---------------D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 83 LHVSVRDSLRKLQTDWIDILYVHW---WDYMSSIEEvMDSlhiLVQQGKVLYLGVSD-TPA---WVVSAAnyyatshGKT 155
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWpgpGPYVETWRA-LEE---LYEEGLIRAIGVSNfDPEhleELLAET-------GVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 156 P------FSIYQGKWNVLNRDFERDIIPMArhfgmalapWDVMGGGrfqskKAMEErkkngeglrtfvggpeqtelevki 229
Cdd:COG0656 146 PavnqveLHPYLQQRELLAFCREHGIVVEA---------YSPLGRG-----KLLDD------------------------ 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190409293 230 sEALNKIAEEHGTeSVTAIAIAYVRskAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIVTFDVGFP 302
Cdd:COG0656 188 -PVLAEIAEKHGK-TPAQVVLRWHL--QRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGP 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
17-289 |
6.10e-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: 86.94 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 17 YEAGGNCIDTANSYQNEESeiwIGEWMK-SRKLRDQIVIATKFTGDYKKYEvgggksanycgnhkhSLHVSVRDSLRKLQ 95
Cdd:cd19073 24 LELGYRHIDTAEIYNNEAE---VGEAIAeSGVPREDLFITTKVWRDHLRPE---------------DLKKSVDRSLEKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 96 TDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYAT--SHGKTPFSIYQGKWNVLNRDFE 172
Cdd:cd19073 86 TDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNfTIELLEEALDISPLpiAVNQVEFHPFLYQAELLEYCRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 173 RDIIPMARhfgMALApwdvmgggrfqskkameerkkNGEGLRtfvggpeqtelevkiSEALNKIAEEHGTESVTaIAIAY 252
Cdd:cd19073 166 NDIVITAY---SPLA---------------------RGEVLR---------------DPVIQEIAEKYDKTPAQ-VALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 190409293 253 VRSkaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIE 289
Cdd:cd19073 206 LVQ--KGIVVIPKASSEDHLKENLAIFDWELTSEDVA 240
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-295 |
6.20e-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: 88.42 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNeeSEIWIGE----WMKSRKLRDQIVIATKFTGDYKKYEVGggksanycg 77
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEfrkrLRRERDAADDVQIHTKWVPDPGELTMT--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 78 nhKHSLHVSVRDSLRKLQTDWIDILYVHWWDY-MSSIEEVMDSLHILVQQGKVLYLGVS--DTPAWvvsaanYYATSHGK 154
Cdd:cd19101 87 --RAYVEAAIDRSLKRLGVDRLDLVQFHWWDYsDPGYLDAAKHLAELQEEGKIRHLGLTnfDTERL------REILDAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 155 TPFSiYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERKKNGEGLRTF-----------VGGPeqt 223
Cdd:cd19101 159 PIVS-NQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGG-LLSEKYLGVPEPTGPALETRslqkyklmideWGGW--- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190409293 224 ELEVKISEALNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19101 234 DLFQELLRTLKAIADKHGV-SIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAVL 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-293 |
1.44e-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: 87.00 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 14 DAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKFTgdykkyEVGGGKSANycgnhkhslhvSVRD---- 89
Cdd:cd19103 39 DKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYP-REDYIISTKFT------PQIAGQSAD-----------PVADmleg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 90 SLRKLQTDWIDILYVHwwdYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAtshGKTPFSIY--QGKWNVL 167
Cdd:cd19103 101 SLARLGTDYIDIYWIH---NPADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEIL---AKAGVSLSavQNHYSLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 168 NRDFERD-IIPMARHFGMALAPWDV----MGGGRFQSKKAMEERKKNGEGLRtfvggPEQTELEvKISEALNKIAEEHGT 242
Cdd:cd19103 175 YRSSEEAgILDYCKENGITFFAYMVleqgALSGKYDTKHPLPEGSGRAETYN-----PLLPQLE-ELTAVMAEIGAKHGA 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 190409293 243 eSVTAIAIAYVRskAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLES 293
Cdd:cd19103 249 -SIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQ 296
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-277 |
2.07e-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: 84.29 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIG----EWMKSRKL-RDQIVIATK---FTGD----------YKKYEVG 68
Cdd:cd19099 21 EEYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIkRDEVVIVTKagyIPGDgdeplrplkyLEEKLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 69 GGKSANYCGNHKHSLH-----VSVRDSLRKLQTDWIDILYVH----------WWDYMSSIEEVMDSLHILVQQGKVLYLG 133
Cdd:cd19099 101 GLIDVADSAGLRHCISpayleDQIERSLKRLGLDTIDLYLLHnpeeqllelgEEEFYDRLEEAFEALEEAVAEGKIRYYG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 134 VS-DTPAWVVSAANYYATS--------------HG----KTPFSIYQ-----GKWNVLNRDFErdIIPMARHFGMAlapw 189
Cdd:cd19099 181 IStWDGFRAPPALPGHLSLeklvaaaeevggdnHHfkviQLPLNLLEpealtEKNTVKGEALS--LLEAAKELGLG---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 190 dVMGGgrfqskkameerkkngeglRTFVGGPEQTELevkiseALNKIAEEHGTESVTAIAIAYVRSkAKNVF-PLVGGRK 268
Cdd:cd19099 255 -VIAS-------------------RPLNQGQLLGEL------RLADLLALPGGATLAQRALQFARS-TPGVDsALVGMRR 307
|
....*....
gi 190409293 269 IEHLKQNIE 277
Cdd:cd19099 308 PEHVDENLA 316
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
4-295 |
1.10e-17 |
|
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: 82.34 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLR-DQIVIATK-FTGDYKKYEVGGGKsanycgnhKH 81
Cdd:cd19160 30 ISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRrSSYVVTTKiYWGGQAETERGLSR--------KH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 82 SLHvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQ 161
Cdd:cd19160 102 IIE-GLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRDFERDIIPMARH-FGMALAPWDVMGGGRFQSK------KAMEERKKNGEGLRTFVGGPEQTELEVKISEaLN 234
Cdd:cd19160 181 AEYHLFQREKVEMQLPELYHkIGVGSVTWSPLACGLITGKydgrvpDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKE-LH 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190409293 235 KIAEEHGTeSVTAIAIAY-VRSKAKNVFpLVGGRKIEHLKQNIEALSI--KLTPEQIEYLESIV 295
Cdd:cd19160 260 PIADRLGC-TVAQLAIAWcLRSEGVSSV-LLGVSSAEQLIENLGSIQVlsQLTPQTVMEIDALL 321
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
25-289 |
4.98e-17 |
|
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: 80.19 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 25 DTANSYQNE--ESEIWIGEWMKS--RKLRDQIVIATKFTGDYKKYEVGGGKSANYcgnhkhsLHVSVRDSLRKLQTDWID 100
Cdd:cd19150 48 DLANNYGPPpgSAEENFGRILREdfAGYRDELIISTKAGYDMWPGPYGEWGSRKY-------LLASLDQSLKRMGLDYVD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 101 ILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYATShgKTPFSIYQGKWNVLNRDFERD-IIPM 178
Cdd:cd19150 121 IFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSySPERTREAAAILREL--GTPLLIHQPSYNMLNRWVEESgLLDT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 179 ARHFGMALAPWDVMGGGRFQSKKAmeerkkNG--EGLRTFVGG---PE-QTELEVKISEALNKIAEEHGtESVTAIAIAY 252
Cdd:cd19150 199 LQELGVGCIAFTPLAQGLLTDKYL------NGipEGSRASKERslsPKmLTEANLNSIRALNEIAQKRG-QSLAQMALAW 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 190409293 253 VRSKAKNVFPLVGGRKIEHLKQNIEAL-SIKLTPEQIE 289
Cdd:cd19150 272 VLRDGRVTSALIGASRPEQLEENVGALdNLTFSADELA 309
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
7-292 |
5.08e-17 |
|
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: 79.98 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEI---WIGEWMKSR-KLRDQIVIATKFTGDYKKYEVGGGKSAnycgnhkhs 82
Cdd:cd19077 25 EEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYpEYADKVVLSVKGGLDPDTLRPDGSPEA--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 83 LHVSVRDSLRKL-QTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyyatsHGKTPFSIYQ 161
Cdd:cd19077 96 VRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRA------HAVHPIAAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 162 GKWNVLNRD-FERDIIPMARHFGMALAPWDVMG----GGRFQSKKAMEERKKNGeGLRTFvgGPEQTELEVKISEALNKI 236
Cdd:cd19077 170 VEYSLFSREiEENGVLETCAELGIPIIAYSPLGrgllTGRIKSLADIPEGDFRR-HLDRF--NGENFEKNLKLVDALQEL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 190409293 237 AEEHGTeSVTAIAIAYVRSKAKNVF-PLVGGRKIEHLKQNIEALSIKLTPEQIEYLE 292
Cdd:cd19077 247 AEKKGC-TPAQLALAWILAQSGPKIiPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
7-294 |
6.73e-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: 78.84 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEEseiWIGEWMKSRKL-RDQIVIATKFTGDykkyevgggksaNYcgnHKHSLHV 85
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMYGNEA---QVGEAIAASGVpRDELFLTTKVWPD------------NY---SPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 86 SVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAanyyATSHGKTPFSIYQGKWN 165
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE----AVELSEAPLFTNQVEYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 166 VLNRdfERDIIPMARHFGMALAPWDVMGGGrfqskkameerkkngeglrtfvggpeqtelEVKISEALNKIAEEHGtESV 245
Cdd:cd19140 159 PYLD--QRKLLDAAREHGIALTAYSPLARG------------------------------EVLKDPVLQEIGRKHG-KTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190409293 246 TAIAIAYVRSKaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:cd19140 206 AQVALRWLLQQ-EGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-285 |
8.29e-17 |
|
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: 79.41 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKL-RDQIVIATKFtgdykkyeVGGGKSANYCG-NH 79
Cdd:cd19141 25 SQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWrRSSYVITTKI--------FWGGKAETERGlSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 80 KHSLHvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSI 159
Cdd:cd19141 97 KHIIE-GLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 160 YQGKWNVLNRDFERDIIPMARH-FGMALAPWD-VMGG---GRFQSKKAMEERK--KNGEGLRTFVGGPEQTELEVKISEa 232
Cdd:cd19141 176 EQAEYHLFQREKVEMQLPELFHkIGVGAMTWSpLACGilsGKYDDGVPEYSRAslKGYQWLKEKILSEEGRRQQAKLKE- 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 233 LNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSI--KLTP 285
Cdd:cd19141 255 LQIIADRLGC-TLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVlpKLTP 308
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
12-280 |
3.71e-16 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 78.11 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 12 LLDAFYEAGGNCIDTANSY-----QNEESeiwIGEWMKS--RKLRDQIVIATKFTGDYKKYEVGGGKSANYcgnhkhsLH 84
Cdd:PRK09912 48 ILRKAFDLGITHFDLANNYgpppgSAEEN---FGRLLREdfAAYRDELIISTKAGYDMWPGPYGSGGSRKY-------LL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 85 VSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYatSHGKTPFSIYQGK 163
Cdd:PRK09912 118 ASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSySPERTQKMVELL--REWKIPLLIHQPS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 164 WNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSK--------KAMEERKKNGEGLRTFVggpeQTELEVKISEALN 234
Cdd:PRK09912 196 YNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdSRMHREGNKVRGLTPKM----LTEANLNSLRLLN 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 190409293 235 KIAEEHGtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALS 280
Cdd:PRK09912 272 EMAQQRG-QSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALN 316
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
2-295 |
1.81e-14 |
|
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: 73.15 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLR-DQIVIATKFtgdykkyeVGGGKSANYCGNHK 80
Cdd:cd19159 26 GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRrSSLVITTKL--------YWGGKAETERGLSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIY 160
Cdd:cd19159 98 KHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARH-FGMALAPWDVMGGGRFQSK------KAMEERKKNGEGLRTFVGGPEQTELEVKISEaL 233
Cdd:cd19159 178 QAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLACGIISGKygngvpESSRASLKCYQWLKERIVSEEGRKQQNKLKD-L 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190409293 234 NKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSI--KLTPEQIEYLESIV 295
Cdd:cd19159 257 SPIAERLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 319
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
2-295 |
8.11e-14 |
|
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: 70.88 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLR-DQIVIATKFtgdykkyeVGGGKSANYCGNHK 80
Cdd:cd19158 26 GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRrSSLVITTKI--------FWGGKAETERGLSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIY 160
Cdd:cd19158 98 KHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 161 QGKWNVLNRDFERDIIPMARH-FGMALAPWDVMG----GGRFQSKKAMEERK--KNGEGLRTFVGGPEQTELEVKISEaL 233
Cdd:cd19158 178 QAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKYDSGIPPYSRAslKGYQWLKDKILSEEGRRQQAKLKE-L 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190409293 234 NKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSI--KLTPEQIEYLESIV 295
Cdd:cd19158 257 QAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSIL 319
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
2-135 |
1.08e-12 |
|
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: 67.19 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKfTGdykKYEVGGGKSANYcgNHKH 81
Cdd:cd19163 28 GPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIP-RDSYYLATK-VG---RYGLDPDKMFDF--SAER 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 190409293 82 SLHvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMD----SLHILVQQGKVLYLGVS 135
Cdd:cd19163 101 ITK-SVEESLKRLGLDYIDIIQVHDIEFAPSLDQILNetlpALQKLKEEGKVRFIGIT 157
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-289 |
3.17e-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: 65.45 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMK-SRKLRDQIVIATKFTGDykkyevgggksaNYcgnHKHSLHVSVRDSLRKLQT 96
Cdd:cd19139 25 ELGYRHIDTAQIYDNEAA---VGQAIAeSGVPRDELFITTKIWID------------NL---SKDKLLPSLEESLEKLRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 97 DWIDILYVHW--WDYMSSIEEVMDSLHILVQQGKVLYLGVSDtpawvvsaanyyatshgktpFSIYQ--------GKWNV 166
Cdd:cd19139 87 DYVDLTLIHWpsPNDEVPVEEYIGALAEAKEQGLTRHIGVSN--------------------FTIALldeaiavvGAGAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 167 LNRDFE-------RDIIPMARHFGMALAPWDVMGGGrfqskKAMEErkkngeglrtfvggpeqtelevkisEALNKIAEE 239
Cdd:cd19139 147 ATNQIElspylqnRKLVAHCKQHGIHVTSYMTLAYG-----KVLDD-------------------------PVLAAIAER 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 190409293 240 HGTeSVTAIAIAYVRSKAKNVFPlvGGRKIEHLKQNIEALSIKLTPEQIE 289
Cdd:cd19139 197 HGA-TPAQIALAWAMARGYAVIP--SSTKREHLRSNLLALDLTLDADDMA 243
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-294 |
3.66e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 66.13 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSrkLRDQIVIATKftgdykkYEVGGGKSanycGNHK 80
Cdd:cd19104 26 MGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKG--LPAGPYITTK-------VRLDPDDL----GDIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HSLHVSVRDSLRKLQTDWIDILYVH------------------WWDYMssiEEVMDSLHILVQQGKVLYLGVSdtpAWVV 142
Cdd:cd19104 93 GQIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvggtlsttDVLGL---GGVADAFERLRSEGKIRFIGIT---GLGN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 143 SAANYYATSHGKtpFSIYQGKWNVLN-----------RDFE-RDIIPMARHFGMALAPWDVMGGGrfqskkAMEERKKNG 210
Cdd:cd19104 167 PPAIRELLDSGK--FDAVQVYYNLLNpsaaearprgwSAQDyGGIIDAAAEHGVGVMGIRVLAAG------ALTTSLDRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 211 EGLRTFVGGPEQTELEVkiSEALNKIAEEHGtESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSI-KLTPEQIE 289
Cdd:cd19104 239 REAPPTSDSDVAIDFRR--AAAFRALAREWG-ETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAgPLPAENLA 315
|
....*
gi 190409293 290 YLESI 294
Cdd:cd19104 316 RLEAL 320
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
7-286 |
3.69e-12 |
|
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: 65.84 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKsRKLRDQIVIATKfTGDYKKY--EVGGGKSANYCGNHKHSLH 84
Cdd:cd19162 19 DEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA-RHPRAEYVVSTK-VGRLLEPgaAGRPAGADRRFDFSADGIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 85 VSVRDSLRKLQTDWIDILYVHWWD--YMSSIEEVMDSLHILVQQGKVLYLGVSDTpawVVSAANYYATSHGKTPFSIyQG 162
Cdd:cd19162 97 RSIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVVGAIGVGVT---DWAALLRAARRADVDVVMV-AG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 163 KWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFqskkAMEERkkngEGLRTFVGGPEQTELEVkiSEALNKIAEEHGT 242
Cdd:cd19162 173 RYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL----ATDDP----AGDRYDYRPATPEVLAR--ARRLAAVCRRYGV 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 190409293 243 ESVTAiAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPE 286
Cdd:cd19162 243 PLPAA-ALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
2-208 |
4.32e-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: 65.28 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKlRDQIVIATKF-TGDYKKYEvgggksanycGNHK 80
Cdd:cd19096 16 DSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGP-REKFYLATKLpPWSVKSAE----------DFRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 81 HslhvsVRDSLRKLQTDWIDILYVHWWDyMSSIEEVMDSLHIL------VQQGKVLYLGVS--DTPAWVVSAANYYatsh 152
Cdd:cd19096 85 I-----LEESLKRLGVDYIDFYLLHGLN-SPEWLEKARKGGLLeflekaKKEGLIRHIGFSfhDSPELLKEILDSY---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190409293 153 gktPFSIYQGKWNVLNRDFERDI--IPMARHFGMALApwdVM---GGGRF--QSKKAMEERKK 208
Cdd:cd19096 155 ---DFDFVQLQYNYLDQENQAGRpgIEYAAKKGMGVI---IMeplKGGGLanNPPEALAILCG 211
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-295 |
4.84e-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: 65.83 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 6 KEQAFELLDAFYEAGGNCIDTANSYQneESEIWIGEWMKSRKL-RDQIVIATK----FTGDYK----KYEVgggksanyc 76
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSYG--RAEEFLGSWLRSRNIaPDAVFVGSKwgytYTADWQvdaaVHEV--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 77 gnHKHSLHVSVR--DSLRKLQTDWIDILYVHWWDYMSSI---EEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATS 151
Cdd:cd19098 103 --KDHSLARLLKqwEETRSLLGKHLDLYQIHSATLESGVledADVLAALAELKAEGVKIGLSLSGPQQAETLRRALEIEI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 152 HGKTPFSIYQGKWNVlnrdFERDIIP---MARHFGMALAPWDVMGGGRFqskkameerkkngeglrtfVGGPEQTELEVK 228
Cdd:cd19098 181 DGARLFDSVQATWNL----LEQSAGEaleEAHEAGMGVIVKEALANGRL-------------------TDRNPSPELAPL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190409293 229 iSEALNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIV 295
Cdd:cd19098 238 -MAVLKAVADRLGV-TPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALADLA 302
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
5-294 |
1.20e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 64.22 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 5 NKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMksRKLRDQIVIATKftgdykkyeVGGGKSANYCGNHKHS-- 82
Cdd:PRK10376 38 DRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREAL--HPYPDDLTIVTK---------VGARRGEDGSWLPAFSpa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 83 -LHVSVRDSLRKLQTDWIDILYVH-WWDYMS----SIEEVMDSLHILVQQGKVLYLGVSD-TPAWVVSAanyyatsHGKT 155
Cdd:PRK10376 107 eLRRAVHDNLRNLGLDVLDVVNLRlMGDGHGpaegSIEEPLTVLAELQRQGLVRHIGLSNvTPTQVAEA-------RKIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 156 PFSIYQGKWNVLNRDFERDIIPMARHfGMALAPWDVMGGgrFQskkameerkkngeglrtfvggPEQtelevkiSEALNK 235
Cdd:PRK10376 180 EIVCVQNHYNLAHRADDALIDALARD-GIAYVPFFPLGG--FT---------------------PLQ-------SSTLSD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 190409293 236 IAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:PRK10376 229 VAASLGA-TPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
3-286 |
4.46e-11 |
|
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: 62.73 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 3 SMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKsRKLRDQIVIATKftgdykkyeVG-------GGKSANY 75
Cdd:cd19161 16 AVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLR-EKPRDEFVLSTK---------VGrllkparEGSVPDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 76 CGnHKHSLHV-------------SVRDSLRKLQTDWIDILYVHWWDYMSSIEE--------VMDS----LHILVQQG--K 128
Cdd:cd19161 86 NG-FVDPLPFeivydysydgimrSFEDSLQRLGLNRIDILYVHDIGVYTHGDRkerhhfaqLMSGgfkaLEELKKAGviK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 129 VLYLGVSDTPAwVVSAANYYatshgktPFSIY--QGKWNVLNRDFERDIIPMARHFGMALAPwdvmgGGRFQSKKAmeer 206
Cdd:cd19161 165 AFGLGVNEVQI-CLEALDEA-------DLDCFllAGRYSLLDQSAEEEFLPRCEQRGTSLVI-----GGVFNSGIL---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 207 KKNGEGLRTFVGGPEQTELEVKISEaLNKIAEEHGTESVTAiAIAYV-RSKA-KNVfpLVGGRKIEHLKQNIEALSIKLt 284
Cdd:cd19161 228 ATGTKSGAKFNYGDAPAEIISRVME-IEKICDAYNVPLAAA-ALQFPlRHPAvASV--LTGARNPAQLRQNVEAFQTDI- 302
|
..
gi 190409293 285 PE 286
Cdd:cd19161 303 PE 304
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
11-138 |
5.56e-11 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 62.29 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 11 ELLDAFYEAGGNCIDTANSYQneESEIWIGEWMKS-RKL--RDQIVIATKfTGDYkkyevgGGKSANYCGNHkhsLHVSV 87
Cdd:cd19164 38 DIVRRALELGIRAFDTSPYYG--PSEIILGRALKAlRDEfpRDTYFIITK-VGRY------GPDDFDYSPEW---IRASV 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 190409293 88 RDSLRKLQTDWIDILYVHWWDYMSSiEEVMDSLHILVQ---QGKVLYLGVSDTP 138
Cdd:cd19164 106 ERSLRRLHTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGISGYP 158
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
11-142 |
2.17e-10 |
|
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: 60.63 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 11 ELLDAFYEA---GGNCIDTANSYQNEESEIWIGEWMKSRKL-RDQIVIATKftgdykkyeVGGGKSanycGNHKHS---L 83
Cdd:cd19153 34 EAVAIVAEAfaaGINHFDTSPYYGAESSEAVLGKALAALQVpRSSYTVATK---------VGRYRD----SEFDYSaerV 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190409293 84 HVSVRDSLRKLQTDWIDILYVH---WWDYMSSIEEVMDSLHILVQQGKVLYLGVS----DTPAWVV 142
Cdd:cd19153 101 RASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIGIAgyplDTLTRAT 166
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
24-289 |
3.27e-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: 59.94 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 24 IDTANSYQNEESeiwIGE-WMKSRKLRDQIVIATKFtgdykkyevgGGKSANYCGnhkhslhvSVRDSLRKLQTDWIDIL 102
Cdd:cd19120 42 IDTAEMYGNEKE---VGEaLKESGVPREDLFITTKV----------SPGIKDPRE--------ALRKSLAKLGVDYVDLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 103 YVH--WWDYMS--SIEEVMDSLHILVQQGKVLYLGVSdtpawvvsaaNYYAT------SHGKTPFSIYQGKWNVLNRDFE 172
Cdd:cd19120 101 LIHspFFAKEGgpTLAEAWAELEALKDAGLVRSIGVS----------NFRIEdleellDTAKIKPAVNQIEFHPYLYPQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 173 RDIIPMARHFGMA------LAPwdvmgggrfqskkameerkkngegLRTFVGGPeqtelevkISEALNKIAEEHGtESVT 246
Cdd:cd19120 171 PALLEYCREHGIVvsayspLSP------------------------LTRDAGGP--------LDPVLEKIAEKYG-VTPA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 190409293 247 AIAIAYVRskAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIE 289
Cdd:cd19120 218 QVLLRWAL--QKGIVVVTTSSKEERMKEYLEAFDFELTEEEVE 258
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
4-294 |
3.38e-08 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 54.04 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGE----WMKSRKL-RDQIVIATKFTGDYKKYEvgggksanycgn 78
Cdd:cd19111 14 SPPEEVRAAVDYALFVGYRHIDTALSYQNEKA---IGEalkwWLKNGKLkREEVFITTKLPPVYLEFK------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 79 hkhSLHVSVRDSLRKLQTDWIDILYVHW-W------------DYMSSIEEVMDSLHILVQQGKVLYLGVSDtpaWVVSAA 145
Cdd:cd19111 79 ---DTEKSLEKSLENLKLPYVDLYLIHHpCgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSN---FNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 146 NyYATSHGKTPFSIYQGKWNVLNRdfERDIIPMARHFGMALAPWDVMGggrfqskkameerkknGEGLRTFVGGPEQ-TE 224
Cdd:cd19111 153 N-KILAYAKVKPSNLQLECHAYLQ--QRELRKFCNKKNIVVTAYAPLG----------------SPGRANQSLWPDQpDL 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 225 LEvkiSEALNKIAEEHGtESVTAIAIAYVRSkaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:cd19111 214 LE---DPTVLAIAKELD-KTPAQVLLRFVLQ--RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTL 277
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-136 |
6.37e-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: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkhSLHV 85
Cdd:cd19131 23 DEAASAVREALEVGYRSIDTAAIYGNEEG---VGKAIRASGVpREELFITTKLWNSDQGYD---------------STLR 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 190409293 86 SVRDSLRKLQTDWIDILYVHWwdYMSSIEEVMDSLHILVQ---QGKVLYLGVSD 136
Cdd:cd19131 85 AFDESLRKLGLDYVDLYLIHW--PVPAQDKYVETWKALIElkkEGRVKSIGVSN 136
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
13-135 |
9.47e-08 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 52.19 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 13 LDAFyEAGGNCIDTANSYQNEESeiwIGEWMK-SRKLRDQIVIATKFTGDYKKYEvgggksanycgNHKHSLHvsvrDSL 91
Cdd:cd19133 30 LEAI-KAGYRLIDTAAAYGNEEA---VGRAIKkSGIPREELFITTKLWIQDAGYE-----------KAKKAFE----RSL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 92 RKLQTDWIDILYVHW--------WDYMssiEEvmdslhiLVQQGKVLYLGVS 135
Cdd:cd19133 91 KRLGLDYLDLYLIHQpfgdvygaWRAM---EE-------LYKEGKIRAIGVS 132
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
4-135 |
2.02e-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: 51.50 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 4 MNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkhS 82
Cdd:cd19132 17 LKGDEGVEAVVAALQAGYRLLDTAFNYENEGA---VGEAVRRSGVpREELFVTTKLPGRHHGYE---------------E 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 190409293 83 LHVSVRDSLRKLQTDWIDILYVHWWD-----YMSSIEEVMDslhiLVQQGKVLYLGVS 135
Cdd:cd19132 79 ALRTIEESLYRLGLDYVDLYLIHWPNpsrdlYVEAWQALIE----AREEGLVRSIGVS 132
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
18-136 |
7.87e-07 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 49.64 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWM-KSRKLRDQIVIATKFTGDykkyevgggksaNYCgnhKHSLHVSVRDSLRKLQT 96
Cdd:PRK11172 27 ELGYRAIDTAQIYDNEAA---VGQAIaESGVPRDELFITTKIWID------------NLA---KDKLIPSLKESLQKLRT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 190409293 97 DWIDILYVHW--WDYMSSIEEVMDSLHILVQQGKVLYLGVSD 136
Cdd:PRK11172 89 DYVDLTLIHWpsPNDEVSVEEFMQALLEAKKQGLTREIGISN 130
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
2-138 |
9.76e-07 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.78 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 2 GSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKL-RDQIVIATKfTGDYKKyevGGGKSANycgnhk 80
Cdd:PLN02587 26 GPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIpREKYVVSTK-CGRYGE---GFDFSAE------ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190409293 81 hSLHVSVRDSLRKLQTDWIDILYVHWWDYMS---SIEEVMDSLHILVQQGKVLYLGVSDTP 138
Cdd:PLN02587 96 -RVTKSVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESGKVRFIGITGLP 155
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
18-136 |
1.90e-06 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 48.53 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDykkyevgggksanycgNHKHSlHVSVRDSLRKLQT 96
Cdd:PRK11565 39 EVGYRSIDTAAIYKNEEG---VGKALKEASVaREELFITTKLWND----------------DHKRP-REALEESLKKLQL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 190409293 97 DWIDILYVHWWD-----YMSSIEEVMDslhiLVQQGKVLYLGVSD 136
Cdd:PRK11565 99 DYVDLYLMHWPVpaidhYVEAWKGMIE----LQKEGLIKSIGVCN 139
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
24-135 |
2.43e-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: 48.09 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 24 IDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATK-FTGDYKkYEvgggksanycgnhkhSLHVSVRDSLRKLQTDWIDI 101
Cdd:cd19135 43 IDTAKRYGCEEL---LGKAIKESGVpREDLFLTTKlWPSDYG-YE---------------STKQAFEASLKRLGVDYLDL 103
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 190409293 102 LYVHWWDYMSS-------IEEVMDSLHILVQQGKVLYLGVS 135
Cdd:cd19135 104 YLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVS 144
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
7-135 |
3.00e-06 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 48.01 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 7 EQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMKS-----RKLRDQIVIATKFTgdykKYEVGGGKSANYCGNhkh 81
Cdd:cd19136 15 EEVRQAVDAALKAGYRLIDTASVYRNEAD---IGKALRDllpkyGLSREDIFITSKLA----PKDQGYEKARAACLG--- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190409293 82 slhvsvrdSLRKLQTDWIDILYVHW--------------------WdymssieEVMDSLHilvQQGKVLYLGVS 135
Cdd:cd19136 85 --------SLERLGTDYLDLYLIHWpgvqglkpsdprnaelrresW-------RALEDLY---KEGKLRAIGVS 140
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
18-136 |
3.03e-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: 47.82 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYKKYEvgGGKSAnycgnhkhslhvsVRDSLRKLQT 96
Cdd:cd19126 34 ENGYRSIDTAAIYKNEEG---VGEAIRESGVpREELFVTTKLWNDDQRAR--RTEDA-------------FQESLDRLGL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 190409293 97 DWIDILYVHW---------WDYMssiEEVMDSlhilvqqGKVLYLGVSD 136
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 ... |
18-294 |
1.31e-05 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 46.12 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEEsEIW--IGEWMKSRKL-RDQIVIATKFTGDYKKyevgggksanycgnhKHSLHVSVRDSLRKL 94
Cdd:cd19116 36 EAGYRHIDTAYLYGNEA-EVGeaIREKIAEGVVkREDLFITTKLWNSYHE---------------REQVEPALRESLKRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 95 QTDWIDILYVHWwdYMSSIEEVMDSLHILVQQGKVLYLgvsDTpaW-----VVSaaNYYATSHGKTPFSIYQgkwnvLNR 169
Cdd:cd19116 100 GLDYVDLYLIHW--PVAFKENNDSESNGDGSLSDIDYL---ET--WrgmedLVK--LGLTRSIGVSNFNSEQ-----INR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 170 DFER-DIIPMARHfgMALAPwdvmgggRFQSKKAMEERKKNGEGLRTF--VGGPE---QTELEVKI-SEALNKIAEEHGt 242
Cdd:cd19116 166 LLSNcNIKPAVNQ--IEVHP-------TLTQEKLVAYCQSNGIVVMAYspFGRLVprgQTNPPPRLdDPTLVAIAKKYG- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 243 ESVTAIAIAYVRSkaKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:cd19116 236 KTTAQIVLRYLID--RGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSF 285
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
13-105 |
1.37e-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: 45.98 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 13 LDAFYEAGGNCIDTANSYQNEESeiwIG----EWMKSRKL-RDQIVIATKFTgdykkyevgggksanYCGNHKHSLHVSV 87
Cdd:cd19155 31 VDTALEAGYRHIDTAYVYRNEAA---IGnvlkKWIDSGKVkREELFIVTKLP---------------PGGNRREKVEKFL 92
|
90
....*....|....*...
gi 190409293 88 RDSLRKLQTDWIDILYVH 105
Cdd:cd19155 93 LKSLEKLQLDYVDLYLIH 110
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
18-105 |
1.58e-05 |
|
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: 45.87 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEEsEIW--IGEWMKSRKL-RDQIVIATKFtgdykkyevgggksanycGNHKHS---LHVSVRDSL 91
Cdd:cd19154 36 KAGYRLIDTAFLYQNEE-AIGeaLAELLEEGVVkREDLFITTKL------------------WTHEHApedVEEALRESL 96
|
90
....*....|....
gi 190409293 92 RKLQTDWIDILYVH 105
Cdd:cd19154 97 KKLQLEYVDLYLIH 110
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
18-294 |
1.59e-05 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 45.86 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEeSEIW--IGEWMKSRKL-RDQIVIATKFtgdykkyevgggksanYCGNHKHSlhvSVRDSLRK- 93
Cdd:cd19123 36 EAGYRHIDCAAIYGNE-AEIGaaLAEVFKEGKVkREDLWITSKL----------------WNNSHAPE---DVLPALEKt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 94 ---LQTDWIDILYVHW--------------WDYMS----SIEEVMDSLHILVQQGKVLYLGVSDtpawvvsaanyyatsh 152
Cdd:cd19123 96 ladLQLDYLDLYLMHWpvalkkgvgfpesgEDLLSlspiPLEDTWRAMEELVDKGLCRHIGVSN---------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 153 gktpFSIYQgkwnvlnrdfERDIIPMARHF----GMALAPWdvmgggrFQSKKAMEERKKNGEGLRTF--VGGPE----- 221
Cdd:cd19123 160 ----FSVKK----------LEDLLATARIKpavnQVELHPY-------LQQPELLAFCRDNGIHLTAYspLGSGDrpaam 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 222 QTELEVKISE--ALNKIAEEHGTeSVTAIAIAYVRSKAKNVFPLVGGRkiEHLKQNIEALSIKLTPEQIEYLESI 294
Cdd:cd19123 219 KAEGEPVLLEdpVINKIAEKHGA-SPAQVLIAWAIQRGTVVIPKSVNP--ERIQQNLEAAEVELDASDMATIAAL 290
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-136 |
5.41e-05 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 44.03 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 8 QAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYkkyevgggksanycgnHKHsLHVS 86
Cdd:cd19117 28 EVAKAVEAALKAGYRHIDTAAIYGNEEE---VGQGIKDSGVpREEIFITTKLWCTW----------------HRR-VEEA 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190409293 87 VRDSLRKLQTDWIDILYVHW-------------------------WDYMSSIEEVMDslhiLVQQGKVLYLGVSD 136
Cdd:cd19117 88 LDQSLKKLGLDYVDLYLMHWpvpldpdgndflfkkddgtkdhepdWDFIKTWELMQK----LPATGKVKAIGVSN 158
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
18-136 |
1.51e-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: 42.76 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMK-SRKLRDQIVIATKFTGDYKKYEvgggksanycgnhkhSLHVSVRDSLRKLQT 96
Cdd:cd19157 35 KNGYRSIDTAAIYGNEEG---VGKGIKeSGIPREELFITSKVWNADQGYD---------------STLKAFEASLERLGL 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 190409293 97 DWIDILYVHwWDYMSSIEEVMDSLHILVQQGKVLYLGVSD 136
Cdd:cd19157 97 DYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVSN 135
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
18-136 |
2.04e-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: 42.12 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDYKKYEvgggksanycgnhkhSLHVSVRDSLRKLQT 96
Cdd:cd19156 34 EAGYRHIDTAAIYKNEEG---VGQGIRESGVpREEVFVTTKLWNSDQGYE---------------STLAAFEESLEKLGL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 190409293 97 DWIDILYVHwWDYMSSIEEVMDSLHILVQQGKVLYLGVSD 136
Cdd:cd19156 96 DYVDLYLIH-WPVKGKFKDTWKAFEKLYKEKKVRAIGVSN 134
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
24-136 |
2.24e-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: 42.01 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 24 IDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATK-FTGDYKKYEvgggksanycgnhkhSLHvSVRDSLRKLQTDWIDI 101
Cdd:cd19127 39 IDTAAAYGNERE---VGEGIRRSGVdRSDIFVTTKlWISDYGYDK---------------ALR-GFDASLRRLGLDYVDL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 190409293 102 LYVHW-----WDymSSIEEVMDSLHILVqQGKVLYLGVSD 136
Cdd:cd19127 100 YLLHWpvpndFD--RTIQAYKALEKLLA-EGRVRAIGVSN 136
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
18-136 |
2.38e-03 |
|
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: 39.12 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMKSRKL-RDQIVIATKFTGDykkyevgggksanycgNHKHS-LHVSVRDSLRKLQ 95
Cdd:cd19130 34 EVGYRHIDTAAIYGNEEG---VGAAIAASGIpRDELFVTTKLWND----------------RHDGDePAAAFAESLAKLG 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 190409293 96 TDWIDILYVHW-----------WDYMSSieevmdslhiLVQQGKVLYLGVSD 136
Cdd:cd19130 95 LDQVDLYLVHWptpaagnyvhtWEAMIE----------LRAAGRTRSIGVSN 136
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
1-106 |
4.60e-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: 38.30 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 1 MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESeiwIGEWM-KSRKLRDQIVIATKFTGDykkyEVGGGKSANYCgnh 79
Cdd:cd19134 18 VGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAA---VGRAIaASGIPRGELFVTTKLATP----DQGFTASQAAC--- 87
|
90 100
....*....|....*....|....*..
gi 190409293 80 khslhvsvRDSLRKLQTDWIDILYVHW 106
Cdd:cd19134 88 --------RASLERLGLDYVDLYLIHW 106
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|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
18-106 |
7.75e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 37.59 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190409293 18 EAGGNCIDTANSYQNEESeiwIGEWMKSR------KlRDQIVIATKFtgdykkyevgggksanYCGNHKHSL-HVSVRDS 90
Cdd:cd19108 38 DAGFRHIDSAYLYQNEEE---VGQAIRSKiadgtvK-REDIFYTSKL----------------WCTFHRPELvRPALEKS 97
|
90
....*....|....*.
gi 190409293 91 LRKLQTDWIDILYVHW 106
Cdd:cd19108 98 LKKLQLDYVDLYLIHF 113
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